HEADER ANTITUMOR PROTEIN 16-JUN-25 9P4C TITLE CRYSTAL STRUCTURE OF MESOTHELIN C-TERMINAL PEPTIDE-RO4 FAB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN OF THE RO4 FAB FRAGMENT; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEAVY CHAIN OF THE RO4 FAB FRAGMENT; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MESOTHELIN, CLEAVED FORM; COMPND 11 CHAIN: M; COMPND 12 FRAGMENT: C-TERMINAL PEPTIDE (UNP RESIDUES 590-606); COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_TAXID: 9986; SOURCE 4 EXPRESSION_SYSTEM: ORYCTOLAGUS CUNICULUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9986; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 8 ORGANISM_TAXID: 9986; SOURCE 9 EXPRESSION_SYSTEM: ORYCTOLAGUS CUNICULUS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9986; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606 KEYWDS MESOTHELIN, ANTIBODY, IMMUNE SYSTEM, ANTITUMOR PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.ZHAN,C.MASLANKA,D.XIA REVDAT 1 12-NOV-25 9P4C 0 JRNL AUTH J.ZHAN,D.XIA JRNL TITL STRUCTURAL ANALYSIS OF MONOCLONAL ANTIBODY RO4 WITH JRNL TITL 2 MESOTHELIN C-TERMINAL PEPTIDE JRNL REF ANTIB THER 2025 JRNL REFN ESSN 2516-4236 JRNL DOI 10.1093/ABT/TBAF022 REMARK 2 REMARK 2 RESOLUTION. 1.52 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.76 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2 REMARK 3 NUMBER OF REFLECTIONS : 64809 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.151 REMARK 3 R VALUE (WORKING SET) : 0.149 REMARK 3 FREE R VALUE : 0.180 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 3262 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 24.7600 - 4.3100 0.99 2858 182 0.1453 0.1471 REMARK 3 2 4.3100 - 3.4200 0.99 2859 149 0.1319 0.1502 REMARK 3 3 3.4200 - 2.9900 0.99 2824 145 0.1415 0.1753 REMARK 3 4 2.9900 - 2.7200 0.99 2839 135 0.1490 0.2022 REMARK 3 5 2.7200 - 2.5200 0.99 2799 156 0.1497 0.1642 REMARK 3 6 2.5200 - 2.3800 0.99 2842 120 0.1473 0.2087 REMARK 3 7 2.3800 - 2.2600 0.98 2765 142 0.1380 0.1879 REMARK 3 8 2.2600 - 2.1600 0.98 2783 162 0.1377 0.1485 REMARK 3 9 2.1600 - 2.0800 0.98 2791 141 0.1401 0.1730 REMARK 3 10 2.0800 - 2.0000 0.97 2765 139 0.1387 0.2084 REMARK 3 11 2.0000 - 1.9400 0.97 2731 159 0.1390 0.1593 REMARK 3 12 1.9400 - 1.8900 0.97 2768 125 0.1477 0.1979 REMARK 3 13 1.8900 - 1.8400 0.97 2763 135 0.1484 0.1929 REMARK 3 14 1.8400 - 1.7900 0.97 2726 163 0.1546 0.1862 REMARK 3 15 1.7900 - 1.7500 0.96 2754 134 0.1618 0.1913 REMARK 3 16 1.7500 - 1.7100 0.96 2728 149 0.1688 0.2273 REMARK 3 17 1.7100 - 1.6800 0.96 2706 156 0.1723 0.2010 REMARK 3 18 1.6800 - 1.6500 0.96 2741 121 0.1777 0.1905 REMARK 3 19 1.6500 - 1.6200 0.94 2656 151 0.1828 0.2406 REMARK 3 20 1.6200 - 1.5900 0.91 2566 142 0.1995 0.2494 REMARK 3 21 1.5900 - 1.5700 0.89 2534 134 0.2272 0.2861 REMARK 3 22 1.5700 - 1.5400 0.74 2072 112 0.2240 0.2474 REMARK 3 23 1.5400 - 1.5200 0.60 1677 110 0.2548 0.3069 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.149 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.142 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.07 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.009 3311 REMARK 3 ANGLE : 1.067 4532 REMARK 3 CHIRALITY : 0.062 552 REMARK 3 PLANARITY : 0.009 572 REMARK 3 DIHEDRAL : 12.090 1145 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9P4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000296732. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-NOV-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64882 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 19.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57 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 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: BALBES REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, PH 6.5 AND 16% PEG REMARK 280 10000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 46.48000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.41750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 46.48000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.41750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4880 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19110 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, M 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: 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER L 31 -125.23 53.93 REMARK 500 THR L 52 -44.58 70.43 REMARK 500 LYS L 143 76.41 45.30 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 758 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH L 759 DISTANCE = 6.02 ANGSTROMS REMARK 525 HOH L 760 DISTANCE = 6.08 ANGSTROMS REMARK 525 HOH H 649 DISTANCE = 6.07 ANGSTROMS DBREF 9P4C L 1 216 PDB 9P4C 9P4C 1 216 DBREF 9P4C H 1 211 PDB 9P4C 9P4C 1 211 DBREF 9P4C M 582 598 UNP Q13421 MSLN_HUMAN 590 606 SEQRES 1 L 216 ALA ASP VAL VAL MET THR GLN THR PRO SER SER VAL SER SEQRES 2 L 216 ALA ALA VAL GLY GLY THR VAL THR MET LYS CYS GLN ALA SEQRES 3 L 216 SER GLN SER ILE SER THR ALA LEU VAL TRP TYR GLN GLN SEQRES 4 L 216 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE ARG SER THR SEQRES 5 L 216 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 6 L 216 SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER ASP SEQRES 7 L 216 LEU GLU CYS ALA ASP ALA ALA THR TYR TYR CYS GLN SER SEQRES 8 L 216 ALA ALA LEU ILE GLY GLY VAL VAL PHE GLY ALA PHE GLY SEQRES 9 L 216 GLY GLY THR GLU VAL VAL VAL ARG GLY ASP PRO VAL ALA SEQRES 10 L 216 PRO THR VAL LEU ILE PHE PRO PRO ALA ALA ASP GLN VAL SEQRES 11 L 216 ALA THR GLY THR VAL THR ILE VAL CYS VAL ALA ASN LYS SEQRES 12 L 216 TYR PHE PRO ASP VAL THR VAL THR TRP GLU VAL ASP GLY SEQRES 13 L 216 THR THR GLN THR THR GLY ILE GLU ASN SER LYS THR PRO SEQRES 14 L 216 GLN ASN SER ALA ASP CYS THR TYR ASN LEU SER SER THR SEQRES 15 L 216 LEU THR LEU THR SER THR GLN TYR ASN SER HIS LYS GLU SEQRES 16 L 216 TYR THR CYS LYS VAL THR GLN GLY THR THR SER VAL VAL SEQRES 17 L 216 GLN SER PHE ASN ARG GLY ASP CYS SEQRES 1 H 211 PCA SER LEU GLU GLU SER GLY GLY GLY LEU VAL THR PRO SEQRES 2 H 211 GLY GLY ILE LEU THR LEU THR CYS THR ALA SER GLY PHE SEQRES 3 H 211 ASP ILE SER ARG HIS TYR MET THR TRP VAL ARG GLN ALA SEQRES 4 H 211 PRO GLY GLU GLY LEU GLU TRP ILE GLY SER ILE TYR GLY SEQRES 5 H 211 GLY SER THR TYR TYR ALA SER TRP ALA LYS GLY ARG PHE SEQRES 6 H 211 THR ILE SER LYS THR SER SER THR THR VAL ASP LEU LYS SEQRES 7 H 211 MET THR SER LEU THR THR GLU ASP THR ALA THR TYR PHE SEQRES 8 H 211 CYS VAL ARG GLY VAL GLY GLY GLY LEU TRP GLY PRO GLY SEQRES 9 H 211 THR LEU VAL THR VAL SER SER GLY GLN PRO LYS ALA PRO SEQRES 10 H 211 SER VAL PHE PRO LEU ALA PRO CYS CYS GLY ASP THR PRO SEQRES 11 H 211 SER SER THR VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 12 H 211 LEU PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY THR SEQRES 13 H 211 LEU THR ASN GLY VAL ARG THR PHE PRO SER VAL ARG GLN SEQRES 14 H 211 SER SER GLY LEU TYR SER LEU SER SER VAL VAL SER VAL SEQRES 15 H 211 THR SER SER SER GLN PRO VAL THR CYS ASN VAL ALA HIS SEQRES 16 H 211 PRO ALA THR ASN THR LYS VAL ASP LYS THR VAL ALA PRO SEQRES 17 H 211 SER THR CYS SEQRES 1 M 17 ILE PRO ASN GLY TYR LEU VAL LEU ASP LEU SER MET GLN SEQRES 2 M 17 GLU ALA LEU SER HET PCA H 1 14 HET GOL L 301 14 HETNAM PCA PYROGLUTAMIC ACID HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 PCA C5 H7 N O3 FORMUL 4 GOL C3 H8 O3 FORMUL 5 HOH *742(H2 O) HELIX 1 AA1 GLU L 80 ALA L 84 5 5 HELIX 2 AA2 GLN L 129 THR L 132 5 4 HELIX 3 AA3 SER L 187 SER L 192 1 6 HELIX 4 AA4 GLY L 214 CYS L 216 5 3 HELIX 5 AA5 ASP H 27 HIS H 31 5 5 HELIX 6 AA6 THR H 83 THR H 87 5 5 HELIX 7 AA7 SER H 154 THR H 156 5 3 HELIX 8 AA8 THR H 183 GLN H 187 5 5 HELIX 9 AA9 PRO H 196 ASN H 199 5 4 HELIX 10 AB1 LEU M 591 LEU M 597 1 7 SHEET 1 AA1 4 MET L 5 THR L 8 0 SHEET 2 AA1 4 VAL L 20 ALA L 26 -1 O LYS L 23 N THR L 8 SHEET 3 AA1 4 GLN L 71 ILE L 76 -1 O ILE L 76 N VAL L 20 SHEET 4 AA1 4 PHE L 63 SER L 68 -1 N LYS L 64 O THR L 75 SHEET 1 AA2 6 SER L 11 ALA L 15 0 SHEET 2 AA2 6 THR L 107 ARG L 112 1 O ARG L 112 N ALA L 14 SHEET 3 AA2 6 ALA L 85 SER L 91 -1 N ALA L 85 O VAL L 109 SHEET 4 AA2 6 LEU L 34 GLN L 39 -1 N TYR L 37 O TYR L 88 SHEET 5 AA2 6 LYS L 46 ARG L 50 -1 O LYS L 46 N GLN L 38 SHEET 6 AA2 6 THR L 54 LEU L 55 -1 O THR L 54 N ARG L 50 SHEET 1 AA3 3 VAL L 98 PHE L 100 0 SHEET 2 AA3 3 ALA L 93 ILE L 95 -1 N ALA L 93 O PHE L 100 SHEET 3 AA3 3 VAL M 588 ASP M 590 -1 O LEU M 589 N LEU L 94 SHEET 1 AA4 4 THR L 119 PHE L 123 0 SHEET 2 AA4 4 THR L 134 TYR L 144 -1 O ASN L 142 N THR L 119 SHEET 3 AA4 4 TYR L 177 THR L 186 -1 O TYR L 177 N TYR L 144 SHEET 4 AA4 4 ILE L 163 LYS L 167 -1 N GLU L 164 O THR L 182 SHEET 1 AA5 4 THR L 157 THR L 158 0 SHEET 2 AA5 4 THR L 149 VAL L 154 -1 N VAL L 154 O THR L 157 SHEET 3 AA5 4 GLU L 195 GLN L 202 -1 O LYS L 199 N THR L 151 SHEET 4 AA5 4 THR L 205 ASN L 212 -1 O VAL L 207 N VAL L 200 SHEET 1 AA6 4 SER H 2 SER H 6 0 SHEET 2 AA6 4 LEU H 17 SER H 24 -1 O THR H 20 N SER H 6 SHEET 3 AA6 4 THR H 74 MET H 79 -1 O VAL H 75 N CYS H 21 SHEET 4 AA6 4 PHE H 65 SER H 71 -1 N THR H 66 O LYS H 78 SHEET 1 AA7 6 LEU H 10 VAL H 11 0 SHEET 2 AA7 6 THR H 105 VAL H 109 1 O THR H 108 N VAL H 11 SHEET 3 AA7 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 105 SHEET 4 AA7 6 MET H 33 GLN H 38 -1 N VAL H 36 O PHE H 91 SHEET 5 AA7 6 LEU H 44 TYR H 51 -1 O GLY H 48 N TRP H 35 SHEET 6 AA7 6 SER H 54 TYR H 57 -1 O SER H 54 N TYR H 51 SHEET 1 AA8 4 LEU H 10 VAL H 11 0 SHEET 2 AA8 4 THR H 105 VAL H 109 1 O THR H 108 N VAL H 11 SHEET 3 AA8 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 105 SHEET 4 AA8 4 LEU H 100 TRP H 101 -1 O LEU H 100 N ARG H 94 SHEET 1 AA9 4 SER H 118 LEU H 122 0 SHEET 2 AA9 4 VAL H 134 TYR H 143 -1 O LYS H 141 N SER H 118 SHEET 3 AA9 4 TYR H 174 VAL H 182 -1 O LEU H 176 N VAL H 140 SHEET 4 AA9 4 VAL H 161 THR H 163 -1 N ARG H 162 O VAL H 179 SHEET 1 AB1 4 SER H 118 LEU H 122 0 SHEET 2 AB1 4 VAL H 134 TYR H 143 -1 O LYS H 141 N SER H 118 SHEET 3 AB1 4 TYR H 174 VAL H 182 -1 O LEU H 176 N VAL H 140 SHEET 4 AB1 4 VAL H 167 ARG H 168 -1 N VAL H 167 O SER H 175 SHEET 1 AB2 3 THR H 149 TRP H 152 0 SHEET 2 AB2 3 VAL H 189 HIS H 195 -1 O ASN H 192 N THR H 151 SHEET 3 AB2 3 THR H 200 VAL H 206 -1 O VAL H 202 N VAL H 193 SSBOND 1 CYS L 24 CYS L 89 1555 1555 2.08 SSBOND 2 CYS L 81 CYS L 175 1555 1555 2.05 SSBOND 3 CYS L 139 CYS L 198 1555 1555 2.01 SSBOND 4 CYS L 216 CYS H 125 1555 1555 2.04 SSBOND 5 CYS H 21 CYS H 92 1555 1555 2.07 SSBOND 6 CYS H 126 CYS H 211 1555 1555 2.03 SSBOND 7 CYS H 138 CYS H 191 1555 1555 2.03 LINK C PCA H 1 N SER H 2 1555 1555 1.33 CISPEP 1 THR L 8 PRO L 9 0 -8.94 CISPEP 2 PHE L 145 PRO L 146 0 1.97 CISPEP 3 LEU H 144 PRO H 145 0 -10.42 CISPEP 4 GLU H 146 PRO H 147 0 -1.72 CISPEP 5 GLN H 187 PRO H 188 0 -3.75 CRYST1 92.960 98.835 66.595 90.00 131.97 90.00 C 1 2 1 4 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 0.010757 0.000000 0.009676 0.00000 SCALE2 0.000000 0.010118 0.000000 0.00000 SCALE3 0.000000 0.000000 0.020197 0.00000