PDB Full entry for 1JOH HEADER PEPTIDE ANTIBIOTIC 11-OCT-97 1JOH TITLE THE STRUCTURE OF ANTIAMOEBIN I, A MEMBRANE-ACTIVE PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIAMOEBIN I; COMPND 3 CHAIN: A, B; COMPND 4 BIOLOGICAL_UNIT: MONOMERS OR DIMERS AGGREGATE IN THE COMPND 5 MEMBRANE TO FACILITATE ION TRANSPORT SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: EMERCELLIOPSIS SP. KEYWDS ANTIAMOEBIN, PEPTAIBOL, PEPTIDE ANTIBIOTIC EXPDTA X-RAY DIFFRACTION AUTHOR C.F.SNOOK,B.A.WALLACE REVDAT 1 20-JAN-99 1JOH 0 JRNL AUTH C.F.SNOOK,G.A.WOOLLEY,G.OLIVA,V.PATTABHI,S.F.WOOD, JRNL AUTH 2 T.L.BLUNDELL,B.A.WALLACE JRNL TITL THE STRUCTURE AND FUNCTION OF ANTIAMOEBIN I, A JRNL TITL 2 PROLINE-RICH MEMBRANE-ACTIVE POLYPEPTIDE JRNL REF STRUCTURE (LONDON) V. 6 783 1998 JRNL REFN ASTM STRUE6 UK ISSN 0969-2126 2005 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.F.SNOOK,B.A.WALLACE REMARK 1 TITL THE MOLECULAR REPLACEMENT SOLUTION OF A SMALL REMARK 1 TITL 2 POLYPEPTIDE THAT REQUIRED HIGH RESOLUTION DATA TO REMARK 1 TITL 3 SOLVE REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN 0353 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.F.SNOOK REMARK 1 REF THE STRUCTURE AND FUNCTION 1997 REMARK 1 REF 2 OF ANTIAMOEBIN I, A REMARK 1 REF 3 MEMBRANE-ACTIVE PEPTIDE REMARK 1 PUBL LONDON : UNIVERSITY OF LONDON (THESIS) REMARK 1 REFN ASTM UK ISBN 2188 REMARK 1 REFERENCE 3 REMARK 1 AUTH G.OLIVA REMARK 1 REF MOLECULAR REDUNDANCY AND 1988 REMARK 1 REF 2 PROTEIN CRYSTALLOGRAPHY : REMARK 1 REF 3 X-RAY STRUCTURE ANALYSIS OF REMARK 1 REF 4 ANTIAMOEBIN I, BOVINE REMARK 1 REF 5 PANCREATIC POLYPEPTIDE AND REMARK 1 REF 6 HUMAN SERUM AMYLOID P REMARK 1 REF 7 COMPONENT REMARK 1 PUBL LONDON : UNIVERSITY OF LONDON (THESIS) REMARK 1 REFN ASTM UK ISBN 2189 REMARK 2 REMARK 2 RESOLUTION. 1.4 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : SHELXL-93 REMARK 3 AUTHORS : G.M.SHELDRICK REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.4 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF). REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1558 REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 4359 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.1355 REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 3567 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 238 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 160 REMARK 3 SOLVENT ATOMS : 30 REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 268.00 REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 1074 REMARK 3 NUMBER OF RESTRAINTS : 982 REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.036 REMARK 3 ANGLE DISTANCES (A) : 3.152 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000 REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.000 REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.000 REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.000 REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.016 REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005 REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.022 REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.065 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED: NULL REMARK 3 REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER REMARK 3 SPECIAL CASE: HETATM DATA FROM CCSD REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT STARTED USING 10.0 TO REMARK 3 2.5A AND DATA CUT-OFF AT 2 SIGMA IN X-PLOR. HIGH REMARK 3 RESOLUTION LIMIT INCREASED TO 2.0A, LOW RESOLUTION REMARK 3 DECREASED TO 25.0A AND DATA CUT-OFF DECREASED TO 0.0 SIGMA REMARK 3 AT 2.0A RESOLUTION. RESOLUTION INCREASED FROM 2.0A TO REMARK 3 1.4A WITH ALL DATA USING SHELXL-93. REFINEMENT CEASED REMARK 3 AFTER RESIDUES 1 TO 5 IN B-CHAIN IDENTIFIED AS DISORDERED REMARK 3 IN DENSITY. REMARK 4 REMARK 4 1JOH COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996 REMARK 6 REMARK 6 BIOMOLECULE ANTIAMOEBIN I IS ACTIVE AS A MONOMER THAT REMARK 6 INSERTS INTO THE LIPID BILAYER AND AGGREGATES IN A REMARK 6 MANNER THAT ALLOWS CHARGE DISSIPATION. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 1986 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : SEALED TUBE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : 290 4-CIRCLE REMARK 200 DIFFRACTOMETER REMARK 200 DETECTOR MANUFACTURER : HILGER-WATTS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6715 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.2 REMARK 200 RESOLUTION RANGE LOW (A) : 25. REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7 REMARK 200 DATA REDUNDANCY : 1 REMARK 200 R MERGE (I) : 1.2 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REMARK 200 REPLACEMENT REMARK 200 SOFTWARE USED: AMORE (CCP4 VERSION) REMARK 200 STARTING MODEL: RESIDUES 6 - 16 OF LEU1-ZERVAMICIN WITH ALL REMARK 200 NON-EQUIVALENT SIDE-CHAINS TRIMMED TO ALA. REMARK 200 REMARK 200 REMARK: USED NORMALISED STRUCTURE FACTORS REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 28. REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: ANTIAMOEBIN I WAS DISSOLVED IN REMARK 280 METHANOL AT 170 MG/ML AND GENTLY HEATED TO 303 K. THE REMARK 280 CLOSED VESSEL WAS THEN ALLOWED TO COOL TO ROOM REMARK 280 TEMPERATURE (293 K). LEFT AT RT UNTIL CRYSTALS APPEARED. REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,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 REMARK 290 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O PHL A 17 C MOH 1 1556 1.76 REMARK 500 O MOH 19 O MOH 21 1556 1.99 REMARK 500 C PHL A 17 C MOH 1 1556 2.10 REMARK 500 REMARK 500 REMARK: NULL 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 DISTANCE REMARK 500 O MOH 21 - C ARG 5 1.84 REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: INSPECTION OF RAMACHANDRAN PLOT FROM REMARK 650 PROCHECK, LATER USE OF PROMOTIF GAVE RESIDUES 2-9 ALPHA REMARK 650 HELIX, RESIDUES 10-12 3/10-HELIX, AND RESIDUES 13-17 TWO REMARK 650 OVERLAPPING TYPE I BETA-TURNS. REMARK 999 REMARK 999 SEQUENCE REMARK 999 REFERENCE: PANDEY, R.C., H.MENG, J.C.COOK JR, REMARK 999 K.L.RINEHART JR., J.AM.CHEM.SOC., V.99, (1977), 5203-5205. DBREF 1JOH A 1 17 PDB 1JOH 1JOH 1 17 DBREF 1JOH B 1 17 PDB 1JOH 1JOH 1 17 SEQRES 1 A 17 ACE PHE AIB AIB AIB DIV GLY LEU AIB AIB HYP GLN DIV SEQRES 2 A 17 HYP AIB PRO PHL SEQRES 1 B 17 ACE PHE AIB AIB AIB DIV GLY LEU AIB AIB HYP GLN DIV SEQRES 2 B 17 HYP AIB PRO PHL MODRES 1JOH DIV A 6 VAL D-ISOVALINE MODRES 1JOH DIV A 13 VAL D-ISOVALINE MODRES 1JOH HYP A 14 PRO GAMMA-HYDROXPROLINE MODRES 1JOH PHL A 17 PHE L-PHENYLALANINOL MODRES 1JOH DIV B 6 VAL D-ISOVALINE MODRES 1JOH HYP B 11 PRO GAMMA-HYDROXPROLINE MODRES 1JOH DIV B 13 VAL D-ISOVALINE MODRES 1JOH HYP B 14 PRO GAMMA-HYDROXPROLINE MODRES 1JOH PHL B 17 PHE L-PHENYLALANINOL HET ACE A 1 3 HET AIB A 3 6 HET AIB A 4 6 HET AIB A 5 6 HET DIV A 6 7 HET AIB A 9 6 HET AIB A 10 6 HET HYP A 11 8 HET DIV A 13 7 HET HYP A 14 8 HET AIB A 15 6 HET PHL A 17 11 HET ACE B 1 3 HET AIB B 3 6 HET AIB B 4 6 HET AIB B 5 6 HET DIV B 6 7 HET AIB B 9 6 HET AIB B 10 6 HET HYP B 11 8 HET DIV B 13 7 HET HYP B 14 8 HET AIB B 15 6 HET PHL B 17 11 HET MOH 1 2 HET MOH 2 2 HET MOH 3 2 HET MOH 4 2 HET MOH 5 2 HET MOH 6 2 HET MOH 7 2 HET MOH 8 1 HET MOH 9 1 HET MOH 10 1 HET MOH 11 1 HET MOH 12 1 HET MOH 13 1 HET MOH 14 1 HET MOH 15 1 HET MOH 16 1 HET MOH 17 1 HET MOH 18 1 HET MOH 19 1 HET MOH 20 1 HET MOH 21 1 HET MOH 22 1 HET MOH 23 1 HETNAM ACE ACETYL GROUP HETNAM AIB ALPHA-AMINOISOBUTYRIC ACID HETNAM DIV D-ISOVALINE HETNAM HYP 4-HYDROXYPROLINE HETNAM PHL L-PHENYLALANINOL HETNAM MOH METHANOL HETSYN HYP HYDROXYPROLINE FORMUL 1 ACE C2 H3 O1 FORMUL 1 AIB 6(C4 H9 N1 O2) FORMUL 1 DIV 2(C5 H11 N1 O2) FORMUL 1 HYP 2(C5 H9 N1 O3) FORMUL 1 PHL C9 H13 N1 O1 FORMUL 2 ACE C2 H3 O1 FORMUL 2 AIB 6(C4 H9 N1 O2) FORMUL 2 DIV 2(C5 H11 N1 O2) FORMUL 2 HYP 2(C5 H9 N1 O3) FORMUL 2 PHL C9 H13 N1 O1 FORMUL 3 MOH 23(C1 H4 O1) HELIX 1 1 PHE A 2 AIB A 9 1 SEE REMARK 650 8 HELIX 2 2 AIB A 10 GLN A 12 1 SEE REMARK 650 3 TURN 1 1 HYP A 14 PHL A 17 1 SEE REMARK 650 TURN 2 2 HYP B 14 PHL B 17 1 SEE REMARK 650 LINK C ACE A 1 N PHE A 2 LINK N AIB A 3 C PHE A 2 LINK C AIB A 3 N AIB A 4 LINK C AIB A 4 N AIB A 5 LINK C AIB A 5 N DIV A 6 LINK C DIV A 6 N GLY A 7 LINK N AIB A 9 C LEU A 8 LINK C AIB A 9 N AIB A 10 LINK C AIB A 10 N HYP A 11 LINK C HYP A 11 N GLN A 12 LINK N DIV A 13 C GLN A 12 LINK C DIV A 13 N HYP A 14 LINK C HYP A 14 N AIB A 15 LINK C AIB A 15 N PRO A 16 LINK N PHL A 17 C PRO A 16 LINK C ACE B 1 N PHE B 2 LINK N AIB B 3 C PHE B 2 LINK C AIB B 3 N AIB B 4 LINK C AIB B 4 N AIB B 5 LINK C AIB B 5 N DIV B 6 LINK C DIV B 6 N GLY B 7 LINK N AIB B 9 C LEU B 8 LINK C AIB B 9 N AIB B 10 LINK C AIB B 10 N HYP B 11 LINK C HYP B 11 N GLN B 12 LINK N DIV B 13 C GLN B 12 LINK C DIV B 13 N HYP B 14 LINK C HYP B 14 N AIB B 15 LINK C AIB B 15 N PRO B 16 LINK N PHL B 17 C PRO B 16 CRYST1 26.530 28.820 9.060 88.90 96.64 123.85 P 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.037693 0.025281 0.005782 0.00000 SCALE2 0.000000 0.041780 0.002293 0.00000 SCALE3 0.000000 0.000000 0.111288 0.00000 MTRIX1 1 0.000000 1.000000 0.000000 0.00000 1 MTRIX2 1 1.000000 0.000000 0.000000 0.00000 1 MTRIX3 1 0.000000 0.000000 -1.000000 115.46000 1 HETATM 1 C ACE A 1 2.849 -3.303 6.755 1.00 8.83 C HETATM 2 O ACE A 1 3.769 -3.853 5.982 1.00 22.92 O HETATM 3 CH3 ACE A 1 2.419 -2.235 6.503 1.00 4.21 C ATOM 4 N PHE A 2 2.432 -4.074 7.771 1.00 7.96 N ATOM 5 CA PHE A 2 1.337 -3.613 8.648 1.00 7.17 C ATOM 6 C PHE A 2 1.691 -2.333 9.360 1.00 6.64 C ATOM 7 O PHE A 2 0.928 -1.330 9.208 1.00 7.33 O ATOM 8 CB PHE A 2 1.038 -4.740 9.652 1.00 8.33 C ATOM 9 CG PHE A 2 -0.151 -4.431 10.566 1.00 8.62 C ATOM 10 CD1 PHE A 2 -1.429 -4.737 10.137 1.00 11.83 C ATOM 11 CD2 PHE A 2 0.061 -3.900 11.832 1.00 10.07 C ATOM 12 CE1 PHE A 2 -2.529 -4.522 10.975 1.00 11.43 C ATOM 13 CE2 PHE A 2 -1.042 -3.639 12.638 1.00 12.54 C ATOM 14 CZ PHE A 2 -2.308 -3.970 12.211 1.00 10.36 C HETATM 15 N AIB A 3 2.770 -2.270 10.120 1.00 6.21 N HETATM 16 CA AIB A 3 3.157 -1.040 10.817 1.00 7.61 C HETATM 17 C AIB A 3 3.293 0.115 9.820 1.00 8.28 C HETATM 18 O1 AIB A 3 2.831 1.246 10.068 1.00 8.19 O HETATM 19 CB1 AIB A 3 4.545 -1.217 11.467 1.00 10.28 C HETATM 20 CB2 AIB A 3 2.126 -0.739 11.915 1.00 7.96 C HETATM 21 N AIB A 4 3.974 -0.164 8.707 1.00 7.79 N HETATM 22 CA AIB A 4 4.232 0.853 7.686 1.00 7.70 C HETATM 23 C AIB A 4 2.966 1.513 7.180 1.00 7.96 C HETATM 24 O1 AIB A 4 2.890 2.740 6.965 1.00 8.35 O HETATM 25 CB1 AIB A 4 4.884 0.147 6.447 1.00 10.30 C HETATM 26 CB2 AIB A 4 5.230 1.883 8.222 1.00 8.15 C HETATM 27 N AIB A 5 1.934 0.729 6.981 1.00 6.27 N HETATM 28 CA AIB A 5 0.663 1.236 6.468 1.00 6.89 C HETATM 29 C AIB A 5 0.185 2.406 7.316 1.00 7.88 C HETATM 30 O1 AIB A 5 -0.100 3.493 6.823 1.00 8.54 O HETATM 31 CB1 AIB A 5 -0.373 0.109 6.503 1.00 8.47 C HETATM 32 CB2 AIB A 5 0.836 1.718 5.011 1.00 9.23 C HETATM 33 N DIV A 6 0.167 2.148 8.634 1.00 7.12 N HETATM 34 CA DIV A 6 -0.253 3.141 9.610 1.00 7.05 C HETATM 35 CB1 DIV A 6 -1.713 3.539 9.354 1.00 9.23 C HETATM 36 CG1 DIV A 6 -2.397 4.188 10.534 1.00 25.33 C HETATM 37 CB2 DIV A 6 -0.100 2.475 11.023 1.00 8.89 C HETATM 38 C DIV A 6 0.593 4.375 9.564 1.00 5.89 C HETATM 39 O DIV A 6 0.167 5.539 9.554 1.00 8.17 O ATOM 40 N GLY A 7 1.912 4.182 9.598 1.00 6.19 N ATOM 41 CA GLY A 7 2.886 5.254 9.704 1.00 7.19 C ATOM 42 C GLY A 7 2.914 6.174 8.512 1.00 5.35 C ATOM 43 O GLY A 7 3.063 7.385 8.629 1.00 7.75 O ATOM 44 N LEU A 8 2.780 5.597 7.330 1.00 5.64 N ATOM 45 CA LEU A 8 2.854 6.397 6.095 1.00 6.70 C ATOM 46 C LEU A 8 1.574 7.165 5.870 1.00 6.54 C ATOM 47 O LEU A 8 1.656 8.343 5.433 1.00 7.30 O ATOM 48 CB LEU A 8 3.220 5.497 4.921 1.00 7.21 C ATOM 49 CG LEU A 8 4.556 4.764 5.027 1.00 7.63 C ATOM 50 CD1 LEU A 8 4.764 3.818 3.841 1.00 11.77 C ATOM 51 CD2 LEU A 8 5.731 5.755 5.065 1.00 16.31 C HETATM 52 N AIB A 9 0.409 6.608 6.146 1.00 4.35 N HETATM 53 CA AIB A 9 -0.870 7.294 6.066 1.00 5.85 C HETATM 54 C AIB A 9 -1.001 8.403 7.100 1.00 5.94 C HETATM 55 O1 AIB A 9 -1.715 9.391 6.881 1.00 6.16 O HETATM 56 CB1 AIB A 9 -2.001 6.270 6.447 1.00 6.76 C HETATM 57 CB2 AIB A 9 -1.177 7.821 4.660 1.00 8.38 C HETATM 58 N AIB A 10 -0.413 8.141 8.272 1.00 5.08 N HETATM 59 CA AIB A 10 -0.770 8.895 9.491 1.00 4.94 C HETATM 60 C AIB A 10 -0.834 10.381 9.327 1.00 6.40 C HETATM 61 O1 AIB A 10 -1.777 11.044 9.800 1.00 5.57 O HETATM 62 CB1 AIB A 10 0.221 8.564 10.615 1.00 7.11 C HETATM 63 CB2 AIB A 10 -2.196 8.362 9.895 1.00 7.37 C HETATM 64 N HYP A 11 0.143 11.039 8.731 1.00 4.40 N HETATM 65 CA HYP A 11 0.131 12.494 8.662 1.00 6.09 C HETATM 66 C HYP A 11 -1.009 13.013 7.815 1.00 5.05 C HETATM 67 O HYP A 11 -1.261 14.254 7.917 1.00 8.19 O HETATM 68 CB HYP A 11 1.480 12.860 8.029 1.00 7.19 C HETATM 69 CG HYP A 11 2.340 11.650 8.211 1.00 5.68 C HETATM 70 CD HYP A 11 1.376 10.469 8.125 1.00 5.74 C HETATM 71 OD HYP A 11 2.921 11.622 9.531 1.00 5.58 O ATOM 72 N GLN A 12 -1.654 12.215 7.006 1.00 3.92 N ATOM 73 CA GLN A 12 -2.721 12.693 6.138 1.00 5.80 C ATOM 74 C GLN A 12 -4.078 12.603 6.823 1.00 7.39 C ATOM 75 O GLN A 12 -5.049 13.233 6.380 1.00 7.66 O ATOM 76 CB GLN A 12 -2.789 11.904 4.829 1.00 5.53 C ATOM 77 CG GLN A 12 -1.453 11.787 4.130 1.00 5.88 C ATOM 78 CD GLN A 12 -0.667 13.054 4.056 1.00 7.55 C ATOM 79 OE1 GLN A 12 0.621 13.046 4.204 1.00 10.44 O ATOM 80 NE2 GLN A 12 -1.256 14.166 3.823 1.00 6.08 N HETATM 81 N DIV A 13 -4.148 11.862 7.933 1.00 6.43 N HETATM 82 CA DIV A 13 -5.419 11.605 8.616 1.00 7.28 C HETATM 83 CB1 DIV A 13 -6.309 10.714 7.757 1.00 8.98 C HETATM 84 CG1 DIV A 13 -5.691 9.373 7.401 1.00 13.62 C HETATM 85 CB2 DIV A 13 -5.067 10.879 9.967 1.00 9.55 C HETATM 86 C DIV A 13 -6.229 12.824 8.969 1.00 7.72 C HETATM 87 O DIV A 13 -7.475 12.754 8.957 1.00 8.18 O HETATM 88 N HYP A 14 -5.644 13.938 9.337 1.00 6.35 N HETATM 89 CA HYP A 14 -6.432 15.123 9.713 1.00 8.98 C HETATM 90 C HYP A 14 -7.180 15.789 8.577 1.00 9.98 C HETATM 91 O HYP A 14 -8.037 16.659 8.873 1.00 8.86 O HETATM 92 CB HYP A 14 -5.426 16.095 10.312 1.00 9.83 C HETATM 93 CG HYP A 14 -4.302 15.171 10.797 1.00 10.14 C HETATM 94 CD HYP A 14 -4.205 14.149 9.686 1.00 9.14 C HETATM 95 OD HYP A 14 -4.696 14.594 12.046 1.00 9.64 O HETATM 96 N AIB A 15 -6.799 15.551 7.333 1.00 8.32 N HETATM 97 CA AIB A 15 -7.356 16.335 6.212 1.00 9.38 C HETATM 98 C AIB A 15 -8.852 16.516 6.238 1.00 7.17 C HETATM 99 O1 AIB A 15 -9.338 17.629 5.905 1.00 9.81 O HETATM 100 CB1 AIB A 15 -7.001 15.658 4.893 1.00 11.12 C HETATM 101 CB2 AIB A 15 -6.657 17.731 6.270 1.00 11.85 C ATOM 102 N PRO A 16 -9.671 15.519 6.457 1.00 6.27 N ATOM 103 CA PRO A 16 -11.127 15.750 6.362 1.00 7.12 C ATOM 104 C PRO A 16 -11.667 16.516 7.581 1.00 7.10 C ATOM 105 O PRO A 16 -12.813 16.988 7.491 1.00 8.18 O ATOM 106 CB PRO A 16 -11.715 14.349 6.376 1.00 12.38 C ATOM 107 CG PRO A 16 -10.630 13.399 6.597 1.00 15.47 C ATOM 108 CD PRO A 16 -9.354 14.097 6.706 1.00 8.76 C HETATM 109 C PHL A 17 -11.017 18.626 10.000 1.00 9.22 C HETATM 110 O PHL A 17 -11.698 19.267 11.032 1.00 10.13 O HETATM 111 CA PHL A 17 -11.446 17.174 9.928 1.00 7.79 C HETATM 112 N PHL A 17 -10.941 16.569 8.676 1.00 8.43 N HETATM 113 CB PHL A 17 -10.894 16.353 11.096 1.00 9.14 C HETATM 114 CG PHL A 17 -11.366 14.934 11.120 1.00 10.68 C HETATM 115 CD1 PHL A 17 -12.662 14.608 11.496 1.00 14.34 C HETATM 116 CD2 PHL A 17 -10.525 13.900 10.713 1.00 13.72 C HETATM 117 CE1 PHL A 17 -13.121 13.312 11.481 1.00 15.62 C HETATM 118 CE2 PHL A 17 -10.955 12.597 10.731 1.00 16.10 C HETATM 119 CZ PHL A 17 -12.240 12.287 11.124 1.00 14.97 C TER 120 PHL A 17 HETATM 121 C ACE B 1 2.587 26.291 3.660 1.00 24.85 C HETATM 122 O ACE B 1 1.702 26.968 3.061 1.00 29.42 O HETATM 123 CH3 ACE B 1 2.872 25.053 3.359 1.00 10.13 C ATOM 124 N PHE B 2 3.272 26.808 4.680 1.00 28.86 N ATOM 125 CA PHE B 2 4.220 26.024 5.445 1.00 34.44 C ATOM 126 C PHE B 2 3.657 25.348 6.683 1.00 33.73 C ATOM 127 O PHE B 2 4.245 25.535 7.784 1.00 45.01 O ATOM 128 CB PHE B 2 5.493 26.802 5.689 1.00 42.04 C ATOM 129 CG PHE B 2 5.701 27.953 4.701 1.00 45.62 C ATOM 130 CD1 PHE B 2 6.284 27.726 3.468 1.00 48.24 C ATOM 131 CD2 PHE B 2 5.283 29.232 5.012 1.00 46.77 C ATOM 132 CE1 PHE B 2 6.484 28.774 2.583 1.00 50.12 C ATOM 133 CE2 PHE B 2 5.442 30.281 4.125 1.00 45.36 C ATOM 134 CZ PHE B 2 6.060 30.053 2.903 1.00 48.80 C HETATM 135 N AIB B 3 2.612 24.605 6.553 1.00 28.84 N HETATM 136 CA AIB B 3 1.780 23.730 7.269 1.00 30.29 C HETATM 137 C AIB B 3 1.469 22.494 6.359 1.00 27.68 C HETATM 138 O1 AIB B 3 1.822 21.383 6.683 1.00 31.21 O HETATM 139 CB1 AIB B 3 0.404 24.344 7.608 1.00 39.62 C HETATM 140 CB2 AIB B 3 2.423 23.175 8.543 1.00 39.95 C HETATM 141 N AIB B 4 0.977 22.871 5.191 1.00 21.13 N HETATM 142 CA AIB B 4 0.806 21.893 4.119 1.00 26.81 C HETATM 143 C AIB B 4 2.182 21.241 3.860 1.00 26.03 C HETATM 144 O1 AIB B 4 2.277 20.061 3.609 1.00 23.45 O HETATM 145 CB1 AIB B 4 0.415 22.647 2.835 1.00 25.87 C HETATM 146 CB2 AIB B 4 -0.197 20.829 4.493 1.00 29.60 C HETATM 147 N AIB B 5 3.215 22.120 3.879 1.00 17.16 N HETATM 148 CA AIB B 5 4.511 21.589 3.452 1.00 15.10 C HETATM 149 C AIB B 5 4.928 20.396 4.293 1.00 9.75 C HETATM 150 O1 AIB B 5 5.249 19.314 3.752 1.00 10.68 O HETATM 151 CB1 AIB B 5 5.568 22.677 3.485 1.00 14.02 C HETATM 152 CB2 AIB B 5 4.315 21.110 1.972 1.00 19.92 C HETATM 153 N DIV B 6 4.963 20.569 5.604 1.00 7.57 N HETATM 154 CA DIV B 6 5.401 19.558 6.529 1.00 8.21 C HETATM 155 CB1 DIV B 6 6.886 19.276 6.417 1.00 10.05 C HETATM 156 CG1 DIV B 6 7.792 20.473 6.710 1.00 14.33 C HETATM 157 CB2 DIV B 6 5.049 19.986 7.977 1.00 10.30 C HETATM 158 C DIV B 6 4.644 18.251 6.251 1.00 8.19 C HETATM 159 O DIV B 6 5.182 17.157 6.236 1.00 7.86 O ATOM 160 N GLY B 7 3.316 18.385 6.075 1.00 6.46 N ATOM 161 CA GLY B 7 2.443 17.239 5.931 1.00 7.68 C ATOM 162 C GLY B 7 2.679 16.447 4.655 1.00 8.32 C ATOM 163 O GLY B 7 2.580 15.227 4.648 1.00 8.71 O ATOM 164 N LEU B 8 2.966 17.149 3.551 1.00 6.85 N ATOM 165 CA LEU B 8 3.168 16.442 2.276 1.00 6.67 C ATOM 166 C LEU B 8 4.502 15.737 2.188 1.00 6.52 C ATOM 167 O LEU B 8 4.624 14.656 1.581 1.00 6.34 O ATOM 168 CB LEU B 8 2.990 17.446 1.125 1.00 9.41 C ATOM 169 CG LEU B 8 1.631 18.187 1.170 1.00 9.79 C ATOM 170 CD1 LEU B 8 1.465 19.094 -0.021 1.00 13.50 C ATOM 171 CD2 LEU B 8 0.484 17.207 1.304 1.00 14.37 C HETATM 172 N AIB B 9 5.548 16.307 2.799 1.00 6.56 N HETATM 173 CA AIB B 9 6.852 15.712 2.909 1.00 5.48 C HETATM 174 C AIB B 9 6.835 14.494 3.813 1.00 6.95 C HETATM 175 O1 AIB B 9 7.565 13.522 3.611 1.00 6.68 O HETATM 176 CB1 AIB B 9 7.808 16.749 3.575 1.00 7.60 C HETATM 177 CB2 AIB B 9 7.430 15.347 1.532 1.00 7.93 C HETATM 178 N AIB B 10 6.011 14.587 4.878 1.00 5.09 N HETATM 179 CA AIB B 10 6.137 13.658 6.017 1.00 5.66 C HETATM 180 C AIB B 10 6.248 12.207 5.647 1.00 5.17 C HETATM 181 O1 AIB B 10 7.122 11.494 6.236 1.00 5.95 O HETATM 182 CB1 AIB B 10 4.917 13.883 6.935 1.00 6.85 C HETATM 183 CB2 AIB B 10 7.428 14.077 6.810 1.00 6.63 C HETATM 184 N HYP B 11 5.415 11.643 4.799 1.00 4.51 N HETATM 185 CA HYP B 11 5.483 10.202 4.542 1.00 6.03 C HETATM 186 C HYP B 11 6.795 9.767 3.916 1.00 8.18 C HETATM 187 O HYP B 11 7.079 8.549 3.902 1.00 7.49 O HETATM 188 CB HYP B 11 4.328 9.923 3.590 1.00 7.79 C HETATM 189 CG HYP B 11 3.401 11.092 3.732 1.00 4.97 C HETATM 190 CD HYP B 11 4.332 12.263 4.034 1.00 4.93 C HETATM 191 OD HYP B 11 2.551 10.876 4.916 1.00 6.05 O ATOM 192 N GLN B 12 7.567 10.679 3.352 1.00 6.63 N ATOM 193 CA GLN B 12 8.850 10.274 2.747 1.00 5.77 C ATOM 194 C GLN B 12 9.980 10.282 3.738 1.00 5.60 C ATOM 195 O GLN B 12 11.080 9.745 3.411 1.00 7.87 O ATOM 196 CB GLN B 12 9.170 11.244 1.593 1.00 6.51 C ATOM 197 CG GLN B 12 8.013 11.438 0.611 1.00 6.31 C ATOM 198 CD GLN B 12 7.370 10.189 0.127 1.00 7.07 C ATOM 199 OE1 GLN B 12 8.104 9.173 -0.156 1.00 9.28 O ATOM 200 NE2 GLN B 12 6.068 10.100 0.027 1.00 7.28 N HETATM 201 N DIV B 13 9.830 10.804 4.941 1.00 5.65 N HETATM 202 CA DIV B 13 10.873 10.914 5.934 1.00 5.28 C HETATM 203 CB1 DIV B 13 11.941 11.949 5.483 1.00 7.70 C HETATM 204 CG1 DIV B 13 11.297 13.303 5.149 1.00 11.10 C HETATM 205 CB2 DIV B 13 10.266 11.396 7.275 1.00 7.30 C HETATM 206 C DIV B 13 11.616 9.613 6.189 1.00 7.25 C HETATM 207 O DIV B 13 12.813 9.628 6.476 1.00 8.66 O HETATM 208 N HYP B 14 10.928 8.457 6.201 1.00 6.47 N HETATM 209 CA HYP B 14 11.632 7.219 6.508 1.00 8.28 C HETATM 210 C HYP B 14 12.565 6.719 5.428 1.00 10.34 C HETATM 211 O HYP B 14 13.320 5.761 5.758 1.00 11.64 O HETATM 212 CB HYP B 14 10.535 6.172 6.760 1.00 9.09 C HETATM 213 CG HYP B 14 9.316 7.013 7.131 1.00 7.61 C HETATM 214 CD HYP B 14 9.447 8.234 6.201 1.00 5.53 C HETATM 215 OD HYP B 14 9.419 7.423 8.500 1.00 9.83 O HETATM 216 N AIB B 15 12.524 7.257 4.234 1.00 10.66 N HETATM 217 CA AIB B 15 13.325 6.713 3.103 1.00 11.53 C HETATM 218 C AIB B 15 14.764 6.441 3.459 1.00 9.90 C HETATM 219 O1 AIB B 15 15.283 5.340 3.096 1.00 12.59 O HETATM 220 CB1 AIB B 15 13.270 7.708 1.931 1.00 12.28 C HETATM 221 CB2 AIB B 15 12.634 5.383 2.694 1.00 14.81 C ATOM 222 N PRO B 16 15.488 7.310 4.102 1.00 10.42 N ATOM 223 CA PRO B 16 16.912 6.996 4.392 1.00 9.30 C ATOM 224 C PRO B 16 17.140 6.032 5.514 1.00 11.65 C ATOM 225 O PRO B 16 18.318 5.587 5.684 1.00 13.90 O ATOM 226 CB PRO B 16 17.531 8.328 4.691 1.00 13.60 C ATOM 227 CG PRO B 16 16.504 9.364 4.525 1.00 14.88 C ATOM 228 CD PRO B 16 15.175 8.674 4.611 1.00 13.40 C HETATM 229 C PHL B 17 15.775 3.475 7.194 1.00 21.21 C HETATM 230 O PHL B 17 16.542 2.697 6.392 1.00 21.67 O HETATM 231 CA PHL B 17 16.323 4.855 7.486 1.00 13.92 C HETATM 232 N PHL B 17 16.133 5.718 6.298 1.00 9.75 N HETATM 233 CB PHL B 17 15.610 5.514 8.681 1.00 16.99 C HETATM 234 CG PHL B 17 16.010 6.930 8.916 1.00 10.79 C HETATM 235 CD1 PHL B 17 17.183 7.212 9.645 1.00 14.32 C HETATM 236 CD2 PHL B 17 15.295 8.012 8.463 1.00 11.28 C HETATM 237 CE1 PHL B 17 17.565 8.517 9.860 1.00 15.52 C HETATM 238 CE2 PHL B 17 15.670 9.312 8.636 1.00 13.03 C HETATM 239 CZ PHL B 17 16.860 9.577 9.334 1.00 16.57 C TER 240 PHL B 17 HETATM 241 C MOH 1 -9.104 19.596 2.871 1.00 32.55 C HETATM 242 O MOH 1 -9.039 19.786 4.245 1.00 13.06 O HETATM 243 C MOH 2 14.846 2.101 2.670 1.00 38.93 C HETATM 244 O MOH 2 14.655 2.391 4.036 1.00 31.98 O HETATM 245 C MOH 3 -15.131 17.431 4.958 1.00 16.57 C HETATM 246 O MOH 3 -16.001 17.489 6.099 1.00 24.27 O HETATM 247 C MOH 4 -16.077 15.353 10.500 1.00 18.86 C HETATM 248 O MOH 4 -15.846 14.932 9.164 1.00 31.76 O HETATM 249 C MOH 5 8.576 6.323 1.956 1.00 19.11 C HETATM 250 O MOH 5 7.320 6.849 1.620 1.00 32.20 O HETATM 251 C MOH 6 -7.258 10.203 12.697 1.00 15.38 C HETATM 252 O MOH 6 -7.658 11.552 12.569 1.00 23.12 O HETATM 253 C MOH 7 -2.431 16.770 5.992 1.00 34.52 C HETATM 254 O MOH 7 -2.152 18.081 5.549 1.00 45.41 O HETATM 255 O MOH 8 -3.148 -0.104 11.715 1.00 37.97 O HETATM 256 O MOH 9 4.341 28.668 8.342 1.00 41.90 O HETATM 257 O MOH 10 -2.572 19.932 3.594 1.00 59.74 O HETATM 258 O MOH 11 11.917 2.498 5.871 1.00 47.73 O HETATM 259 O MOH 12 -6.707 19.782 2.905 1.00 45.01 O HETATM 260 O MOH 13 14.848 5.767 8.783 1.00 38.20 O HETATM 261 O MOH 14 9.031 3.274 5.523 1.00 46.44 O HETATM 262 O MOH 15 -6.975 23.471 4.885 1.00 56.37 O HETATM 263 O MOH 16 -1.900 22.062 1.538 1.00 51.92 O HETATM 264 O MOH 17 12.172 2.480 8.190 1.00 54.82 O HETATM 265 O MOH 18 -2.782 20.731 8.046 1.00 53.23 O HETATM 266 O MOH 19 8.255 4.166 9.062 1.00 48.65 O HETATM 267 O MOH 20 9.578 0.127 8.470 1.00 57.75 O HETATM 268 O MOH 21 8.367 4.496 1.820 1.00 71.46 O HETATM 269 O MOH 22 9.293 0.709 10.916 1.00 59.91 O HETATM 270 O MOH 23 12.757 -0.012 5.636 1.00 49.42 O CONECT 1 2 3 4 CONECT 2 1 CONECT 3 1 CONECT 4 1 5 CONECT 6 5 7 15 CONECT 15 6 16 CONECT 16 15 17 19 20 CONECT 17 16 18 21 CONECT 18 17 CONECT 19 16 CONECT 20 16 CONECT 21 17 22 CONECT 22 21 23 25 26 CONECT 23 22 24 27 CONECT 24 23 CONECT 25 22 CONECT 26 22 CONECT 27 23 28 CONECT 28 27 29 31 32 CONECT 29 28 30 33 CONECT 30 29 CONECT 31 28 CONECT 32 28 CONECT 33 29 34 CONECT 34 33 35 37 38 CONECT 35 34 36 CONECT 36 35 CONECT 37 34 CONECT 38 34 39 40 CONECT 39 38 CONECT 40 38 41 CONECT 46 45 47 52 CONECT 52 46 53 CONECT 53 52 54 56 57 CONECT 54 53 55 58 CONECT 55 54 CONECT 56 53 CONECT 57 53 CONECT 58 54 59 CONECT 59 58 60 62 63 CONECT 60 59 61 64 CONECT 61 60 CONECT 62 59 CONECT 63 59 CONECT 64 60 65 70 CONECT 65 64 66 68 CONECT 66 65 67 72 CONECT 67 66 CONECT 68 65 69 CONECT 69 68 70 71 CONECT 70 64 69 CONECT 71 69 CONECT 72 66 73 CONECT 74 73 75 81 CONECT 81 74 82 CONECT 82 81 83 85 86 CONECT 83 82 84 CONECT 84 83 CONECT 85 82 CONECT 86 82 87 88 CONECT 87 86 CONECT 88 86 89 94 CONECT 89 88 90 92 CONECT 90 89 91 96 CONECT 91 90 CONECT 92 89 93 CONECT 93 92 94 95 CONECT 94 88 93 CONECT 95 93 CONECT 96 90 97 CONECT 97 96 98 100 101 CONECT 98 97 99 102 CONECT 99 98 CONECT 100 97 CONECT 101 97 CONECT 102 98 103 108 CONECT 104 103 105 112 CONECT 109 110 111 CONECT 110 109 CONECT 111 109 112 113 CONECT 112 104 111 CONECT 113 111 114 CONECT 114 113 115 116 CONECT 115 114 117 CONECT 116 114 118 CONECT 117 115 119 CONECT 118 116 119 CONECT 119 117 118 CONECT 121 122 123 124 CONECT 122 121 CONECT 123 121 CONECT 124 121 125 CONECT 126 125 127 135 CONECT 135 126 136 CONECT 136 135 137 139 140 CONECT 137 136 138 141 CONECT 138 137 CONECT 139 136 CONECT 140 136 CONECT 141 137 142 CONECT 142 141 143 145 146 CONECT 143 142 144 147 CONECT 144 143 CONECT 145 142 CONECT 146 142 CONECT 147 143 148 CONECT 148 147 149 151 152 CONECT 149 148 150 153 CONECT 150 149 CONECT 151 148 CONECT 152 148 CONECT 153 149 154 CONECT 154 153 155 157 158 CONECT 155 154 156 CONECT 156 155 CONECT 157 154 CONECT 158 154 159 160 CONECT 159 158 CONECT 160 158 161 CONECT 166 165 167 172 CONECT 172 166 173 CONECT 173 172 174 176 177 CONECT 174 173 175 178 CONECT 175 174 CONECT 176 173 CONECT 177 173 CONECT 178 174 179 CONECT 179 178 180 182 183 CONECT 180 179 181 184 CONECT 181 180 CONECT 182 179 CONECT 183 179 CONECT 184 180 185 190 CONECT 185 184 186 188 CONECT 186 185 187 192 CONECT 187 186 CONECT 188 185 189 CONECT 189 188 190 191 CONECT 190 184 189 CONECT 191 189 CONECT 192 186 193 CONECT 194 193 195 201 CONECT 201 194 202 CONECT 202 201 203 205 206 CONECT 203 202 204 CONECT 204 203 CONECT 205 202 CONECT 206 202 207 208 CONECT 207 206 CONECT 208 206 209 214 CONECT 209 208 210 212 CONECT 210 209 211 216 CONECT 211 210 CONECT 212 209 213 CONECT 213 212 214 215 CONECT 214 208 213 CONECT 215 213 CONECT 216 210 217 CONECT 217 216 218 220 221 CONECT 218 217 219 222 CONECT 219 218 CONECT 220 217 CONECT 221 217 CONECT 222 218 223 228 CONECT 224 223 225 232 CONECT 229 230 231 CONECT 230 229 CONECT 231 229 232 233 CONECT 232 224 231 CONECT 233 231 234 CONECT 234 233 235 236 CONECT 235 234 237 CONECT 236 234 238 CONECT 237 235 239 CONECT 238 236 239 CONECT 239 237 238 CONECT 241 242 CONECT 242 241 CONECT 243 244 CONECT 244 243 CONECT 245 246 CONECT 246 245 CONECT 247 248 CONECT 248 247 CONECT 249 250 CONECT 250 249 CONECT 251 252 CONECT 252 251 CONECT 253 254 CONECT 254 253 MASTER 224 0 47 2 0 2 0 9 268 2 190 4 END