try: from SimpleSession.versions.v34 import beginRestore,\ registerAfterModelsCB, reportRestoreError except ImportError: from chimera import UserError raise UserError('Cannot open session that was saved in a' ' newer version of Chimera; update your version') import chimera from chimera import replyobj replyobj.status('Beginning session restore...', \ blankAfter=0) beginRestore() def restoreCoreModels(): from SimpleSession.versions.v34 import init, restoreCamera, \ restoreMolecules, restoreColors, restoreSurfaces, \ restoreVRML, restorePseudoBondGroups molInfo = {'ballScale': (1, 0.25, {}), 'ribbonHidesMainchain': (1, True, {}), 'pointSize': (1, 1, {}), 'name': (1, '1W6K.pdb', {}), 'color': (1, 0, {}), 'optional': {}, 'pdbHeaders': [{'KEYWDS': ['KEYWDS CYCLASE, CHOLESTEROL, LANOSTEROL, MONOTOPIC MEMBRANE ', 'KEYWDS 2 PROTEIN, B-OCTYL-GLUCOSIDE, ISOMERASE, STEROID BIOSYNTHESIS '], 'SEQRES': ['SEQRES 1 A 732 MET THR GLU GLY THR CYS LEU ARG ARG ARG GLY GLY PRO ', 'SEQRES 2 A 732 TYR LYS THR GLU PRO ALA THR ASP LEU GLY ARG TRP ARG ', 'SEQRES 3 A 732 LEU ASN CYS GLU ARG GLY ARG GLN THR TRP THR TYR LEU ', 'SEQRES 4 A 732 GLN ASP GLU ARG ALA GLY ARG GLU GLN THR GLY LEU GLU ', 'SEQRES 5 A 732 ALA TYR ALA LEU GLY LEU ASP THR LYS ASN TYR PHE LYS ', 'SEQRES 6 A 732 ASP LEU PRO LYS ALA HIS THR ALA PHE GLU GLY ALA LEU ', 'SEQRES 7 A 732 ASN GLY MET THR PHE TYR VAL GLY LEU GLN ALA GLU ASP ', 'SEQRES 8 A 732 GLY HIS TRP THR GLY ASP TYR GLY GLY PRO LEU PHE LEU ', 'SEQRES 9 A 732 LEU PRO GLY LEU LEU ILE THR CYS HIS VAL ALA ARG ILE ', 'SEQRES 10 A 732 PRO LEU PRO ALA GLY TYR ARG GLU GLU ILE VAL ARG TYR ', 'SEQRES 11 A 732 LEU ARG SER VAL GLN LEU PRO ASP GLY GLY TRP GLY LEU ', 'SEQRES 12 A 732 HIS ILE GLU ASP LYS SER THR VAL PHE GLY THR ALA LEU ', 'SEQRES 13 A 732 ASN TYR VAL SER LEU ARG ILE LEU GLY VAL GLY PRO ASP ', 'SEQRES 14 A 732 ASP PRO ASP LEU VAL ARG ALA ARG ASN ILE LEU HIS LYS ', 'SEQRES 15 A 732 LYS GLY GLY ALA VAL ALA ILE PRO SER TRP GLY LYS PHE ', 'SEQRES 16 A 732 TRP LEU ALA VAL LEU ASN VAL TYR SER TRP GLU GLY LEU ', 'SEQRES 17 A 732 ASN THR LEU PHE PRO GLU MET TRP LEU PHE PRO ASP TRP ', 'SEQRES 18 A 732 ALA PRO ALA HIS PRO SER THR LEU TRP CYS HIS CYS ARG ', 'SEQRES 19 A 732 GLN VAL TYR LEU PRO MET SER TYR CYS TYR ALA VAL ARG ', 'SEQRES 20 A 732 LEU SER ALA ALA GLU ASP PRO LEU VAL GLN SER LEU ARG ', 'SEQRES 21 A 732 GLN GLU LEU TYR VAL GLU ASP PHE ALA SER ILE ASP TRP ', 'SEQRES 22 A 732 LEU ALA GLN ARG ASN ASN VAL ALA PRO ASP GLU LEU TYR ', 'SEQRES 23 A 732 THR PRO HIS SER TRP LEU LEU ARG VAL VAL TYR ALA LEU ', 'SEQRES 24 A 732 LEU ASN LEU TYR GLU HIS HIS HIS SER ALA HIS LEU ARG ', 'SEQRES 25 A 732 GLN ARG ALA VAL GLN LYS LEU TYR GLU HIS ILE VAL ALA ', 'SEQRES 26 A 732 ASP ASP ARG PHE THR LYS SER ILE SER ILE GLY PRO ILE ', 'SEQRES 27 A 732 SER LYS THR ILE ASN MET LEU VAL ARG TRP TYR VAL ASP ', 'SEQRES 28 A 732 GLY PRO ALA SER THR ALA PHE GLN GLU HIS VAL SER ARG ', 'SEQRES 29 A 732 ILE PRO ASP TYR LEU TRP MET GLY LEU ASP GLY MET LYS ', 'SEQRES 30 A 732 MET GLN GLY THR ASN GLY SER GLN ILE TRP ASP THR ALA ', 'SEQRES 31 A 732 PHE ALA ILE GLN ALA LEU LEU GLU ALA GLY GLY HIS HIS ', 'SEQRES 32 A 732 ARG PRO GLU PHE SER SER CYS LEU GLN LYS ALA HIS GLU ', 'SEQRES 33 A 732 PHE LEU ARG LEU SER GLN VAL PRO ASP ASN PRO PRO ASP ', 'SEQRES 34 A 732 TYR GLN LYS TYR TYR ARG GLN MET ARG LYS GLY GLY PHE ', 'SEQRES 35 A 732 SER PHE SER THR LEU ASP CYS GLY TRP ILE VAL SER ASP ', 'SEQRES 36 A 732 CYS THR ALA GLU ALA LEU LYS ALA VAL LEU LEU LEU GLN ', 'SEQRES 37 A 732 GLU LYS CYS PRO HIS VAL THR GLU HIS ILE PRO ARG GLU ', 'SEQRES 38 A 732 ARG LEU CYS ASP ALA VAL ALA VAL LEU LEU ASN MET ARG ', 'SEQRES 39 A 732 ASN PRO ASP GLY GLY PHE ALA THR TYR GLU THR LYS ARG ', 'SEQRES 40 A 732 GLY GLY HIS LEU LEU GLU LEU LEU ASN PRO SER GLU VAL ', 'SEQRES 41 A 732 PHE GLY ASP ILE MET ILE ASP TYR THR TYR VAL GLU CYS ', 'SEQRES 42 A 732 THR SER ALA VAL MET GLN ALA LEU LYS TYR PHE HIS LYS ', 'SEQRES 43 A 732 ARG PHE PRO GLU HIS ARG ALA ALA GLU ILE ARG GLU THR ', 'SEQRES 44 A 732 LEU THR GLN GLY LEU GLU PHE CYS ARG ARG GLN GLN ARG ', 'SEQRES 45 A 732 ALA ASP GLY SER TRP GLU GLY SER TRP GLY VAL CYS PHE ', 'SEQRES 46 A 732 THR TYR GLY THR TRP PHE GLY LEU GLU ALA PHE ALA CYS ', 'SEQRES 47 A 732 MET GLY GLN THR TYR ARG ASP GLY THR ALA CYS ALA GLU ', 'SEQRES 48 A 732 VAL SER ARG ALA CYS ASP PHE LEU LEU SER ARG GLN MET ', 'SEQRES 49 A 732 ALA ASP GLY GLY TRP GLY GLU ASP PHE GLU SER CYS GLU ', 'SEQRES 50 A 732 GLU ARG ARG TYR VAL GLN SER ALA GLN SER GLN ILE HIS ', 'SEQRES 51 A 732 ASN THR CYS TRP ALA MET MET GLY LEU MET ALA VAL ARG ', 'SEQRES 52 A 732 HIS PRO ASP ILE GLU ALA GLN GLU ARG GLY VAL ARG CYS ', 'SEQRES 53 A 732 LEU LEU GLU LYS GLN LEU PRO ASN GLY ASP TRP PRO GLN ', 'SEQRES 54 A 732 GLU ASN ILE ALA GLY VAL PHE ASN LYS SER CYS ALA ILE ', 'SEQRES 55 A 732 SER TYR THR SER TYR ARG ASN ILE PHE PRO ILE TRP ALA ', 'SEQRES 56 A 732 LEU GLY ARG PHE SER GLN LEU TYR PRO GLU ARG ALA LEU ', 'SEQRES 57 A 732 ALA GLY HIS PRO '], 'DBREF': ['DBREF 1W6K A 1 732 UNP P48449 ERG7_HUMAN 1 732 '], 'TITLE': ['TITLE STRUCTURE OF HUMAN OSC IN COMPLEX WITH LANOSTEROL '], 'CISPEP': ['CISPEP 1 GLY A 12 PRO A 13 0 2.76 ', 'CISPEP 2 VAL A 583 CYS A 584 0 -18.47 '], 'HELIX': ['HELIX 1 1 ASP A 21 GLY A 23 5 3 ', 'HELIX 2 2 THR A 49 GLY A 57 1 9 ', 'HELIX 3 3 THR A 72 GLY A 86 1 15 ', 'HELIX 4 4 PHE A 103 ARG A 116 1 14 ', 'HELIX 5 5 GLY A 122 GLN A 135 1 14 ', 'HELIX 6 6 THR A 150 LEU A 164 1 15 ', 'HELIX 7 7 ASP A 170 LYS A 183 1 14 ', 'HELIX 8 8 GLY A 185 ILE A 189 5 5 ', 'HELIX 9 9 PRO A 190 LEU A 200 1 11 ', 'HELIX 10 10 SER A 204 LEU A 208 5 5 ', 'HELIX 11 11 PHE A 212 PHE A 218 5 7 ', 'HELIX 12 12 HIS A 225 LEU A 229 5 5 ', 'HELIX 13 13 TRP A 230 VAL A 246 1 17 ', 'HELIX 14 14 ASP A 253 GLN A 261 1 9 ', 'HELIX 15 15 ASP A 267 ILE A 271 5 5 ', 'HELIX 16 16 TRP A 273 ARG A 277 5 5 ', 'HELIX 17 17 ALA A 281 LEU A 285 5 5 ', 'HELIX 18 18 SER A 290 HIS A 306 1 17 ', 'HELIX 19 19 SER A 308 LYS A 331 1 24 ', 'HELIX 20 20 GLY A 336 GLY A 352 1 17 ', 'HELIX 21 21 SER A 355 ARG A 364 1 10 ', 'HELIX 22 22 ILE A 365 ASP A 367 5 3 ', 'HELIX 23 23 SER A 384 ALA A 399 1 16 ', 'HELIX 24 24 GLY A 400 ARG A 404 5 5 ', 'HELIX 25 25 ARG A 404 GLU A 406 5 3 ', 'HELIX 26 26 PHE A 407 GLN A 422 1 16 ', 'HELIX 27 27 ASP A 429 TYR A 434 5 6 ', 'HELIX 28 28 VAL A 453 CYS A 471 1 19 ', 'HELIX 29 29 PRO A 479 ASN A 492 1 14 ', 'HELIX 30 30 GLY A 509 ASN A 516 5 8 ', 'HELIX 31 31 TYR A 530 PHE A 548 1 19 ', 'HELIX 32 32 ARG A 552 GLN A 571 1 20 ', 'HELIX 33 33 CYS A 584 MET A 599 1 16 ', 'HELIX 34 34 CYS A 609 SER A 621 1 13 ', 'HELIX 35 35 PHE A 633 ARG A 639 1 7 ', 'HELIX 36 36 GLN A 648 VAL A 662 1 15 ', 'HELIX 37 37 ASP A 666 GLN A 681 1 16 ', 'HELIX 38 38 SER A 706 TYR A 723 1 18 ', 'HELIX 39 39 ARG A 726 GLY A 730 5 5 '], 'REMARK': ['REMARK 1 ', 'REMARK 1 REFERENCE 1 ', "REMARK 1 AUTH A.RUF,F.MULLER,B.D'ARCY,M.STIHLE,E.KUZNIR, ", 'REMARK 1 AUTH 2 C.HANDSCHIN,O.MORAND,R.THOMA ', 'REMARK 1 TITL THE MONOTOPIC MEMBRANE PROTEIN HUMAN OSC IS ACTIVE ', 'REMARK 1 TITL 2 AS MONOMER ', 'REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMM. V. 315 247 2004 ', 'REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X ', 'REMARK 2 ', 'REMARK 2 RESOLUTION. 2.10 ANGSTROMS. ', 'REMARK 3 ', 'REMARK 3 REFINEMENT. ', 'REMARK 3 PROGRAM : AUTOBUSTER ', 'REMARK 3 ', 'REMARK 3 DATA USED IN REFINEMENT. ', 'REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 ', 'REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 ', 'REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 ', 'REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL ', 'REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL ', 'REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL ', 'REMARK 3 NUMBER OF REFLECTIONS : 0 ', 'REMARK 3 ', 'REMARK 3 FIT TO DATA USED IN REFINEMENT. ', 'REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT ', 'REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM ', 'REMARK 3 R VALUE (WORKING SET) : 0.147 ', 'REMARK 3 FREE R VALUE : 0.188 ', 'REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 ', 'REMARK 3 FREE R VALUE TEST SET COUNT : NULL ', 'REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL ', 'REMARK 3 ', 'REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. ', 'REMARK 3 TOTAL NUMBER OF BINS USED : NULL ', 'REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL ', 'REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL ', 'REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL ', 'REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL ', 'REMARK 3 BIN R VALUE (WORKING SET) : NULL ', 'REMARK 3 BIN FREE R VALUE : NULL ', 'REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL ', 'REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL ', 'REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL ', 'REMARK 3 ', 'REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. ', 'REMARK 3 PROTEIN ATOMS : 5816 ', 'REMARK 3 NUCLEIC ACID ATOMS : 0 ', 'REMARK 3 HETEROGEN ATOMS : 116 ', 'REMARK 3 SOLVENT ATOMS : NULL ', 'REMARK 3 ', 'REMARK 3 B VALUES. ', 'REMARK 3 FROM WILSON PLOT (A**2) : NULL ', 'REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL ', 'REMARK 3 OVERALL ANISOTROPIC B VALUE. ', 'REMARK 3 B11 (A**2) : NULL ', 'REMARK 3 B22 (A**2) : NULL ', 'REMARK 3 B33 (A**2) : NULL ', 'REMARK 3 B12 (A**2) : NULL ', 'REMARK 3 B13 (A**2) : NULL ', 'REMARK 3 B23 (A**2) : NULL ', 'REMARK 3 ', 'REMARK 3 ESTIMATED COORDINATE ERROR. ', 'REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL ', 'REMARK 3 ESD FROM SIGMAA (A) : NULL ', 'REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL ', 'REMARK 3 ', 'REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. ', 'REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL ', 'REMARK 3 ESD FROM C-V SIGMAA (A) : NULL ', 'REMARK 3 ', 'REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. ', 'REMARK 3 BOND LENGTHS (A) : NULL ', 'REMARK 3 BOND ANGLES (DEGREES) : NULL ', 'REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL ', 'REMARK 3 IMPROPER ANGLES (DEGREES) : NULL ', 'REMARK 3 ', 'REMARK 3 ISOTROPIC THERMAL MODEL : NULL ', 'REMARK 3 ', 'REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA ', 'REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL ', 'REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL ', 'REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL ', 'REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL ', 'REMARK 3 ', 'REMARK 3 NCS MODEL : NULL ', 'REMARK 3 ', 'REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT ', 'REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL ', 'REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL ', 'REMARK 3 ', 'REMARK 3 PARAMETER FILE 1 : NULL ', 'REMARK 3 TOPOLOGY FILE 1 : NULL ', 'REMARK 3 ', 'REMARK 3 OTHER REFINEMENT REMARKS: NULL ', 'REMARK 4 ', 'REMARK 4 1W6K COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 ', 'REMARK 4 ', 'REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. ', 'REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) ', 'REMARK 100 ', 'REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . ', 'REMARK 100 THE EBI ID CODE IS EBI-20825 . ', 'REMARK 200 ', 'REMARK 200 EXPERIMENTAL DETAILS ', 'REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION ', 'REMARK 200 DATE OF DATA COLLECTION : 15-OCT-2002 ', 'REMARK 200 TEMPERATURE (KELVIN) : 100.0 ', 'REMARK 200 PH : NULL ', 'REMARK 200 NUMBER OF CRYSTALS USED : 1 ', 'REMARK 200 ', 'REMARK 200 SYNCHROTRON (Y/N) : Y ', 'REMARK 200 RADIATION SOURCE : SLS ', 'REMARK 200 BEAMLINE : X06SA ', 'REMARK 200 X-RAY GENERATOR MODEL : NULL ', 'REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M ', 'REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 ', 'REMARK 200 MONOCHROMATOR : NULL ', 'REMARK 200 OPTICS : NULL ', 'REMARK 200 ', 'REMARK 200 DETECTOR TYPE : CCD ', 'REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH ', 'REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO ', 'REMARK 200 DATA SCALING SOFTWARE : SCALEPACK ', 'REMARK 200 ', 'REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79898 ', 'REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 ', 'REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 ', 'REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 ', 'REMARK 200 ', 'REMARK 200 OVERALL. ', 'REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 ', 'REMARK 200 DATA REDUNDANCY : 5.000 ', 'REMARK 200 R MERGE (I) : 0.08000 ', 'REMARK 200 R SYM (I) : NULL ', 'REMARK 200 FOR THE DATA SET : 14.4000 ', 'REMARK 200 ', 'REMARK 200 IN THE HIGHEST RESOLUTION SHELL. ', 'REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 ', 'REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 ', 'REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3 ', 'REMARK 200 DATA REDUNDANCY IN SHELL : 5.00 ', 'REMARK 200 R MERGE FOR SHELL (I) : 0.49000 ', 'REMARK 200 R SYM FOR SHELL (I) : NULL ', 'REMARK 200 FOR SHELL : 3.100 ', 'REMARK 200 ', 'REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH ', 'REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER ', 'REMARK 200 SOFTWARE USED: NULL ', 'REMARK 200 STARTING MODEL: NULL ', 'REMARK 200 ', 'REMARK 200 REMARK: NULL ', 'REMARK 280 ', 'REMARK 280 CRYSTAL ', 'REMARK 280 SOLVENT CONTENT, VS (%): 65.33 ', 'REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55 ', 'REMARK 280 ', 'REMARK 280 CRYSTALLIZATION CONDITIONS: NULL ', 'REMARK 290 ', 'REMARK 290 CRYSTALLOGRAPHIC SYMMETRY ', 'REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 ', 'REMARK 290 ', 'REMARK 290 SYMOP SYMMETRY ', 'REMARK 290 NNNMMM OPERATOR ', 'REMARK 290 1555 X,Y,Z ', 'REMARK 290 2555 -X,-Y,1/2+Z ', 'REMARK 290 3555 -X,Y,1/2-Z ', 'REMARK 290 4555 X,-Y,-Z ', 'REMARK 290 5555 1/2+X,1/2+Y,Z ', 'REMARK 290 6555 1/2-X,1/2-Y,1/2+Z ', 'REMARK 290 7555 1/2-X,1/2+Y,1/2-Z ', 'REMARK 290 8555 1/2+X,1/2-Y,-Z ', 'REMARK 290 ', 'REMARK 290 WHERE NNN -> OPERATOR NUMBER ', 'REMARK 290 MMM -> TRANSLATION VECTOR ', 'REMARK 290 ', 'REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS ', 'REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM ', 'REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY ', 'REMARK 290 RELATED MOLECULES. ', 'REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 ', 'REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.00300 ', 'REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.00300 ', 'REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 ', 'REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 ', 'REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 94.78500 ', 'REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 100.73600 ', 'REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 ', 'REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 94.78500 ', 'REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 100.73600 ', 'REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 31.00300 ', 'REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 94.78500 ', 'REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.73600 ', 'REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 31.00300 ', 'REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 94.78500 ', 'REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 100.73600 ', 'REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 ', 'REMARK 290 ', 'REMARK 290 REMARK: NULL ', 'REMARK 300 ', 'REMARK 300 BIOMOLECULE: 1 ', 'REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT ', 'REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR ', 'REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). ', 'REMARK 350 ', 'REMARK 350 GENERATING THE BIOMOLECULE ', 'REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN ', 'REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE ', 'REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS ', 'REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND ', 'REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. ', 'REMARK 350 ', 'REMARK 350 BIOMOLECULE: 1 ', 'REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, Z ', 'REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 ', 'REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 ', 'REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 ', 'REMARK 465 ', 'REMARK 465 MISSING RESIDUES ', 'REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE ', 'REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN ', 'REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) ', 'REMARK 465 ', 'REMARK 465 M RES C SSSEQI ', 'REMARK 465 MET A 1 ', 'REMARK 465 THR A 2 ', 'REMARK 465 GLU A 3 ', 'REMARK 465 GLY A 4 ', 'REMARK 465 THR A 5 ', 'REMARK 465 GLU A 42 ', 'REMARK 465 ARG A 43 ', 'REMARK 500 ', 'REMARK 500 GEOMETRY AND STEREOCHEMISTRY ', 'REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT ', 'REMARK 500 ', 'REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. ', 'REMARK 500 ', 'REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI ', 'REMARK 500 O HOH Z 122 O HOH Z 302 2.15 ', 'REMARK 500 O HOH Z 454 O HOH Z 954 2.15 ', 'REMARK 500 O HOH Z 508 O HOH Z 513 2.18 ', 'REMARK 500 O HOH Z 94 O HOH Z 95 2.19 ', 'REMARK 500 ', 'REMARK 500 GEOMETRY AND STEREOCHEMISTRY ', 'REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS ', 'REMARK 500 ', 'REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES ', 'REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE ', 'REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN ', 'REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). ', 'REMARK 500 ', 'REMARK 500 STANDARD TABLE: ', 'REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) ', 'REMARK 500 ', 'REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 ', 'REMARK 500 ', 'REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION ', 'REMARK 500 MET A 215 SD MET A 215 CE 0.145 ', 'REMARK 500 MET A 656 SD MET A 656 CE 0.134 ', 'REMARK 500 ', 'REMARK 500 GEOMETRY AND STEREOCHEMISTRY ', 'REMARK 500 SUBTOPIC: COVALENT BOND ANGLES ', 'REMARK 500 ', 'REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES ', 'REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE ', 'REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN ', 'REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). ', 'REMARK 500 ', 'REMARK 500 STANDARD TABLE: ', 'REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) ', 'REMARK 500 ', 'REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 ', 'REMARK 500 ', 'REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 ', 'REMARK 500 ARG A 129 CB - CG - CD ANGL. DEV. = -9.9 DEGREES ', 'REMARK 500 THR A 381 N - CA - C ANGL. DEV. = -9.8 DEGREES ', 'REMARK 500 ILE A 478 N - CA - C ANGL. DEV. =-11.3 DEGREES ', 'REMARK 500 ARG A 604 CB - CA - C ANGL. DEV. =-10.2 DEGREES ', 'REMARK 500 ARG A 604 CG - CD - NE ANGL. DEV. =-14.9 DEGREES ', 'REMARK 500 PHE A 711 N - CA - C ANGL. DEV. = 10.5 DEGREES ', 'REMARK 500 PRO A 732 CB - CA - C ANGL. DEV. =-10.2 DEGREES ', 'REMARK 500 PRO A 732 C - N - CD ANGL. DEV. =-12.3 DEGREES ', 'REMARK 500 ', 'REMARK 500 GEOMETRY AND STEREOCHEMISTRY ', 'REMARK 500 SUBTOPIC: TORSION ANGLES ', 'REMARK 500 ', 'REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: ', 'REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; ', 'REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). ', 'REMARK 500 ', 'REMARK 500 STANDARD TABLE: ', 'REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) ', 'REMARK 500 ', 'REMARK 500 M RES CSSEQI PSI PHI ', 'REMARK 500 GLU A 519 -41.00 68.74 ', 'REMARK 500 LYS A 698 -32.20 75.24 ', 'REMARK 525 ', 'REMARK 525 SOLVENT ', 'REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED ', 'REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE ', 'REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL ', 'REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE ', 'REMARK 525 NUMBER; I=INSERTION CODE): ', 'REMARK 525 ', 'REMARK 525 M RES CSSEQI ', 'REMARK 525 HOH Z 22 DISTANCE = 7.55 ANGSTROMS ', 'REMARK 525 HOH Z 239 DISTANCE = 6.47 ANGSTROMS ', 'REMARK 525 HOH Z 261 DISTANCE = 5.78 ANGSTROMS ', 'REMARK 525 HOH Z 295 DISTANCE = 5.70 ANGSTROMS ', 'REMARK 525 HOH Z 376 DISTANCE = 5.62 ANGSTROMS ', 'REMARK 800 ', 'REMARK 800 SITE ', 'REMARK 800 SITE_IDENTIFIER: AC1 ', 'REMARK 800 SITE_DESCRIPTION: LAN BINDING SITE FOR CHAIN A '], 'SCALE1': ['SCALE1 0.005275 0.000000 0.000000 0.00000 '], 'SCALE2': ['SCALE2 0.000000 0.004963 0.000000 0.00000 '], 'AUTHOR': ["AUTHOR R.THOMA,T.SCHULZ-GASCH,B.D'ARCY,J.BENZ,J.AEBI,H.DEHMLOW, ", 'AUTHOR 2 M.HENNIG,A.RUF '], 'CRYST1': ['CRYST1 189.570 201.472 62.006 90.00 90.00 90.00 C 2 2 21 8 '], 'ORIGX1': ['ORIGX1 1.000000 0.000000 0.000000 0.00000 '], 'ORIGX3': ['ORIGX3 0.000000 0.000000 1.000000 0.00000 '], 'ORIGX2': ['ORIGX2 0.000000 1.000000 0.000000 0.00000 '], 'SOURCE': ['SOURCE MOL_ID: 1; ', 'SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; ', 'SOURCE 3 ORGANISM_COMMON: HUMAN; ', 'SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS; ', 'SOURCE 5 EXPRESSION_SYSTEM_STRAIN: GS115; ', 'SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PPICZB '], 'FORMUL': ['FORMUL 2 BOG 8(C14 H28 O6) ', 'FORMUL 10 LAN C30 H50 O ', 'FORMUL 11 HOH *963(H2 O) '], 'HETNAM': ['HETNAM BOG B-OCTYLGLUCOSIDE ', 'HETNAM LAN LANOSTEROL '], 'COMPND': ['COMPND MOL_ID: 1; ', 'COMPND 2 MOLECULE: LANOSTEROL SYNTHASE; ', 'COMPND 3 CHAIN: A; ', 'COMPND 4 SYNONYM: OXIDOSQUALENE--LANOSTEROL CYCLASE, OXIDO SQUALENE ', 'COMPND 5 CYCLASE, 2,3-EPOXYSQUALENE--LANOSTEROL CYCLASE, OSC; ', 'COMPND 6 EC: 5.4.99.7; ', 'COMPND 7 ENGINEERED: YES '], 'REVDAT': ['REVDAT 2 23-DEC-04 1W6K 1 REMARK ', 'REVDAT 1 29-OCT-04 1W6K 0 '], 'HET': ['HET BOG A1732 7 ', 'HET BOG A1733 20 ', 'HET BOG A1734 6 ', 'HET BOG A1735 20 ', 'HET BOG A1736 7 ', 'HET BOG A1737 8 ', 'HET BOG A1738 8 ', 'HET BOG A1739 9 ', 'HET LAN A1740 31 '], 'SHEET': ['SHEET 1 AA 2 TRP A 25 GLU A 30 0 ', 'SHEET 2 AA 2 ARG A 33 TYR A 38 -1 O ARG A 33 N GLU A 30 ', 'SHEET 1 AB 2 LEU A 369 GLY A 372 0 ', 'SHEET 2 AB 2 GLY A 375 MET A 378 -1 O GLY A 375 N GLY A 372 ', 'SHEET 1 AC 2 GLY A 694 PHE A 696 0 ', 'SHEET 2 AC 2 CYS A 700 ILE A 702 -1 O CYS A 700 N PHE A 696 '], 'SITE': ['SITE 1 AC1 8 LEU A 274 ARG A 277 ASN A 301 LEU A 302 ', 'SITE 2 AC1 8 HIS A 305 HIS A 306 HOH Z 958 HOH Z 959 ', 'SITE 1 AC2 2 TRP A 291 LEU A 511 ', 'SITE 1 AC3 7 PRO A 288 HIS A 289 SER A 290 TRP A 291 ', 'SITE 2 AC3 7 ARG A 294 HOH Z 961 HOH Z 962 ', 'SITE 1 AC6 1 TRP A 291 ', 'SITE 1 AC8 3 MET A 215 LEU A 515 HOH Z 416 ', 'SITE 1 AC9 15 TYR A 98 TRP A 192 TRP A 230 HIS A 232 ', 'SITE 2 AC9 15 TRP A 387 PHE A 444 ASP A 455 THR A 502 ', 'SITE 3 AC9 15 TYR A 503 TRP A 581 PHE A 696 ASN A 697 ', 'SITE 4 AC9 15 TYR A 704 HOH Z 602 HOH Z 813 '], 'HEADER': ['HEADER ISOMERASE 19-AUG-04 1W6K '], 'EXPDTA': ['EXPDTA X-RAY DIFFRACTION '], 'SCALE3': ['SCALE3 0.000000 0.000000 0.016127 0.00000 '], 'JRNL': ["JRNL AUTH R.THOMA,T.SCHULZ-GASCH,B.D'ARCY,J.BENZ,J.AEBI, ", 'JRNL AUTH 2 H.DEHMLOW,M.HENNIG,M.STIHLE,A.RUF ', 'JRNL TITL INSIGHT INTO STEROID SCAFFOLD FORMATION FROM THE ', 'JRNL TITL 2 STRUCTURE OF HUMAN OXIDOSQUALENE CYCLASE. ', 'JRNL REF NATURE V. 432 118 2004 ', 'JRNL REFN ASTM NATUAS UK ISSN 0028-0836 ']}], 'ids': (1, (0, 0), {}), 'surfaceOpacity': (1, -1, {}), 'autochain': (1, True, {}), 'vdwDensity': (1, 5, {}), 'hidden': (1, False, {}), 'lineWidth': (1, 1, {}), 'stickScale': (1, 1, {}), 'display': (1, True, {})} resInfo = {'insert': (1697, ' ', {}), 'name': (1697, 'HOH', {'ILE': [102, 109, 119, 137, 155, 171, 181, 263, 315, 325, 327, 330, 334, 357, 378, 385, 444, 470, 516, 518, 548, 641, 659, 684, 694, 702, 705], 'GLN': [28, 34, 40, 80, 127, 227, 249, 253, 268, 305, 309, 351, 371, 377, 386, 404, 414, 423, 428, 460, 531, 554, 562, 563, 593, 615, 635, 638, 640, 662, 673, 681, 713], 'GLY': [5, 6, 17, 26, 37, 42, 49, 68, 72, 78, 84, 88, 91, 92, 99, 114, 131, 132, 134, 145, 157, 159, 176, 177, 185, 199, 328, 344, 364, 367, 372, 375, 392, 393, 432, 433, 442, 490, 491, 500, 501, 514, 555, 567, 571, 574, 580, 584, 592, 598, 619, 620, 622, 650, 665, 677, 686, 709, 722], 'GLU': [11, 24, 39, 44, 67, 82, 117, 118, 138, 198, 206, 244, 254, 258, 276, 296, 313, 352, 390, 398, 408, 451, 461, 468, 473, 496, 505, 511, 524, 542, 547, 550, 557, 570, 586, 603, 623, 626, 629, 630, 660, 663, 671, 682, 717], 'BOG': [725, 726, 727, 728, 729, 730, 731, 732], 'CYS': [0, 23, 104, 223, 225, 235, 402, 441, 448, 463, 476, 525, 559, 576, 590, 601, 608, 628, 645, 668, 692], 'ASP': [15, 35, 51, 58, 83, 89, 130, 139, 161, 162, 164, 212, 245, 259, 264, 275, 318, 319, 343, 359, 366, 380, 417, 421, 440, 447, 477, 489, 515, 519, 566, 597, 609, 618, 624, 658, 678], 'SER': [125, 141, 152, 183, 196, 219, 233, 241, 250, 262, 282, 300, 324, 326, 331, 347, 355, 376, 400, 401, 413, 435, 437, 446, 510, 527, 568, 572, 605, 613, 627, 636, 639, 691, 695, 698, 712], 'LYS': [9, 53, 57, 61, 140, 174, 175, 186, 310, 323, 332, 369, 405, 424, 431, 454, 462, 498, 534, 538, 672, 690], 'PRO': [7, 12, 60, 93, 98, 110, 112, 129, 160, 163, 182, 205, 211, 215, 218, 231, 246, 274, 280, 329, 345, 358, 397, 416, 419, 420, 464, 471, 488, 509, 541, 657, 675, 680, 704, 716, 724], 'ASN': [22, 54, 71, 149, 170, 193, 201, 270, 271, 293, 335, 374, 418, 484, 487, 508, 643, 676, 683, 689, 701], 'VAL': [77, 106, 120, 126, 143, 151, 158, 166, 179, 191, 194, 228, 238, 248, 257, 272, 287, 288, 308, 316, 338, 342, 354, 415, 445, 456, 466, 479, 481, 512, 523, 529, 575, 604, 634, 654, 666, 687], 'THR': [10, 14, 29, 31, 41, 52, 64, 74, 87, 103, 142, 146, 202, 220, 279, 322, 333, 348, 373, 381, 438, 449, 467, 494, 497, 521, 526, 551, 553, 578, 581, 594, 599, 644, 697], 'HIS': [63, 85, 105, 136, 173, 217, 224, 281, 297, 298, 299, 302, 314, 353, 394, 395, 407, 465, 469, 502, 537, 543, 642, 656, 723], 'TRP': [19, 30, 86, 133, 184, 188, 197, 208, 213, 222, 265, 283, 340, 362, 379, 443, 569, 573, 582, 621, 646, 679, 706], 'LAN': [733], 'PHE': [56, 66, 75, 95, 144, 187, 204, 210, 260, 321, 350, 383, 399, 409, 434, 436, 492, 513, 536, 540, 558, 577, 583, 588, 610, 625, 688, 703, 711], 'ALA': [13, 36, 45, 47, 62, 65, 69, 81, 107, 113, 147, 168, 178, 180, 190, 214, 216, 237, 242, 243, 261, 267, 273, 290, 301, 307, 317, 346, 349, 382, 384, 387, 391, 406, 450, 452, 455, 478, 480, 493, 528, 532, 545, 546, 565, 587, 589, 600, 602, 607, 617, 637, 647, 653, 661, 685, 693, 707, 719, 721], 'MET': [73, 207, 232, 336, 363, 368, 370, 429, 485, 517, 530, 591, 616, 648, 649, 652], 'LEU': [1, 16, 21, 33, 43, 48, 50, 59, 70, 79, 94, 96, 97, 100, 101, 111, 123, 128, 135, 148, 153, 156, 165, 172, 189, 192, 200, 203, 209, 221, 230, 240, 247, 251, 255, 266, 277, 284, 285, 291, 292, 294, 303, 311, 337, 361, 365, 388, 389, 403, 410, 412, 439, 453, 457, 458, 459, 475, 482, 483, 503, 504, 506, 507, 533, 552, 556, 585, 611, 612, 651, 669, 670, 674, 708, 714, 720], 'ARG': [2, 3, 4, 18, 20, 25, 27, 38, 108, 116, 121, 124, 154, 167, 169, 226, 239, 252, 269, 286, 304, 306, 320, 339, 356, 396, 411, 427, 430, 472, 474, 486, 499, 539, 544, 549, 560, 561, 564, 596, 606, 614, 631, 632, 655, 664, 667, 700, 710, 718], 'TYR': [8, 32, 46, 55, 76, 90, 115, 122, 150, 195, 229, 234, 236, 256, 278, 289, 295, 312, 341, 360, 422, 425, 426, 495, 520, 522, 535, 579, 595, 633, 696, 699, 715]}), 'chain': (1697, 'Z', {'A': (None, [(0, 734)])}), 'ss': (1697, (False, False, False), {(True, False, False): (None, [(15, 3), (41, 9), (64, 15), (95, 14), (114, 14), (142, 15), (162, 14), (177, 16), (196, 5), (204, 7), (217, 22), (245, 9), (259, 5), (265, 5), (273, 5), (282, 17), (300, 24), (328, 17), (347, 13), (376, 39), (421, 6), (445, 19), (471, 14), (501, 8), (522, 19), (544, 20), (576, 16), (601, 13), (625, 7), (640, 15), (658, 16), (698, 18), (718, 5)]), (False, True, False): (None, [(19, 6), (27, 6), (361, 4), (367, 4), (686, 3), (692, 3)])}), 'molecule': (1697, 0, {}), 'ribbonColor': (1697, None, {1: (None, [(0, 1)]), 2: (None, [(1, 1)]), 3: (None, [(2, 1)]), 4: (None, [(3, 1)]), 5: (None, [(4, 1)]), 6: (None, [(5, 1)]), 7: (None, [(6, 1)]), 8: (None, [(7, 1)]), 9: (None, [(8, 1)]), 10: (None, [(9, 1)]), 11: (None, [(10, 1)]), 12: (None, [(11, 1)]), 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(None, [(1554, 5), (5593, 1)]), 225: (None, [(1559, 9), (5592, 1)]), 226: (None, [(1568, 5), (5591, 1)]), 227: (None, [(1573, 10), (5590, 1)]), 228: (None, [(1583, 8), (5589, 1)]), 229: (None, [(1591, 6), (5588, 1)]), 230: (None, [(1597, 11), (5587, 1)]), 231: (None, [(1608, 7), (5586, 1)]), 232: (None, [(1615, 6), (5585, 1)]), 233: (None, [(1621, 7), (5584, 1)]), 234: (None, [(1628, 5), (5583, 1)]), 235: (None, [(1633, 11), (5582, 1)]), 236: (None, [(1644, 5), (5581, 1)]), 237: (None, [(1649, 11), (5580, 1)]), 238: (None, [(1660, 4), (5579, 1)]), 239: (None, [(1664, 6), (5578, 1)]), 240: (None, [(1670, 10), (5577, 1)]), 241: (None, [(1680, 7), (5576, 1)]), 242: (None, [(1687, 5), (5575, 1)]), 243: (None, [(1692, 4), (5574, 1)]), 244: (None, [(1696, 4), (5573, 1)]), 245: (None, [(1700, 8), (5572, 1)]), 246: (None, [(1708, 7), (5571, 1)]), 247: (None, [(1715, 6), (5570, 1)]), 248: (None, [(1721, 7), (5569, 1)]), 249: (None, [(1728, 6), (5568, 1)]), 250: (None, [(1734, 8), (5567, 1)]), 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(None, [(2711, 4), (5432, 1)]), 386: (None, [(2715, 7), (5431, 1)]), 387: (None, [(2722, 8), (5430, 1)]), 388: (None, [(2730, 4), (5429, 1)]), 389: (None, [(2734, 7), (5428, 1)]), 390: (None, [(2741, 7), (5427, 1)]), 391: (None, [(2748, 8), (5426, 1)]), 392: (None, [(2756, 4), (5425, 1)]), 393: (None, [(2760, 3), (5424, 1)]), 394: (None, [(2763, 3), (5423, 1)]), 395: (None, [(2766, 9), (5422, 1)]), 396: (None, [(2775, 9), (5421, 1)]), 397: (None, [(2784, 10), (5420, 1)]), 398: (None, [(2794, 6), (5419, 1)]), 399: (None, [(2800, 8), (5418, 1)]), 400: (None, [(2808, 10), (5417, 1)]), 401: (None, [(2818, 5), (5416, 1)]), 402: (None, [(2823, 5), (5415, 1)]), 403: (None, [(2828, 5), (5414, 1)]), 404: (None, [(2833, 7), (5413, 1)]), 405: (None, [(2840, 8), (5412, 1)]), 406: (None, [(2848, 8), (5411, 1)]), 407: (None, [(2856, 4), (5410, 1)]), 408: (None, [(2860, 9), (5409, 1)]), 409: (None, [(2869, 8), (5408, 1)]), 410: (None, [(2877, 10), (5407, 1)]), 411: (None, [(2887, 7), (5406, 1)]), 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