Starting phenix.real_space_refine on Fri Dec 8 12:10:14 2023 by dcliebschner =============================================================================== Processing files: ------------------------------------------------------------------------------- Found model, /net/marbles/raid1/dorothee/rerefine/cryoem/data_no_H/6x62_22068/12_2023/6x62_22068_neut.pdb Found real_map, /net/marbles/raid1/dorothee/rerefine/cryoem/data_no_H/6x62_22068/12_2023/6x62_22068.map Processing PHIL parameters: ------------------------------------------------------------------------------- Adding command-line PHIL: ------------------------- refinement.macro_cycles=10 scattering_table=electron resolution=3.5 write_initial_geo_file=False Final processed PHIL parameters: ------------------------------------------------------------------------------- data_manager { real_map_files = "/net/marbles/raid1/dorothee/rerefine/cryoem/data_no_H/6x62_22068/12_2023/6x62_22068.map" default_real_map = "/net/marbles/raid1/dorothee/rerefine/cryoem/data_no_H/6x62_22068/12_2023/6x62_22068.map" model { file = "/net/marbles/raid1/dorothee/rerefine/cryoem/data_no_H/6x62_22068/12_2023/6x62_22068_neut.pdb" } default_model = "/net/marbles/raid1/dorothee/rerefine/cryoem/data_no_H/6x62_22068/12_2023/6x62_22068_neut.pdb" } resolution = 3.5 write_initial_geo_file = False refinement { macro_cycles = 10 } qi { qm_restraints { package { program = *test } } } Starting job =============================================================================== ------------------------------------------------------------------------------- Citation: ********* Afonine PV, Poon BK, Read RJ, Sobolev OV, Terwilliger TC, Urzhumtsev A, Adams PD. (2018) Real-space refinement in PHENIX for cryo-EM and crystallography. Acta Cryst. D74:531-544. Validating inputs Origin is already at (0, 0, 0), no shifts will be applied ------------------------------------------------------------------------------- Processing inputs ***************** Set random seed Set to: 0 Set model cs if undefined Decide on map wrapping Map wrapping is set to: False Normalize map: mean=0, sd=1 Input map: mean= 0.000 sd= 0.004 Set stop_for_unknowns flag Set to: True Assert model is a single copy model Assert all atoms have isotropic ADPs Construct map_model_manager Extract box with map and model Check model and map are aligned Set scattering table Set to: electron Number of scattering types: 4 Type Number sf(0) Gaussians S 273 5.16 5 C 68484 2.51 5 N 19708 2.21 5 O 20605 1.98 5 sf(0) = scattering factor at diffraction angle 0. Process input model Symmetric amino acids flipped Residue "AC ARG 75": "NH1" <-> "NH2" Residue "AC ARG 148": "NH1" <-> "NH2" Residue "AC GLU 174": "OE1" <-> "OE2" Residue "AC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AC GLU 196": "OE1" <-> "OE2" Residue "AC ASP 205": "OD1" <-> "OD2" Residue "AC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AC ASP 230": "OD1" <-> "OD2" Residue "DH ARG 294": "NH1" <-> "NH2" Residue "DH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DH GLU 360": "OE1" <-> "OE2" Residue "DK ASP 86": "OD1" <-> "OD2" Residue "DK ARG 90": "NH1" <-> "NH2" Residue "DK ARG 128": "NH1" <-> "NH2" Residue "DK ARG 130": "NH1" <-> "NH2" Residue "DK ARG 138": "NH1" <-> "NH2" Residue "DK ARG 152": "NH1" <-> "NH2" Residue "DK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Dd PHE 25": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Dd GLU 59": "OE1" <-> "OE2" Residue "Dd GLU 92": "OE1" <-> "OE2" Residue "Dd ARG 107": "NH1" <-> "NH2" Residue "Dd ARG 133": "NH1" <-> "NH2" Residue "Dd TYR 148": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Dd ARG 157": "NH1" <-> "NH2" Residue "Dd TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "EC ARG 75": "NH1" <-> "NH2" Residue "EC ARG 148": "NH1" <-> "NH2" Residue "EC GLU 174": "OE1" <-> "OE2" Residue "EC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "EC GLU 196": "OE1" <-> "OE2" Residue "EC ASP 205": "OD1" <-> "OD2" Residue "EC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "EC ASP 230": "OD1" <-> "OD2" Residue "ED ASP 35": "OD1" <-> "OD2" Residue "ED GLU 54": "OE1" <-> "OE2" Residue "ED ARG 82": "NH1" <-> "NH2" Residue "ED ASP 86": "OD1" <-> "OD2" Residue "ED PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "ED ARG 107": "NH1" <-> "NH2" Residue "ED ARG 133": "NH1" <-> "NH2" Residue "ED ASP 136": "OD1" <-> "OD2" Residue "ED ARG 157": "NH1" <-> "NH2" Residue "ED TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "EH ARG 294": "NH1" <-> "NH2" Residue "EH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "EH GLU 360": "OE1" <-> "OE2" Residue "EK ASP 86": "OD1" <-> "OD2" Residue "EK ARG 90": "NH1" <-> "NH2" Residue "EK ARG 128": "NH1" <-> "NH2" Residue "EK ARG 130": "NH1" <-> "NH2" Residue "EK ARG 138": "NH1" <-> "NH2" Residue "EK ARG 152": "NH1" <-> "NH2" Residue "EK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "EK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Ed GLU 54": "OE1" <-> "OE2" Residue "Ed GLU 93": "OE1" <-> "OE2" Residue "Ed ARG 107": "NH1" <-> "NH2" Residue "Ed ASP 125": "OD1" <-> "OD2" Residue "Ed GLU 126": "OE1" <-> "OE2" Residue "Ed GLU 130": "OE1" <-> "OE2" Residue "Ed ARG 133": "NH1" <-> "NH2" Residue "Ed ASP 136": "OD1" <-> "OD2" Residue "Ed ARG 157": "NH1" <-> "NH2" Residue "FC ARG 75": "NH1" <-> "NH2" Residue "FC ARG 148": "NH1" <-> "NH2" Residue "FC GLU 174": "OE1" <-> "OE2" Residue "FC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "FC GLU 196": "OE1" <-> "OE2" Residue "FC ASP 205": "OD1" <-> "OD2" Residue "FC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "FC ASP 230": "OD1" <-> "OD2" Residue "FD TYR 77": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "FD ARG 82": "NH1" <-> "NH2" Residue "FD GLU 92": "OE1" <-> "OE2" Residue "FD PHE 104": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "FD ARG 107": "NH1" <-> "NH2" Residue "FD GLU 130": "OE1" <-> "OE2" Residue "FD ARG 133": "NH1" <-> "NH2" Residue "FD ASP 134": "OD1" <-> "OD2" Residue "FD GLU 155": "OE1" <-> "OE2" Residue "FD ARG 157": "NH1" <-> "NH2" Residue "FH ARG 294": "NH1" <-> "NH2" Residue "FH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "FH GLU 360": "OE1" <-> "OE2" Residue "FK ASP 86": "OD1" <-> "OD2" Residue "FK ARG 90": "NH1" <-> "NH2" Residue "FK ARG 128": "NH1" <-> "NH2" Residue "FK ARG 130": "NH1" <-> "NH2" Residue "FK ARG 138": "NH1" <-> "NH2" Residue "FK ARG 152": "NH1" <-> "NH2" Residue "FK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "FK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Fd ASP 86": "OD1" <-> "OD2" Residue "Fd GLU 92": "OE1" <-> "OE2" Residue "Fd GLU 93": "OE1" <-> "OE2" Residue "Fd ARG 107": "NH1" <-> "NH2" Residue "Fd ASP 125": "OD1" <-> "OD2" Residue "Fd ARG 133": "NH1" <-> "NH2" Residue "Fd ASP 136": "OD1" <-> "OD2" Residue "Fd ARG 157": "NH1" <-> "NH2" Residue "GC ARG 75": "NH1" <-> "NH2" Residue "GC ARG 148": "NH1" <-> "NH2" Residue "GC GLU 174": "OE1" <-> "OE2" Residue "GC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "GC GLU 196": "OE1" <-> "OE2" Residue "GC ASP 205": "OD1" <-> "OD2" Residue "GC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "GC ASP 230": "OD1" <-> "OD2" Residue "GD GLU 43": "OE1" <-> "OE2" Residue "GD ARG 82": "NH1" <-> "NH2" Residue "GD GLU 92": "OE1" <-> "OE2" Residue "GD GLU 93": "OE1" <-> "OE2" Residue "GD PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "GD ARG 107": "NH1" <-> "NH2" Residue "GD GLU 130": "OE1" <-> "OE2" Residue "GD ARG 133": "NH1" <-> "NH2" Residue "GD ASP 136": "OD1" <-> "OD2" Residue "GD ARG 157": "NH1" <-> "NH2" Residue "GH ARG 294": "NH1" <-> "NH2" Residue "GH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "GH GLU 360": "OE1" <-> "OE2" Residue "GK ASP 86": "OD1" <-> "OD2" Residue "GK ARG 90": "NH1" <-> "NH2" Residue "GK ARG 128": "NH1" <-> "NH2" Residue "GK ARG 130": "NH1" <-> "NH2" Residue "GK ARG 138": "NH1" <-> "NH2" Residue "GK ARG 152": "NH1" <-> "NH2" Residue "GK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "GK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AD ASP 35": "OD1" <-> "OD2" Residue "AD ARG 82": "NH1" <-> "NH2" Residue "AD ARG 107": "NH1" <-> "NH2" Residue "AD ARG 133": "NH1" <-> "NH2" Residue "AD ASP 134": "OD1" <-> "OD2" Residue "AD ARG 157": "NH1" <-> "NH2" Residue "Gd ASP 35": "OD1" <-> "OD2" Residue "Gd TYR 77": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Gd ARG 107": "NH1" <-> "NH2" Residue "Gd ARG 133": "NH1" <-> "NH2" Residue "Gd ASP 134": "OD1" <-> "OD2" Residue "Gd ASP 136": "OD1" <-> "OD2" Residue "Gd ARG 157": "NH1" <-> "NH2" Residue "Gd TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "HC ARG 75": "NH1" <-> "NH2" Residue "HC ARG 148": "NH1" <-> "NH2" Residue "HC GLU 174": "OE1" <-> "OE2" Residue "HC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "HC GLU 196": "OE1" <-> "OE2" Residue "HC ASP 205": "OD1" <-> "OD2" Residue "HC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "HC ASP 230": "OD1" <-> "OD2" Residue "HD ASP 35": "OD1" <-> "OD2" Residue "HD GLU 43": "OE1" <-> "OE2" Residue "HD ARG 82": "NH1" <-> "NH2" Residue "HD GLU 93": "OE1" <-> "OE2" Residue "HD PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "HD ARG 107": "NH1" <-> "NH2" Residue "HD ASP 125": "OD1" <-> "OD2" Residue "HD ARG 133": "NH1" <-> "NH2" Residue "HD ASP 136": "OD1" <-> "OD2" Residue "HD ARG 157": "NH1" <-> "NH2" Residue "HH ARG 294": "NH1" <-> "NH2" Residue "HH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "HH GLU 360": "OE1" <-> "OE2" Residue "HK ASP 86": "OD1" <-> "OD2" Residue "HK ARG 90": "NH1" <-> "NH2" Residue "HK ARG 128": "NH1" <-> "NH2" Residue "HK ARG 130": "NH1" <-> "NH2" Residue "HK ARG 138": "NH1" <-> "NH2" Residue "HK ARG 152": "NH1" <-> "NH2" Residue "HK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "HK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Hd ARG 107": "NH1" <-> "NH2" Residue "Hd ARG 133": "NH1" <-> "NH2" Residue "Hd ARG 157": "NH1" <-> "NH2" Residue "IC ARG 75": "NH1" <-> "NH2" Residue "IC ARG 148": "NH1" <-> "NH2" Residue "IC GLU 174": "OE1" <-> "OE2" Residue "IC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "IC GLU 196": "OE1" <-> "OE2" Residue "IC ASP 205": "OD1" <-> "OD2" Residue "IC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "IC ASP 230": "OD1" <-> "OD2" Residue "ID ARG 82": "NH1" <-> "NH2" Residue "ID GLU 92": "OE1" <-> "OE2" Residue "ID ARG 107": "NH1" <-> "NH2" Residue "ID ARG 133": "NH1" <-> "NH2" Residue "ID ASP 134": "OD1" <-> "OD2" Residue "ID ARG 157": "NH1" <-> "NH2" Residue "IH ARG 294": "NH1" <-> "NH2" Residue "IH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "IH GLU 360": "OE1" <-> "OE2" Residue "IK ASP 86": "OD1" <-> "OD2" Residue "IK ARG 90": "NH1" <-> "NH2" Residue "IK ARG 128": "NH1" <-> "NH2" Residue "IK ARG 130": "NH1" <-> "NH2" Residue "IK ARG 138": "NH1" <-> "NH2" Residue "IK ARG 152": "NH1" <-> "NH2" Residue "IK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "IK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Id GLU 54": "OE1" <-> "OE2" Residue "Id GLU 92": "OE1" <-> "OE2" Residue "Id ARG 107": "NH1" <-> "NH2" Residue "Id ASP 125": "OD1" <-> "OD2" Residue "Id GLU 126": "OE1" <-> "OE2" Residue "Id GLU 130": "OE1" <-> "OE2" Residue "Id ARG 133": "NH1" <-> "NH2" Residue "Id ASP 136": "OD1" <-> "OD2" Residue "Id GLU 155": "OE1" <-> "OE2" Residue "Id ARG 157": "NH1" <-> "NH2" Residue "Id TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JC ARG 75": "NH1" <-> "NH2" Residue "JC ARG 148": "NH1" <-> "NH2" Residue "JC GLU 174": "OE1" <-> "OE2" Residue "JC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JC GLU 196": "OE1" <-> "OE2" Residue "JC ASP 205": "OD1" <-> "OD2" Residue "JC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JC ASP 230": "OD1" <-> "OD2" Residue "JD GLU 59": "OE1" <-> "OE2" Residue "JD TYR 77": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JD ARG 82": "NH1" <-> "NH2" Residue "JD GLU 92": "OE1" <-> "OE2" Residue "JD PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JD ARG 107": "NH1" <-> "NH2" Residue "JD ARG 133": "NH1" <-> "NH2" Residue "JD ASP 134": "OD1" <-> "OD2" Residue "JD ASP 136": "OD1" <-> "OD2" Residue "JD ARG 157": "NH1" <-> "NH2" Residue "JH ARG 294": "NH1" <-> "NH2" Residue "JH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JH GLU 360": "OE1" <-> "OE2" Residue "JK ASP 86": "OD1" <-> "OD2" Residue "JK ARG 90": "NH1" <-> "NH2" Residue "JK ARG 128": "NH1" <-> "NH2" Residue "JK ARG 130": "NH1" <-> "NH2" Residue "JK ARG 138": "NH1" <-> "NH2" Residue "JK ARG 152": "NH1" <-> "NH2" Residue "JK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "JK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AH ARG 294": "NH1" <-> "NH2" Residue "AH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AH GLU 360": "OE1" <-> "OE2" Residue "Jd GLU 59": "OE1" <-> "OE2" Residue "Jd TYR 77": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Jd GLU 92": "OE1" <-> "OE2" Residue "Jd GLU 93": "OE1" <-> "OE2" Residue "Jd ARG 107": "NH1" <-> "NH2" Residue "Jd ASP 125": "OD1" <-> "OD2" Residue "Jd ARG 133": "NH1" <-> "NH2" Residue "Jd ASP 136": "OD1" <-> "OD2" Residue "Jd ARG 157": "NH1" <-> "NH2" Residue "KC ARG 75": "NH1" <-> "NH2" Residue "KC ARG 148": "NH1" <-> "NH2" Residue "KC GLU 174": "OE1" <-> "OE2" Residue "KC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KC GLU 196": "OE1" <-> "OE2" Residue "KC ASP 205": "OD1" <-> "OD2" Residue "KC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KC ASP 230": "OD1" <-> "OD2" Residue "KD ASP 35": "OD1" <-> "OD2" Residue "KD GLU 43": "OE1" <-> "OE2" Residue "KD ARG 82": "NH1" <-> "NH2" Residue "KD GLU 93": "OE1" <-> "OE2" Residue "KD PHE 104": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KD PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KD ARG 107": "NH1" <-> "NH2" Residue "KD GLU 130": "OE1" <-> "OE2" Residue "KD ARG 133": "NH1" <-> "NH2" Residue "KD ASP 136": "OD1" <-> "OD2" Residue "KD ARG 157": "NH1" <-> "NH2" Residue "KD TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KH ARG 294": "NH1" <-> "NH2" Residue "KH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KH GLU 360": "OE1" <-> "OE2" Residue "KK ASP 86": "OD1" <-> "OD2" Residue "KK ARG 90": "NH1" <-> "NH2" Residue "KK ARG 128": "NH1" <-> "NH2" Residue "KK ARG 130": "NH1" <-> "NH2" Residue "KK ARG 138": "NH1" <-> "NH2" Residue "KK ARG 152": "NH1" <-> "NH2" Residue "KK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "KK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Kd GLU 59": "OE1" <-> "OE2" Residue "Kd ARG 107": "NH1" <-> "NH2" Residue "Kd GLU 130": "OE1" <-> "OE2" Residue "Kd ARG 133": "NH1" <-> "NH2" Residue "Kd ARG 157": "NH1" <-> "NH2" Residue "LC ARG 75": "NH1" <-> "NH2" Residue "LC ARG 148": "NH1" <-> "NH2" Residue "LC GLU 174": "OE1" <-> "OE2" Residue "LC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "LC GLU 196": "OE1" <-> "OE2" Residue "LC ASP 205": "OD1" <-> "OD2" Residue "LC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "LC ASP 230": "OD1" <-> "OD2" Residue "LD ASP 35": "OD1" <-> "OD2" Residue "LD ASP 68": "OD1" <-> "OD2" Residue "LD ARG 82": "NH1" <-> "NH2" Residue "LD PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "LD ARG 107": "NH1" <-> "NH2" Residue "LD ARG 133": "NH1" <-> "NH2" Residue "LD ASP 134": "OD1" <-> "OD2" Residue "LD ARG 157": "NH1" <-> "NH2" Residue "LH ARG 294": "NH1" <-> "NH2" Residue "LH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "LH GLU 360": "OE1" <-> "OE2" Residue "LK ASP 86": "OD1" <-> "OD2" Residue "LK ARG 90": "NH1" <-> "NH2" Residue "LK ARG 128": "NH1" <-> "NH2" Residue "LK ARG 130": "NH1" <-> "NH2" Residue "LK ARG 138": "NH1" <-> "NH2" Residue "LK ARG 152": "NH1" <-> "NH2" Residue "LK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "LK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Ld GLU 59": "OE1" <-> "OE2" Residue "Ld ARG 107": "NH1" <-> "NH2" Residue "Ld ASP 125": "OD1" <-> "OD2" Residue "Ld ARG 133": "NH1" <-> "NH2" Residue "Ld ASP 134": "OD1" <-> "OD2" Residue "Ld ARG 157": "NH1" <-> "NH2" Residue "MC ARG 75": "NH1" <-> "NH2" Residue "MC ARG 148": "NH1" <-> "NH2" Residue "MC GLU 174": "OE1" <-> "OE2" Residue "MC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "MC GLU 196": "OE1" <-> "OE2" Residue "MC ASP 205": "OD1" <-> "OD2" Residue "MC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "MC ASP 230": "OD1" <-> "OD2" Residue "MD GLU 59": "OE1" <-> "OE2" Residue "MD ASP 68": "OD1" <-> "OD2" Residue "MD ARG 82": "NH1" <-> "NH2" Residue "MD GLU 93": "OE1" <-> "OE2" Residue "MD ARG 107": "NH1" <-> "NH2" Residue "MD GLU 130": "OE1" <-> "OE2" Residue "MD ARG 133": "NH1" <-> "NH2" Residue "MD ARG 157": "NH1" <-> "NH2" Residue "MH ARG 294": "NH1" <-> "NH2" Residue "MH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "MH GLU 360": "OE1" <-> "OE2" Residue "MK ASP 86": "OD1" <-> "OD2" Residue "MK ARG 90": "NH1" <-> "NH2" Residue "MK ARG 128": "NH1" <-> "NH2" Residue "MK ARG 130": "NH1" <-> "NH2" Residue "MK ARG 138": "NH1" <-> "NH2" Residue "MK ARG 152": "NH1" <-> "NH2" Residue "MK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "MK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Md GLU 43": "OE1" <-> "OE2" Residue "Md ASP 50": "OD1" <-> "OD2" Residue "Md ASP 68": "OD1" <-> "OD2" Residue "Md ARG 107": "NH1" <-> "NH2" Residue "Md ASP 125": "OD1" <-> "OD2" Residue "Md ARG 133": "NH1" <-> "NH2" Residue "Md GLU 155": "OE1" <-> "OE2" Residue "Md ARG 157": "NH1" <-> "NH2" Residue "Md TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AK ASP 86": "OD1" <-> "OD2" Residue "AK ARG 90": "NH1" <-> "NH2" Residue "AK ARG 128": "NH1" <-> "NH2" Residue "AK ARG 130": "NH1" <-> "NH2" Residue "AK ARG 138": "NH1" <-> "NH2" Residue "AK ARG 152": "NH1" <-> "NH2" Residue "AK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "AK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "N ASP 108": "OD1" <-> "OD2" Residue "N ASP 121": "OD1" <-> "OD2" Residue "N ARG 139": "NH1" <-> "NH2" Residue "N TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "N GLU 206": "OE1" <-> "OE2" Residue "N ASP 210": "OD1" <-> "OD2" Residue "N PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "O ASP 108": "OD1" <-> "OD2" Residue "O ASP 121": "OD1" <-> "OD2" Residue "O ARG 139": "NH1" <-> "NH2" Residue "O TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "O GLU 206": "OE1" <-> "OE2" Residue "O ASP 210": "OD1" <-> "OD2" Residue "O PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "P ASP 108": "OD1" <-> "OD2" Residue "P ASP 121": "OD1" <-> "OD2" Residue "P ARG 139": "NH1" <-> "NH2" Residue "P TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "P GLU 206": "OE1" <-> "OE2" Residue "P ASP 210": "OD1" <-> "OD2" Residue "P PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Q ASP 108": "OD1" <-> "OD2" Residue "Q ASP 121": "OD1" <-> "OD2" Residue "Q ARG 139": "NH1" <-> "NH2" Residue "Q TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Q GLU 206": "OE1" <-> "OE2" Residue "Q ASP 210": "OD1" <-> "OD2" Residue "Q PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "R ASP 108": "OD1" <-> "OD2" Residue "R ASP 121": "OD1" <-> "OD2" Residue "R ARG 139": "NH1" <-> "NH2" Residue "R TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "R GLU 206": "OE1" <-> "OE2" Residue "R ASP 210": "OD1" <-> "OD2" Residue "R PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "S ASP 108": "OD1" <-> "OD2" Residue "S ASP 121": "OD1" <-> "OD2" Residue "S ARG 139": "NH1" <-> "NH2" Residue "S TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "S GLU 206": "OE1" <-> "OE2" Residue "S ASP 210": "OD1" <-> "OD2" Residue "S PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "T ASP 108": "OD1" <-> "OD2" Residue "T ASP 121": "OD1" <-> "OD2" Residue "T ARG 139": "NH1" <-> "NH2" Residue "T TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "T GLU 206": "OE1" <-> "OE2" Residue "T ASP 210": "OD1" <-> "OD2" Residue "T PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "U ASP 108": "OD1" <-> "OD2" Residue "U ASP 121": "OD1" <-> "OD2" Residue "U ARG 139": "NH1" <-> "NH2" Residue "U TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "U GLU 206": "OE1" <-> "OE2" Residue "U ASP 210": "OD1" <-> "OD2" Residue "U PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "V ASP 108": "OD1" <-> "OD2" Residue "V ASP 121": "OD1" <-> "OD2" Residue "V ARG 139": "NH1" <-> "NH2" Residue "V TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "V GLU 206": "OE1" <-> "OE2" Residue "V ASP 210": "OD1" <-> "OD2" Residue "V PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "W ASP 108": "OD1" <-> "OD2" Residue "W ASP 121": "OD1" <-> "OD2" Residue "W ARG 139": "NH1" <-> "NH2" Residue "W TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "W GLU 206": "OE1" <-> "OE2" Residue "W ASP 210": "OD1" <-> "OD2" Residue "W PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "X ASP 108": "OD1" <-> "OD2" Residue "X ASP 121": "OD1" <-> "OD2" Residue "X ARG 139": "NH1" <-> "NH2" Residue "X TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "X GLU 206": "OE1" <-> "OE2" Residue "X ASP 210": "OD1" <-> "OD2" Residue "X PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Y ASP 108": "OD1" <-> "OD2" Residue "Y ASP 121": "OD1" <-> "OD2" Residue "Y ARG 139": "NH1" <-> "NH2" Residue "Y TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Y GLU 206": "OE1" <-> "OE2" Residue "Y ASP 210": "OD1" <-> "OD2" Residue "Y PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Z ASP 108": "OD1" <-> "OD2" Residue "Z ASP 121": "OD1" <-> "OD2" Residue "Z ARG 139": "NH1" <-> "NH2" Residue "Z TYR 145": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Z GLU 206": "OE1" <-> "OE2" Residue "Z ASP 210": "OD1" <-> "OD2" Residue "Z PHE 234": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Ad ASP 35": "OD1" <-> "OD2" Residue "Ad GLU 54": "OE1" <-> "OE2" Residue "Ad ARG 107": "NH1" <-> "NH2" Residue "Ad GLU 126": "OE1" <-> "OE2" Residue "Ad ARG 133": "NH1" <-> "NH2" Residue "Ad ASP 136": "OD1" <-> "OD2" Residue "Ad TYR 148": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Ad GLU 155": "OE1" <-> "OE2" Residue "Ad ARG 157": "NH1" <-> "NH2" Residue "BC ARG 75": "NH1" <-> "NH2" Residue "BC ARG 148": "NH1" <-> "NH2" Residue "BC GLU 174": "OE1" <-> "OE2" Residue "BC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "BC GLU 196": "OE1" <-> "OE2" Residue "BC ASP 205": "OD1" <-> "OD2" Residue "BC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "BC ASP 230": "OD1" <-> "OD2" Residue "BD PHE 25": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "BD TYR 77": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "BD ARG 82": "NH1" <-> "NH2" Residue "BD ARG 107": "NH1" <-> "NH2" Residue "BD GLU 130": "OE1" <-> "OE2" Residue "BD ARG 133": "NH1" <-> "NH2" Residue "BD ARG 157": "NH1" <-> "NH2" Residue "BH ARG 294": "NH1" <-> "NH2" Residue "BH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "BH GLU 360": "OE1" <-> "OE2" Residue "BK ASP 86": "OD1" <-> "OD2" Residue "BK ARG 90": "NH1" <-> "NH2" Residue "BK ARG 128": "NH1" <-> "NH2" Residue "BK ARG 130": "NH1" <-> "NH2" Residue "BK ARG 138": "NH1" <-> "NH2" Residue "BK ARG 152": "NH1" <-> "NH2" Residue "BK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "BK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Bd ASP 50": "OD1" <-> "OD2" Residue "Bd ARG 107": "NH1" <-> "NH2" Residue "Bd ASP 125": "OD1" <-> "OD2" Residue "Bd ARG 133": "NH1" <-> "NH2" Residue "Bd ARG 157": "NH1" <-> "NH2" Residue "CC ARG 75": "NH1" <-> "NH2" Residue "CC ARG 148": "NH1" <-> "NH2" Residue "CC GLU 174": "OE1" <-> "OE2" Residue "CC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "CC GLU 196": "OE1" <-> "OE2" Residue "CC ASP 205": "OD1" <-> "OD2" Residue "CC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "CC ASP 230": "OD1" <-> "OD2" Residue "CD ASP 35": "OD1" <-> "OD2" Residue "CD GLU 59": "OE1" <-> "OE2" Residue "CD ARG 82": "NH1" <-> "NH2" Residue "CD GLU 93": "OE1" <-> "OE2" Residue "CD ARG 107": "NH1" <-> "NH2" Residue "CD GLU 126": "OE1" <-> "OE2" Residue "CD ARG 133": "NH1" <-> "NH2" Residue "CD ASP 134": "OD1" <-> "OD2" Residue "CD ASP 136": "OD1" <-> "OD2" Residue "CD ARG 157": "NH1" <-> "NH2" Residue "CH ARG 294": "NH1" <-> "NH2" Residue "CH TYR 338": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "CH GLU 360": "OE1" <-> "OE2" Residue "CK ASP 86": "OD1" <-> "OD2" Residue "CK ARG 90": "NH1" <-> "NH2" Residue "CK ARG 128": "NH1" <-> "NH2" Residue "CK ARG 130": "NH1" <-> "NH2" Residue "CK ARG 138": "NH1" <-> "NH2" Residue "CK ARG 152": "NH1" <-> "NH2" Residue "CK PHE 155": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "CK TYR 168": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "Cd GLU 54": "OE1" <-> "OE2" Residue "Cd ARG 107": "NH1" <-> "NH2" Residue "Cd ASP 125": "OD1" <-> "OD2" Residue "Cd GLU 130": "OE1" <-> "OE2" Residue "Cd ARG 133": "NH1" <-> "NH2" Residue "Cd ASP 134": "OD1" <-> "OD2" Residue "Cd ASP 136": "OD1" <-> "OD2" Residue "Cd ARG 157": "NH1" <-> "NH2" Residue "Cd TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DC ARG 75": "NH1" <-> "NH2" Residue "DC ARG 148": "NH1" <-> "NH2" Residue "DC GLU 174": "OE1" <-> "OE2" Residue "DC TYR 179": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DC GLU 196": "OE1" <-> "OE2" Residue "DC ASP 205": "OD1" <-> "OD2" Residue "DC TYR 225": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DC ASP 230": "OD1" <-> "OD2" Residue "DD ASP 35": "OD1" <-> "OD2" Residue "DD GLU 59": "OE1" <-> "OE2" Residue "DD TYR 77": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DD ARG 82": "NH1" <-> "NH2" Residue "DD PHE 106": "CD1" <-> "CD2" "CE1" <-> "CE2" Residue "DD ARG 107": "NH1" <-> "NH2" Residue "DD ARG 133": "NH1" <-> "NH2" Residue "DD ASP 136": "OD1" <-> "OD2" Residue "DD GLU 155": "OE1" <-> "OE2" Residue "DD ARG 157": "NH1" <-> "NH2" Residue "DD TYR 158": "CD1" <-> "CD2" "CE1" <-> "CE2" Time to flip residues: 0.21s Monomer Library directory: "/net/cci-filer2/raid1/xp/phenix/phenix-1.21rc1-5172/modules/chem_data/mon_lib" Total number of atoms: 109070 Number of models: 1 Model: "" Number of chains: 117 Chain: "AC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "DH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "DK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "DX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "DY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "DZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Dd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "EC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "ED" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "EH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "EK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "EX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "EY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "EZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Ed" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "FC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "FD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "FH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "FK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "FX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "FY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "FZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Fd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "GC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "GD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "GH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "GK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "AD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "GX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "GY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "GZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Gd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "HC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "HD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "HH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "HK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "HX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "HY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "HZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Hd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "IC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "ID" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "IH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "IK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "IX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "IY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "IZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Id" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "JC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "JD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "JH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "JK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "JX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "JY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "AH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "JZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Jd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "KC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "KD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "KH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "KK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "KX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "KY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "KZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Kd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "LC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "LD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "LH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "LK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "LX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "LY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "LZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Ld" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "MC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "MD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "MH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "MK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "MX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "MY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "MZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Md" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "AK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "N" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "O" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "P" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "Q" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "R" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "S" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "T" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "U" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "V" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "W" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "X" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "Y" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "Z" Number of atoms: 1108 Number of conformers: 1 Conformer: "" Number of residues, atoms: 136, 1108 Classifications: {'peptide': 136} Link IDs: {'PTRANS': 4, 'TRANS': 131} Chain: "AX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "AY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "AZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Ad" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "BC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "BD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "BH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "BK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "BX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "BY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "BZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Bd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "CC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "CD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Chain: "CH" Number of atoms: 678 Number of conformers: 1 Conformer: "" Number of residues, atoms: 89, 678 Classifications: {'peptide': 89} Link IDs: {'PTRANS': 7, 'TRANS': 81} Chain: "CK" Number of atoms: 1152 Number of conformers: 1 Conformer: "" Number of residues, atoms: 148, 1152 Classifications: {'peptide': 148} Link IDs: {'PTRANS': 5, 'TRANS': 142} Chain: "CX" Number of atoms: 1140 Number of conformers: 1 Conformer: "" Number of residues, atoms: 228, 1140 Classifications: {'peptide': 228} Link IDs: {'TRANS': 227} Chain: "CY" Number of atoms: 260 Number of conformers: 1 Conformer: "" Number of residues, atoms: 52, 260 Classifications: {'peptide': 52} Link IDs: {'TRANS': 51} Chain: "CZ" Number of atoms: 350 Number of conformers: 1 Conformer: "" Number of residues, atoms: 70, 350 Classifications: {'peptide': 70} Link IDs: {'TRANS': 69} Chain: "Cd" Number of atoms: 1066 Number of conformers: 1 Conformer: "" Number of residues, atoms: 138, 1066 Classifications: {'peptide': 138} Link IDs: {'PTRANS': 10, 'TRANS': 127} Chain: "DC" Number of atoms: 1596 Number of conformers: 1 Conformer: "" Number of residues, atoms: 200, 1596 Classifications: {'peptide': 200} Link IDs: {'PTRANS': 9, 'TRANS': 190} Chain breaks: 1 Chain: "DD" Number of atoms: 1040 Number of conformers: 1 Conformer: "" Number of residues, atoms: 135, 1040 Classifications: {'peptide': 135} Link IDs: {'PTRANS': 10, 'TRANS': 124} Time building chain proxies: 42.17, per 1000 atoms: 0.39 Number of scatterers: 109070 At special positions: 0 Unit cell: (393.6, 393.6, 101.68, 90, 90, 90) Space group: P 1 (No. 1) Number of sites at special positions: 0 Number of scattering types: 4 Type Number sf(0) S 273 16.00 O 20605 8.00 N 19708 7.00 C 68484 6.00 sf(0) = scattering factor at diffraction angle 0. Number of disulfides: simple=0, symmetry=0 Automatic linking Parameters for automatic linking Linking & cutoffs Metal : Auto - 3.50 Amino acid : False - 1.90 Carbohydrate : True - 1.99 Ligands : True - 1.99 Small molecules : False - 1.98 Amino acid - RNA/DNA : False Number of custom bonds: simple=0, symmetry=0 Time building additional restraints: 29.70 Conformation dependent library (CDL) restraints added in 15.3 seconds 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. Adding C-beta torsion restraints... Number of C-beta restraints generated: 30056 Finding SS restraints... Secondary structure from input PDB file: 299 helices and 195 sheets defined 27.4% alpha, 24.5% beta 0 base pairs and 0 stacking pairs defined. Time for finding SS restraints: 8.67 Creating SS restraints... Processing helix chain 'AC' and resid 58 through 86 removed outlier: 4.113A pdb=" N GLNAC 69 " --> pdb=" O SERAC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALAAC 70 " --> pdb=" O VALAC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNAC 86 " --> pdb=" O GLNAC 82 " (cutoff:3.500A) Processing helix chain 'AC' and resid 86 through 94 Processing helix chain 'AC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALAC 100 " --> pdb=" O ASNAC 97 " (cutoff:3.500A) Processing helix chain 'AC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPAC 152 " --> pdb=" O ARGAC 148 " (cutoff:3.500A) Processing helix chain 'AC' and resid 174 through 218 Processing helix chain 'DH' and resid 278 through 282 Processing helix chain 'DK' and resid 49 through 63 Processing helix chain 'DK' and resid 80 through 84 Processing helix chain 'DK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUDK 98 " --> pdb=" O ALADK 94 " (cutoff:3.500A) Processing helix chain 'DK' and resid 125 through 147 Processing helix chain 'Dd' and resid 35 through 63 removed outlier: 4.314A pdb=" N SERDd 47 " --> pdb=" O GLUDd 43 " (cutoff:3.500A) Processing helix chain 'Dd' and resid 90 through 102 removed outlier: 4.069A pdb=" N LEUDd 94 " --> pdb=" O PRODd 90 " (cutoff:3.500A) Processing helix chain 'Dd' and resid 128 through 139 Processing helix chain 'EC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNEC 69 " --> pdb=" O SEREC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALAEC 70 " --> pdb=" O VALEC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNEC 86 " --> pdb=" O GLNEC 82 " (cutoff:3.500A) Processing helix chain 'EC' and resid 86 through 94 Processing helix chain 'EC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALEC 100 " --> pdb=" O ASNEC 97 " (cutoff:3.500A) Processing helix chain 'EC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPEC 152 " --> pdb=" O ARGEC 148 " (cutoff:3.500A) Processing helix chain 'EC' and resid 174 through 218 Processing helix chain 'ED' and resid 37 through 60 Processing helix chain 'ED' and resid 64 through 68 removed outlier: 3.936A pdb=" N ASPED 68 " --> pdb=" O PROED 65 " (cutoff:3.500A) Processing helix chain 'ED' and resid 91 through 102 Processing helix chain 'ED' and resid 127 through 140 Processing helix chain 'EH' and resid 278 through 282 Processing helix chain 'EK' and resid 49 through 63 Processing helix chain 'EK' and resid 80 through 84 Processing helix chain 'EK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUEK 98 " --> pdb=" O ALAEK 94 " (cutoff:3.500A) Processing helix chain 'EK' and resid 125 through 147 Processing helix chain 'Ed' and resid 35 through 63 removed outlier: 3.882A pdb=" N SEREd 47 " --> pdb=" O GLUEd 43 " (cutoff:3.500A) Processing helix chain 'Ed' and resid 90 through 102 removed outlier: 4.099A pdb=" N LEUEd 94 " --> pdb=" O PROEd 90 " (cutoff:3.500A) Processing helix chain 'Ed' and resid 128 through 139 Processing helix chain 'FC' and resid 59 through 86 removed outlier: 4.113A pdb=" N GLNFC 69 " --> pdb=" O SERFC 65 " (cutoff:3.500A) removed outlier: 3.773A pdb=" N ALAFC 70 " --> pdb=" O VALFC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNFC 86 " --> pdb=" O GLNFC 82 " (cutoff:3.500A) Processing helix chain 'FC' and resid 86 through 94 Processing helix chain 'FC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALFC 100 " --> pdb=" O ASNFC 97 " (cutoff:3.500A) Processing helix chain 'FC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPFC 152 " --> pdb=" O ARGFC 148 " (cutoff:3.500A) Processing helix chain 'FC' and resid 174 through 218 Processing helix chain 'FD' and resid 37 through 60 Processing helix chain 'FD' and resid 64 through 68 removed outlier: 4.130A pdb=" N ASPFD 68 " --> pdb=" O PROFD 65 " (cutoff:3.500A) Processing helix chain 'FD' and resid 91 through 103 Processing helix chain 'FD' and resid 128 through 140 Processing helix chain 'FH' and resid 278 through 282 Processing helix chain 'FK' and resid 49 through 63 Processing helix chain 'FK' and resid 80 through 84 Processing helix chain 'FK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUFK 98 " --> pdb=" O ALAFK 94 " (cutoff:3.500A) Processing helix chain 'FK' and resid 125 through 147 Processing helix chain 'Fd' and resid 35 through 63 removed outlier: 4.447A pdb=" N SERFd 47 " --> pdb=" O GLUFd 43 " (cutoff:3.500A) Processing helix chain 'Fd' and resid 90 through 102 removed outlier: 4.152A pdb=" N LEUFd 94 " --> pdb=" O PROFd 90 " (cutoff:3.500A) Processing helix chain 'Fd' and resid 128 through 139 Processing helix chain 'GC' and resid 59 through 86 removed outlier: 4.113A pdb=" N GLNGC 69 " --> pdb=" O SERGC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALAGC 70 " --> pdb=" O VALGC 66 " (cutoff:3.500A) removed outlier: 3.654A pdb=" N GLNGC 86 " --> pdb=" O GLNGC 82 " (cutoff:3.500A) Processing helix chain 'GC' and resid 86 through 94 Processing helix chain 'GC' and resid 96 through 100 removed outlier: 3.898A pdb=" N VALGC 100 " --> pdb=" O ASNGC 97 " (cutoff:3.500A) Processing helix chain 'GC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPGC 152 " --> pdb=" O ARGGC 148 " (cutoff:3.500A) Processing helix chain 'GC' and resid 174 through 218 Processing helix chain 'GD' and resid 35 through 60 removed outlier: 4.119A pdb=" N LYSGD 40 " --> pdb=" O ASPGD 36 " (cutoff:3.500A) Processing helix chain 'GD' and resid 64 through 68 removed outlier: 4.020A pdb=" N ASPGD 68 " --> pdb=" O PROGD 65 " (cutoff:3.500A) Processing helix chain 'GD' and resid 91 through 102 Processing helix chain 'GD' and resid 128 through 140 Processing helix chain 'GH' and resid 278 through 282 Processing helix chain 'GK' and resid 49 through 63 Processing helix chain 'GK' and resid 80 through 84 Processing helix chain 'GK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUGK 98 " --> pdb=" O ALAGK 94 " (cutoff:3.500A) Processing helix chain 'GK' and resid 125 through 147 Processing helix chain 'AD' and resid 37 through 60 Processing helix chain 'AD' and resid 64 through 68 removed outlier: 4.018A pdb=" N ASPAD 68 " --> pdb=" O PROAD 65 " (cutoff:3.500A) Processing helix chain 'AD' and resid 91 through 102 Processing helix chain 'AD' and resid 127 through 140 Processing helix chain 'Gd' and resid 35 through 63 removed outlier: 3.957A pdb=" N SERGd 47 " --> pdb=" O GLUGd 43 " (cutoff:3.500A) Processing helix chain 'Gd' and resid 90 through 102 removed outlier: 4.201A pdb=" N LEUGd 94 " --> pdb=" O PROGd 90 " (cutoff:3.500A) Processing helix chain 'Gd' and resid 128 through 139 Processing helix chain 'HC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNHC 69 " --> pdb=" O SERHC 65 " (cutoff:3.500A) removed outlier: 3.773A pdb=" N ALAHC 70 " --> pdb=" O VALHC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNHC 86 " --> pdb=" O GLNHC 82 " (cutoff:3.500A) Processing helix chain 'HC' and resid 86 through 94 Processing helix chain 'HC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALHC 100 " --> pdb=" O ASNHC 97 " (cutoff:3.500A) Processing helix chain 'HC' and resid 147 through 152 removed outlier: 3.655A pdb=" N TRPHC 152 " --> pdb=" O ARGHC 148 " (cutoff:3.500A) Processing helix chain 'HC' and resid 174 through 218 Processing helix chain 'HD' and resid 37 through 60 Processing helix chain 'HD' and resid 64 through 68 removed outlier: 4.094A pdb=" N ASPHD 68 " --> pdb=" O PROHD 65 " (cutoff:3.500A) Processing helix chain 'HD' and resid 91 through 102 Processing helix chain 'HD' and resid 128 through 140 Processing helix chain 'HH' and resid 278 through 282 Processing helix chain 'HK' and resid 49 through 63 Processing helix chain 'HK' and resid 80 through 84 Processing helix chain 'HK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUHK 98 " --> pdb=" O ALAHK 94 " (cutoff:3.500A) Processing helix chain 'HK' and resid 125 through 147 Processing helix chain 'Hd' and resid 35 through 63 removed outlier: 4.179A pdb=" N SERHd 47 " --> pdb=" O GLUHd 43 " (cutoff:3.500A) Processing helix chain 'Hd' and resid 90 through 103 removed outlier: 4.079A pdb=" N LEUHd 94 " --> pdb=" O PROHd 90 " (cutoff:3.500A) Processing helix chain 'Hd' and resid 128 through 139 Processing helix chain 'IC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNIC 69 " --> pdb=" O SERIC 65 " (cutoff:3.500A) removed outlier: 3.773A pdb=" N ALAIC 70 " --> pdb=" O VALIC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNIC 86 " --> pdb=" O GLNIC 82 " (cutoff:3.500A) Processing helix chain 'IC' and resid 86 through 94 Processing helix chain 'IC' and resid 96 through 100 removed outlier: 3.898A pdb=" N VALIC 100 " --> pdb=" O ASNIC 97 " (cutoff:3.500A) Processing helix chain 'IC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPIC 152 " --> pdb=" O ARGIC 148 " (cutoff:3.500A) Processing helix chain 'IC' and resid 174 through 218 Processing helix chain 'ID' and resid 37 through 60 Processing helix chain 'ID' and resid 64 through 68 removed outlier: 4.151A pdb=" N ASPID 68 " --> pdb=" O PROID 65 " (cutoff:3.500A) Processing helix chain 'ID' and resid 91 through 102 Processing helix chain 'ID' and resid 128 through 140 Processing helix chain 'IH' and resid 278 through 282 Processing helix chain 'IK' and resid 49 through 63 Processing helix chain 'IK' and resid 80 through 84 Processing helix chain 'IK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUIK 98 " --> pdb=" O ALAIK 94 " (cutoff:3.500A) Processing helix chain 'IK' and resid 125 through 147 Processing helix chain 'Id' and resid 35 through 63 removed outlier: 3.708A pdb=" N SERId 47 " --> pdb=" O GLUId 43 " (cutoff:3.500A) Processing helix chain 'Id' and resid 90 through 102 removed outlier: 4.067A pdb=" N LEUId 94 " --> pdb=" O PROId 90 " (cutoff:3.500A) Processing helix chain 'Id' and resid 128 through 139 Processing helix chain 'JC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNJC 69 " --> pdb=" O SERJC 65 " (cutoff:3.500A) removed outlier: 3.773A pdb=" N ALAJC 70 " --> pdb=" O VALJC 66 " (cutoff:3.500A) removed outlier: 3.654A pdb=" N GLNJC 86 " --> pdb=" O GLNJC 82 " (cutoff:3.500A) Processing helix chain 'JC' and resid 86 through 94 Processing helix chain 'JC' and resid 96 through 100 removed outlier: 3.898A pdb=" N VALJC 100 " --> pdb=" O ASNJC 97 " (cutoff:3.500A) Processing helix chain 'JC' and resid 147 through 152 removed outlier: 3.655A pdb=" N TRPJC 152 " --> pdb=" O ARGJC 148 " (cutoff:3.500A) Processing helix chain 'JC' and resid 174 through 218 Processing helix chain 'JD' and resid 37 through 60 Processing helix chain 'JD' and resid 64 through 68 removed outlier: 4.167A pdb=" N ASPJD 68 " --> pdb=" O PROJD 65 " (cutoff:3.500A) Processing helix chain 'JD' and resid 91 through 102 Processing helix chain 'JD' and resid 128 through 140 Processing helix chain 'JH' and resid 278 through 282 Processing helix chain 'JK' and resid 49 through 63 Processing helix chain 'JK' and resid 80 through 84 Processing helix chain 'JK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUJK 98 " --> pdb=" O ALAJK 94 " (cutoff:3.500A) Processing helix chain 'JK' and resid 125 through 147 Processing helix chain 'AH' and resid 278 through 282 Processing helix chain 'Jd' and resid 35 through 63 removed outlier: 3.910A pdb=" N SERJd 47 " --> pdb=" O GLUJd 43 " (cutoff:3.500A) Processing helix chain 'Jd' and resid 90 through 102 removed outlier: 4.044A pdb=" N LEUJd 94 " --> pdb=" O PROJd 90 " (cutoff:3.500A) Processing helix chain 'Jd' and resid 128 through 139 Processing helix chain 'KC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNKC 69 " --> pdb=" O SERKC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALAKC 70 " --> pdb=" O VALKC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNKC 86 " --> pdb=" O GLNKC 82 " (cutoff:3.500A) Processing helix chain 'KC' and resid 86 through 94 Processing helix chain 'KC' and resid 96 through 100 removed outlier: 3.898A pdb=" N VALKC 100 " --> pdb=" O ASNKC 97 " (cutoff:3.500A) Processing helix chain 'KC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPKC 152 " --> pdb=" O ARGKC 148 " (cutoff:3.500A) Processing helix chain 'KC' and resid 174 through 218 Processing helix chain 'KD' and resid 35 through 60 removed outlier: 4.187A pdb=" N LYSKD 40 " --> pdb=" O ASPKD 36 " (cutoff:3.500A) Processing helix chain 'KD' and resid 64 through 68 removed outlier: 3.954A pdb=" N ASPKD 68 " --> pdb=" O PROKD 65 " (cutoff:3.500A) Processing helix chain 'KD' and resid 91 through 102 Processing helix chain 'KD' and resid 128 through 140 Processing helix chain 'KH' and resid 278 through 282 Processing helix chain 'KK' and resid 49 through 63 Processing helix chain 'KK' and resid 80 through 84 Processing helix chain 'KK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUKK 98 " --> pdb=" O ALAKK 94 " (cutoff:3.500A) Processing helix chain 'KK' and resid 125 through 147 Processing helix chain 'Kd' and resid 35 through 63 removed outlier: 4.177A pdb=" N SERKd 47 " --> pdb=" O GLUKd 43 " (cutoff:3.500A) Processing helix chain 'Kd' and resid 90 through 102 removed outlier: 4.128A pdb=" N LEUKd 94 " --> pdb=" O PROKd 90 " (cutoff:3.500A) Processing helix chain 'Kd' and resid 128 through 139 Processing helix chain 'LC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNLC 69 " --> pdb=" O SERLC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALALC 70 " --> pdb=" O VALLC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNLC 86 " --> pdb=" O GLNLC 82 " (cutoff:3.500A) Processing helix chain 'LC' and resid 86 through 94 Processing helix chain 'LC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALLC 100 " --> pdb=" O ASNLC 97 " (cutoff:3.500A) Processing helix chain 'LC' and resid 147 through 152 removed outlier: 3.655A pdb=" N TRPLC 152 " --> pdb=" O ARGLC 148 " (cutoff:3.500A) Processing helix chain 'LC' and resid 174 through 218 Processing helix chain 'LD' and resid 37 through 60 Processing helix chain 'LD' and resid 64 through 68 removed outlier: 4.083A pdb=" N ASPLD 68 " --> pdb=" O PROLD 65 " (cutoff:3.500A) Processing helix chain 'LD' and resid 91 through 102 Processing helix chain 'LD' and resid 128 through 140 Processing helix chain 'LH' and resid 278 through 282 Processing helix chain 'LK' and resid 49 through 63 Processing helix chain 'LK' and resid 80 through 84 Processing helix chain 'LK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEULK 98 " --> pdb=" O ALALK 94 " (cutoff:3.500A) Processing helix chain 'LK' and resid 125 through 147 Processing helix chain 'Ld' and resid 35 through 63 removed outlier: 4.157A pdb=" N SERLd 47 " --> pdb=" O GLULd 43 " (cutoff:3.500A) Processing helix chain 'Ld' and resid 90 through 102 removed outlier: 4.074A pdb=" N LEULd 94 " --> pdb=" O PROLd 90 " (cutoff:3.500A) Processing helix chain 'Ld' and resid 128 through 139 Processing helix chain 'MC' and resid 59 through 86 removed outlier: 4.113A pdb=" N GLNMC 69 " --> pdb=" O SERMC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALAMC 70 " --> pdb=" O VALMC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNMC 86 " --> pdb=" O GLNMC 82 " (cutoff:3.500A) Processing helix chain 'MC' and resid 86 through 94 Processing helix chain 'MC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALMC 100 " --> pdb=" O ASNMC 97 " (cutoff:3.500A) Processing helix chain 'MC' and resid 147 through 152 removed outlier: 3.655A pdb=" N TRPMC 152 " --> pdb=" O ARGMC 148 " (cutoff:3.500A) Processing helix chain 'MC' and resid 174 through 218 Processing helix chain 'MD' and resid 35 through 60 removed outlier: 4.163A pdb=" N LYSMD 40 " --> pdb=" O ASPMD 36 " (cutoff:3.500A) Processing helix chain 'MD' and resid 64 through 68 removed outlier: 4.099A pdb=" N ASPMD 68 " --> pdb=" O PROMD 65 " (cutoff:3.500A) Processing helix chain 'MD' and resid 91 through 102 Processing helix chain 'MD' and resid 128 through 140 Processing helix chain 'MH' and resid 278 through 282 Processing helix chain 'MK' and resid 49 through 63 Processing helix chain 'MK' and resid 80 through 84 Processing helix chain 'MK' and resid 94 through 107 removed outlier: 4.089A pdb=" N LEUMK 98 " --> pdb=" O ALAMK 94 " (cutoff:3.500A) Processing helix chain 'MK' and resid 125 through 147 Processing helix chain 'Md' and resid 35 through 63 removed outlier: 3.922A pdb=" N SERMd 47 " --> pdb=" O GLUMd 43 " (cutoff:3.500A) Processing helix chain 'Md' and resid 90 through 102 removed outlier: 4.113A pdb=" N LEUMd 94 " --> pdb=" O PROMd 90 " (cutoff:3.500A) Processing helix chain 'Md' and resid 128 through 139 Processing helix chain 'AK' and resid 49 through 63 Processing helix chain 'AK' and resid 80 through 84 Processing helix chain 'AK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUAK 98 " --> pdb=" O ALAAK 94 " (cutoff:3.500A) Processing helix chain 'AK' and resid 125 through 147 Processing helix chain 'N' and resid 101 through 112 Processing helix chain 'N' and resid 129 through 133 Processing helix chain 'N' and resid 141 through 143 No H-bonds generated for 'chain 'N' and resid 141 through 143' Processing helix chain 'N' and resid 144 through 155 removed outlier: 3.869A pdb=" N LEU N 148 " --> pdb=" O CYS N 144 " (cutoff:3.500A) Processing helix chain 'N' and resid 174 through 196 Processing helix chain 'N' and resid 219 through 227 Processing helix chain 'O' and resid 101 through 112 Processing helix chain 'O' and resid 129 through 133 Processing helix chain 'O' and resid 141 through 143 No H-bonds generated for 'chain 'O' and resid 141 through 143' Processing helix chain 'O' and resid 144 through 155 removed outlier: 3.869A pdb=" N LEU O 148 " --> pdb=" O CYS O 144 " (cutoff:3.500A) Processing helix chain 'O' and resid 174 through 196 Processing helix chain 'O' and resid 219 through 227 Processing helix chain 'P' and resid 101 through 112 Processing helix chain 'P' and resid 129 through 133 Processing helix chain 'P' and resid 141 through 143 No H-bonds generated for 'chain 'P' and resid 141 through 143' Processing helix chain 'P' and resid 144 through 155 removed outlier: 3.869A pdb=" N LEU P 148 " --> pdb=" O CYS P 144 " (cutoff:3.500A) Processing helix chain 'P' and resid 174 through 196 Processing helix chain 'P' and resid 219 through 227 Processing helix chain 'Q' and resid 101 through 112 Processing helix chain 'Q' and resid 129 through 133 Processing helix chain 'Q' and resid 141 through 143 No H-bonds generated for 'chain 'Q' and resid 141 through 143' Processing helix chain 'Q' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU Q 148 " --> pdb=" O CYS Q 144 " (cutoff:3.500A) Processing helix chain 'Q' and resid 174 through 196 Processing helix chain 'Q' and resid 219 through 227 Processing helix chain 'R' and resid 101 through 112 Processing helix chain 'R' and resid 129 through 133 Processing helix chain 'R' and resid 141 through 143 No H-bonds generated for 'chain 'R' and resid 141 through 143' Processing helix chain 'R' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU R 148 " --> pdb=" O CYS R 144 " (cutoff:3.500A) Processing helix chain 'R' and resid 174 through 196 Processing helix chain 'R' and resid 219 through 227 Processing helix chain 'S' and resid 101 through 112 Processing helix chain 'S' and resid 129 through 133 Processing helix chain 'S' and resid 141 through 143 No H-bonds generated for 'chain 'S' and resid 141 through 143' Processing helix chain 'S' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU S 148 " --> pdb=" O CYS S 144 " (cutoff:3.500A) Processing helix chain 'S' and resid 174 through 196 Processing helix chain 'S' and resid 219 through 227 Processing helix chain 'T' and resid 101 through 112 Processing helix chain 'T' and resid 129 through 133 Processing helix chain 'T' and resid 141 through 143 No H-bonds generated for 'chain 'T' and resid 141 through 143' Processing helix chain 'T' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU T 148 " --> pdb=" O CYS T 144 " (cutoff:3.500A) Processing helix chain 'T' and resid 174 through 196 Processing helix chain 'T' and resid 219 through 227 Processing helix chain 'U' and resid 101 through 112 Processing helix chain 'U' and resid 129 through 133 Processing helix chain 'U' and resid 141 through 143 No H-bonds generated for 'chain 'U' and resid 141 through 143' Processing helix chain 'U' and resid 144 through 155 removed outlier: 3.869A pdb=" N LEU U 148 " --> pdb=" O CYS U 144 " (cutoff:3.500A) Processing helix chain 'U' and resid 174 through 196 Processing helix chain 'U' and resid 219 through 227 Processing helix chain 'V' and resid 101 through 112 Processing helix chain 'V' and resid 129 through 133 Processing helix chain 'V' and resid 141 through 143 No H-bonds generated for 'chain 'V' and resid 141 through 143' Processing helix chain 'V' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU V 148 " --> pdb=" O CYS V 144 " (cutoff:3.500A) Processing helix chain 'V' and resid 174 through 196 Processing helix chain 'V' and resid 219 through 227 Processing helix chain 'W' and resid 101 through 112 Processing helix chain 'W' and resid 129 through 133 Processing helix chain 'W' and resid 141 through 143 No H-bonds generated for 'chain 'W' and resid 141 through 143' Processing helix chain 'W' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU W 148 " --> pdb=" O CYS W 144 " (cutoff:3.500A) Processing helix chain 'W' and resid 174 through 196 Processing helix chain 'W' and resid 219 through 227 Processing helix chain 'X' and resid 101 through 112 Processing helix chain 'X' and resid 129 through 133 Processing helix chain 'X' and resid 141 through 143 No H-bonds generated for 'chain 'X' and resid 141 through 143' Processing helix chain 'X' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU X 148 " --> pdb=" O CYS X 144 " (cutoff:3.500A) Processing helix chain 'X' and resid 174 through 196 Processing helix chain 'X' and resid 219 through 227 Processing helix chain 'Y' and resid 101 through 112 Processing helix chain 'Y' and resid 129 through 133 Processing helix chain 'Y' and resid 141 through 143 No H-bonds generated for 'chain 'Y' and resid 141 through 143' Processing helix chain 'Y' and resid 144 through 155 removed outlier: 3.870A pdb=" N LEU Y 148 " --> pdb=" O CYS Y 144 " (cutoff:3.500A) Processing helix chain 'Y' and resid 174 through 196 Processing helix chain 'Y' and resid 219 through 227 Processing helix chain 'Z' and resid 101 through 112 Processing helix chain 'Z' and resid 129 through 133 Processing helix chain 'Z' and resid 141 through 143 No H-bonds generated for 'chain 'Z' and resid 141 through 143' Processing helix chain 'Z' and resid 144 through 155 removed outlier: 3.869A pdb=" N LEU Z 148 " --> pdb=" O CYS Z 144 " (cutoff:3.500A) Processing helix chain 'Z' and resid 174 through 196 Processing helix chain 'Z' and resid 219 through 227 Processing helix chain 'Ad' and resid 35 through 63 removed outlier: 4.138A pdb=" N SERAd 47 " --> pdb=" O GLUAd 43 " (cutoff:3.500A) Processing helix chain 'Ad' and resid 90 through 102 removed outlier: 4.156A pdb=" N LEUAd 94 " --> pdb=" O PROAd 90 " (cutoff:3.500A) Processing helix chain 'Ad' and resid 128 through 139 Processing helix chain 'BC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNBC 69 " --> pdb=" O SERBC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALABC 70 " --> pdb=" O VALBC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNBC 86 " --> pdb=" O GLNBC 82 " (cutoff:3.500A) Processing helix chain 'BC' and resid 86 through 94 Processing helix chain 'BC' and resid 96 through 100 removed outlier: 3.898A pdb=" N VALBC 100 " --> pdb=" O ASNBC 97 " (cutoff:3.500A) Processing helix chain 'BC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPBC 152 " --> pdb=" O ARGBC 148 " (cutoff:3.500A) Processing helix chain 'BC' and resid 174 through 218 Processing helix chain 'BD' and resid 35 through 60 removed outlier: 4.114A pdb=" N LYSBD 40 " --> pdb=" O ASPBD 36 " (cutoff:3.500A) Processing helix chain 'BD' and resid 64 through 68 removed outlier: 4.189A pdb=" N ASPBD 68 " --> pdb=" O PROBD 65 " (cutoff:3.500A) Processing helix chain 'BD' and resid 91 through 102 Processing helix chain 'BD' and resid 128 through 140 Processing helix chain 'BH' and resid 278 through 282 Processing helix chain 'BK' and resid 49 through 63 Processing helix chain 'BK' and resid 80 through 84 Processing helix chain 'BK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUBK 98 " --> pdb=" O ALABK 94 " (cutoff:3.500A) Processing helix chain 'BK' and resid 125 through 147 Processing helix chain 'Bd' and resid 35 through 63 removed outlier: 4.157A pdb=" N SERBd 47 " --> pdb=" O GLUBd 43 " (cutoff:3.500A) Processing helix chain 'Bd' and resid 90 through 102 removed outlier: 4.157A pdb=" N LEUBd 94 " --> pdb=" O PROBd 90 " (cutoff:3.500A) Processing helix chain 'Bd' and resid 128 through 139 Processing helix chain 'CC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNCC 69 " --> pdb=" O SERCC 65 " (cutoff:3.500A) removed outlier: 3.773A pdb=" N ALACC 70 " --> pdb=" O VALCC 66 " (cutoff:3.500A) removed outlier: 3.653A pdb=" N GLNCC 86 " --> pdb=" O GLNCC 82 " (cutoff:3.500A) Processing helix chain 'CC' and resid 86 through 94 Processing helix chain 'CC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALCC 100 " --> pdb=" O ASNCC 97 " (cutoff:3.500A) Processing helix chain 'CC' and resid 147 through 152 removed outlier: 3.655A pdb=" N TRPCC 152 " --> pdb=" O ARGCC 148 " (cutoff:3.500A) Processing helix chain 'CC' and resid 174 through 218 Processing helix chain 'CD' and resid 37 through 60 Processing helix chain 'CD' and resid 64 through 68 removed outlier: 4.003A pdb=" N ASPCD 68 " --> pdb=" O PROCD 65 " (cutoff:3.500A) Processing helix chain 'CD' and resid 91 through 102 Processing helix chain 'CD' and resid 128 through 140 Processing helix chain 'CH' and resid 278 through 282 Processing helix chain 'CK' and resid 49 through 63 Processing helix chain 'CK' and resid 80 through 84 Processing helix chain 'CK' and resid 94 through 107 removed outlier: 4.088A pdb=" N LEUCK 98 " --> pdb=" O ALACK 94 " (cutoff:3.500A) Processing helix chain 'CK' and resid 125 through 147 Processing helix chain 'Cd' and resid 35 through 63 removed outlier: 4.246A pdb=" N SERCd 47 " --> pdb=" O GLUCd 43 " (cutoff:3.500A) Processing helix chain 'Cd' and resid 90 through 102 removed outlier: 4.110A pdb=" N LEUCd 94 " --> pdb=" O PROCd 90 " (cutoff:3.500A) Processing helix chain 'Cd' and resid 128 through 139 Processing helix chain 'DC' and resid 59 through 86 removed outlier: 4.114A pdb=" N GLNDC 69 " --> pdb=" O SERDC 65 " (cutoff:3.500A) removed outlier: 3.772A pdb=" N ALADC 70 " --> pdb=" O VALDC 66 " (cutoff:3.500A) removed outlier: 3.654A pdb=" N GLNDC 86 " --> pdb=" O GLNDC 82 " (cutoff:3.500A) Processing helix chain 'DC' and resid 86 through 94 Processing helix chain 'DC' and resid 96 through 100 removed outlier: 3.897A pdb=" N VALDC 100 " --> pdb=" O ASNDC 97 " (cutoff:3.500A) Processing helix chain 'DC' and resid 147 through 152 removed outlier: 3.656A pdb=" N TRPDC 152 " --> pdb=" O ARGDC 148 " (cutoff:3.500A) Processing helix chain 'DC' and resid 174 through 218 Processing helix chain 'DD' and resid 37 through 60 Processing helix chain 'DD' and resid 64 through 68 removed outlier: 4.203A pdb=" N ASPDD 68 " --> pdb=" O PRODD 65 " (cutoff:3.500A) Processing helix chain 'DD' and resid 91 through 102 Processing helix chain 'DD' and resid 128 through 140 Processing sheet with id=AA1, first strand: chain 'AC' and resid 105 through 106 Processing sheet with id=AA2, first strand: chain 'BC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRBC 225 " --> pdb=" O THRBC 250 " (cutoff:3.500A) Processing sheet with id=AA3, first strand: chain 'BC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRBC 225 " --> pdb=" O THRBC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEAC 125 " --> pdb=" O LEUAC 119 " (cutoff:3.500A) removed outlier: 6.847A pdb=" N LEUAC 119 " --> pdb=" O ILEAC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEAC 127 " --> pdb=" O LEUAC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEUAC 117 " --> pdb=" O ILEAC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPAC 129 " --> pdb=" O ASNAC 115 " (cutoff:3.500A) removed outlier: 4.703A pdb=" N ASNAC 115 " --> pdb=" O THRBH 330 " (cutoff:3.500A) removed outlier: 4.597A pdb=" N THRBH 330 " --> pdb=" O ASNAC 115 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALABH 303 " --> pdb=" O VALBH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALBH 298 " --> pdb=" O ALABH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALABH 305 " --> pdb=" O LEUBH 296 " (cutoff:3.500A) removed outlier: 4.145A pdb=" N VALBH 297 " --> pdb=" O GLUBH 360 " (cutoff:3.500A) Processing sheet with id=AA4, first strand: chain 'AC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRAC 225 " --> pdb=" O THRAC 250 " (cutoff:3.500A) Processing sheet with id=AA5, first strand: chain 'AC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRAC 225 " --> pdb=" O THRAC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEMC 125 " --> pdb=" O LEUMC 119 " (cutoff:3.500A) removed outlier: 6.845A pdb=" N LEUMC 119 " --> pdb=" O ILEMC 125 " (cutoff:3.500A) removed outlier: 6.673A pdb=" N ILEMC 127 " --> pdb=" O LEUMC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEUMC 117 " --> pdb=" O ILEMC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPMC 129 " --> pdb=" O ASNMC 115 " (cutoff:3.500A) removed outlier: 4.694A pdb=" N ASNMC 115 " --> pdb=" O THRAH 330 " (cutoff:3.500A) removed outlier: 4.570A pdb=" N THRAH 330 " --> pdb=" O ASNMC 115 " (cutoff:3.500A) removed outlier: 6.186A pdb=" N ALAAH 303 " --> pdb=" O VALAH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALAH 298 " --> pdb=" O ALAAH 303 " (cutoff:3.500A) removed outlier: 3.974A pdb=" N ALAAH 305 " --> pdb=" O LEUAH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALAH 297 " --> pdb=" O GLUAH 360 " (cutoff:3.500A) Processing sheet with id=AA6, first strand: chain 'DH' and resid 319 through 320 removed outlier: 4.146A pdb=" N VALDH 297 " --> pdb=" O GLUDH 360 " (cutoff:3.500A) removed outlier: 3.976A pdb=" N ALADH 305 " --> pdb=" O LEUDH 296 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALDH 298 " --> pdb=" O ALADH 303 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALADH 303 " --> pdb=" O VALDH 298 " (cutoff:3.500A) removed outlier: 4.599A pdb=" N THRDH 330 " --> pdb=" O ASNCC 115 " (cutoff:3.500A) removed outlier: 4.680A pdb=" N ASNCC 115 " --> pdb=" O THRDH 330 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPCC 129 " --> pdb=" O ASNCC 115 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUCC 117 " --> pdb=" O ILECC 127 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILECC 127 " --> pdb=" O LEUCC 117 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUCC 119 " --> pdb=" O ILECC 125 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILECC 125 " --> pdb=" O LEUCC 119 " (cutoff:3.500A) removed outlier: 6.453A pdb=" N TYRDC 225 " --> pdb=" O THRDC 250 " (cutoff:3.500A) Processing sheet with id=AA7, first strand: chain 'DH' and resid 319 through 320 removed outlier: 4.146A pdb=" N VALDH 297 " --> pdb=" O GLUDH 360 " (cutoff:3.500A) removed outlier: 3.976A pdb=" N ALADH 305 " --> pdb=" O LEUDH 296 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALDH 298 " --> pdb=" O ALADH 303 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALADH 303 " --> pdb=" O VALDH 298 " (cutoff:3.500A) removed outlier: 4.599A pdb=" N THRDH 330 " --> pdb=" O ASNCC 115 " (cutoff:3.500A) removed outlier: 4.680A pdb=" N ASNCC 115 " --> pdb=" O THRDH 330 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPCC 129 " --> pdb=" O ASNCC 115 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUCC 117 " --> pdb=" O ILECC 127 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILECC 127 " --> pdb=" O LEUCC 117 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUCC 119 " --> pdb=" O ILECC 125 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILECC 125 " --> pdb=" O LEUCC 119 " (cutoff:3.500A) Processing sheet with id=AA8, first strand: chain 'DK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGDK 185 " --> pdb=" O ALADK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALADK 113 " --> pdb=" O ARGDK 185 " (cutoff:3.500A) removed outlier: 6.833A pdb=" N VALDd 85 " --> pdb=" O LYSDd 124 " (cutoff:3.500A) removed outlier: 5.047A pdb=" N LYSDd 124 " --> pdb=" O VALDd 85 " (cutoff:3.500A) Processing sheet with id=AA9, first strand: chain 'DX' and resid 17 through 18 Processing sheet with id=AB1, first strand: chain 'DX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALADX 41 " --> pdb=" O ALADX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALADX 59 " --> pdb=" O ALADX 41 " (cutoff:3.500A) removed outlier: 6.810A pdb=" N ALADX 56 " --> pdb=" O ALADX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALADX 75 " --> pdb=" O ALADX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALADX 58 " --> pdb=" O ALADX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALADX 77 " --> pdb=" O ALADX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALADX 60 " --> pdb=" O ALADX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALADX 91 " --> pdb=" O ALADX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALADX 110 " --> pdb=" O ALADX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALADX 93 " --> pdb=" O ALADX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALADX 112 " --> pdb=" O ALADX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALADX 95 " --> pdb=" O ALADX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALADX 109 " --> pdb=" O ALADX 130 " (cutoff:3.500A) removed outlier: 8.019A pdb=" N ALADX 132 " --> pdb=" O ALADX 109 " (cutoff:3.500A) removed outlier: 6.370A pdb=" N ALADX 111 " --> pdb=" O ALADX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALADX 129 " --> pdb=" O ALADX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALADX 151 " --> pdb=" O ALADX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALADX 131 " --> pdb=" O ALADX 151 " (cutoff:3.500A) removed outlier: 7.954A pdb=" N ALADX 164 " --> pdb=" O ALADX 182 " (cutoff:3.500A) removed outlier: 5.482A pdb=" N ALADX 184 " --> pdb=" O ALADX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALADX 166 " --> pdb=" O ALADX 184 " (cutoff:3.500A) removed outlier: 7.196A pdb=" N ALADX 186 " --> pdb=" O ALADX 166 " (cutoff:3.500A) removed outlier: 3.936A pdb=" N ALADX 168 " --> pdb=" O ALADX 186 " (cutoff:3.500A) removed outlier: 7.135A pdb=" N ALADX 188 " --> pdb=" O ALADX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALADX 170 " --> pdb=" O ALADX 188 " (cutoff:3.500A) Processing sheet with id=AB2, first strand: chain 'DX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALADX 47 " --> pdb=" O ALADX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALADX 64 " --> pdb=" O ALADX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AB2 Processing sheet with id=AB3, first strand: chain 'DX' and resid 99 through 102 removed outlier: 6.713A pdb=" N ALADX 119 " --> pdb=" O ALADX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALADX 141 " --> pdb=" O ALADX 159 " (cutoff:3.500A) removed outlier: 6.611A pdb=" N ALADX 177 " --> pdb=" O ALADX 195 " (cutoff:3.500A) Processing sheet with id=AB4, first strand: chain 'DY' and resid 2 through 4 Processing sheet with id=AB5, first strand: chain 'DY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALADY 42 " --> pdb=" O ALADY 34 " (cutoff:3.500A) removed outlier: 4.049A pdb=" N ALADY 40 " --> pdb=" O ALADY 36 " (cutoff:3.500A) Processing sheet with id=AB6, first strand: chain 'DZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALADZ 18 " --> pdb=" O ALADZ 9 " (cutoff:3.500A) removed outlier: 5.825A pdb=" N ALADZ 11 " --> pdb=" O ALADZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALADZ 16 " --> pdb=" O ALADZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALADZ 26 " --> pdb=" O ALADZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALADZ 19 " --> pdb=" O ALADZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALADZ 24 " --> pdb=" O ALADZ 19 " (cutoff:3.500A) Processing sheet with id=AB7, first strand: chain 'Dd' and resid 105 through 109 removed outlier: 3.589A pdb=" N VALDd 153 " --> pdb=" O TYRDd 148 " (cutoff:3.500A) Processing sheet with id=AB8, first strand: chain 'EC' and resid 105 through 106 Processing sheet with id=AB9, first strand: chain 'FC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRFC 225 " --> pdb=" O THRFC 250 " (cutoff:3.500A) Processing sheet with id=AC1, first strand: chain 'FC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRFC 225 " --> pdb=" O THRFC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEEC 125 " --> pdb=" O LEUEC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUEC 119 " --> pdb=" O ILEEC 125 " (cutoff:3.500A) removed outlier: 6.673A pdb=" N ILEEC 127 " --> pdb=" O LEUEC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEUEC 117 " --> pdb=" O ILEEC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPEC 129 " --> pdb=" O ASNEC 115 " (cutoff:3.500A) removed outlier: 4.668A pdb=" N ASNEC 115 " --> pdb=" O THRFH 330 " (cutoff:3.500A) removed outlier: 4.561A pdb=" N THRFH 330 " --> pdb=" O ASNEC 115 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAFH 303 " --> pdb=" O VALFH 298 " (cutoff:3.500A) removed outlier: 5.128A pdb=" N VALFH 298 " --> pdb=" O ALAFH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALAFH 305 " --> pdb=" O LEUFH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALFH 297 " --> pdb=" O GLUFH 360 " (cutoff:3.500A) Processing sheet with id=AC2, first strand: chain 'EC' and resid 225 through 231 removed outlier: 6.452A pdb=" N TYREC 225 " --> pdb=" O THREC 250 " (cutoff:3.500A) Processing sheet with id=AC3, first strand: chain 'EC' and resid 225 through 231 removed outlier: 6.452A pdb=" N TYREC 225 " --> pdb=" O THREC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEDC 125 " --> pdb=" O LEUDC 119 " (cutoff:3.500A) removed outlier: 6.845A pdb=" N LEUDC 119 " --> pdb=" O ILEDC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEDC 127 " --> pdb=" O LEUDC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEUDC 117 " --> pdb=" O ILEDC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPDC 129 " --> pdb=" O ASNDC 115 " (cutoff:3.500A) removed outlier: 4.732A pdb=" N ASNDC 115 " --> pdb=" O THREH 330 " (cutoff:3.500A) removed outlier: 4.647A pdb=" N THREH 330 " --> pdb=" O ASNDC 115 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAEH 303 " --> pdb=" O VALEH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALEH 298 " --> pdb=" O ALAEH 303 " (cutoff:3.500A) removed outlier: 3.976A pdb=" N ALAEH 305 " --> pdb=" O LEUEH 296 " (cutoff:3.500A) removed outlier: 4.147A pdb=" N VALEH 297 " --> pdb=" O GLUEH 360 " (cutoff:3.500A) Processing sheet with id=AC4, first strand: chain 'ED' and resid 85 through 87 Processing sheet with id=AC5, first strand: chain 'ED' and resid 105 through 109 removed outlier: 5.996A pdb=" N ARGED 105 " --> pdb=" O VALED 154 " (cutoff:3.500A) removed outlier: 7.794A pdb=" N LEUED 156 " --> pdb=" O ARGED 105 " (cutoff:3.500A) removed outlier: 6.748A pdb=" N ARGED 107 " --> pdb=" O LEUED 156 " (cutoff:3.500A) Processing sheet with id=AC6, first strand: chain 'EK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGEK 185 " --> pdb=" O ALAEK 113 " (cutoff:3.500A) removed outlier: 5.624A pdb=" N ALAEK 113 " --> pdb=" O ARGEK 185 " (cutoff:3.500A) removed outlier: 6.772A pdb=" N VALEd 85 " --> pdb=" O LYSEd 124 " (cutoff:3.500A) removed outlier: 5.010A pdb=" N LYSEd 124 " --> pdb=" O VALEd 85 " (cutoff:3.500A) Processing sheet with id=AC7, first strand: chain 'EX' and resid 17 through 18 Processing sheet with id=AC8, first strand: chain 'EX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALAEX 41 " --> pdb=" O ALAEX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALAEX 59 " --> pdb=" O ALAEX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAEX 56 " --> pdb=" O ALAEX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAEX 75 " --> pdb=" O ALAEX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALAEX 58 " --> pdb=" O ALAEX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAEX 77 " --> pdb=" O ALAEX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAEX 60 " --> pdb=" O ALAEX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAEX 91 " --> pdb=" O ALAEX 108 " (cutoff:3.500A) removed outlier: 4.233A pdb=" N ALAEX 110 " --> pdb=" O ALAEX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALAEX 93 " --> pdb=" O ALAEX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAEX 112 " --> pdb=" O ALAEX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAEX 95 " --> pdb=" O ALAEX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAEX 109 " --> pdb=" O ALAEX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAEX 132 " --> pdb=" O ALAEX 109 " (cutoff:3.500A) removed outlier: 6.368A pdb=" N ALAEX 111 " --> pdb=" O ALAEX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAEX 129 " --> pdb=" O ALAEX 149 " (cutoff:3.500A) removed outlier: 7.225A pdb=" N ALAEX 151 " --> pdb=" O ALAEX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALAEX 131 " --> pdb=" O ALAEX 151 " (cutoff:3.500A) removed outlier: 7.954A pdb=" N ALAEX 164 " --> pdb=" O ALAEX 182 " (cutoff:3.500A) removed outlier: 5.482A pdb=" N ALAEX 184 " --> pdb=" O ALAEX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALAEX 166 " --> pdb=" O ALAEX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAEX 186 " --> pdb=" O ALAEX 166 " (cutoff:3.500A) removed outlier: 3.936A pdb=" N ALAEX 168 " --> pdb=" O ALAEX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAEX 188 " --> pdb=" O ALAEX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAEX 170 " --> pdb=" O ALAEX 188 " (cutoff:3.500A) Processing sheet with id=AC9, first strand: chain 'EX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALAEX 47 " --> pdb=" O ALAEX 67 " (cutoff:3.500A) removed outlier: 6.237A pdb=" N ALAEX 64 " --> pdb=" O ALAEX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AC9 Processing sheet with id=AD1, first strand: chain 'EX' and resid 99 through 102 removed outlier: 6.714A pdb=" N ALAEX 119 " --> pdb=" O ALAEX 140 " (cutoff:3.500A) removed outlier: 3.913A pdb=" N ALAEX 141 " --> pdb=" O ALAEX 159 " (cutoff:3.500A) removed outlier: 6.611A pdb=" N ALAEX 177 " --> pdb=" O ALAEX 195 " (cutoff:3.500A) Processing sheet with id=AD2, first strand: chain 'EY' and resid 2 through 4 Processing sheet with id=AD3, first strand: chain 'EY' and resid 34 through 36 removed outlier: 3.666A pdb=" N ALAEY 42 " --> pdb=" O ALAEY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALAEY 40 " --> pdb=" O ALAEY 36 " (cutoff:3.500A) Processing sheet with id=AD4, first strand: chain 'EZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALAEZ 18 " --> pdb=" O ALAEZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAEZ 11 " --> pdb=" O ALAEZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALAEZ 16 " --> pdb=" O ALAEZ 11 " (cutoff:3.500A) removed outlier: 5.593A pdb=" N ALAEZ 26 " --> pdb=" O ALAEZ 17 " (cutoff:3.500A) removed outlier: 6.723A pdb=" N ALAEZ 19 " --> pdb=" O ALAEZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALAEZ 24 " --> pdb=" O ALAEZ 19 " (cutoff:3.500A) Processing sheet with id=AD5, first strand: chain 'Ed' and resid 105 through 109 Processing sheet with id=AD6, first strand: chain 'FC' and resid 105 through 106 Processing sheet with id=AD7, first strand: chain 'GC' and resid 225 through 231 removed outlier: 6.454A pdb=" N TYRGC 225 " --> pdb=" O THRGC 250 " (cutoff:3.500A) Processing sheet with id=AD8, first strand: chain 'GC' and resid 225 through 231 removed outlier: 6.454A pdb=" N TYRGC 225 " --> pdb=" O THRGC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEFC 125 " --> pdb=" O LEUFC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUFC 119 " --> pdb=" O ILEFC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEFC 127 " --> pdb=" O LEUFC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEUFC 117 " --> pdb=" O ILEFC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPFC 129 " --> pdb=" O ASNFC 115 " (cutoff:3.500A) removed outlier: 4.844A pdb=" N ASNFC 115 " --> pdb=" O THRGH 330 " (cutoff:3.500A) removed outlier: 4.720A pdb=" N THRGH 330 " --> pdb=" O ASNFC 115 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAGH 303 " --> pdb=" O VALGH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALGH 298 " --> pdb=" O ALAGH 303 " (cutoff:3.500A) removed outlier: 3.976A pdb=" N ALAGH 305 " --> pdb=" O LEUGH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALGH 297 " --> pdb=" O GLUGH 360 " (cutoff:3.500A) Processing sheet with id=AD9, first strand: chain 'FD' and resid 82 through 90 removed outlier: 6.560A pdb=" N ALAFD 83 " --> pdb=" O ASPFD 125 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ASPFD 125 " --> pdb=" O ALAFD 83 " (cutoff:3.500A) Processing sheet with id=AE1, first strand: chain 'FD' and resid 105 through 109 removed outlier: 5.884A pdb=" N ARGFD 105 " --> pdb=" O VALFD 154 " (cutoff:3.500A) removed outlier: 7.703A pdb=" N LEUFD 156 " --> pdb=" O ARGFD 105 " (cutoff:3.500A) removed outlier: 6.682A pdb=" N ARGFD 107 " --> pdb=" O LEUFD 156 " (cutoff:3.500A) Processing sheet with id=AE2, first strand: chain 'FK' and resid 66 through 70 removed outlier: 4.450A pdb=" N ARGFK 185 " --> pdb=" O ALAFK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALAFK 113 " --> pdb=" O ARGFK 185 " (cutoff:3.500A) removed outlier: 7.251A pdb=" N VALFd 85 " --> pdb=" O LYSFd 124 " (cutoff:3.500A) removed outlier: 5.147A pdb=" N LYSFd 124 " --> pdb=" O VALFd 85 " (cutoff:3.500A) Processing sheet with id=AE3, first strand: chain 'FX' and resid 17 through 18 Processing sheet with id=AE4, first strand: chain 'FX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALAFX 41 " --> pdb=" O ALAFX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALAFX 59 " --> pdb=" O ALAFX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAFX 56 " --> pdb=" O ALAFX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAFX 75 " --> pdb=" O ALAFX 56 " (cutoff:3.500A) removed outlier: 6.614A pdb=" N ALAFX 58 " --> pdb=" O ALAFX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAFX 77 " --> pdb=" O ALAFX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAFX 60 " --> pdb=" O ALAFX 77 " (cutoff:3.500A) removed outlier: 6.468A pdb=" N ALAFX 91 " --> pdb=" O ALAFX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALAFX 110 " --> pdb=" O ALAFX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALAFX 93 " --> pdb=" O ALAFX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAFX 112 " --> pdb=" O ALAFX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAFX 95 " --> pdb=" O ALAFX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAFX 109 " --> pdb=" O ALAFX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAFX 132 " --> pdb=" O ALAFX 109 " (cutoff:3.500A) removed outlier: 6.368A pdb=" N ALAFX 111 " --> pdb=" O ALAFX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAFX 129 " --> pdb=" O ALAFX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALAFX 151 " --> pdb=" O ALAFX 129 " (cutoff:3.500A) removed outlier: 6.352A pdb=" N ALAFX 131 " --> pdb=" O ALAFX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAFX 164 " --> pdb=" O ALAFX 182 " (cutoff:3.500A) removed outlier: 5.482A pdb=" N ALAFX 184 " --> pdb=" O ALAFX 164 " (cutoff:3.500A) removed outlier: 4.324A pdb=" N ALAFX 166 " --> pdb=" O ALAFX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAFX 186 " --> pdb=" O ALAFX 166 " (cutoff:3.500A) removed outlier: 3.936A pdb=" N ALAFX 168 " --> pdb=" O ALAFX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAFX 188 " --> pdb=" O ALAFX 168 " (cutoff:3.500A) removed outlier: 4.058A pdb=" N ALAFX 170 " --> pdb=" O ALAFX 188 " (cutoff:3.500A) Processing sheet with id=AE5, first strand: chain 'FX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALAFX 47 " --> pdb=" O ALAFX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALAFX 64 " --> pdb=" O ALAFX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AE5 Processing sheet with id=AE6, first strand: chain 'FX' and resid 99 through 102 removed outlier: 6.712A pdb=" N ALAFX 119 " --> pdb=" O ALAFX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAFX 141 " --> pdb=" O ALAFX 159 " (cutoff:3.500A) removed outlier: 6.611A pdb=" N ALAFX 177 " --> pdb=" O ALAFX 195 " (cutoff:3.500A) Processing sheet with id=AE7, first strand: chain 'FY' and resid 2 through 4 Processing sheet with id=AE8, first strand: chain 'FY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAFY 42 " --> pdb=" O ALAFY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALAFY 40 " --> pdb=" O ALAFY 36 " (cutoff:3.500A) Processing sheet with id=AE9, first strand: chain 'FZ' and resid 8 through 11 removed outlier: 6.833A pdb=" N ALAFZ 18 " --> pdb=" O ALAFZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAFZ 11 " --> pdb=" O ALAFZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALAFZ 16 " --> pdb=" O ALAFZ 11 " (cutoff:3.500A) removed outlier: 5.593A pdb=" N ALAFZ 26 " --> pdb=" O ALAFZ 17 " (cutoff:3.500A) removed outlier: 6.723A pdb=" N ALAFZ 19 " --> pdb=" O ALAFZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALAFZ 24 " --> pdb=" O ALAFZ 19 " (cutoff:3.500A) Processing sheet with id=AF1, first strand: chain 'Fd' and resid 105 through 109 removed outlier: 5.978A pdb=" N ARGFd 105 " --> pdb=" O VALFd 154 " (cutoff:3.500A) removed outlier: 7.794A pdb=" N LEUFd 156 " --> pdb=" O ARGFd 105 " (cutoff:3.500A) removed outlier: 6.668A pdb=" N ARGFd 107 " --> pdb=" O LEUFd 156 " (cutoff:3.500A) removed outlier: 7.933A pdb=" N TYRFd 158 " --> pdb=" O ARGFd 107 " (cutoff:3.500A) removed outlier: 7.031A pdb=" N LEUFd 109 " --> pdb=" O TYRFd 158 " (cutoff:3.500A) removed outlier: 3.570A pdb=" N VALFd 153 " --> pdb=" O TYRFd 148 " (cutoff:3.500A) Processing sheet with id=AF2, first strand: chain 'GC' and resid 105 through 106 Processing sheet with id=AF3, first strand: chain 'HC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRHC 225 " --> pdb=" O THRHC 250 " (cutoff:3.500A) Processing sheet with id=AF4, first strand: chain 'HC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRHC 225 " --> pdb=" O THRHC 250 " (cutoff:3.500A) removed outlier: 6.789A pdb=" N ILEGC 125 " --> pdb=" O LEUGC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUGC 119 " --> pdb=" O ILEGC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEGC 127 " --> pdb=" O LEUGC 117 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUGC 117 " --> pdb=" O ILEGC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPGC 129 " --> pdb=" O ASNGC 115 " (cutoff:3.500A) removed outlier: 4.222A pdb=" N THRGC 116 " --> pdb=" O SERHH 328 " (cutoff:3.500A) removed outlier: 6.526A pdb=" N SERHH 328 " --> pdb=" O THRGC 116 " (cutoff:3.500A) removed outlier: 6.186A pdb=" N ALAHH 303 " --> pdb=" O VALHH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALHH 298 " --> pdb=" O ALAHH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALAHH 305 " --> pdb=" O LEUHH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALHH 297 " --> pdb=" O GLUHH 360 " (cutoff:3.500A) Processing sheet with id=AF5, first strand: chain 'GD' and resid 82 through 90 removed outlier: 6.477A pdb=" N ALAGD 83 " --> pdb=" O ASPGD 125 " (cutoff:3.500A) removed outlier: 4.159A pdb=" N ASPGD 125 " --> pdb=" O ALAGD 83 " (cutoff:3.500A) Processing sheet with id=AF6, first strand: chain 'GD' and resid 105 through 109 removed outlier: 5.961A pdb=" N ARGGD 105 " --> pdb=" O VALGD 154 " (cutoff:3.500A) removed outlier: 7.754A pdb=" N LEUGD 156 " --> pdb=" O ARGGD 105 " (cutoff:3.500A) removed outlier: 6.818A pdb=" N ARGGD 107 " --> pdb=" O LEUGD 156 " (cutoff:3.500A) Processing sheet with id=AF7, first strand: chain 'GK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGGK 185 " --> pdb=" O ALAGK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALAGK 113 " --> pdb=" O ARGGK 185 " (cutoff:3.500A) removed outlier: 7.153A pdb=" N VALGd 85 " --> pdb=" O LYSGd 124 " (cutoff:3.500A) removed outlier: 5.280A pdb=" N LYSGd 124 " --> pdb=" O VALGd 85 " (cutoff:3.500A) Processing sheet with id=AF8, first strand: chain 'AD' and resid 85 through 90 Processing sheet with id=AF9, first strand: chain 'AD' and resid 105 through 109 removed outlier: 5.981A pdb=" N ARGAD 105 " --> pdb=" O VALAD 154 " (cutoff:3.500A) removed outlier: 7.734A pdb=" N LEUAD 156 " --> pdb=" O ARGAD 105 " (cutoff:3.500A) removed outlier: 6.590A pdb=" N ARGAD 107 " --> pdb=" O LEUAD 156 " (cutoff:3.500A) removed outlier: 8.225A pdb=" N TYRAD 158 " --> pdb=" O ARGAD 107 " (cutoff:3.500A) removed outlier: 7.517A pdb=" N LEUAD 109 " --> pdb=" O TYRAD 158 " (cutoff:3.500A) Processing sheet with id=AG1, first strand: chain 'GX' and resid 17 through 18 Processing sheet with id=AG2, first strand: chain 'GX' and resid 40 through 41 removed outlier: 8.193A pdb=" N ALAGX 41 " --> pdb=" O ALAGX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALAGX 59 " --> pdb=" O ALAGX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAGX 56 " --> pdb=" O ALAGX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAGX 75 " --> pdb=" O ALAGX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALAGX 58 " --> pdb=" O ALAGX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAGX 77 " --> pdb=" O ALAGX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAGX 60 " --> pdb=" O ALAGX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAGX 91 " --> pdb=" O ALAGX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALAGX 110 " --> pdb=" O ALAGX 91 " (cutoff:3.500A) removed outlier: 3.742A pdb=" N ALAGX 93 " --> pdb=" O ALAGX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAGX 112 " --> pdb=" O ALAGX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAGX 95 " --> pdb=" O ALAGX 112 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAGX 109 " --> pdb=" O ALAGX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAGX 132 " --> pdb=" O ALAGX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALAGX 111 " --> pdb=" O ALAGX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAGX 129 " --> pdb=" O ALAGX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALAGX 151 " --> pdb=" O ALAGX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALAGX 131 " --> pdb=" O ALAGX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAGX 164 " --> pdb=" O ALAGX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALAGX 184 " --> pdb=" O ALAGX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALAGX 166 " --> pdb=" O ALAGX 184 " (cutoff:3.500A) removed outlier: 7.196A pdb=" N ALAGX 186 " --> pdb=" O ALAGX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALAGX 168 " --> pdb=" O ALAGX 186 " (cutoff:3.500A) removed outlier: 7.135A pdb=" N ALAGX 188 " --> pdb=" O ALAGX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAGX 170 " --> pdb=" O ALAGX 188 " (cutoff:3.500A) Processing sheet with id=AG3, first strand: chain 'GX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALAGX 47 " --> pdb=" O ALAGX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALAGX 64 " --> pdb=" O ALAGX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AG3 Processing sheet with id=AG4, first strand: chain 'GX' and resid 99 through 102 removed outlier: 6.714A pdb=" N ALAGX 119 " --> pdb=" O ALAGX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAGX 141 " --> pdb=" O ALAGX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALAGX 177 " --> pdb=" O ALAGX 195 " (cutoff:3.500A) Processing sheet with id=AG5, first strand: chain 'GY' and resid 2 through 4 Processing sheet with id=AG6, first strand: chain 'GY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAGY 42 " --> pdb=" O ALAGY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALAGY 40 " --> pdb=" O ALAGY 36 " (cutoff:3.500A) Processing sheet with id=AG7, first strand: chain 'GZ' and resid 8 through 11 removed outlier: 6.833A pdb=" N ALAGZ 18 " --> pdb=" O ALAGZ 9 " (cutoff:3.500A) removed outlier: 5.825A pdb=" N ALAGZ 11 " --> pdb=" O ALAGZ 16 " (cutoff:3.500A) removed outlier: 7.446A pdb=" N ALAGZ 16 " --> pdb=" O ALAGZ 11 " (cutoff:3.500A) removed outlier: 5.593A pdb=" N ALAGZ 26 " --> pdb=" O ALAGZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALAGZ 19 " --> pdb=" O ALAGZ 24 " (cutoff:3.500A) removed outlier: 6.102A pdb=" N ALAGZ 24 " --> pdb=" O ALAGZ 19 " (cutoff:3.500A) Processing sheet with id=AG8, first strand: chain 'Gd' and resid 105 through 109 removed outlier: 5.973A pdb=" N ARGGd 105 " --> pdb=" O VALGd 154 " (cutoff:3.500A) removed outlier: 7.727A pdb=" N LEUGd 156 " --> pdb=" O ARGGd 105 " (cutoff:3.500A) removed outlier: 6.684A pdb=" N ARGGd 107 " --> pdb=" O LEUGd 156 " (cutoff:3.500A) removed outlier: 7.906A pdb=" N TYRGd 158 " --> pdb=" O ARGGd 107 " (cutoff:3.500A) removed outlier: 7.186A pdb=" N LEUGd 109 " --> pdb=" O TYRGd 158 " (cutoff:3.500A) removed outlier: 3.588A pdb=" N VALGd 153 " --> pdb=" O TYRGd 148 " (cutoff:3.500A) Processing sheet with id=AG9, first strand: chain 'HC' and resid 105 through 106 Processing sheet with id=AH1, first strand: chain 'IC' and resid 225 through 231 removed outlier: 6.452A pdb=" N TYRIC 225 " --> pdb=" O THRIC 250 " (cutoff:3.500A) Processing sheet with id=AH2, first strand: chain 'IC' and resid 225 through 231 removed outlier: 6.452A pdb=" N TYRIC 225 " --> pdb=" O THRIC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEHC 125 " --> pdb=" O LEUHC 119 " (cutoff:3.500A) removed outlier: 6.845A pdb=" N LEUHC 119 " --> pdb=" O ILEHC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEHC 127 " --> pdb=" O LEUHC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEUHC 117 " --> pdb=" O ILEHC 127 " (cutoff:3.500A) removed outlier: 6.795A pdb=" N ASPHC 129 " --> pdb=" O ASNHC 115 " (cutoff:3.500A) removed outlier: 4.091A pdb=" N THRHC 116 " --> pdb=" O SERIH 328 " (cutoff:3.500A) removed outlier: 6.399A pdb=" N SERIH 328 " --> pdb=" O THRHC 116 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAIH 303 " --> pdb=" O VALIH 298 " (cutoff:3.500A) removed outlier: 5.126A pdb=" N VALIH 298 " --> pdb=" O ALAIH 303 " (cutoff:3.500A) removed outlier: 3.976A pdb=" N ALAIH 305 " --> pdb=" O LEUIH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALIH 297 " --> pdb=" O GLUIH 360 " (cutoff:3.500A) Processing sheet with id=AH3, first strand: chain 'HD' and resid 82 through 90 removed outlier: 6.365A pdb=" N ALAHD 83 " --> pdb=" O ASPHD 125 " (cutoff:3.500A) removed outlier: 4.193A pdb=" N ASPHD 125 " --> pdb=" O ALAHD 83 " (cutoff:3.500A) Processing sheet with id=AH4, first strand: chain 'HD' and resid 105 through 109 removed outlier: 5.955A pdb=" N ARGHD 105 " --> pdb=" O VALHD 154 " (cutoff:3.500A) removed outlier: 7.656A pdb=" N LEUHD 156 " --> pdb=" O ARGHD 105 " (cutoff:3.500A) removed outlier: 6.559A pdb=" N ARGHD 107 " --> pdb=" O LEUHD 156 " (cutoff:3.500A) Processing sheet with id=AH5, first strand: chain 'HK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGHK 185 " --> pdb=" O ALAHK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALAHK 113 " --> pdb=" O ARGHK 185 " (cutoff:3.500A) removed outlier: 6.782A pdb=" N VALHd 85 " --> pdb=" O LYSHd 124 " (cutoff:3.500A) removed outlier: 4.991A pdb=" N LYSHd 124 " --> pdb=" O VALHd 85 " (cutoff:3.500A) Processing sheet with id=AH6, first strand: chain 'HX' and resid 17 through 18 Processing sheet with id=AH7, first strand: chain 'HX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALAHX 41 " --> pdb=" O ALAHX 57 " (cutoff:3.500A) removed outlier: 6.656A pdb=" N ALAHX 59 " --> pdb=" O ALAHX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAHX 56 " --> pdb=" O ALAHX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAHX 75 " --> pdb=" O ALAHX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALAHX 58 " --> pdb=" O ALAHX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAHX 77 " --> pdb=" O ALAHX 58 " (cutoff:3.500A) removed outlier: 6.396A pdb=" N ALAHX 60 " --> pdb=" O ALAHX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAHX 91 " --> pdb=" O ALAHX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALAHX 110 " --> pdb=" O ALAHX 91 " (cutoff:3.500A) removed outlier: 3.742A pdb=" N ALAHX 93 " --> pdb=" O ALAHX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAHX 112 " --> pdb=" O ALAHX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAHX 95 " --> pdb=" O ALAHX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAHX 109 " --> pdb=" O ALAHX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAHX 132 " --> pdb=" O ALAHX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALAHX 111 " --> pdb=" O ALAHX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAHX 129 " --> pdb=" O ALAHX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALAHX 151 " --> pdb=" O ALAHX 129 " (cutoff:3.500A) removed outlier: 6.352A pdb=" N ALAHX 131 " --> pdb=" O ALAHX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAHX 164 " --> pdb=" O ALAHX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALAHX 184 " --> pdb=" O ALAHX 164 " (cutoff:3.500A) removed outlier: 4.326A pdb=" N ALAHX 166 " --> pdb=" O ALAHX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAHX 186 " --> pdb=" O ALAHX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALAHX 168 " --> pdb=" O ALAHX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAHX 188 " --> pdb=" O ALAHX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAHX 170 " --> pdb=" O ALAHX 188 " (cutoff:3.500A) Processing sheet with id=AH8, first strand: chain 'HX' and resid 46 through 48 removed outlier: 6.984A pdb=" N ALAHX 47 " --> pdb=" O ALAHX 67 " (cutoff:3.500A) removed outlier: 6.237A pdb=" N ALAHX 64 " --> pdb=" O ALAHX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AH8 Processing sheet with id=AH9, first strand: chain 'HX' and resid 99 through 102 removed outlier: 6.714A pdb=" N ALAHX 119 " --> pdb=" O ALAHX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAHX 141 " --> pdb=" O ALAHX 159 " (cutoff:3.500A) removed outlier: 6.609A pdb=" N ALAHX 177 " --> pdb=" O ALAHX 195 " (cutoff:3.500A) Processing sheet with id=AI1, first strand: chain 'HY' and resid 2 through 4 Processing sheet with id=AI2, first strand: chain 'HY' and resid 34 through 36 removed outlier: 3.666A pdb=" N ALAHY 42 " --> pdb=" O ALAHY 34 " (cutoff:3.500A) removed outlier: 4.049A pdb=" N ALAHY 40 " --> pdb=" O ALAHY 36 " (cutoff:3.500A) Processing sheet with id=AI3, first strand: chain 'HZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALAHZ 18 " --> pdb=" O ALAHZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAHZ 11 " --> pdb=" O ALAHZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALAHZ 16 " --> pdb=" O ALAHZ 11 " (cutoff:3.500A) removed outlier: 5.593A pdb=" N ALAHZ 26 " --> pdb=" O ALAHZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALAHZ 19 " --> pdb=" O ALAHZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALAHZ 24 " --> pdb=" O ALAHZ 19 " (cutoff:3.500A) Processing sheet with id=AI4, first strand: chain 'Hd' and resid 105 through 109 Processing sheet with id=AI5, first strand: chain 'IC' and resid 105 through 106 Processing sheet with id=AI6, first strand: chain 'JC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRJC 225 " --> pdb=" O THRJC 250 " (cutoff:3.500A) Processing sheet with id=AI7, first strand: chain 'JC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRJC 225 " --> pdb=" O THRJC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEIC 125 " --> pdb=" O LEUIC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUIC 119 " --> pdb=" O ILEIC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEIC 127 " --> pdb=" O LEUIC 117 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUIC 117 " --> pdb=" O ILEIC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPIC 129 " --> pdb=" O ASNIC 115 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N THRIC 116 " --> pdb=" O SERJH 328 " (cutoff:3.500A) removed outlier: 6.453A pdb=" N SERJH 328 " --> pdb=" O THRIC 116 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAJH 303 " --> pdb=" O VALJH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALJH 298 " --> pdb=" O ALAJH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALAJH 305 " --> pdb=" O LEUJH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALJH 297 " --> pdb=" O GLUJH 360 " (cutoff:3.500A) Processing sheet with id=AI8, first strand: chain 'ID' and resid 82 through 90 removed outlier: 6.487A pdb=" N ALAID 83 " --> pdb=" O ASPID 125 " (cutoff:3.500A) removed outlier: 4.262A pdb=" N ASPID 125 " --> pdb=" O ALAID 83 " (cutoff:3.500A) Processing sheet with id=AI9, first strand: chain 'ID' and resid 105 through 109 Processing sheet with id=AJ1, first strand: chain 'IK' and resid 66 through 70 removed outlier: 4.450A pdb=" N ARGIK 185 " --> pdb=" O ALAIK 113 " (cutoff:3.500A) removed outlier: 5.624A pdb=" N ALAIK 113 " --> pdb=" O ARGIK 185 " (cutoff:3.500A) removed outlier: 7.115A pdb=" N VALId 85 " --> pdb=" O LYSId 124 " (cutoff:3.500A) removed outlier: 5.071A pdb=" N LYSId 124 " --> pdb=" O VALId 85 " (cutoff:3.500A) Processing sheet with id=AJ2, first strand: chain 'IX' and resid 17 through 18 Processing sheet with id=AJ3, first strand: chain 'IX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALAIX 41 " --> pdb=" O ALAIX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALAIX 59 " --> pdb=" O ALAIX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAIX 56 " --> pdb=" O ALAIX 73 " (cutoff:3.500A) removed outlier: 5.322A pdb=" N ALAIX 75 " --> pdb=" O ALAIX 56 " (cutoff:3.500A) removed outlier: 6.614A pdb=" N ALAIX 58 " --> pdb=" O ALAIX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAIX 77 " --> pdb=" O ALAIX 58 " (cutoff:3.500A) removed outlier: 6.396A pdb=" N ALAIX 60 " --> pdb=" O ALAIX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAIX 91 " --> pdb=" O ALAIX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALAIX 110 " --> pdb=" O ALAIX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALAIX 93 " --> pdb=" O ALAIX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAIX 112 " --> pdb=" O ALAIX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAIX 95 " --> pdb=" O ALAIX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAIX 109 " --> pdb=" O ALAIX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAIX 132 " --> pdb=" O ALAIX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALAIX 111 " --> pdb=" O ALAIX 132 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAIX 129 " --> pdb=" O ALAIX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALAIX 151 " --> pdb=" O ALAIX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALAIX 131 " --> pdb=" O ALAIX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAIX 164 " --> pdb=" O ALAIX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALAIX 184 " --> pdb=" O ALAIX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALAIX 166 " --> pdb=" O ALAIX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAIX 186 " --> pdb=" O ALAIX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALAIX 168 " --> pdb=" O ALAIX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAIX 188 " --> pdb=" O ALAIX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAIX 170 " --> pdb=" O ALAIX 188 " (cutoff:3.500A) Processing sheet with id=AJ4, first strand: chain 'IX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALAIX 47 " --> pdb=" O ALAIX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALAIX 64 " --> pdb=" O ALAIX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AJ4 Processing sheet with id=AJ5, first strand: chain 'IX' and resid 99 through 102 removed outlier: 6.714A pdb=" N ALAIX 119 " --> pdb=" O ALAIX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAIX 141 " --> pdb=" O ALAIX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALAIX 177 " --> pdb=" O ALAIX 195 " (cutoff:3.500A) Processing sheet with id=AJ6, first strand: chain 'IY' and resid 2 through 4 Processing sheet with id=AJ7, first strand: chain 'IY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAIY 42 " --> pdb=" O ALAIY 34 " (cutoff:3.500A) removed outlier: 4.049A pdb=" N ALAIY 40 " --> pdb=" O ALAIY 36 " (cutoff:3.500A) Processing sheet with id=AJ8, first strand: chain 'IZ' and resid 8 through 11 removed outlier: 6.833A pdb=" N ALAIZ 18 " --> pdb=" O ALAIZ 9 " (cutoff:3.500A) removed outlier: 5.825A pdb=" N ALAIZ 11 " --> pdb=" O ALAIZ 16 " (cutoff:3.500A) removed outlier: 7.446A pdb=" N ALAIZ 16 " --> pdb=" O ALAIZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALAIZ 26 " --> pdb=" O ALAIZ 17 " (cutoff:3.500A) removed outlier: 6.723A pdb=" N ALAIZ 19 " --> pdb=" O ALAIZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALAIZ 24 " --> pdb=" O ALAIZ 19 " (cutoff:3.500A) Processing sheet with id=AJ9, first strand: chain 'Id' and resid 105 through 109 removed outlier: 3.627A pdb=" N VALId 153 " --> pdb=" O TYRId 148 " (cutoff:3.500A) Processing sheet with id=AK1, first strand: chain 'JC' and resid 105 through 106 Processing sheet with id=AK2, first strand: chain 'KC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRKC 225 " --> pdb=" O THRKC 250 " (cutoff:3.500A) Processing sheet with id=AK3, first strand: chain 'KC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRKC 225 " --> pdb=" O THRKC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEJC 125 " --> pdb=" O LEUJC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUJC 119 " --> pdb=" O ILEJC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEJC 127 " --> pdb=" O LEUJC 117 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUJC 117 " --> pdb=" O ILEJC 127 " (cutoff:3.500A) removed outlier: 6.795A pdb=" N ASPJC 129 " --> pdb=" O ASNJC 115 " (cutoff:3.500A) removed outlier: 4.061A pdb=" N THRJC 116 " --> pdb=" O SERKH 328 " (cutoff:3.500A) removed outlier: 6.388A pdb=" N SERKH 328 " --> pdb=" O THRJC 116 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAKH 303 " --> pdb=" O VALKH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALKH 298 " --> pdb=" O ALAKH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALAKH 305 " --> pdb=" O LEUKH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALKH 297 " --> pdb=" O GLUKH 360 " (cutoff:3.500A) Processing sheet with id=AK4, first strand: chain 'JD' and resid 82 through 90 removed outlier: 6.436A pdb=" N ALAJD 83 " --> pdb=" O ASPJD 125 " (cutoff:3.500A) removed outlier: 4.299A pdb=" N ASPJD 125 " --> pdb=" O ALAJD 83 " (cutoff:3.500A) Processing sheet with id=AK5, first strand: chain 'JD' and resid 105 through 109 removed outlier: 5.961A pdb=" N ARGJD 105 " --> pdb=" O VALJD 154 " (cutoff:3.500A) removed outlier: 7.758A pdb=" N LEUJD 156 " --> pdb=" O ARGJD 105 " (cutoff:3.500A) removed outlier: 6.575A pdb=" N ARGJD 107 " --> pdb=" O LEUJD 156 " (cutoff:3.500A) Processing sheet with id=AK6, first strand: chain 'JK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGJK 185 " --> pdb=" O ALAJK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALAJK 113 " --> pdb=" O ARGJK 185 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N VALJd 85 " --> pdb=" O LYSJd 124 " (cutoff:3.500A) removed outlier: 5.073A pdb=" N LYSJd 124 " --> pdb=" O VALJd 85 " (cutoff:3.500A) Processing sheet with id=AK7, first strand: chain 'JX' and resid 17 through 18 Processing sheet with id=AK8, first strand: chain 'JX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALAJX 41 " --> pdb=" O ALAJX 57 " (cutoff:3.500A) removed outlier: 6.656A pdb=" N ALAJX 59 " --> pdb=" O ALAJX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAJX 56 " --> pdb=" O ALAJX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAJX 75 " --> pdb=" O ALAJX 56 " (cutoff:3.500A) removed outlier: 6.614A pdb=" N ALAJX 58 " --> pdb=" O ALAJX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAJX 77 " --> pdb=" O ALAJX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAJX 60 " --> pdb=" O ALAJX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAJX 91 " --> pdb=" O ALAJX 108 " (cutoff:3.500A) removed outlier: 4.234A pdb=" N ALAJX 110 " --> pdb=" O ALAJX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALAJX 93 " --> pdb=" O ALAJX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAJX 112 " --> pdb=" O ALAJX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAJX 95 " --> pdb=" O ALAJX 112 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAJX 109 " --> pdb=" O ALAJX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAJX 132 " --> pdb=" O ALAJX 109 " (cutoff:3.500A) removed outlier: 6.368A pdb=" N ALAJX 111 " --> pdb=" O ALAJX 132 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAJX 129 " --> pdb=" O ALAJX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALAJX 151 " --> pdb=" O ALAJX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALAJX 131 " --> pdb=" O ALAJX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAJX 164 " --> pdb=" O ALAJX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALAJX 184 " --> pdb=" O ALAJX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALAJX 166 " --> pdb=" O ALAJX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAJX 186 " --> pdb=" O ALAJX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALAJX 168 " --> pdb=" O ALAJX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAJX 188 " --> pdb=" O ALAJX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAJX 170 " --> pdb=" O ALAJX 188 " (cutoff:3.500A) Processing sheet with id=AK9, first strand: chain 'JX' and resid 46 through 48 removed outlier: 6.984A pdb=" N ALAJX 47 " --> pdb=" O ALAJX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALAJX 64 " --> pdb=" O ALAJX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AK9 Processing sheet with id=AL1, first strand: chain 'JX' and resid 99 through 102 removed outlier: 6.713A pdb=" N ALAJX 119 " --> pdb=" O ALAJX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAJX 141 " --> pdb=" O ALAJX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALAJX 177 " --> pdb=" O ALAJX 195 " (cutoff:3.500A) Processing sheet with id=AL2, first strand: chain 'JY' and resid 2 through 4 Processing sheet with id=AL3, first strand: chain 'JY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAJY 42 " --> pdb=" O ALAJY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALAJY 40 " --> pdb=" O ALAJY 36 " (cutoff:3.500A) Processing sheet with id=AL4, first strand: chain 'JZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALAJZ 18 " --> pdb=" O ALAJZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAJZ 11 " --> pdb=" O ALAJZ 16 " (cutoff:3.500A) removed outlier: 7.446A pdb=" N ALAJZ 16 " --> pdb=" O ALAJZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALAJZ 26 " --> pdb=" O ALAJZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALAJZ 19 " --> pdb=" O ALAJZ 24 " (cutoff:3.500A) removed outlier: 6.104A pdb=" N ALAJZ 24 " --> pdb=" O ALAJZ 19 " (cutoff:3.500A) Processing sheet with id=AL5, first strand: chain 'Jd' and resid 105 through 109 Processing sheet with id=AL6, first strand: chain 'KC' and resid 105 through 106 Processing sheet with id=AL7, first strand: chain 'LC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRLC 225 " --> pdb=" O THRLC 250 " (cutoff:3.500A) Processing sheet with id=AL8, first strand: chain 'LC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRLC 225 " --> pdb=" O THRLC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILEKC 125 " --> pdb=" O LEUKC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEUKC 119 " --> pdb=" O ILEKC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEKC 127 " --> pdb=" O LEUKC 117 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUKC 117 " --> pdb=" O ILEKC 127 " (cutoff:3.500A) removed outlier: 6.795A pdb=" N ASPKC 129 " --> pdb=" O ASNKC 115 " (cutoff:3.500A) removed outlier: 4.258A pdb=" N THRKC 116 " --> pdb=" O SERLH 328 " (cutoff:3.500A) removed outlier: 6.526A pdb=" N SERLH 328 " --> pdb=" O THRKC 116 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALALH 303 " --> pdb=" O VALLH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALLH 298 " --> pdb=" O ALALH 303 " (cutoff:3.500A) removed outlier: 3.976A pdb=" N ALALH 305 " --> pdb=" O LEULH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALLH 297 " --> pdb=" O GLULH 360 " (cutoff:3.500A) Processing sheet with id=AL9, first strand: chain 'KD' and resid 82 through 90 removed outlier: 6.266A pdb=" N ALAKD 83 " --> pdb=" O ASPKD 125 " (cutoff:3.500A) removed outlier: 4.222A pdb=" N ASPKD 125 " --> pdb=" O ALAKD 83 " (cutoff:3.500A) Processing sheet with id=AM1, first strand: chain 'KD' and resid 105 through 109 removed outlier: 5.848A pdb=" N ARGKD 105 " --> pdb=" O VALKD 154 " (cutoff:3.500A) removed outlier: 7.813A pdb=" N LEUKD 156 " --> pdb=" O ARGKD 105 " (cutoff:3.500A) removed outlier: 6.848A pdb=" N ARGKD 107 " --> pdb=" O LEUKD 156 " (cutoff:3.500A) removed outlier: 8.439A pdb=" N TYRKD 158 " --> pdb=" O ARGKD 107 " (cutoff:3.500A) removed outlier: 7.735A pdb=" N LEUKD 109 " --> pdb=" O TYRKD 158 " (cutoff:3.500A) Processing sheet with id=AM2, first strand: chain 'KK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGKK 185 " --> pdb=" O ALAKK 113 " (cutoff:3.500A) removed outlier: 5.624A pdb=" N ALAKK 113 " --> pdb=" O ARGKK 185 " (cutoff:3.500A) removed outlier: 6.883A pdb=" N VALKd 85 " --> pdb=" O LYSKd 124 " (cutoff:3.500A) removed outlier: 5.076A pdb=" N LYSKd 124 " --> pdb=" O VALKd 85 " (cutoff:3.500A) Processing sheet with id=AM3, first strand: chain 'KX' and resid 17 through 18 Processing sheet with id=AM4, first strand: chain 'KX' and resid 40 through 41 removed outlier: 8.193A pdb=" N ALAKX 41 " --> pdb=" O ALAKX 57 " (cutoff:3.500A) removed outlier: 6.656A pdb=" N ALAKX 59 " --> pdb=" O ALAKX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAKX 56 " --> pdb=" O ALAKX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAKX 75 " --> pdb=" O ALAKX 56 " (cutoff:3.500A) removed outlier: 6.614A pdb=" N ALAKX 58 " --> pdb=" O ALAKX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALAKX 77 " --> pdb=" O ALAKX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAKX 60 " --> pdb=" O ALAKX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAKX 91 " --> pdb=" O ALAKX 108 " (cutoff:3.500A) removed outlier: 4.233A pdb=" N ALAKX 110 " --> pdb=" O ALAKX 91 " (cutoff:3.500A) removed outlier: 3.742A pdb=" N ALAKX 93 " --> pdb=" O ALAKX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAKX 112 " --> pdb=" O ALAKX 93 " (cutoff:3.500A) removed outlier: 4.162A pdb=" N ALAKX 95 " --> pdb=" O ALAKX 112 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAKX 109 " --> pdb=" O ALAKX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAKX 132 " --> pdb=" O ALAKX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALAKX 111 " --> pdb=" O ALAKX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAKX 129 " --> pdb=" O ALAKX 149 " (cutoff:3.500A) removed outlier: 7.225A pdb=" N ALAKX 151 " --> pdb=" O ALAKX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALAKX 131 " --> pdb=" O ALAKX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAKX 164 " --> pdb=" O ALAKX 182 " (cutoff:3.500A) removed outlier: 5.482A pdb=" N ALAKX 184 " --> pdb=" O ALAKX 164 " (cutoff:3.500A) removed outlier: 4.326A pdb=" N ALAKX 166 " --> pdb=" O ALAKX 184 " (cutoff:3.500A) removed outlier: 7.196A pdb=" N ALAKX 186 " --> pdb=" O ALAKX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALAKX 168 " --> pdb=" O ALAKX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAKX 188 " --> pdb=" O ALAKX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAKX 170 " --> pdb=" O ALAKX 188 " (cutoff:3.500A) Processing sheet with id=AM5, first strand: chain 'KX' and resid 46 through 48 removed outlier: 6.984A pdb=" N ALAKX 47 " --> pdb=" O ALAKX 67 " (cutoff:3.500A) removed outlier: 6.237A pdb=" N ALAKX 64 " --> pdb=" O ALAKX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AM5 Processing sheet with id=AM6, first strand: chain 'KX' and resid 99 through 102 removed outlier: 6.713A pdb=" N ALAKX 119 " --> pdb=" O ALAKX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAKX 141 " --> pdb=" O ALAKX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALAKX 177 " --> pdb=" O ALAKX 195 " (cutoff:3.500A) Processing sheet with id=AM7, first strand: chain 'KY' and resid 2 through 4 Processing sheet with id=AM8, first strand: chain 'KY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAKY 42 " --> pdb=" O ALAKY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALAKY 40 " --> pdb=" O ALAKY 36 " (cutoff:3.500A) Processing sheet with id=AM9, first strand: chain 'KZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALAKZ 18 " --> pdb=" O ALAKZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAKZ 11 " --> pdb=" O ALAKZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALAKZ 16 " --> pdb=" O ALAKZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALAKZ 26 " --> pdb=" O ALAKZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALAKZ 19 " --> pdb=" O ALAKZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALAKZ 24 " --> pdb=" O ALAKZ 19 " (cutoff:3.500A) Processing sheet with id=AN1, first strand: chain 'Kd' and resid 105 through 109 removed outlier: 3.576A pdb=" N VALKd 153 " --> pdb=" O TYRKd 148 " (cutoff:3.500A) Processing sheet with id=AN2, first strand: chain 'LC' and resid 105 through 106 Processing sheet with id=AN3, first strand: chain 'MC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRMC 225 " --> pdb=" O THRMC 250 " (cutoff:3.500A) Processing sheet with id=AN4, first strand: chain 'MC' and resid 225 through 231 removed outlier: 6.453A pdb=" N TYRMC 225 " --> pdb=" O THRMC 250 " (cutoff:3.500A) removed outlier: 6.788A pdb=" N ILELC 125 " --> pdb=" O LEULC 119 " (cutoff:3.500A) removed outlier: 6.846A pdb=" N LEULC 119 " --> pdb=" O ILELC 125 " (cutoff:3.500A) removed outlier: 6.673A pdb=" N ILELC 127 " --> pdb=" O LEULC 117 " (cutoff:3.500A) removed outlier: 6.727A pdb=" N LEULC 117 " --> pdb=" O ILELC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPLC 129 " --> pdb=" O ASNLC 115 " (cutoff:3.500A) removed outlier: 4.767A pdb=" N ASNLC 115 " --> pdb=" O THRMH 330 " (cutoff:3.500A) removed outlier: 4.627A pdb=" N THRMH 330 " --> pdb=" O ASNLC 115 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALAMH 303 " --> pdb=" O VALMH 298 " (cutoff:3.500A) removed outlier: 5.126A pdb=" N VALMH 298 " --> pdb=" O ALAMH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALAMH 305 " --> pdb=" O LEUMH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALMH 297 " --> pdb=" O GLUMH 360 " (cutoff:3.500A) Processing sheet with id=AN5, first strand: chain 'LD' and resid 82 through 90 removed outlier: 6.832A pdb=" N ALALD 83 " --> pdb=" O ASPLD 125 " (cutoff:3.500A) removed outlier: 4.278A pdb=" N ASPLD 125 " --> pdb=" O ALALD 83 " (cutoff:3.500A) Processing sheet with id=AN6, first strand: chain 'LD' and resid 105 through 109 Processing sheet with id=AN7, first strand: chain 'LK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGLK 185 " --> pdb=" O ALALK 113 " (cutoff:3.500A) removed outlier: 5.622A pdb=" N ALALK 113 " --> pdb=" O ARGLK 185 " (cutoff:3.500A) removed outlier: 6.815A pdb=" N VALLd 85 " --> pdb=" O LYSLd 124 " (cutoff:3.500A) removed outlier: 5.095A pdb=" N LYSLd 124 " --> pdb=" O VALLd 85 " (cutoff:3.500A) Processing sheet with id=AN8, first strand: chain 'LX' and resid 17 through 18 Processing sheet with id=AN9, first strand: chain 'LX' and resid 40 through 41 removed outlier: 8.193A pdb=" N ALALX 41 " --> pdb=" O ALALX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALALX 59 " --> pdb=" O ALALX 41 " (cutoff:3.500A) removed outlier: 6.810A pdb=" N ALALX 56 " --> pdb=" O ALALX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALALX 75 " --> pdb=" O ALALX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALALX 58 " --> pdb=" O ALALX 75 " (cutoff:3.500A) removed outlier: 5.766A pdb=" N ALALX 77 " --> pdb=" O ALALX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALALX 60 " --> pdb=" O ALALX 77 " (cutoff:3.500A) removed outlier: 6.466A pdb=" N ALALX 91 " --> pdb=" O ALALX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALALX 110 " --> pdb=" O ALALX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALALX 93 " --> pdb=" O ALALX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALALX 112 " --> pdb=" O ALALX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALALX 95 " --> pdb=" O ALALX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALALX 109 " --> pdb=" O ALALX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALALX 132 " --> pdb=" O ALALX 109 " (cutoff:3.500A) removed outlier: 6.368A pdb=" N ALALX 111 " --> pdb=" O ALALX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALALX 129 " --> pdb=" O ALALX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALALX 151 " --> pdb=" O ALALX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALALX 131 " --> pdb=" O ALALX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALALX 164 " --> pdb=" O ALALX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALALX 184 " --> pdb=" O ALALX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALALX 166 " --> pdb=" O ALALX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALALX 186 " --> pdb=" O ALALX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALALX 168 " --> pdb=" O ALALX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALALX 188 " --> pdb=" O ALALX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALALX 170 " --> pdb=" O ALALX 188 " (cutoff:3.500A) Processing sheet with id=AO1, first strand: chain 'LX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALALX 47 " --> pdb=" O ALALX 67 " (cutoff:3.500A) removed outlier: 6.237A pdb=" N ALALX 64 " --> pdb=" O ALALX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AO1 Processing sheet with id=AO2, first strand: chain 'LX' and resid 99 through 102 removed outlier: 6.713A pdb=" N ALALX 119 " --> pdb=" O ALALX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALALX 141 " --> pdb=" O ALALX 159 " (cutoff:3.500A) removed outlier: 6.611A pdb=" N ALALX 177 " --> pdb=" O ALALX 195 " (cutoff:3.500A) Processing sheet with id=AO3, first strand: chain 'LY' and resid 2 through 4 Processing sheet with id=AO4, first strand: chain 'LY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALALY 42 " --> pdb=" O ALALY 34 " (cutoff:3.500A) removed outlier: 4.049A pdb=" N ALALY 40 " --> pdb=" O ALALY 36 " (cutoff:3.500A) Processing sheet with id=AO5, first strand: chain 'LZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALALZ 18 " --> pdb=" O ALALZ 9 " (cutoff:3.500A) removed outlier: 5.825A pdb=" N ALALZ 11 " --> pdb=" O ALALZ 16 " (cutoff:3.500A) removed outlier: 7.448A pdb=" N ALALZ 16 " --> pdb=" O ALALZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALALZ 26 " --> pdb=" O ALALZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALALZ 19 " --> pdb=" O ALALZ 24 " (cutoff:3.500A) removed outlier: 6.104A pdb=" N ALALZ 24 " --> pdb=" O ALALZ 19 " (cutoff:3.500A) Processing sheet with id=AO6, first strand: chain 'Ld' and resid 105 through 109 removed outlier: 6.032A pdb=" N ARGLd 105 " --> pdb=" O VALLd 154 " (cutoff:3.500A) removed outlier: 7.669A pdb=" N LEULd 156 " --> pdb=" O ARGLd 105 " (cutoff:3.500A) removed outlier: 6.478A pdb=" N ARGLd 107 " --> pdb=" O LEULd 156 " (cutoff:3.500A) removed outlier: 8.002A pdb=" N TYRLd 158 " --> pdb=" O ARGLd 107 " (cutoff:3.500A) removed outlier: 7.078A pdb=" N LEULd 109 " --> pdb=" O TYRLd 158 " (cutoff:3.500A) removed outlier: 3.663A pdb=" N VALLd 153 " --> pdb=" O TYRLd 148 " (cutoff:3.500A) Processing sheet with id=AO7, first strand: chain 'MC' and resid 105 through 106 Processing sheet with id=AO8, first strand: chain 'MD' and resid 82 through 90 removed outlier: 6.320A pdb=" N ALAMD 83 " --> pdb=" O ASPMD 125 " (cutoff:3.500A) removed outlier: 4.210A pdb=" N ASPMD 125 " --> pdb=" O ALAMD 83 " (cutoff:3.500A) Processing sheet with id=AO9, first strand: chain 'MD' and resid 105 through 109 removed outlier: 5.937A pdb=" N ARGMD 105 " --> pdb=" O VALMD 154 " (cutoff:3.500A) removed outlier: 7.743A pdb=" N LEUMD 156 " --> pdb=" O ARGMD 105 " (cutoff:3.500A) removed outlier: 6.747A pdb=" N ARGMD 107 " --> pdb=" O LEUMD 156 " (cutoff:3.500A) Processing sheet with id=AP1, first strand: chain 'MK' and resid 66 through 70 removed outlier: 4.450A pdb=" N ARGMK 185 " --> pdb=" O ALAMK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALAMK 113 " --> pdb=" O ARGMK 185 " (cutoff:3.500A) removed outlier: 7.085A pdb=" N VALMd 85 " --> pdb=" O LYSMd 124 " (cutoff:3.500A) removed outlier: 5.150A pdb=" N LYSMd 124 " --> pdb=" O VALMd 85 " (cutoff:3.500A) Processing sheet with id=AP2, first strand: chain 'MX' and resid 17 through 18 Processing sheet with id=AP3, first strand: chain 'MX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALAMX 41 " --> pdb=" O ALAMX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALAMX 59 " --> pdb=" O ALAMX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALAMX 56 " --> pdb=" O ALAMX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALAMX 75 " --> pdb=" O ALAMX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALAMX 58 " --> pdb=" O ALAMX 75 " (cutoff:3.500A) removed outlier: 5.766A pdb=" N ALAMX 77 " --> pdb=" O ALAMX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAMX 60 " --> pdb=" O ALAMX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAMX 91 " --> pdb=" O ALAMX 108 " (cutoff:3.500A) removed outlier: 4.232A pdb=" N ALAMX 110 " --> pdb=" O ALAMX 91 " (cutoff:3.500A) removed outlier: 3.740A pdb=" N ALAMX 93 " --> pdb=" O ALAMX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALAMX 112 " --> pdb=" O ALAMX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAMX 95 " --> pdb=" O ALAMX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAMX 109 " --> pdb=" O ALAMX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAMX 132 " --> pdb=" O ALAMX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALAMX 111 " --> pdb=" O ALAMX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAMX 129 " --> pdb=" O ALAMX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALAMX 151 " --> pdb=" O ALAMX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALAMX 131 " --> pdb=" O ALAMX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAMX 164 " --> pdb=" O ALAMX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALAMX 184 " --> pdb=" O ALAMX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALAMX 166 " --> pdb=" O ALAMX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAMX 186 " --> pdb=" O ALAMX 166 " (cutoff:3.500A) removed outlier: 3.936A pdb=" N ALAMX 168 " --> pdb=" O ALAMX 186 " (cutoff:3.500A) removed outlier: 7.135A pdb=" N ALAMX 188 " --> pdb=" O ALAMX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAMX 170 " --> pdb=" O ALAMX 188 " (cutoff:3.500A) Processing sheet with id=AP4, first strand: chain 'MX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALAMX 47 " --> pdb=" O ALAMX 67 " (cutoff:3.500A) removed outlier: 6.237A pdb=" N ALAMX 64 " --> pdb=" O ALAMX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AP4 Processing sheet with id=AP5, first strand: chain 'MX' and resid 99 through 102 removed outlier: 6.713A pdb=" N ALAMX 119 " --> pdb=" O ALAMX 140 " (cutoff:3.500A) removed outlier: 3.913A pdb=" N ALAMX 141 " --> pdb=" O ALAMX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALAMX 177 " --> pdb=" O ALAMX 195 " (cutoff:3.500A) Processing sheet with id=AP6, first strand: chain 'MY' and resid 2 through 4 Processing sheet with id=AP7, first strand: chain 'MY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAMY 42 " --> pdb=" O ALAMY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALAMY 40 " --> pdb=" O ALAMY 36 " (cutoff:3.500A) Processing sheet with id=AP8, first strand: chain 'MZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALAMZ 18 " --> pdb=" O ALAMZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAMZ 11 " --> pdb=" O ALAMZ 16 " (cutoff:3.500A) removed outlier: 7.448A pdb=" N ALAMZ 16 " --> pdb=" O ALAMZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALAMZ 26 " --> pdb=" O ALAMZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALAMZ 19 " --> pdb=" O ALAMZ 24 " (cutoff:3.500A) removed outlier: 6.104A pdb=" N ALAMZ 24 " --> pdb=" O ALAMZ 19 " (cutoff:3.500A) Processing sheet with id=AP9, first strand: chain 'Md' and resid 105 through 109 removed outlier: 3.572A pdb=" N VALMd 153 " --> pdb=" O TYRMd 148 " (cutoff:3.500A) Processing sheet with id=AQ1, first strand: chain 'AK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGAK 185 " --> pdb=" O ALAAK 113 " (cutoff:3.500A) removed outlier: 5.623A pdb=" N ALAAK 113 " --> pdb=" O ARGAK 185 " (cutoff:3.500A) removed outlier: 6.836A pdb=" N VALAd 85 " --> pdb=" O LYSAd 124 " (cutoff:3.500A) removed outlier: 5.063A pdb=" N LYSAd 124 " --> pdb=" O VALAd 85 " (cutoff:3.500A) Processing sheet with id=AQ2, first strand: chain 'N' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG N 228 " --> pdb=" O PHE N 168 " (cutoff:3.500A) Processing sheet with id=AQ3, first strand: chain 'O' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG O 228 " --> pdb=" O PHE O 168 " (cutoff:3.500A) Processing sheet with id=AQ4, first strand: chain 'P' and resid 115 through 119 removed outlier: 3.554A pdb=" N ARG P 228 " --> pdb=" O PHE P 168 " (cutoff:3.500A) Processing sheet with id=AQ5, first strand: chain 'Q' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG Q 228 " --> pdb=" O PHE Q 168 " (cutoff:3.500A) Processing sheet with id=AQ6, first strand: chain 'R' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG R 228 " --> pdb=" O PHE R 168 " (cutoff:3.500A) Processing sheet with id=AQ7, first strand: chain 'S' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG S 228 " --> pdb=" O PHE S 168 " (cutoff:3.500A) Processing sheet with id=AQ8, first strand: chain 'T' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG T 228 " --> pdb=" O PHE T 168 " (cutoff:3.500A) Processing sheet with id=AQ9, first strand: chain 'U' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG U 228 " --> pdb=" O PHE U 168 " (cutoff:3.500A) Processing sheet with id=AR1, first strand: chain 'V' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG V 228 " --> pdb=" O PHE V 168 " (cutoff:3.500A) Processing sheet with id=AR2, first strand: chain 'W' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG W 228 " --> pdb=" O PHE W 168 " (cutoff:3.500A) Processing sheet with id=AR3, first strand: chain 'X' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG X 228 " --> pdb=" O PHE X 168 " (cutoff:3.500A) Processing sheet with id=AR4, first strand: chain 'Y' and resid 115 through 119 removed outlier: 3.553A pdb=" N ARG Y 228 " --> pdb=" O PHE Y 168 " (cutoff:3.500A) Processing sheet with id=AR5, first strand: chain 'Z' and resid 115 through 119 removed outlier: 3.552A pdb=" N ARG Z 228 " --> pdb=" O PHE Z 168 " (cutoff:3.500A) Processing sheet with id=AR6, first strand: chain 'AX' and resid 17 through 18 Processing sheet with id=AR7, first strand: chain 'AX' and resid 40 through 41 removed outlier: 8.193A pdb=" N ALAAX 41 " --> pdb=" O ALAAX 57 " (cutoff:3.500A) removed outlier: 6.655A pdb=" N ALAAX 59 " --> pdb=" O ALAAX 41 " (cutoff:3.500A) removed outlier: 6.810A pdb=" N ALAAX 56 " --> pdb=" O ALAAX 73 " (cutoff:3.500A) removed outlier: 5.322A pdb=" N ALAAX 75 " --> pdb=" O ALAAX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALAAX 58 " --> pdb=" O ALAAX 75 " (cutoff:3.500A) removed outlier: 5.768A pdb=" N ALAAX 77 " --> pdb=" O ALAAX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALAAX 60 " --> pdb=" O ALAAX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALAAX 91 " --> pdb=" O ALAAX 108 " (cutoff:3.500A) removed outlier: 4.233A pdb=" N ALAAX 110 " --> pdb=" O ALAAX 91 " (cutoff:3.500A) removed outlier: 3.742A pdb=" N ALAAX 93 " --> pdb=" O ALAAX 110 " (cutoff:3.500A) removed outlier: 3.692A pdb=" N ALAAX 112 " --> pdb=" O ALAAX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALAAX 95 " --> pdb=" O ALAAX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALAAX 109 " --> pdb=" O ALAAX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALAAX 132 " --> pdb=" O ALAAX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALAAX 111 " --> pdb=" O ALAAX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALAAX 129 " --> pdb=" O ALAAX 149 " (cutoff:3.500A) removed outlier: 7.225A pdb=" N ALAAX 151 " --> pdb=" O ALAAX 129 " (cutoff:3.500A) removed outlier: 6.352A pdb=" N ALAAX 131 " --> pdb=" O ALAAX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALAAX 164 " --> pdb=" O ALAAX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALAAX 184 " --> pdb=" O ALAAX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALAAX 166 " --> pdb=" O ALAAX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALAAX 186 " --> pdb=" O ALAAX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALAAX 168 " --> pdb=" O ALAAX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALAAX 188 " --> pdb=" O ALAAX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALAAX 170 " --> pdb=" O ALAAX 188 " (cutoff:3.500A) Processing sheet with id=AR8, first strand: chain 'AX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALAAX 47 " --> pdb=" O ALAAX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALAAX 64 " --> pdb=" O ALAAX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AR8 Processing sheet with id=AR9, first strand: chain 'AX' and resid 99 through 102 removed outlier: 6.714A pdb=" N ALAAX 119 " --> pdb=" O ALAAX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALAAX 141 " --> pdb=" O ALAAX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALAAX 177 " --> pdb=" O ALAAX 195 " (cutoff:3.500A) Processing sheet with id=AS1, first strand: chain 'AY' and resid 2 through 4 Processing sheet with id=AS2, first strand: chain 'AY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALAAY 42 " --> pdb=" O ALAAY 34 " (cutoff:3.500A) removed outlier: 4.049A pdb=" N ALAAY 40 " --> pdb=" O ALAAY 36 " (cutoff:3.500A) Processing sheet with id=AS3, first strand: chain 'AZ' and resid 8 through 11 removed outlier: 6.833A pdb=" N ALAAZ 18 " --> pdb=" O ALAAZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALAAZ 11 " --> pdb=" O ALAAZ 16 " (cutoff:3.500A) removed outlier: 7.446A pdb=" N ALAAZ 16 " --> pdb=" O ALAAZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALAAZ 26 " --> pdb=" O ALAAZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALAAZ 19 " --> pdb=" O ALAAZ 24 " (cutoff:3.500A) removed outlier: 6.102A pdb=" N ALAAZ 24 " --> pdb=" O ALAAZ 19 " (cutoff:3.500A) Processing sheet with id=AS4, first strand: chain 'Ad' and resid 105 through 109 removed outlier: 5.957A pdb=" N ARGAd 105 " --> pdb=" O VALAd 154 " (cutoff:3.500A) removed outlier: 7.666A pdb=" N LEUAd 156 " --> pdb=" O ARGAd 105 " (cutoff:3.500A) removed outlier: 6.334A pdb=" N ARGAd 107 " --> pdb=" O LEUAd 156 " (cutoff:3.500A) removed outlier: 7.732A pdb=" N TYRAd 158 " --> pdb=" O ARGAd 107 " (cutoff:3.500A) removed outlier: 6.914A pdb=" N LEUAd 109 " --> pdb=" O TYRAd 158 " (cutoff:3.500A) removed outlier: 3.563A pdb=" N VALAd 153 " --> pdb=" O TYRAd 148 " (cutoff:3.500A) Processing sheet with id=AS5, first strand: chain 'BC' and resid 105 through 106 Processing sheet with id=AS6, first strand: chain 'CC' and resid 225 through 231 removed outlier: 6.452A pdb=" N TYRCC 225 " --> pdb=" O THRCC 250 " (cutoff:3.500A) Processing sheet with id=AS7, first strand: chain 'CC' and resid 225 through 231 removed outlier: 6.452A pdb=" N TYRCC 225 " --> pdb=" O THRCC 250 " (cutoff:3.500A) removed outlier: 6.787A pdb=" N ILEBC 125 " --> pdb=" O LEUBC 119 " (cutoff:3.500A) removed outlier: 6.845A pdb=" N LEUBC 119 " --> pdb=" O ILEBC 125 " (cutoff:3.500A) removed outlier: 6.672A pdb=" N ILEBC 127 " --> pdb=" O LEUBC 117 " (cutoff:3.500A) removed outlier: 6.728A pdb=" N LEUBC 117 " --> pdb=" O ILEBC 127 " (cutoff:3.500A) removed outlier: 6.796A pdb=" N ASPBC 129 " --> pdb=" O ASNBC 115 " (cutoff:3.500A) removed outlier: 4.731A pdb=" N ASNBC 115 " --> pdb=" O THRCH 330 " (cutoff:3.500A) removed outlier: 4.632A pdb=" N THRCH 330 " --> pdb=" O ASNBC 115 " (cutoff:3.500A) removed outlier: 6.187A pdb=" N ALACH 303 " --> pdb=" O VALCH 298 " (cutoff:3.500A) removed outlier: 5.127A pdb=" N VALCH 298 " --> pdb=" O ALACH 303 " (cutoff:3.500A) removed outlier: 3.975A pdb=" N ALACH 305 " --> pdb=" O LEUCH 296 " (cutoff:3.500A) removed outlier: 4.146A pdb=" N VALCH 297 " --> pdb=" O GLUCH 360 " (cutoff:3.500A) Processing sheet with id=AS8, first strand: chain 'BD' and resid 82 through 87 removed outlier: 5.927A pdb=" N VALBD 85 " --> pdb=" O LYSBD 124 " (cutoff:3.500A) removed outlier: 4.771A pdb=" N LYSBD 124 " --> pdb=" O VALBD 85 " (cutoff:3.500A) removed outlier: 7.060A pdb=" N TRPBD 87 " --> pdb=" O SERBD 122 " (cutoff:3.500A) removed outlier: 4.601A pdb=" N SERBD 122 " --> pdb=" O TRPBD 87 " (cutoff:3.500A) Processing sheet with id=AS9, first strand: chain 'BD' and resid 105 through 109 removed outlier: 6.022A pdb=" N ARGBD 105 " --> pdb=" O VALBD 154 " (cutoff:3.500A) removed outlier: 7.699A pdb=" N LEUBD 156 " --> pdb=" O ARGBD 105 " (cutoff:3.500A) removed outlier: 6.577A pdb=" N ARGBD 107 " --> pdb=" O LEUBD 156 " (cutoff:3.500A) Processing sheet with id=AT1, first strand: chain 'BK' and resid 66 through 70 removed outlier: 4.450A pdb=" N ARGBK 185 " --> pdb=" O ALABK 113 " (cutoff:3.500A) removed outlier: 5.624A pdb=" N ALABK 113 " --> pdb=" O ARGBK 185 " (cutoff:3.500A) removed outlier: 6.764A pdb=" N VALBd 85 " --> pdb=" O LYSBd 124 " (cutoff:3.500A) removed outlier: 5.068A pdb=" N LYSBd 124 " --> pdb=" O VALBd 85 " (cutoff:3.500A) Processing sheet with id=AT2, first strand: chain 'BX' and resid 17 through 18 Processing sheet with id=AT3, first strand: chain 'BX' and resid 40 through 41 removed outlier: 8.192A pdb=" N ALABX 41 " --> pdb=" O ALABX 57 " (cutoff:3.500A) removed outlier: 6.656A pdb=" N ALABX 59 " --> pdb=" O ALABX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALABX 56 " --> pdb=" O ALABX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALABX 75 " --> pdb=" O ALABX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALABX 58 " --> pdb=" O ALABX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALABX 77 " --> pdb=" O ALABX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALABX 60 " --> pdb=" O ALABX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALABX 91 " --> pdb=" O ALABX 108 " (cutoff:3.500A) removed outlier: 4.233A pdb=" N ALABX 110 " --> pdb=" O ALABX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALABX 93 " --> pdb=" O ALABX 110 " (cutoff:3.500A) removed outlier: 3.693A pdb=" N ALABX 112 " --> pdb=" O ALABX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALABX 95 " --> pdb=" O ALABX 112 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALABX 109 " --> pdb=" O ALABX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALABX 132 " --> pdb=" O ALABX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALABX 111 " --> pdb=" O ALABX 132 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALABX 129 " --> pdb=" O ALABX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALABX 151 " --> pdb=" O ALABX 129 " (cutoff:3.500A) removed outlier: 6.354A pdb=" N ALABX 131 " --> pdb=" O ALABX 151 " (cutoff:3.500A) removed outlier: 7.954A pdb=" N ALABX 164 " --> pdb=" O ALABX 182 " (cutoff:3.500A) removed outlier: 5.483A pdb=" N ALABX 184 " --> pdb=" O ALABX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALABX 166 " --> pdb=" O ALABX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALABX 186 " --> pdb=" O ALABX 166 " (cutoff:3.500A) removed outlier: 3.936A pdb=" N ALABX 168 " --> pdb=" O ALABX 186 " (cutoff:3.500A) removed outlier: 7.135A pdb=" N ALABX 188 " --> pdb=" O ALABX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALABX 170 " --> pdb=" O ALABX 188 " (cutoff:3.500A) Processing sheet with id=AT4, first strand: chain 'BX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALABX 47 " --> pdb=" O ALABX 67 " (cutoff:3.500A) removed outlier: 6.237A pdb=" N ALABX 64 " --> pdb=" O ALABX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AT4 Processing sheet with id=AT5, first strand: chain 'BX' and resid 99 through 102 removed outlier: 6.712A pdb=" N ALABX 119 " --> pdb=" O ALABX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALABX 141 " --> pdb=" O ALABX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALABX 177 " --> pdb=" O ALABX 195 " (cutoff:3.500A) Processing sheet with id=AT6, first strand: chain 'BY' and resid 2 through 4 Processing sheet with id=AT7, first strand: chain 'BY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALABY 42 " --> pdb=" O ALABY 34 " (cutoff:3.500A) removed outlier: 4.050A pdb=" N ALABY 40 " --> pdb=" O ALABY 36 " (cutoff:3.500A) Processing sheet with id=AT8, first strand: chain 'BZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALABZ 18 " --> pdb=" O ALABZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALABZ 11 " --> pdb=" O ALABZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALABZ 16 " --> pdb=" O ALABZ 11 " (cutoff:3.500A) removed outlier: 5.593A pdb=" N ALABZ 26 " --> pdb=" O ALABZ 17 " (cutoff:3.500A) removed outlier: 6.723A pdb=" N ALABZ 19 " --> pdb=" O ALABZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALABZ 24 " --> pdb=" O ALABZ 19 " (cutoff:3.500A) Processing sheet with id=AT9, first strand: chain 'Bd' and resid 105 through 109 Processing sheet with id=AU1, first strand: chain 'CC' and resid 105 through 106 Processing sheet with id=AU2, first strand: chain 'CD' and resid 82 through 90 removed outlier: 5.922A pdb=" N VALCD 85 " --> pdb=" O LYSCD 124 " (cutoff:3.500A) removed outlier: 5.004A pdb=" N LYSCD 124 " --> pdb=" O VALCD 85 " (cutoff:3.500A) removed outlier: 6.903A pdb=" N TRPCD 87 " --> pdb=" O SERCD 122 " (cutoff:3.500A) removed outlier: 4.881A pdb=" N SERCD 122 " --> pdb=" O TRPCD 87 " (cutoff:3.500A) removed outlier: 7.365A pdb=" N GLYCD 89 " --> pdb=" O SERCD 120 " (cutoff:3.500A) removed outlier: 5.487A pdb=" N SERCD 120 " --> pdb=" O GLYCD 89 " (cutoff:3.500A) Processing sheet with id=AU3, first strand: chain 'CD' and resid 105 through 109 Processing sheet with id=AU4, first strand: chain 'CK' and resid 66 through 70 removed outlier: 4.451A pdb=" N ARGCK 185 " --> pdb=" O ALACK 113 " (cutoff:3.500A) removed outlier: 5.624A pdb=" N ALACK 113 " --> pdb=" O ARGCK 185 " (cutoff:3.500A) removed outlier: 6.816A pdb=" N VALCd 85 " --> pdb=" O LYSCd 124 " (cutoff:3.500A) removed outlier: 5.062A pdb=" N LYSCd 124 " --> pdb=" O VALCd 85 " (cutoff:3.500A) Processing sheet with id=AU5, first strand: chain 'CX' and resid 17 through 18 Processing sheet with id=AU6, first strand: chain 'CX' and resid 40 through 41 removed outlier: 8.193A pdb=" N ALACX 41 " --> pdb=" O ALACX 57 " (cutoff:3.500A) removed outlier: 6.656A pdb=" N ALACX 59 " --> pdb=" O ALACX 41 " (cutoff:3.500A) removed outlier: 6.811A pdb=" N ALACX 56 " --> pdb=" O ALACX 73 " (cutoff:3.500A) removed outlier: 5.323A pdb=" N ALACX 75 " --> pdb=" O ALACX 56 " (cutoff:3.500A) removed outlier: 6.613A pdb=" N ALACX 58 " --> pdb=" O ALACX 75 " (cutoff:3.500A) removed outlier: 5.767A pdb=" N ALACX 77 " --> pdb=" O ALACX 58 " (cutoff:3.500A) removed outlier: 6.397A pdb=" N ALACX 60 " --> pdb=" O ALACX 77 " (cutoff:3.500A) removed outlier: 6.467A pdb=" N ALACX 91 " --> pdb=" O ALACX 108 " (cutoff:3.500A) removed outlier: 4.233A pdb=" N ALACX 110 " --> pdb=" O ALACX 91 " (cutoff:3.500A) removed outlier: 3.741A pdb=" N ALACX 93 " --> pdb=" O ALACX 110 " (cutoff:3.500A) removed outlier: 3.692A pdb=" N ALACX 112 " --> pdb=" O ALACX 93 " (cutoff:3.500A) removed outlier: 4.163A pdb=" N ALACX 95 " --> pdb=" O ALACX 112 " (cutoff:3.500A) removed outlier: 6.690A pdb=" N ALACX 109 " --> pdb=" O ALACX 130 " (cutoff:3.500A) removed outlier: 8.020A pdb=" N ALACX 132 " --> pdb=" O ALACX 109 " (cutoff:3.500A) removed outlier: 6.369A pdb=" N ALACX 111 " --> pdb=" O ALACX 132 " (cutoff:3.500A) removed outlier: 6.691A pdb=" N ALACX 129 " --> pdb=" O ALACX 149 " (cutoff:3.500A) removed outlier: 7.224A pdb=" N ALACX 151 " --> pdb=" O ALACX 129 " (cutoff:3.500A) removed outlier: 6.353A pdb=" N ALACX 131 " --> pdb=" O ALACX 151 " (cutoff:3.500A) removed outlier: 7.955A pdb=" N ALACX 164 " --> pdb=" O ALACX 182 " (cutoff:3.500A) removed outlier: 5.482A pdb=" N ALACX 184 " --> pdb=" O ALACX 164 " (cutoff:3.500A) removed outlier: 4.325A pdb=" N ALACX 166 " --> pdb=" O ALACX 184 " (cutoff:3.500A) removed outlier: 7.195A pdb=" N ALACX 186 " --> pdb=" O ALACX 166 " (cutoff:3.500A) removed outlier: 3.935A pdb=" N ALACX 168 " --> pdb=" O ALACX 186 " (cutoff:3.500A) removed outlier: 7.136A pdb=" N ALACX 188 " --> pdb=" O ALACX 168 " (cutoff:3.500A) removed outlier: 4.057A pdb=" N ALACX 170 " --> pdb=" O ALACX 188 " (cutoff:3.500A) Processing sheet with id=AU7, first strand: chain 'CX' and resid 46 through 48 removed outlier: 6.983A pdb=" N ALACX 47 " --> pdb=" O ALACX 67 " (cutoff:3.500A) removed outlier: 6.236A pdb=" N ALACX 64 " --> pdb=" O ALACX 82 " (cutoff:3.500A) No H-bonds generated for sheet with id=AU7 Processing sheet with id=AU8, first strand: chain 'CX' and resid 99 through 102 removed outlier: 6.714A pdb=" N ALACX 119 " --> pdb=" O ALACX 140 " (cutoff:3.500A) removed outlier: 3.914A pdb=" N ALACX 141 " --> pdb=" O ALACX 159 " (cutoff:3.500A) removed outlier: 6.610A pdb=" N ALACX 177 " --> pdb=" O ALACX 195 " (cutoff:3.500A) Processing sheet with id=AU9, first strand: chain 'CY' and resid 2 through 4 Processing sheet with id=AV1, first strand: chain 'CY' and resid 34 through 36 removed outlier: 3.665A pdb=" N ALACY 42 " --> pdb=" O ALACY 34 " (cutoff:3.500A) removed outlier: 4.049A pdb=" N ALACY 40 " --> pdb=" O ALACY 36 " (cutoff:3.500A) Processing sheet with id=AV2, first strand: chain 'CZ' and resid 8 through 11 removed outlier: 6.832A pdb=" N ALACZ 18 " --> pdb=" O ALACZ 9 " (cutoff:3.500A) removed outlier: 5.826A pdb=" N ALACZ 11 " --> pdb=" O ALACZ 16 " (cutoff:3.500A) removed outlier: 7.447A pdb=" N ALACZ 16 " --> pdb=" O ALACZ 11 " (cutoff:3.500A) removed outlier: 5.592A pdb=" N ALACZ 26 " --> pdb=" O ALACZ 17 " (cutoff:3.500A) removed outlier: 6.724A pdb=" N ALACZ 19 " --> pdb=" O ALACZ 24 " (cutoff:3.500A) removed outlier: 6.103A pdb=" N ALACZ 24 " --> pdb=" O ALACZ 19 " (cutoff:3.500A) Processing sheet with id=AV3, first strand: chain 'Cd' and resid 105 through 109 Processing sheet with id=AV4, first strand: chain 'DC' and resid 105 through 106 Processing sheet with id=AV5, first strand: chain 'DD' and resid 82 through 90 removed outlier: 7.035A pdb=" N ALADD 83 " --> pdb=" O ASPDD 125 " (cutoff:3.500A) removed outlier: 4.258A pdb=" N ASPDD 125 " --> pdb=" O ALADD 83 " (cutoff:3.500A) Processing sheet with id=AV6, first strand: chain 'DD' and resid 105 through 109 removed outlier: 5.986A pdb=" N ARGDD 105 " --> pdb=" O VALDD 154 " (cutoff:3.500A) removed outlier: 7.836A pdb=" N LEUDD 156 " --> pdb=" O ARGDD 105 " (cutoff:3.500A) removed outlier: 6.925A pdb=" N ARGDD 107 " --> pdb=" O LEUDD 156 " (cutoff:3.500A) removed outlier: 8.291A pdb=" N TYRDD 158 " --> pdb=" O ARGDD 107 " (cutoff:3.500A) removed outlier: 7.469A pdb=" N LEUDD 109 " --> pdb=" O TYRDD 158 " (cutoff:3.500A) 5207 hydrogen bonds defined for protein. 14616 hydrogen bond angles defined for protein. Restraints generated for nucleic acids: 0 hydrogen bonds 0 hydrogen bond angles 0 basepair planarities 0 basepair parallelities 0 stacking parallelities Total time for adding SS restraints: 60.43 Time building geometry restraints manager: 32.96 seconds NOTE: a complete listing of the restraints can be obtained by requesting output of .geo file. Histogram of bond lengths: 1.16 - 1.30: 18774 1.30 - 1.43: 27305 1.43 - 1.57: 64023 1.57 - 1.71: 152 1.71 - 1.85: 480 Bond restraints: 110734 Sorted by residual: bond pdb=" SD METAd 52 " pdb=" CE METAd 52 " ideal model delta sigma weight residual 1.791 1.561 0.230 2.50e-02 1.60e+03 8.50e+01 bond pdb=" CG1 ILEFD 135 " pdb=" CD1 ILEFD 135 " ideal model delta sigma weight residual 1.513 1.158 0.355 3.90e-02 6.57e+02 8.28e+01 bond pdb=" CZ ARGDD 97 " pdb=" NH2 ARGDD 97 " ideal model delta sigma weight residual 1.330 1.214 0.116 1.30e-02 5.92e+03 7.95e+01 bond pdb=" CE LYSAD 26 " pdb=" NZ LYSAD 26 " ideal model delta sigma weight residual 1.489 1.226 0.263 3.00e-02 1.11e+03 7.66e+01 bond pdb=" C LYSMd 111 " pdb=" N SERMd 112 " ideal model delta sigma weight residual 1.328 1.206 0.122 1.44e-02 4.82e+03 7.18e+01 ... (remaining 110729 not shown) Histogram of bond angle deviations from ideal: 53.55 - 75.86: 8 75.86 - 98.17: 81 98.17 - 120.48: 107947 120.48 - 142.78: 43049 142.78 - 165.09: 1 Bond angle restraints: 151086 Sorted by residual: angle pdb=" CD LYSMD 57 " pdb=" CE LYSMD 57 " pdb=" NZ LYSMD 57 " ideal model delta sigma weight residual 111.90 53.55 58.35 3.20e+00 9.77e-02 3.32e+02 angle pdb=" CD LYSKD 27 " pdb=" CE LYSKD 27 " pdb=" NZ LYSKD 27 " ideal model delta sigma weight residual 111.90 57.04 54.86 3.20e+00 9.77e-02 2.94e+02 angle pdb=" CD LYSHD 27 " pdb=" CE LYSHD 27 " pdb=" NZ LYSHD 27 " ideal model delta sigma weight residual 111.90 165.09 -53.19 3.20e+00 9.77e-02 2.76e+02 angle pdb=" CD LYSJD 26 " pdb=" CE LYSJD 26 " pdb=" NZ LYSJD 26 " ideal model delta sigma weight residual 111.90 61.00 50.90 3.20e+00 9.77e-02 2.53e+02 angle pdb=" CD LYSMD 27 " pdb=" CE LYSMD 27 " pdb=" NZ LYSMD 27 " ideal model delta sigma weight residual 111.90 65.96 45.94 3.20e+00 9.77e-02 2.06e+02 ... (remaining 151081 not shown) Histogram of dihedral angle deviations from ideal: 0.00 - 18.00: 60812 18.00 - 35.99: 5320 35.99 - 53.99: 1052 53.99 - 71.98: 253 71.98 - 89.98: 137 Dihedral angle restraints: 67574 sinusoidal: 21710 harmonic: 45864 Sorted by residual: dihedral pdb=" CA LYSMD 124 " pdb=" C LYSMD 124 " pdb=" N ASPMD 125 " pdb=" CA ASPMD 125 " ideal model delta harmonic sigma weight residual 180.00 134.28 45.72 0 5.00e+00 4.00e-02 8.36e+01 dihedral pdb=" CA LYSJD 124 " pdb=" C LYSJD 124 " pdb=" N ASPJD 125 " pdb=" CA ASPJD 125 " ideal model delta harmonic sigma weight residual 180.00 135.54 44.46 0 5.00e+00 4.00e-02 7.91e+01 dihedral pdb=" CA LYSID 124 " pdb=" C LYSID 124 " pdb=" N ASPID 125 " pdb=" CA ASPID 125 " ideal model delta harmonic sigma weight residual 180.00 135.74 44.26 0 5.00e+00 4.00e-02 7.84e+01 ... (remaining 67571 not shown) Histogram of chiral volume deviations from ideal: 0.000 - 0.225: 17707 0.225 - 0.450: 452 0.450 - 0.675: 24 0.675 - 0.900: 0 0.900 - 1.125: 4 Chirality restraints: 18187 Sorted by residual: chirality pdb=" CG LEUBD 79 " pdb=" CB LEUBD 79 " pdb=" CD1 LEUBD 79 " pdb=" CD2 LEUBD 79 " both_signs ideal model delta sigma weight residual False -2.59 -1.46 -1.12 2.00e-01 2.50e+01 3.16e+01 chirality pdb=" CG LEUMD 94 " pdb=" CB LEUMD 94 " pdb=" CD1 LEUMD 94 " pdb=" CD2 LEUMD 94 " both_signs ideal model delta sigma weight residual False -2.59 -1.64 -0.95 2.00e-01 2.50e+01 2.24e+01 chirality pdb=" CG LEUED 94 " pdb=" CB LEUED 94 " pdb=" CD1 LEUED 94 " pdb=" CD2 LEUED 94 " both_signs ideal model delta sigma weight residual False -2.59 -1.64 -0.95 2.00e-01 2.50e+01 2.24e+01 ... (remaining 18184 not shown) Planarity restraints: 19721 Sorted by residual: delta sigma weight rms_deltas residual plane pdb=" CG GLUKD 126 " -0.067 2.00e-02 2.50e+03 1.31e-01 1.71e+02 pdb=" CD GLUKD 126 " 0.226 2.00e-02 2.50e+03 pdb=" OE1 GLUKD 126 " -0.089 2.00e-02 2.50e+03 pdb=" OE2 GLUKD 126 " -0.070 2.00e-02 2.50e+03 delta sigma weight rms_deltas residual plane pdb=" CG GLUDD 126 " 0.054 2.00e-02 2.50e+03 1.08e-01 1.17e+02 pdb=" CD GLUDD 126 " -0.187 2.00e-02 2.50e+03 pdb=" OE1 GLUDD 126 " 0.068 2.00e-02 2.50e+03 pdb=" OE2 GLUDD 126 " 0.064 2.00e-02 2.50e+03 delta sigma weight rms_deltas residual plane pdb=" CG GLULD 126 " -0.051 2.00e-02 2.50e+03 1.03e-01 1.05e+02 pdb=" CD GLULD 126 " 0.178 2.00e-02 2.50e+03 pdb=" OE1 GLULD 126 " -0.065 2.00e-02 2.50e+03 pdb=" OE2 GLULD 126 " -0.061 2.00e-02 2.50e+03 ... (remaining 19718 not shown) Histogram of nonbonded interaction distances: 2.19 - 2.73: 9576 2.73 - 3.27: 102342 3.27 - 3.81: 189193 3.81 - 4.36: 212622 4.36 - 4.90: 364152 Nonbonded interactions: 877885 Sorted by model distance: nonbonded pdb=" OE2 GLUKD 92 " pdb=" OH TYRKD 158 " model vdw 2.185 2.440 nonbonded pdb=" O ALAHC 264 " pdb=" NH2 ARGID 97 " model vdw 2.253 2.520 nonbonded pdb=" OH TYRMD 137 " pdb=" O TYRMd 158 " model vdw 2.258 2.440 nonbonded pdb=" O TYRDd 158 " pdb=" OH TYRDD 137 " model vdw 2.268 2.440 nonbonded pdb=" OH TYRID 137 " pdb=" O TYRId 158 " model vdw 2.273 2.440 ... (remaining 877880 not shown) NOTE: a complete listing of the restraints can be obtained by requesting output of .geo file. Find NCS groups from input model Found NCS groups: ncs_group { reference = chain 'AC' selection = chain 'BC' selection = chain 'CC' selection = chain 'DC' selection = chain 'EC' selection = chain 'FC' selection = chain 'GC' selection = chain 'HC' selection = chain 'IC' selection = chain 'JC' selection = chain 'KC' selection = chain 'LC' selection = chain 'MC' } ncs_group { reference = chain 'AD' selection = (chain 'Ad' and resid 25 through 159) selection = chain 'BD' selection = (chain 'Bd' and resid 25 through 159) selection = chain 'CD' selection = (chain 'Cd' and resid 25 through 159) selection = chain 'DD' selection = (chain 'Dd' and resid 25 through 159) selection = chain 'ED' selection = (chain 'Ed' and resid 25 through 159) selection = chain 'FD' selection = (chain 'Fd' and resid 25 through 159) selection = chain 'GD' selection = (chain 'Gd' and resid 25 through 159) selection = chain 'HD' selection = (chain 'Hd' and resid 25 through 159) selection = chain 'ID' selection = (chain 'Id' and resid 25 through 159) selection = chain 'JD' selection = (chain 'Jd' and resid 25 through 159) selection = chain 'KD' selection = (chain 'Kd' and resid 25 through 159) selection = chain 'LD' selection = (chain 'Ld' and resid 25 through 159) selection = chain 'MD' selection = (chain 'Md' and resid 25 through 159) } ncs_group { reference = chain 'AH' selection = chain 'BH' selection = chain 'CH' selection = chain 'DH' selection = chain 'EH' selection = chain 'FH' selection = chain 'GH' selection = chain 'HH' selection = chain 'IH' selection = chain 'JH' selection = chain 'KH' selection = chain 'LH' selection = chain 'MH' } ncs_group { reference = chain 'AK' selection = chain 'BK' selection = chain 'CK' selection = chain 'DK' selection = chain 'EK' selection = chain 'FK' selection = chain 'GK' selection = chain 'HK' selection = chain 'IK' selection = chain 'JK' selection = chain 'KK' selection = chain 'LK' selection = chain 'MK' } ncs_group { reference = chain 'AX' selection = chain 'BX' selection = chain 'CX' selection = chain 'DX' selection = chain 'EX' selection = chain 'FX' selection = chain 'GX' selection = chain 'HX' selection = chain 'IX' selection = chain 'JX' selection = chain 'KX' selection = chain 'LX' selection = chain 'MX' } ncs_group { reference = chain 'AY' selection = chain 'BY' selection = chain 'CY' selection = chain 'DY' selection = chain 'EY' selection = chain 'FY' selection = chain 'GY' selection = chain 'HY' selection = chain 'IY' selection = chain 'JY' selection = chain 'KY' selection = chain 'LY' selection = chain 'MY' } ncs_group { reference = chain 'AZ' selection = chain 'BZ' selection = chain 'CZ' selection = chain 'DZ' selection = chain 'EZ' selection = chain 'FZ' selection = chain 'GZ' selection = chain 'HZ' selection = chain 'IZ' selection = chain 'JZ' selection = chain 'KZ' selection = chain 'LZ' selection = chain 'MZ' } ncs_group { reference = chain 'N' selection = chain 'O' selection = chain 'P' selection = chain 'Q' selection = chain 'R' selection = chain 'S' selection = chain 'T' selection = chain 'U' selection = chain 'V' selection = chain 'W' selection = chain 'X' selection = chain 'Y' selection = chain 'Z' } Set up NCS constraints No NCS constraints will be used in refinement. Set refine NCS operators Adjust number of macro_cycles Number of macro_cycles: 10 Reset NCS operators Extract rigid body selections Check and reset occupancies Occupancies: min=1.00 max=1.00 mean=1.00 Load rotamer database and sin/cos tables Set ADP refinement strategy ADPs will be refined as group one per residue Make a string to write initial .geo file Internal consistency checks Time: Set random seed: 0.000 Set model cs if undefined: 0.000 Decide on map wrapping: 0.000 Normalize map: mean=0, sd=1: 4.940 Set stop_for_unknowns flag: 0.000 Assert model is a single copy model: 0.000 Assert all atoms have isotropic ADPs: 0.000 Construct map_model_manager: 0.060 Extract box with map and model: 29.710 Check model and map are aligned: 1.140 Set scattering table: 0.710 Process input model: 231.240 Find NCS groups from input model: 6.560 Set up NCS constraints: 2.090 Set refine NCS operators: 0.000 Adjust number of macro_cycles: 0.000 Reset NCS operators: 0.000 Extract rigid body selections: 0.000 Check and reset occupancies: 0.020 Load rotamer database and sin/cos tables:2.660 Set ADP refinement strategy: 0.000 Make a string to write initial .geo file:0.000 Internal consistency checks: 0.000 Total: 279.130 ------------------------------------------------------------------------------- Set refinement monitor ********************** ------------------------------------------------------------------------------- Setup refinement engine *********************** ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.6389 moved from start: 0.0000 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.014 0.355 110734 Z= 0.966 Angle : 1.870 58.350 151086 Z= 1.014 Chirality : 0.089 1.125 18187 Planarity : 0.011 0.142 19721 Dihedral : 15.632 89.977 37518 Min Nonbonded Distance : 2.185 Molprobity Statistics. All-atom Clashscore : 6.98 Ramachandran Plot: Outliers : 0.00 % Allowed : 8.47 % Favored : 91.53 % Rotamer: Outliers : 4.90 % Allowed : 3.72 % Favored : 91.37 % Cbeta Deviations : 0.30 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.54 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -3.87 (0.05), residues: 15288 helix: -2.75 (0.06), residues: 4004 sheet: -1.23 (0.08), residues: 3796 loop : -3.22 (0.05), residues: 7488 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.092 0.006 TRPBK 145 HIS 0.040 0.005 HISAC 103 PHE 0.113 0.007 PHELK 84 TYR 0.119 0.009 TYRIH 338 ARG 0.112 0.004 ARGGD 133 *********************** REFINEMENT MACRO_CYCLE 1 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 5307 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 461 poor density : 4846 time to evaluate : 7.993 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 461 outliers final: 86 residues processed: 4955 average time/residue: 0.9593 time to fit residues: 8084.3826 Evaluate side-chains 3123 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 86 poor density : 3037 time to evaluate : 7.890 Switching outliers to nearest non-outliers outliers start: 86 outliers final: 0 residues processed: 86 average time/residue: 0.8179 time to fit residues: 139.4663 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=5.00 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 1262 optimal weight: 3.9990 chunk 1133 optimal weight: 0.5980 chunk 628 optimal weight: 3.9990 chunk 387 optimal weight: 8.9990 chunk 764 optimal weight: 0.9990 chunk 605 optimal weight: 5.9990 chunk 1171 optimal weight: 0.0980 chunk 453 optimal weight: 1.9990 chunk 712 optimal weight: 2.9990 chunk 872 optimal weight: 1.9990 chunk 1357 optimal weight: 0.9980 overall best weight: 0.9384 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AC 89 ASN AC 97 ASN ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** AC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** AC 123 GLN ** AC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AC 139 HIS AC 241 HIS ** Dd 69 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Dd 75 ASN ** EC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 139 HIS ED 32 ASN ED 80 GLN EH 341 GLN EK 108 GLN ** EK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ed 75 ASN FC 89 ASN FC 97 ASN ** FC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 198 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** FK 108 GLN ** FK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Fd 31 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Fd 75 ASN Fd 80 GLN Fd 138 GLN ** GC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GD 80 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Gd 75 ASN ** HC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** HC 104 ASN ** HC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Hd 31 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 86 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** IK 108 GLN ** IK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Id 75 ASN ** JC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 82 GLN ** JC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** JC 104 ASN JC 118 ASN ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 139 HIS JD 138 GLN JD 146 HIS JH 351 HIS AH 278 ASN Jd 75 ASN ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 118 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Kd 75 ASN ** LC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 89 ASN LC 97 ASN ** LC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** LC 118 ASN ** LC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 241 HIS LH 336 HIS ** LK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ld 75 ASN ** MC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 75 ASN AK 147 GLN ** N 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** N 156 ASN N 160 GLN ** N 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** O 156 ASN O 160 GLN O 196 ASN ** P 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** P 183 GLN Q 112 GLN ** Q 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 156 ASN Q 160 GLN Q 177 HIS Q 196 ASN Q 225 GLN ** R 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** R 149 ASN R 160 GLN R 196 ASN R 217 ASN R 226 ASN ** S 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** S 149 ASN ** S 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** S 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 221 HIS ** S 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** T 112 GLN ** T 156 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** T 160 GLN T 183 GLN ** T 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** U 149 ASN U 156 ASN U 160 GLN U 183 GLN ** U 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** V 196 ASN ** W 156 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** W 196 ASN X 183 GLN X 196 ASN ** Y 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Y 149 ASN Y 156 ASN Y 196 ASN Z 156 ASN Z 183 GLN ** Z 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Z 232 GLN Ad 69 ASN BC 97 ASN ** BC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BH 341 GLN ** BK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** CC 86 GLN CC 97 ASN ** CC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** CC 139 HIS ** CK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 75 ASN ** DC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DC 104 ASN ** DC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DC 139 HIS ** DD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Total number of N/Q/H flips: 85 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.7005 moved from start: 0.4369 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.071 110734 Z= 0.300 Angle : 0.831 10.895 151086 Z= 0.444 Chirality : 0.049 0.255 18187 Planarity : 0.006 0.079 19721 Dihedral : 6.661 30.966 16471 Min Nonbonded Distance : 2.005 Molprobity Statistics. All-atom Clashscore : 19.52 Ramachandran Plot: Outliers : 0.01 % Allowed : 7.23 % Favored : 92.77 % Rotamer: Outliers : 4.63 % Allowed : 19.42 % Favored : 75.95 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.01 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -2.87 (0.06), residues: 15288 helix: -0.75 (0.07), residues: 3887 sheet: -1.10 (0.08), residues: 3432 loop : -2.97 (0.05), residues: 7969 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.037 0.003 TRPHK 145 HIS 0.013 0.002 HISEH 351 PHE 0.024 0.003 PHE Y 133 TYR 0.048 0.003 TYREC 212 ARG 0.015 0.001 ARGCD 97 *********************** REFINEMENT MACRO_CYCLE 2 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 4081 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 435 poor density : 3646 time to evaluate : 7.973 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 435 outliers final: 197 residues processed: 3842 average time/residue: 0.9558 time to fit residues: 6360.4362 Evaluate side-chains 3234 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 197 poor density : 3037 time to evaluate : 7.904 Switching outliers to nearest non-outliers revert: symmetry clash outliers start: 197 outliers final: 1 residues processed: 197 average time/residue: 0.7734 time to fit residues: 299.2385 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=4.50 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 754 optimal weight: 0.8980 chunk 421 optimal weight: 0.7980 chunk 1129 optimal weight: 0.9990 chunk 924 optimal weight: 0.6980 chunk 374 optimal weight: 9.9990 chunk 1360 optimal weight: 7.9990 chunk 1469 optimal weight: 3.9990 chunk 1211 optimal weight: 40.0000 chunk 1348 optimal weight: 0.5980 chunk 463 optimal weight: 50.0000 chunk 1091 optimal weight: 0.6980 overall best weight: 0.7380 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AC 89 ASN ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** AC 104 ASN AC 149 GLN AC 198 ASN ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Dd 69 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 89 ASN EC 97 ASN ** EC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EH 341 GLN EH 351 HIS EK 61 ASN ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ed 75 ASN FC 89 ASN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** FK 61 ASN ** FK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GC 123 GLN GC 137 GLN GC 139 HIS GC 198 ASN GD 80 GLN GH 278 ASN GH 351 HIS ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** HC 137 GLN HC 139 HIS ** HH 356 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HK 61 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Hd 31 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** IC 139 HIS ID 32 ASN IK 61 ASN Id 75 ASN JC 82 GLN ** JC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JD 146 HIS ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JK 147 GLN ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 118 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Kd 75 ASN ** LC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 82 GLN ** LC 97 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 123 GLN ** LC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LD 146 HIS ** LK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Ld 31 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MD 152 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 75 ASN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** N 110 GLN N 112 GLN N 225 GLN O 115 GLN ** O 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** P 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 196 ASN R 115 GLN ** R 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 185 GLN T 156 ASN T 160 GLN T 183 GLN ** T 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** T 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** U 150 ASN U 160 GLN U 177 HIS U 196 ASN V 112 GLN ** V 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** W 156 ASN W 185 GLN X 112 GLN X 183 GLN Z 196 ASN Z 225 GLN Ad 75 ASN BC 82 GLN BC 89 ASN ** BC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** BC 104 ASN ** BC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 149 GLN BH 351 HIS ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BK 147 GLN Bd 75 ASN ** CC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** CC 86 GLN ** CC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** CK 92 ASN ** CK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 75 ASN Cd 138 GLN ** DC 69 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DD 138 GLN Total number of N/Q/H flips: 67 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.7268 moved from start: 0.5524 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.086 110734 Z= 0.245 Angle : 0.756 14.214 151086 Z= 0.402 Chirality : 0.048 0.326 18187 Planarity : 0.005 0.062 19721 Dihedral : 5.990 27.839 16471 Min Nonbonded Distance : 2.049 Molprobity Statistics. All-atom Clashscore : 17.18 Ramachandran Plot: Outliers : 0.00 % Allowed : 6.58 % Favored : 93.42 % Rotamer: Outliers : 4.33 % Allowed : 23.29 % Favored : 72.38 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.00 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -2.32 (0.06), residues: 15288 helix: 0.08 (0.08), residues: 3952 sheet: -0.99 (0.09), residues: 3393 loop : -2.74 (0.05), residues: 7943 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.040 0.002 TRP S 233 HIS 0.011 0.001 HISED 146 PHE 0.031 0.002 PHE T 168 TYR 0.040 0.002 TYRDC 212 ARG 0.014 0.001 ARGLd 82 *********************** REFINEMENT MACRO_CYCLE 3 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3998 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 407 poor density : 3591 time to evaluate : 7.967 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 407 outliers final: 188 residues processed: 3774 average time/residue: 0.9388 time to fit residues: 6117.4748 Evaluate side-chains 3319 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 188 poor density : 3131 time to evaluate : 8.318 Switching outliers to nearest non-outliers revert: symmetry clash outliers start: 188 outliers final: 1 residues processed: 188 average time/residue: 0.8400 time to fit residues: 305.3087 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=4.00 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 1343 optimal weight: 10.0000 chunk 1022 optimal weight: 0.7980 chunk 705 optimal weight: 9.9990 chunk 150 optimal weight: 40.0000 chunk 649 optimal weight: 1.9990 chunk 913 optimal weight: 4.9990 chunk 1364 optimal weight: 0.5980 chunk 1445 optimal weight: 0.0570 chunk 713 optimal weight: 6.9990 chunk 1293 optimal weight: 4.9990 chunk 389 optimal weight: 9.9990 overall best weight: 1.6902 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 86 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** AC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DK 108 GLN ** DK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Dd 69 ASN Dd 75 ASN ** Dd 146 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 82 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ed 75 ASN FC 97 ASN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** FC 241 HIS ** FK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Fd 31 ASN Fd 146 HIS GC 86 GLN GC 97 ASN ** GC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** GC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** GC 198 ASN GC 241 HIS GK 61 ASN ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Gd 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** HC 89 ASN ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** HC 241 HIS HK 61 ASN HK 100 ASN HK 147 GLN HK 157 GLN Hd 75 ASN ** IC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** IC 241 HIS IH 336 HIS ** IK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Id 75 ASN JC 103 HIS JC 118 ASN ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JK 61 ASN ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KC 241 HIS KK 61 ASN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KK 100 ASN Kd 75 ASN ** LC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LK 61 ASN LK 108 GLN LK 147 GLN Ld 31 ASN Ld 146 HIS ** MC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** MD 32 ASN MH 341 GLN MK 61 ASN Md 138 GLN AK 61 ASN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** N 185 GLN ** N 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** N 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** N 232 GLN ** O 112 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** O 115 GLN ** O 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** P 185 GLN ** Q 112 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 160 GLN ** Q 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 225 GLN R 112 GLN ** R 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** R 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** S 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** S 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** S 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** T 112 GLN T 160 GLN U 112 GLN U 160 GLN U 185 GLN ** V 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** W 112 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** W 196 ASN X 150 ASN ** X 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Y 112 GLN Y 150 ASN Y 196 ASN Z 112 GLN ** Z 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Z 150 ASN Ad 75 ASN BC 86 GLN BC 89 ASN ** BC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** BC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 241 HIS BK 61 ASN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Bd 75 ASN Bd 146 HIS ** CC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** CC 149 GLN CC 241 HIS CK 61 ASN ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** CK 108 GLN Cd 75 ASN Cd 138 GLN Cd 146 HIS ** DC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DC 149 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DC 241 HIS Total number of N/Q/H flips: 76 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.7830 moved from start: 0.7928 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.005 0.141 110734 Z= 0.369 Angle : 0.837 13.874 151086 Z= 0.447 Chirality : 0.051 0.325 18187 Planarity : 0.006 0.061 19721 Dihedral : 5.953 30.799 16471 Min Nonbonded Distance : 1.958 Molprobity Statistics. All-atom Clashscore : 19.25 Ramachandran Plot: Outliers : 0.00 % Allowed : 7.91 % Favored : 92.09 % Rotamer: Outliers : 5.84 % Allowed : 24.31 % Favored : 69.85 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.01 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -2.20 (0.06), residues: 15288 helix: 0.17 (0.08), residues: 3939 sheet: -1.10 (0.09), residues: 3315 loop : -2.55 (0.06), residues: 8034 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.055 0.003 TRPFC 147 HIS 0.012 0.002 HISHD 146 PHE 0.044 0.003 PHEID 104 TYR 0.049 0.003 TYR O 132 ARG 0.014 0.001 ARGJd 82 *********************** REFINEMENT MACRO_CYCLE 4 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 4370 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 549 poor density : 3821 time to evaluate : 8.091 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 549 outliers final: 250 residues processed: 4086 average time/residue: 0.9564 time to fit residues: 6757.1553 Evaluate side-chains 3483 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 250 poor density : 3233 time to evaluate : 8.023 Switching outliers to nearest non-outliers outliers start: 250 outliers final: 0 residues processed: 250 average time/residue: 0.7747 time to fit residues: 379.2454 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=3.50 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 1203 optimal weight: 0.7980 chunk 820 optimal weight: 0.6980 chunk 20 optimal weight: 0.1980 chunk 1075 optimal weight: 5.9990 chunk 596 optimal weight: 6.9990 chunk 1233 optimal weight: 30.0000 chunk 998 optimal weight: 30.0000 chunk 1 optimal weight: 1.9990 chunk 737 optimal weight: 5.9990 chunk 1297 optimal weight: 1.9990 chunk 364 optimal weight: 50.0000 overall best weight: 1.1384 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: AC 89 ASN ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** AC 104 ASN AC 123 GLN ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Dd 75 ASN Dd 146 HIS EC 104 ASN ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN ED 146 HIS EH 341 GLN ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EK 108 GLN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** FC 104 ASN ** FC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** FD 69 ASN ** FK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** GC 104 ASN ** GC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Gd 75 ASN ** Gd 80 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** HD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** HH 278 ASN HH 351 HIS HK 100 ASN HK 147 GLN Hd 138 GLN IC 104 ASN IH 351 HIS IK 100 ASN Id 75 ASN ** Id 80 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JD 80 GLN JD 146 HIS ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 89 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** KC 97 ASN ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 118 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KC 149 GLN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 82 GLN LC 104 ASN ** LC 149 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LH 283 HIS ** LH 351 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ld 138 GLN MC 104 ASN ** MC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** MC 149 GLN MD 32 ASN MD 75 ASN ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 138 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** N 196 ASN ** O 112 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** P 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** P 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 112 GLN Q 160 GLN ** Q 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** R 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** R 160 GLN R 196 ASN ** R 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 225 GLN T 160 GLN U 160 GLN U 221 HIS V 112 GLN W 225 GLN ** X 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** X 177 HIS X 196 ASN ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** X 225 GLN ** X 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** X 232 GLN Y 150 ASN Y 196 ASN Z 150 ASN ** Z 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Z 225 GLN Ad 75 ASN ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BD 69 ASN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Bd 80 GLN CC 104 ASN ** CC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** CD 152 GLN ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 138 GLN ** DC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DC 149 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DC 192 ASN DD 138 GLN Total number of N/Q/H flips: 64 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.7887 moved from start: 0.8602 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.086 110734 Z= 0.275 Angle : 0.746 13.410 151086 Z= 0.394 Chirality : 0.047 0.379 18187 Planarity : 0.005 0.094 19721 Dihedral : 5.607 31.088 16471 Min Nonbonded Distance : 1.992 Molprobity Statistics. All-atom Clashscore : 19.30 Ramachandran Plot: Outliers : 0.00 % Allowed : 6.31 % Favored : 93.69 % Rotamer: Outliers : 3.69 % Allowed : 28.44 % Favored : 67.87 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.01 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.87 (0.06), residues: 15288 helix: 0.52 (0.08), residues: 3939 sheet: -0.89 (0.09), residues: 3419 loop : -2.41 (0.06), residues: 7930 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.036 0.002 TRPID 87 HIS 0.008 0.001 HISJC 103 PHE 0.032 0.002 PHE T 168 TYR 0.034 0.002 TYR T 145 ARG 0.011 0.001 ARGEH 294 *********************** REFINEMENT MACRO_CYCLE 5 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3959 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 347 poor density : 3612 time to evaluate : 10.110 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 347 outliers final: 183 residues processed: 3773 average time/residue: 0.9865 time to fit residues: 6448.9859 Evaluate side-chains 3366 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 183 poor density : 3183 time to evaluate : 8.086 Switching outliers to nearest non-outliers outliers start: 183 outliers final: 0 residues processed: 183 average time/residue: 0.8094 time to fit residues: 290.0772 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=3.00 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 486 optimal weight: 30.0000 chunk 1301 optimal weight: 0.9980 chunk 285 optimal weight: 2.9990 chunk 848 optimal weight: 20.0000 chunk 356 optimal weight: 1.9990 chunk 1446 optimal weight: 10.0000 chunk 1200 optimal weight: 0.9980 chunk 669 optimal weight: 20.0000 chunk 120 optimal weight: 1.9990 chunk 478 optimal weight: 9.9990 chunk 759 optimal weight: 0.2980 overall best weight: 1.2584 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** AC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** DH 341 GLN DK 61 ASN ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Dd 138 GLN EC 89 ASN ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EK 108 GLN FC 97 ASN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** FD 31 ASN FK 108 GLN ** FK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GC 103 HIS GC 137 GLN GC 149 GLN ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** HC 149 GLN HD 138 GLN ** HH 278 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** IC 69 GLN IK 100 ASN ** IK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Id 75 ASN Id 80 GLN JC 104 ASN ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JD 146 HIS JH 356 GLN ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Jd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** KC 104 ASN KH 341 GLN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 82 GLN LC 86 GLN ** LC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LH 351 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** MC 86 GLN MC 137 GLN MH 341 GLN ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 138 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AK 100 ASN AK 147 GLN N 185 GLN N 225 GLN ** O 112 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** O 196 ASN ** O 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** P 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** P 149 ASN ** P 171 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** P 196 ASN P 225 GLN ** P 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 196 ASN Q 225 GLN R 185 GLN ** R 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 177 HIS S 196 ASN S 225 GLN S 232 GLN T 160 GLN T 232 GLN U 196 ASN V 112 GLN W 149 ASN W 221 HIS X 150 ASN X 217 ASN X 221 HIS X 225 GLN X 226 ASN Y 150 ASN ** Z 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 149 GLN BD 69 ASN BD 138 GLN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DC 149 GLN Total number of N/Q/H flips: 61 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.7978 moved from start: 0.9325 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.111 110734 Z= 0.291 Angle : 0.755 14.118 151086 Z= 0.397 Chirality : 0.047 0.343 18187 Planarity : 0.005 0.098 19721 Dihedral : 5.484 28.921 16471 Min Nonbonded Distance : 2.019 Molprobity Statistics. All-atom Clashscore : 18.50 Ramachandran Plot: Outliers : 0.01 % Allowed : 7.08 % Favored : 92.92 % Rotamer: Outliers : 3.37 % Allowed : 29.63 % Favored : 67.00 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.00 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.78 (0.06), residues: 15288 helix: 0.72 (0.08), residues: 3913 sheet: -0.94 (0.09), residues: 3354 loop : -2.35 (0.06), residues: 8021 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.038 0.002 TRPHD 87 HIS 0.007 0.001 HIS X 221 PHE 0.027 0.002 PHE Y 135 TYR 0.034 0.002 TYR T 145 ARG 0.022 0.001 ARGBK 136 *********************** REFINEMENT MACRO_CYCLE 6 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3834 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 317 poor density : 3517 time to evaluate : 8.110 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 317 outliers final: 171 residues processed: 3652 average time/residue: 0.9902 time to fit residues: 6262.7962 Evaluate side-chains 3350 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 171 poor density : 3179 time to evaluate : 8.101 Switching outliers to nearest non-outliers revert: symmetry clash revert: symmetry clash outliers start: 171 outliers final: 2 residues processed: 171 average time/residue: 0.7959 time to fit residues: 267.0304 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=2.50 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 1394 optimal weight: 3.9990 chunk 163 optimal weight: 20.0000 chunk 824 optimal weight: 10.9990 chunk 1056 optimal weight: 0.7980 chunk 818 optimal weight: 3.9990 chunk 1217 optimal weight: 50.0000 chunk 807 optimal weight: 9.9990 chunk 1440 optimal weight: 0.2980 chunk 901 optimal weight: 30.0000 chunk 878 optimal weight: 3.9990 chunk 665 optimal weight: 5.9990 overall best weight: 2.6186 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** AC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** AC 149 GLN DH 341 GLN DH 351 HIS ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** DK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Dd 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Dd 152 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 241 HIS ED 32 ASN EH 341 GLN ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EK 108 GLN FC 69 GLN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** FD 32 ASN FK 61 ASN ** FK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GK 108 GLN ** AD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Gd 75 ASN ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** HD 138 GLN HH 278 ASN HH 341 GLN ** HK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Hd 32 ASN Hd 138 GLN IC 137 GLN ID 152 GLN ** IK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** IK 100 ASN IK 108 GLN ** IK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JD 146 HIS ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AH 356 GLN Jd 152 GLN ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KK 108 GLN Kd 146 HIS ** LC 86 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LD 69 ASN LH 341 GLN ** LK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ld 138 GLN MC 86 GLN MC 137 GLN MC 149 GLN MC 241 HIS MH 341 GLN ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 152 GLN AK 61 ASN AK 72 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 112 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** O 221 HIS ** O 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** P 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** P 185 GLN P 196 ASN ** P 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** P 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** R 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 232 GLN T 196 ASN U 225 GLN W 112 GLN W 149 ASN W 196 ASN X 196 ASN ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** X 225 GLN Y 150 ASN Z 112 GLN Ad 146 HIS ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 149 GLN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 75 ASN Cd 80 GLN Cd 138 GLN ** DC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DC 149 GLN DC 219 ASN Total number of N/Q/H flips: 58 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.8142 moved from start: 1.0452 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.007 0.115 110734 Z= 0.454 Angle : 0.856 12.259 151086 Z= 0.453 Chirality : 0.050 0.397 18187 Planarity : 0.006 0.128 19721 Dihedral : 5.890 31.386 16471 Min Nonbonded Distance : 1.923 Molprobity Statistics. All-atom Clashscore : 21.19 Ramachandran Plot: Outliers : 0.01 % Allowed : 7.34 % Favored : 92.65 % Rotamer: Outliers : 3.36 % Allowed : 30.99 % Favored : 65.65 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.03 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.88 (0.06), residues: 15288 helix: 0.49 (0.08), residues: 3926 sheet: -0.95 (0.09), residues: 3289 loop : -2.36 (0.06), residues: 8073 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.041 0.003 TRPAK 145 HIS 0.011 0.002 HISKd 146 PHE 0.037 0.003 PHEMD 104 TYR 0.037 0.003 TYRIK 143 ARG 0.014 0.001 ARG Y 228 *********************** REFINEMENT MACRO_CYCLE 7 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3622 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 316 poor density : 3306 time to evaluate : 10.007 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 316 outliers final: 181 residues processed: 3455 average time/residue: 0.9972 time to fit residues: 5936.9226 Evaluate side-chains 3124 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 181 poor density : 2943 time to evaluate : 8.106 Switching outliers to nearest non-outliers outliers start: 181 outliers final: 0 residues processed: 181 average time/residue: 0.8027 time to fit residues: 285.5348 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=2.00 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 891 optimal weight: 20.0000 chunk 575 optimal weight: 20.0000 chunk 860 optimal weight: 0.9980 chunk 434 optimal weight: 0.6980 chunk 283 optimal weight: 0.8980 chunk 279 optimal weight: 0.0670 chunk 916 optimal weight: 0.8980 chunk 981 optimal weight: 50.0000 chunk 712 optimal weight: 1.9990 chunk 134 optimal weight: 2.9990 chunk 1132 optimal weight: 3.9990 overall best weight: 0.7118 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** AC 149 GLN DH 341 GLN ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Dd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Dd 138 GLN EC 86 GLN EC 89 ASN ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Fd 75 ASN GD 152 GLN ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GK 108 GLN AD 138 GLN ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** HD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** HK 108 GLN ** Hd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** IC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** IK 61 ASN ** IK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** IK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JD 146 HIS ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Jd 75 ASN ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** KD 80 GLN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Kd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 149 GLN LH 341 GLN ** LK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** MC 86 GLN MD 32 ASN MD 69 ASN ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** MK 147 GLN Md 138 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** N 150 ASN N 185 GLN ** O 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** O 196 ASN ** O 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 196 ASN R 177 HIS R 185 GLN ** R 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** R 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 185 GLN U 221 HIS V 150 ASN W 149 ASN W 196 ASN ** X 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Z 110 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Z 183 GLN ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 149 GLN BD 31 ASN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Bd 75 ASN Bd 138 GLN ** CC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 75 ASN DC 82 GLN DC 137 GLN DC 149 GLN DC 241 HIS Total number of N/Q/H flips: 44 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.8074 moved from start: 1.0597 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.084 110734 Z= 0.255 Angle : 0.776 13.379 151086 Z= 0.408 Chirality : 0.048 0.330 18187 Planarity : 0.005 0.080 19721 Dihedral : 5.561 29.162 16471 Min Nonbonded Distance : 2.024 Molprobity Statistics. All-atom Clashscore : 19.85 Ramachandran Plot: Outliers : 0.01 % Allowed : 6.36 % Favored : 93.63 % Rotamer: Outliers : 1.69 % Allowed : 32.74 % Favored : 65.57 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.00 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.79 (0.06), residues: 15288 helix: 0.60 (0.08), residues: 3939 sheet: -1.00 (0.09), residues: 3328 loop : -2.27 (0.06), residues: 8021 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.046 0.002 TRPHD 87 HIS 0.007 0.001 HISFC 103 PHE 0.044 0.002 PHEID 104 TYR 0.033 0.002 TYRMC 94 ARG 0.015 0.001 ARG Y 228 *********************** REFINEMENT MACRO_CYCLE 8 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3510 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 159 poor density : 3351 time to evaluate : 8.000 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 159 outliers final: 74 residues processed: 3410 average time/residue: 0.9598 time to fit residues: 5624.6623 Evaluate side-chains 3153 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 74 poor density : 3079 time to evaluate : 8.065 Switching outliers to nearest non-outliers outliers start: 74 outliers final: 0 residues processed: 74 average time/residue: 0.8189 time to fit residues: 122.5361 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=1.50 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 1310 optimal weight: 0.8980 chunk 1380 optimal weight: 0.0670 chunk 1259 optimal weight: 1.9990 chunk 1342 optimal weight: 3.9990 chunk 808 optimal weight: 5.9990 chunk 584 optimal weight: 7.9990 chunk 1054 optimal weight: 3.9990 chunk 412 optimal weight: 1.9990 chunk 1213 optimal weight: 20.0000 chunk 1269 optimal weight: 0.9980 chunk 1338 optimal weight: 9.9990 overall best weight: 1.1922 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** AC 149 GLN DH 341 GLN DK 61 ASN ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** DK 108 GLN ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN EC 190 GLN EH 283 HIS ** EK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** FC 89 ASN FC 97 ASN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Fd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** GC 86 GLN ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GK 108 GLN AD 138 GLN Gd 75 ASN ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** HD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Hd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Hd 80 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Hd 138 GLN ** IC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** IC 137 GLN IK 61 ASN ** IK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 86 GLN ** JC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** KC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** KD 80 GLN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KK 108 GLN ** LC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 219 ASN LH 341 GLN ** LK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LK 100 ASN LK 157 GLN MC 86 GLN MC 149 GLN MD 32 ASN MH 341 GLN ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 152 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AK 147 GLN N 150 ASN ** O 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 226 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 196 ASN ** R 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** R 217 ASN S 232 GLN T 115 GLN ** U 225 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** V 212 ASN ** X 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Y 196 ASN Y 226 ASN Z 196 ASN ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 149 GLN BD 31 ASN ** BD 69 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** BH 341 GLN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** BK 147 GLN ** Bd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Bd 138 GLN ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 32 ASN Cd 138 GLN DC 69 GLN DC 82 GLN DC 137 GLN DC 149 GLN Total number of N/Q/H flips: 50 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.8098 moved from start: 1.0812 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.081 110734 Z= 0.290 Angle : 0.788 13.645 151086 Z= 0.413 Chirality : 0.048 0.359 18187 Planarity : 0.005 0.108 19721 Dihedral : 5.505 28.693 16471 Min Nonbonded Distance : 1.975 Molprobity Statistics. All-atom Clashscore : 20.61 Ramachandran Plot: Outliers : 0.00 % Allowed : 6.98 % Favored : 93.02 % Rotamer: Outliers : 1.35 % Allowed : 33.54 % Favored : 65.11 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.00 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.78 (0.06), residues: 15288 helix: 0.62 (0.08), residues: 3965 sheet: -1.00 (0.09), residues: 3354 loop : -2.28 (0.06), residues: 7969 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.061 0.002 TRPED 87 HIS 0.008 0.001 HISMd 146 PHE 0.027 0.002 PHE U 168 TYR 0.035 0.002 TYRDC 94 ARG 0.015 0.001 ARG Y 228 *********************** REFINEMENT MACRO_CYCLE 9 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3342 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 127 poor density : 3215 time to evaluate : 8.086 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 127 outliers final: 72 residues processed: 3259 average time/residue: 0.9655 time to fit residues: 5417.0010 Evaluate side-chains 3108 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 72 poor density : 3036 time to evaluate : 7.340 Switching outliers to nearest non-outliers outliers start: 72 outliers final: 0 residues processed: 72 average time/residue: 0.8194 time to fit residues: 119.3386 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=1.00 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 881 optimal weight: 50.0000 chunk 1419 optimal weight: 30.0000 chunk 866 optimal weight: 0.0010 chunk 673 optimal weight: 0.0370 chunk 987 optimal weight: 4.9990 chunk 1489 optimal weight: 0.6980 chunk 1370 optimal weight: 3.9990 chunk 1186 optimal weight: 0.9990 chunk 123 optimal weight: 0.0170 chunk 916 optimal weight: 0.9980 chunk 727 optimal weight: 0.5980 overall best weight: 0.2702 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** DH 341 GLN ** DK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Dd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Dd 138 GLN ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN EH 341 GLN FC 89 ASN ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Fd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GC 149 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GH 283 HIS GH 309 ASN ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** AD 32 ASN ** AD 69 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 82 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 89 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** HD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Hd 80 GLN ** IC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** IC 137 GLN ** IK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 104 ASN ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JH 283 HIS ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Jd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** KC 103 HIS KD 80 GLN KH 341 GLN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Kd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** LC 123 GLN ** LC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LH 341 GLN ** LK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** LK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Ld 78 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** MC 86 GLN MK 61 ASN ** MK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 138 GLN Md 152 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** N 150 ASN N 212 ASN ** O 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** P 171 ASN ** P 232 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Q 196 ASN R 110 GLN ** R 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** S 177 HIS ** S 185 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** S 232 GLN U 185 GLN ** U 221 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** V 177 HIS V 212 ASN ** X 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** X 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** X 183 GLN X 196 ASN ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Y 149 ASN Y 196 ASN ** Z 221 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** BC 69 GLN ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 149 GLN BC 241 HIS BD 31 ASN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Bd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Bd 138 GLN ** CC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 75 ASN DC 82 GLN DC 149 GLN Total number of N/Q/H flips: 44 ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.8032 moved from start: 1.0903 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.003 0.076 110734 Z= 0.232 Angle : 0.782 13.834 151086 Z= 0.408 Chirality : 0.048 0.388 18187 Planarity : 0.005 0.110 19721 Dihedral : 5.337 27.374 16471 Min Nonbonded Distance : 2.044 Molprobity Statistics. All-atom Clashscore : 19.64 Ramachandran Plot: Outliers : 0.00 % Allowed : 6.01 % Favored : 93.99 % Rotamer: Outliers : 0.82 % Allowed : 34.04 % Favored : 65.15 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.00 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.73 (0.06), residues: 15288 helix: 0.62 (0.08), residues: 3978 sheet: -0.84 (0.09), residues: 3263 loop : -2.28 (0.06), residues: 8047 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.071 0.002 TRPHD 87 HIS 0.006 0.001 HIS Z 221 PHE 0.032 0.002 PHE S 135 TYR 0.038 0.002 TYRMC 94 ARG 0.015 0.001 ARGDD 97 ********************** REFINEMENT MACRO_CYCLE 10 OF 10 ************************ ------------------------------------------------------------------------------- Update Rama plot phi/psi targets (oldfield only) ************************************************ 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Re-set Ramachandran plot restraints *********************************** favored: oldfield allowed: oldfield outlier: oldfield 30576 Ramachandran restraints generated. 15288 Oldfield, 0 Emsley, 15288 emsley8k and 0 Phi/Psi/2. ------------------------------------------------------------------------------- Optimize residue side-chains **************************** Evaluate side-chains 3483 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 77 poor density : 3406 time to evaluate : 10.870 Fit side-chains revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash revert: symmetry clash outliers start: 77 outliers final: 33 residues processed: 3429 average time/residue: 0.9911 time to fit residues: 5877.6299 Evaluate side-chains 3174 residues out of total 9399 non-(ALA, GLY, PRO) need fitting. rotamer outliers: 33 poor density : 3141 time to evaluate : 8.073 Switching outliers to nearest non-outliers outliers start: 33 outliers final: 0 residues processed: 33 average time/residue: 0.8220 time to fit residues: 61.7114 ------------------------------------------------------------------------------- Set rotamer restraints ********************** Rotamers are restrained with sigma=1.00 ------------------------------------------------------------------------------- XYZ refinement ************** Weight determination summary: number of chunks: 1495 random chunks: chunk 942 optimal weight: 3.9990 chunk 1263 optimal weight: 4.9990 chunk 363 optimal weight: 0.0970 chunk 1093 optimal weight: 2.9990 chunk 175 optimal weight: 10.0000 chunk 329 optimal weight: 0.8980 chunk 1187 optimal weight: 0.6980 chunk 497 optimal weight: 4.9990 chunk 1219 optimal weight: 0.7980 chunk 150 optimal weight: 30.0000 chunk 218 optimal weight: 0.9980 overall best weight: 0.6978 ------------------------------------------------------------------------------- NQH flips ********* Analyzing N/Q/H residues for possible flip corrections... Flipped N/Q/H residues before XYZ refinement: ** AC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** AC 149 GLN DH 341 GLN DK 147 GLN ** EC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** EC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** EC 149 GLN ** ED 69 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** EK 108 GLN FC 69 GLN ** FC 97 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** FC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** FK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Fd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GC 86 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** GC 149 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** GH 283 HIS ** GK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** AD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Gd 75 ASN ** HC 86 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 89 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** HC 103 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** ** HD 138 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** HK 72 GLN ** Hd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** IC 69 GLN IC 123 GLN ** IK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** IK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 86 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** JC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** JC 149 GLN JD 80 GLN JD 152 GLN JH 341 GLN ** JK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KC 241 HIS KD 80 GLN ** KK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** KK 108 GLN ** LC 137 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** LH 341 GLN ** LK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Ld 78 ASN Ld 152 GLN ** MC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** MD 32 ASN ** MH 341 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** MK 100 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Md 152 GLN ** AK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** N 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 150 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** O 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** O 225 GLN ** P 232 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Q 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** R 110 GLN R 185 GLN ** R 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** S 185 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** S 232 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** T 112 GLN V 212 ASN V 217 ASN V 226 ASN W 226 ASN ** X 115 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** X 185 GLN X 196 ASN ** X 217 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Y 149 ASN ** Y 196 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Z 196 ASN ** Z 221 HIS ** both conformations clash, **PLEASE CHECK MANUALLY** BC 86 GLN ** BC 104 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** BC 258 ASN BD 31 ASN ** BK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** BK 147 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** Bd 75 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CC 123 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** ** CK 87 GLN ** both conformations clash, **PLEASE CHECK MANUALLY** Cd 138 GLN DC 82 GLN DC 149 GLN DC 219 ASN ** DC 258 ASN ** both conformations clash, **PLEASE CHECK MANUALLY** Total number of N/Q/H flips: 42 ------------------------------------------------------------------------------- ADP refinement ************** |-group b-factor refinement (macro cycle = 0; iterations = 0)-----------------| | r_work = 0.3521 r_free = 0.3521 target = 0.104590 restraints weight = None | |-----------------------------------------------------------------------------| |-group b-factor refinement (macro cycle = 1; iterations = 55)----------------| | r_work = 0.3261 r_free = 0.3261 target = 0.089552 restraints weight = 288700.408| |-----------------------------------------------------------------------------| |-group b-factor refinement (macro cycle = 2; iterations = 39)----------------| | r_work = 0.3298 r_free = 0.3298 target = 0.091626 restraints weight = 140578.446| |-----------------------------------------------------------------------------| |-group b-factor refinement (macro cycle = 3; iterations = 40)----------------| | r_work = 0.3321 r_free = 0.3321 target = 0.092945 restraints weight = 85056.245| |-----------------------------------------------------------------------------| r_work (final): 0.3322 ------------------------------------------------------------------------------- Occupancy refinement ******************** ------------------------------------------------------------------------------- Overall statistics ****************** model-to-map fit, CC_mask: 0.8080 moved from start: 1.1020 Geometry Restraints Library: GeoStd + Monomer Library + CDL v1.2 Deviations from Ideal Values - rmsd, rmsZ for bonds and angles. Bond : 0.004 0.074 110734 Z= 0.257 Angle : 0.791 14.085 151086 Z= 0.413 Chirality : 0.048 0.347 18187 Planarity : 0.005 0.102 19721 Dihedral : 5.298 27.916 16471 Min Nonbonded Distance : 1.996 Molprobity Statistics. All-atom Clashscore : 20.45 Ramachandran Plot: Outliers : 0.00 % Allowed : 6.43 % Favored : 93.57 % Rotamer: Outliers : 0.78 % Allowed : 35.08 % Favored : 64.15 % Cbeta Deviations : 0.00 % Peptide Plane: Cis-proline : 0.00 % Cis-general : 0.00 % Twisted Proline : 0.00 % Twisted General : 0.00 % Rama-Z (Ramachandran plot Z-score): Interpretation: bad |Rama-Z| > 3; suspicious 2 < |Rama-Z| < 3; good |Rama-Z| < 2. Scores for whole/helix/sheet/loop are scaled independently; therefore, the values are not related in a simple manner. whole: -1.71 (0.06), residues: 15288 helix: 0.66 (0.08), residues: 3978 sheet: -0.88 (0.09), residues: 3328 loop : -2.26 (0.06), residues: 7982 Max deviation from planes: Type MaxDev MeanDev LineInFile TRP 0.077 0.002 TRPHD 87 HIS 0.012 0.001 HIS Z 221 PHE 0.039 0.002 PHEJD 104 TYR 0.040 0.002 TYRIC 94 ARG 0.013 0.001 ARG V 228 Origin is already at (0, 0, 0), no shifts will be applied =============================================================================== Job complete usr+sys time: 72145.21 seconds wall clock time: 1232 minutes 15.36 seconds (73935.36 seconds total)