HEADER IMMUNE SYSTEM 05-FEB-25 9N6U TITLE CRYSTAL STRUCTURE OF 18F25 MALARIAL ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: 18F25 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 18F25 KAPPA CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_COMMON: MOUSE; SOURCE 11 ORGANISM_TAXID: 10090; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ANTIBODY, MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.YOO,J.P.JULIEN REVDAT 1 15-OCT-25 9N6U 0 JRNL AUTH E.T.BEKKERING,R.YOO,S.HAILEMARIAM,F.HEIDE,D.IVANOCHKO, JRNL AUTH 2 M.JACKMAN,N.I.PROELLOCHS,R.STOTER,G.J.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.JANSEN,M.VERMEULEN,T.BOUSEMA,E.TAKASHIMA, JRNL AUTH 5 J.L.RUBINSTEIN,T.W.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. 1.60 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) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.19 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 57872 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.189 REMARK 3 R VALUE (WORKING SET) : 0.188 REMARK 3 FREE R VALUE : 0.214 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180 REMARK 3 FREE R VALUE TEST SET COUNT : 2997 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 34.1900 - 4.4200 1.00 2837 169 0.1633 0.2141 REMARK 3 2 4.4100 - 3.5000 1.00 2702 152 0.1540 0.1672 REMARK 3 3 3.5000 - 3.0600 1.00 2697 118 0.1716 0.1963 REMARK 3 4 3.0600 - 2.7800 1.00 2643 145 0.1918 0.2024 REMARK 3 5 2.7800 - 2.5800 1.00 2632 154 0.1919 0.1956 REMARK 3 6 2.5800 - 2.4300 1.00 2633 145 0.1941 0.2289 REMARK 3 7 2.4300 - 2.3100 1.00 2609 132 0.1984 0.2313 REMARK 3 8 2.3100 - 2.2100 1.00 2587 152 0.1925 0.2245 REMARK 3 9 2.2100 - 2.1200 1.00 2622 156 0.1888 0.2287 REMARK 3 10 2.1200 - 2.0500 1.00 2588 147 0.1896 0.2356 REMARK 3 11 2.0500 - 1.9900 0.99 2584 131 0.1958 0.2130 REMARK 3 12 1.9900 - 1.9300 1.00 2625 146 0.1952 0.2225 REMARK 3 13 1.9300 - 1.8800 1.00 2559 141 0.2031 0.2205 REMARK 3 14 1.8800 - 1.8300 0.99 2611 136 0.2111 0.2168 REMARK 3 15 1.8300 - 1.7900 0.99 2556 119 0.2178 0.2768 REMARK 3 16 1.7900 - 1.7500 0.99 2611 140 0.2248 0.2373 REMARK 3 17 1.7500 - 1.7200 0.99 2551 128 0.2266 0.2254 REMARK 3 18 1.7200 - 1.6900 0.99 2579 157 0.2279 0.2600 REMARK 3 19 1.6900 - 1.6600 0.99 2524 152 0.2344 0.2507 REMARK 3 20 1.6600 - 1.6300 0.99 2561 134 0.2440 0.2142 REMARK 3 21 1.6300 - 1.6000 0.99 2564 143 0.2504 0.2915 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) : 0.153 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.754 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 12.18 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.12 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 : 0.006 3554 REMARK 3 ANGLE : 0.833 4873 REMARK 3 CHIRALITY : 0.055 544 REMARK 3 PLANARITY : 0.006 624 REMARK 3 DIHEDRAL : 13.038 1310 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 9N6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1000292647. 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 : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 365949 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.103 REMARK 200 RESOLUTION RANGE LOW (A) : 35.196 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.7900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63 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 (%): 46.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA2SO4 20 %W/V PEG 3350, VAPOR REMARK 280 DIFFUSION, 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 18.82100 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.26600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.89800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.26600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.82100 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.89800 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: 4160 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 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 CYS H 216 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 PHE H 48 -60.04 -97.67 REMARK 500 ASP H 144 68.05 66.30 REMARK 500 THR L 30 -121.50 49.19 REMARK 500 ALA L 51 -37.96 69.64 REMARK 500 SER L 52 10.37 -140.52 REMARK 500 ALA L 84 170.45 178.71 REMARK 500 ASN L 138 63.78 62.58 REMARK 500 REMARK 500 REMARK: NULL DBREF 9N6U H 1 216 PDB 9N6U 9N6U 1 216 DBREF 9N6U L 1 214 PDB 9N6U 9N6U 1 214 SEQRES 1 H 221 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA ARG SEQRES 2 H 221 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 221 TYR THR PHE THR ASN TYR TRP MET GLN TRP VAL LYS GLN SEQRES 4 H 221 ARG PRO GLY GLN GLY LEU GLU TRP PHE GLY ALA ILE TYR SEQRES 5 H 221 PRO GLY ASP GLY ASP THR ARG TYR THR GLN LYS PHE LYS SEQRES 6 H 221 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 221 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER SEQRES 8 H 221 ALA VAL TYR TYR CYS ALA ARG SER LEU TYR LEU GLY ALA SEQRES 9 H 221 MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL SER SEQRES 10 H 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 214 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 L 214 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 L 214 GLN ASP VAL THR ASN ASP VAL ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 L 214 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE ILE PHE THR ILE SER SER VAL SEQRES 7 L 214 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 L 214 TYR SER ALA PRO PRO THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE 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 HET PCA H 1 8 HET SO4 H 301 5 HET SO4 H 302 5 HET SO4 H 303 5 HET SO4 L 301 5 HETNAM PCA PYROGLUTAMIC ACID HETNAM SO4 SULFATE ION FORMUL 1 PCA C5 H7 N O3 FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 HOH *604(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 GLN H 61 LYS H 64 5 4 HELIX 3 AA3 ALA H 83 SER H 87 5 5 HELIX 4 AA4 SER H 127 LYS H 129 5 3 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 GLN L 79 LEU L 83 5 5 HELIX 9 AA9 SER L 121 SER L 127 1 7 HELIX 10 AB1 LYS L 183 LYS L 188 1 6 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 MET H 80 N LEU H 20 SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 6 GLU H 10 ALA H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O SER H 108 N GLU H 10 SHEET 3 AA2 6 ALA H 88 SER H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 TRP H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 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 ARG H 58 N ALA H 50 SHEET 1 AA3 4 GLU H 10 ALA H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O SER H 108 N GLU H 10 SHEET 3 AA3 4 ALA H 88 SER H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 MET H 100A TRP H 103 -1 O TYR 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 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 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 5 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O LYS L 24 N THR L 5 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 THR L 63 O THR L 74 SHEET 1 AA8 6 PHE L 10 SER L 14 0 SHEET 2 AA8 6 THR L 102 LYS L 107 1 O GLU L 105 N MET 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 TYR L 53 ARG L 54 -1 O TYR L 53 N TYR L 49 SHEET 1 AA9 4 PHE L 10 SER L 14 0 SHEET 2 AA9 4 THR L 102 LYS L 107 1 O GLU L 105 N MET 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 LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O SER L 177 N CYS L 134 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 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 LYS L 207 N CYS L 194 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 2.05 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.01 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 CISPEP 1 PHE H 146 PRO H 147 0 -7.93 CISPEP 2 GLU H 148 PRO H 149 0 0.40 CISPEP 3 ALA L 94 PRO L 95 0 -0.62 CISPEP 4 TYR L 140 PRO L 141 0 2.80 CRYST1 37.642 81.796 140.532 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 0.026566 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012226 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007116 0.00000