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HEADER IMMUNOGLOBULIN 02-AUG-03 1OL0 TITLE CRYSTAL STRUCTURE OF A CAMELISED HUMAN VH COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN G; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: VARIABLE HEAVY DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: B834 KEYWDS IMMUNOGLOBULIN, CAMELISED VARIABLE HEAVY DOMAIN EXPDTA X-RAY DIFFRACTION AUTHOR T.DOTTORINI,C.K.VAUGHAN,M.A.WALSH,P.LOSURDO,M.SOLLAZZO REVDAT 1 22-JAN-04 1OL0 0 JRNL AUTH T.DOTTORINI,C.K.VAUGHAN,M.A.WALSH,P.LOSURDO, JRNL AUTH 2 M.SOLLAZZO JRNL TITL CRYSTAL STRUCTURE OF A HUMAN VH: REQUIREMENTS FOR JRNL TITL 2 MAINTAINING A MONOMERIC FRAGMENT. JRNL REF BIOCHEMISTRY V. 43 622 2004 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.DIMARCO,M.RIZZI,C.VOLPARI,M.A.WALSH,F.NARJES, REMARK 1 AUTH 2 S.COLARUSSO,R.DEFRANCESCO,V.G.MATASSA,M.SOLLAZZO REMARK 1 TITL INHIBITION OF THE HEPATITIS C VIRUS NS3/4A REMARK 1 TITL 2 PROTEASE. THE CRYSTAL STRUCTURES OF TWO REMARK 1 TITL 3 PROTEASE-INHIBITOR COMPLEXES REMARK 1 REF J.BIOL.CHEM. V. 275 7152 2000 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REFERENCE 2 REMARK 1 AUTH F.MARTIN,C.VOLPARI,C.STEINKUHLER,M.DIMASIBRUNETTI, REMARK 1 AUTH 2 G.BIASIOL,S.ALTAMURA,R.CORTESE,R.DEFRANCESCO, REMARK 1 AUTH 3 M.SOLLAZZO REMARK 1 TITL AFFINITY SELECTION OF A CAMELIZED V(H) DOMAIN REMARK 1 TITL 2 ANTIBODY INHIBITOR OF HEPATITIS C VIRUS NS3 REMARK 1 TITL 3 PROTEASE REMARK 1 REF PROTEIN ENG. V. 10 607 1997 REMARK 1 REFN ASTM PRENE9 UK ISSN 0269-2139 REMARK 1 REFERENCE 3 REMARK 1 AUTH L.RIECHMANN REMARK 1 TITL REARRANGEMENT OF THE FORMER VL INTERFACE IN THE REMARK 1 TITL 2 SOLUTION STRUCTURE OF A CAMELISED, SINGLE ANTIBODY REMARK 1 TITL 3 VH DOMAIN REMARK 1 REF J.MOL.BIOL. V. 259 957 1996 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.24 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0 REMARK 3 NUMBER OF REFLECTIONS : 29892 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT EXCEPT IN LAST REMARK 3 RO REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.156 REMARK 3 R VALUE (WORKING SET) : 0.154 REMARK 3 FREE R VALUE : 0.180 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1506 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1818 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 87 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) : 17.34 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00000 REMARK 3 B22 (A**2) : 0.00000 REMARK 3 B33 (A**2) : 0.00000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OL0 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-13218 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-2000 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : DIAMON 100/GE 220 REMARK 200 OPTICS : TOROIDAL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29910 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83 REMARK 200 COMPLETENESS FOR SHELL (%) : 71.5 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.22700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1HCV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,2/3+Z REMARK 290 3555 -X+Y,-X,1/3+Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,1/3-Z REMARK 290 6555 -X,-X+Y,2/3-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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.85333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.92667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 33.92667 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 67.85333 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 2 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, B, Y, 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 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 Y 57 O HOH Y 147 2.08 REMARK 500 O HOH Y 92 O HOH Y 99 2.10 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 GLY B 9 NZ LYS A 43 2654 2.13 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A DBREF 1OL0 A 1 121 PDB 1OL0 1OL0 1 121 DBREF 1OL0 B 1 121 PDB 1OL0 1OL0 1 121 SEQRES 1 A 121 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 121 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 121 PHE THR PHE SER SER TYR ALA MSE SER TRP PHE ARG GLN SEQRES 4 A 121 ALA PRO GLY LYS GLU ARG GLU ILE VAL SER ALA VAL SER SEQRES 5 A 121 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL ARG SEQRES 6 A 121 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 121 LEU TYR LEU GLN MSE ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 121 ALA VAL TYR TYR CYS ALA ARG GLU PRO ARG ILE PRO ARG SEQRES 9 A 121 PRO PRO SER PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 A 121 THR VAL SER SER SEQRES 1 B 121 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 121 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 121 PHE THR PHE SER SER TYR ALA MSE SER TRP PHE ARG GLN SEQRES 4 B 121 ALA PRO GLY LYS GLU ARG GLU ILE VAL SER ALA VAL SER SEQRES 5 B 121 GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL ARG SEQRES 6 B 121 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 121 LEU TYR LEU GLN MSE ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 121 ALA VAL TYR TYR CYS ALA ARG GLU PRO ARG ILE PRO ARG SEQRES 9 B 121 PRO PRO SER PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 B 121 THR VAL SER SER MODRES 1OL0 MSE A 34 MET SELENOMETHIONINE MODRES 1OL0 MSE A 83 MET SELENOMETHIONINE MODRES 1OL0 MSE B 34 MET SELENOMETHIONINE MODRES 1OL0 MSE B 83 MET SELENOMETHIONINE HET MSE A 34 8 HET MSE A 83 8 HET MSE B 34 8 HET MSE B 83 8 HET SO4 A1122 5 HET SO4 B1122 5 HET SO4 B1123 5 HET SO4 B1124 5 HET SO4 B1125 5 HET GOL A1123 6 HET GOL A1124 6 HET GOL A1125 6 HET GOL A1126 6 HET GOL B1126 6 HETNAM MSE SELENOMETHIONINE HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL FORMUL 1 MSE 4(C5 H11 N O2 SE) FORMUL 3 SO4 5(O4 S 2-) FORMUL 8 GOL 5(C3 H8 O3) FORMUL 13 HOH *388(H2 O) HELIX 1 1 THR A 28 TYR A 32 5 5 HELIX 2 2 ASP A 62 ARG A 65 5 4 HELIX 3 3 ARG A 87 THR A 91 5 5 HELIX 4 4 PRO A 105 ASP A 109 5 5 HELIX 5 5 THR B 28 TYR B 32 5 5 HELIX 6 6 ASP B 62 ARG B 65 5 4 HELIX 7 7 ARG B 87 THR B 91 5 5 HELIX 8 8 PRO B 105 ASP B 109 5 5 SHEET 1 AA 4 GLN A 3 GLY A 8 0 SHEET 2 AA 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA 4 THR A 78 MSE A 83 -1 O LEU A 79 N CYS A 22 SHEET 4 AA 4 PHE A 68 ASP A 73 -1 O THR A 69 N GLN A 82 SHEET 1 AB 6 GLY A 10 VAL A 12 0 SHEET 2 AB 6 THR A 115 VAL A 119 1 O LEU A 116 N GLY A 10 SHEET 3 AB 6 ALA A 92 ARG A 98 -1 O ALA A 92 N VAL A 117 SHEET 4 AB 6 MSE A 34 GLN A 39 -1 O SER A 35 N ALA A 97 SHEET 5 AB 6 GLU A 46 VAL A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AB 6 THR A 58 TYR A 60 -1 O TYR A 59 N ALA A 50 SHEET 1 AC 4 GLY A 10 VAL A 12 0 SHEET 2 AC 4 THR A 115 VAL A 119 1 O LEU A 116 N GLY A 10 SHEET 3 AC 4 ALA A 92 ARG A 98 -1 O ALA A 92 N VAL A 117 SHEET 4 AC 4 TYR A 110 TRP A 111 -1 O TYR A 110 N ARG A 98 SHEET 1 BA 4 GLN B 3 GLY B 8 0 SHEET 2 BA 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 BA 4 THR B 78 MSE B 83 -1 O LEU B 79 N CYS B 22 SHEET 4 BA 4 PHE B 68 ASP B 73 -1 O THR B 69 N GLN B 82 SHEET 1 BB 6 GLY B 10 VAL B 12 0 SHEET 2 BB 6 THR B 115 VAL B 119 1 O LEU B 116 N GLY B 10 SHEET 3 BB 6 ALA B 92 ARG B 98 -1 O ALA B 92 N VAL B 117 SHEET 4 BB 6 MSE B 34 GLN B 39 -1 O SER B 35 N ALA B 97 SHEET 5 BB 6 GLU B 46 VAL B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 BB 6 THR B 58 TYR B 60 -1 O TYR B 59 N ALA B 50 SHEET 1 BC 4 GLY B 10 VAL B 12 0 SHEET 2 BC 4 THR B 115 VAL B 119 1 O LEU B 116 N GLY B 10 SHEET 3 BC 4 ALA B 92 ARG B 98 -1 O ALA B 92 N VAL B 117 SHEET 4 BC 4 TYR B 110 TRP B 111 -1 O TYR B 110 N ARG B 98 SSBOND 1 CYS A 22 CYS A 96 SSBOND 2 CYS B 22 CYS B 96 LINK C ALA A 33 N MSE A 34 LINK C MSE A 34 N SER A 35 LINK C GLN A 82 N MSE A 83 LINK C MSE A 83 N ASN A 84 LINK C ALA B 33 N MSE B 34 LINK C MSE B 34 N SER B 35 LINK C GLN B 82 N MSE B 83 LINK C MSE B 83 N ASN B 84 CISPEP 1 ILE A 102 PRO A 103 0 -1.63 CISPEP 2 ILE B 102 PRO B 103 0 -1.83 SITE 1 AC1 10 GLY A 8 GLU B 44 ARG B 45 HOH Y 74 SITE 2 AC1 10 HOH Y 117 HOH Y 180 HOH Y 181 HOH Y 182 SITE 3 AC1 10 HOH Y 183 HOH Y 184 SITE 1 AC2 4 ARG A 65 ARG B 104 HOH Y 186 HOH Z 105 SITE 1 AC3 5 PHE B 27 THR B 28 TYR B 32 ARG B 101 SITE 2 AC3 5 HOH Y 49 SITE 1 AC4 4 ARG A 104 ARG B 65 HOH Y 91 HOH Y 187 SITE 1 AC5 6 PHE A 27 THR A 28 TYR A 32 ARG A 101 SITE 2 AC5 6 HOH Z 47 HOH Z 197 SITE 1 AC6 7 THR A 58 TYR A 60 THR B 58 TYR B 60 SITE 2 AC6 7 HOH Y 105 HOH Z 130 HOH Z 198 SITE 1 AC7 5 GLU B 46 ASP B 62 SER B 63 HOH Y 188 SITE 2 AC7 5 HOH Y 189 SITE 1 AC8 6 GLN A 13 SER A 120 SER A 121 PRO B 41 SITE 2 AC8 6 HOH Z 16 HOH Z 199 SITE 1 AC9 5 ARG A 19 ARG B 19 HOH Y 118 HOH Z 34 SITE 2 AC9 5 HOH Z 147 SITE 1 BC1 5 PHE A 27 THR A 28 PHE A 29 ASN A 77 SITE 2 BC1 5 HOH Z 49 CRYST1 75.300 75.300 101.780 90.00 90.00 120.00 P 32 2 1 12 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 0.013280 0.007667 0.000000 0.00000 SCALE2 0.000000 0.015335 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009825 0.00000 MTRIX1 1 -0.999943 -0.009568 -0.004770 95.64020 1 MTRIX2 1 0.001752 -0.586769 0.809753 37.70880 1 MTRIX3 1 -0.010547 0.809698 0.586752 -18.93450 1