HEADER IMMUNE SYSTEM 07-FEB-25 9N89 TITLE CRYSTAL STRUCTURE OF 2A2 MALARIAL ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: 2A2 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 2A2 KAPPA CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.YOO,J.P.JULIEN REVDAT 1 15-OCT-25 9N89 0 JRNL AUTH E.BEKKERING,R.YOO,S.HAILEMARIAM,F.HEIDE,D.IVANOCHKO, JRNL AUTH 2 M.JACKMAN,N.I.PROELLOCHS,R.STOTER,G.VAN GEMERT,A.MAEDA, JRNL AUTH 3 T.YUGUCHI,O.T.WANDERS,R.C.VAN DAALEN,M.R.INKLAAR, JRNL AUTH 4 C.M.ANDRADE,P.W.T.C.JANSEN,M.VERMEULEN,T.BOUSEMA, JRNL AUTH 5 E.TAKASHIMA,J.L.RUBINSTEIN,T.W.A.KOOIJ,M.M.JORE,J.P.JULIEN JRNL TITL CRYO-EM STRUCTURE OF ENDOGENOUS PFS230:PFS48/45 COMPLEX WITH JRNL TITL 2 SIX ANTIBODIES REVEALS MECHANISMS OF MALARIA JRNL TITL 3 TRANSMISSION-BLOCKING ACTIVITY JRNL REF IMMUNITY 2025 JRNL REFN ISSN 1074-7613 REMARK 2 REMARK 2 RESOLUTION. 1.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21_5207 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) : 1.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.51 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 131795 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940 REMARK 3 FREE R VALUE TEST SET COUNT : 6511 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 28.5100 - 3.7300 1.00 4468 250 0.1714 0.1736 REMARK 3 2 3.7300 - 2.9600 1.00 4298 230 0.1866 0.1857 REMARK 3 3 2.9600 - 2.5900 1.00 4293 217 0.1989 0.2020 REMARK 3 4 2.5900 - 2.3500 1.00 4244 212 0.1909 0.2292 REMARK 3 5 2.3500 - 2.1800 1.00 4228 219 0.1754 0.1777 REMARK 3 6 2.1800 - 2.0500 1.00 4224 221 0.1722 0.1768 REMARK 3 7 2.0500 - 1.9500 1.00 4197 217 0.1705 0.1779 REMARK 3 8 1.9500 - 1.8700 1.00 4194 234 0.1773 0.1711 REMARK 3 9 1.8700 - 1.7900 1.00 4231 194 0.1787 0.2037 REMARK 3 10 1.7900 - 1.7300 1.00 4189 206 0.1814 0.2001 REMARK 3 11 1.7300 - 1.6800 1.00 4175 221 0.1860 0.1775 REMARK 3 12 1.6800 - 1.6300 1.00 4190 217 0.1783 0.1898 REMARK 3 13 1.6300 - 1.5900 1.00 4199 210 0.1775 0.1932 REMARK 3 14 1.5900 - 1.5500 1.00 4180 219 0.1770 0.1875 REMARK 3 15 1.5500 - 1.5100 1.00 4162 204 0.1844 0.1825 REMARK 3 16 1.5100 - 1.4800 1.00 4166 202 0.1870 0.1998 REMARK 3 17 1.4800 - 1.4500 1.00 4159 216 0.1927 0.2176 REMARK 3 18 1.4500 - 1.4200 1.00 4117 212 0.1949 0.1932 REMARK 3 19 1.4200 - 1.4000 1.00 4175 215 0.1919 0.2077 REMARK 3 20 1.4000 - 1.3700 0.99 4108 232 0.1987 0.2144 REMARK 3 21 1.3700 - 1.3500 0.99 4145 215 0.2013 0.2115 REMARK 3 22 1.3500 - 1.3300 0.99 4107 247 0.1989 0.2029 REMARK 3 23 1.3300 - 1.3100 0.99 4125 207 0.2071 0.2279 REMARK 3 24 1.3100 - 1.2900 0.99 4142 197 0.2081 0.2288 REMARK 3 25 1.2900 - 1.2800 0.99 4090 224 0.2100 0.2238 REMARK 3 26 1.2800 - 1.2600 0.99 4112 214 0.2137 0.2398 REMARK 3 27 1.2600 - 1.2400 0.99 4135 218 0.2183 0.2353 REMARK 3 28 1.2400 - 1.2300 0.99 4091 204 0.2240 0.2380 REMARK 3 29 1.2300 - 1.2100 0.99 4109 222 0.2270 0.2310 REMARK 3 30 1.2100 - 1.2000 0.98 4031 215 0.2241 0.2587 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) : 0.099 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.143 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 9.88 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.84 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 : 0.004 3438 REMARK 3 ANGLE : 0.798 4728 REMARK 3 CHIRALITY : 0.083 545 REMARK 3 PLANARITY : 0.006 618 REMARK 3 DIHEDRAL : 12.241 1257 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 9N89 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292745. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 277 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 : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.920194 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131804 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200 REMARK 200 RESOLUTION RANGE LOW (A) : 28.510 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.8800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.21 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% W/V PEG 4K, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 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 29.98700 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.93600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.34100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.93600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.98700 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.34100 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19240 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L 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 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ASP H 144 66.17 70.12 REMARK 500 ASN L 30 -122.87 57.10 REMARK 500 ALA L 51 -38.49 73.86 REMARK 500 ALA L 84 166.21 179.74 REMARK 500 REMARK 500 REMARK: NULL DBREF 9N89 H 1 216 PDB 9N89 9N89 1 216 DBREF 9N89 L 1 214 PDB 9N89 9N89 1 214 SEQRES 1 H 223 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU GLU LYS SEQRES 2 H 223 PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 H 223 TYR SER ILE THR ASP TYR ASN MET ASN TRP VAL LYS LEU SEQRES 4 H 223 SER ASN GLY LYS SER LEU GLU TRP ILE GLY ASN ILE ASP SEQRES 5 H 223 PRO SER HIS GLY GLY THR THR TYR ASN GLN LYS PHE LYS SEQRES 6 H 223 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 H 223 ALA TYR MET GLN LEU LYS SER LEU THR SER GLU ASP SER SEQRES 8 H 223 ALA VAL TYR HIS CYS ALA ARG SER THR LEU TYR GLY ASN SEQRES 9 H 223 SER ALA MET ASP CYS TRP GLY GLN GLY THR SER VAL THR SEQRES 10 H 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 H 223 SER CYS SEQRES 1 L 214 SER ILE VAL MET THR GLN THR PRO LYS PHE LEU LEU VAL SEQRES 2 L 214 PRO ALA GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN SER VAL ASN ASN ASP VAL THR TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR TYR ALA SER SEQRES 5 L 214 ASN ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 214 GLY TYR GLY THR ASP PHE THR PHE THR ILE SER THR VAL SEQRES 7 L 214 GLN ALA GLU ASP LEU ALA VAL TYR PHE CYS GLN GLN ASP SEQRES 8 L 214 TYR SER SER PRO LEU THR PHE GLY ALA GLY THR LYS LEU SEQRES 9 L 214 GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS FORMUL 3 HOH *365(H2 O) HELIX 1 AA1 SER H 28 THR H 30 5 3 HELIX 2 AA2 GLN H 61 LYS H 64 5 4 HELIX 3 AA3 THR H 83 SER H 87 5 5 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 LEU H 189 5 3 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLN L 79 LEU L 83 5 5 HELIX 8 AA8 SER L 121 SER L 127 1 7 HELIX 9 AA9 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18 SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA2 6 GLU H 10 GLU H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 12 SHEET 3 AA2 6 ALA H 88 THR H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 TYR H 32 LEU H 39 -1 N ASN H 35 O ALA H 93 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O THR H 58 N ASN H 50 SHEET 1 AA3 4 GLU H 10 GLU H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 12 SHEET 3 AA3 4 ALA H 88 THR H 96 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 CYS H 102 TRP H 103 -1 O CYS H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 THR L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N THR L 7 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O PHE L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 GLY L 66 -1 N SER L 65 O THR L 72 SHEET 1 AA8 6 PHE L 10 PRO L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA8 6 VAL L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 ASN L 53 ARG L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 PHE L 10 PRO L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AA9 4 ALA L 84 GLN L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.05 CISPEP 1 PHE H 146 PRO H 147 0 -4.43 CISPEP 2 GLU H 148 PRO H 149 0 0.54 CISPEP 3 THR L 7 PRO L 8 0 -7.45 CISPEP 4 SER L 94 PRO L 95 0 1.53 CISPEP 5 SER L 94 PRO L 95 0 0.84 CISPEP 6 TYR L 140 PRO L 141 0 0.88 CRYST1 59.974 76.682 91.872 90.00 90.00 90.00 P 21 21 21 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 0.016674 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013041 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010885 0.00000