HEADER IMMUNE SYSTEM 28-SEP-24 9DST TITLE CRYSTAL STRUCTURE OF FAB MS-1805 IN COMPLEX WITH N-TERMINAL JUNCTION TITLE 2 PEPTIDE FROM CIRCUMSPOROZOITE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: LIGHT CHAIN OF FAB MS-1805; COMPND 3 CHAIN: D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CIRCUMSPOROZOITE PROTEIN; COMPND 7 CHAIN: A; COMPND 8 SYNONYM: CS,PFCSP; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: HEAVY CHAIN OF FAB MS-1805; COMPND 12 CHAIN: C; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 8 ORGANISM_TAXID: 36329; SOURCE 9 GENE: CSP, PF3D7_0304600; SOURCE 10 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 32630; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ENGINEERED ANTIBODY FOR MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.JAIN,I.A.WILSON REVDAT 1 01-OCT-25 9DST 0 JRNL AUTH M.JAIN,I.A.WILSON JRNL TITL CRYSTAL STRUCTURE OF FAB MS-1805 IN COMPLEX WITH N-TERMINAL JRNL TITL 2 JUNCTION PEPTIDE FROM CIRCUMSPOROZOITE PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.74 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.72 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0 REMARK 3 NUMBER OF REFLECTIONS : 45531 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.330 REMARK 3 FREE R VALUE TEST SET COUNT : 1972 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 26.7200 - 4.1900 0.92 3162 121 0.1608 0.1594 REMARK 3 2 4.1900 - 3.3200 0.96 3228 151 0.1761 0.1837 REMARK 3 3 3.3200 - 2.9000 0.89 3010 127 0.1987 0.2289 REMARK 3 4 2.9000 - 2.6400 0.94 3115 142 0.2145 0.2582 REMARK 3 5 2.6400 - 2.4500 0.95 3193 151 0.2168 0.2674 REMARK 3 6 2.4500 - 2.3100 0.95 3168 155 0.2091 0.2444 REMARK 3 7 2.3100 - 2.1900 0.96 3177 137 0.2036 0.2536 REMARK 3 8 2.1900 - 2.1000 0.88 2945 141 0.2052 0.2393 REMARK 3 9 2.1000 - 2.0100 0.94 3113 142 0.2167 0.3025 REMARK 3 10 2.0100 - 1.9500 0.95 3180 148 0.2082 0.2742 REMARK 3 11 1.9500 - 1.8800 0.95 3199 139 0.2171 0.2482 REMARK 3 12 1.8800 - 1.8300 0.96 3149 153 0.2248 0.2531 REMARK 3 13 1.8300 - 1.7800 0.95 3156 141 0.2520 0.3169 REMARK 3 14 1.7800 - 1.7400 0.82 2764 124 0.2965 0.3244 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) : 0.230 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.060 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 NULL REMARK 3 ANGLE : 1.041 NULL REMARK 3 CHIRALITY : 0.068 524 REMARK 3 PLANARITY : 0.009 607 REMARK 3 DIHEDRAL : 9.245 476 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 9DST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1000288717. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-JUN-24 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 : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.92010 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45572 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 28.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.06900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.47800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.890 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 (%): 49.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, 20% (V/V) 2 REMARK 280 -PROPANOL AND 20% (W/V) POLYETHYLENE GLYCOL 4000, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 38.37200 REMARK 290 SMTRY3 2 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: 4840 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A, C 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 GLY D 1 REMARK 465 CYS D 214 REMARK 465 LYS A -5 REMARK 465 GLN A -4 REMARK 465 PRO A -3 REMARK 465 ALA A -2 REMARK 465 ASP A -1 REMARK 465 GLY A 0 REMARK 465 SER C 128 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 LYS C 214 REMARK 465 SER C 215 REMARK 465 CYS C 216 REMARK 465 ASP C 217 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 OE1 GLU D 165 O HOH D 301 2.13 REMARK 500 O HOH C 465 O HOH C 470 2.14 REMARK 500 REMARK 500 REMARK: NULL 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 D 30 -122.63 51.65 REMARK 500 ALA D 51 -25.12 72.02 REMARK 500 ALA D 84 -178.49 -174.41 REMARK 500 PHE D 95A -141.29 59.15 REMARK 500 ASP C 144 62.29 63.41 REMARK 500 REMARK 500 REMARK: NULL DBREF 9DST D 1 214 PDB 9DST 9DST 1 214 DBREF 9DST A -5 10 UNP Q7K740 CSP_PLAF7 95 110 DBREF 9DST C 1 217 PDB 9DST 9DST 1 217 SEQRES 1 D 215 GLY VAL GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 D 215 SER VAL GLY ASP ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 D 215 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 D 215 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 215 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 215 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 215 ASN SER TYR SER PHE TRP THR PHE GLY GLN GLY THR LYS SEQRES 9 D 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 16 LYS GLN PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN SEQRES 2 A 16 PRO ASN VAL SEQRES 1 C 227 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 227 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 227 PHE THR PHE ASN THR TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 C 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA ILE ILE TRP SEQRES 5 C 227 TYR ASP GLY SER GLN LYS TYR TYR ALA ASP SER VAL GLN SEQRES 6 C 227 GLY ARG PHE THR ILE SER ARG ASP ASN HIS LYS ASN THR SEQRES 7 C 227 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 C 227 ALA VAL TYR PHE CYS VAL ARG VAL ARG PHE SER VAL GLY SEQRES 9 C 227 PRO HIS GLY SER ALA PHE ASP LEU TRP GLY GLN GLY THR SEQRES 10 C 227 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 C 227 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 C 227 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 C 227 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 C 227 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 C 227 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 C 227 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 C 227 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 C 227 GLU PRO LYS SER CYS ASP HET CIT C 301 13 HETNAM CIT CITRIC ACID FORMUL 4 CIT C6 H8 O7 FORMUL 5 HOH *163(H2 O) HELIX 1 AA1 SER D 121 SER D 127 1 7 HELIX 2 AA2 LYS D 183 GLU D 187 1 5 HELIX 3 AA3 THR C 28 TYR C 32 5 5 HELIX 4 AA4 ASP C 61 GLN C 64 5 4 HELIX 5 AA5 ARG C 83 THR C 87 5 5 HELIX 6 AA6 SER C 156 ALA C 158 5 3 HELIX 7 AA7 SER C 187 LEU C 189 5 3 HELIX 8 AA8 LYS C 201 ASN C 204 5 4 SHEET 1 AA1 4 MET D 4 SER D 7 0 SHEET 2 AA1 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AA1 4 GLU D 70 ILE D 75 -1 O LEU D 73 N LEU D 21 SHEET 4 AA1 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AA2 6 THR D 10 ALA D 13 0 SHEET 2 AA2 6 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AA2 6 THR D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AA2 6 LEU D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AA2 6 LYS D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AA2 6 SER D 53 LEU D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AA3 4 THR D 10 ALA D 13 0 SHEET 2 AA3 4 THR D 102 ILE D 106 1 O GLU D 105 N LEU D 11 SHEET 3 AA3 4 THR D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AA3 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AA4 4 SER D 114 PHE D 118 0 SHEET 2 AA4 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AA4 4 TYR D 173 SER D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AA4 4 SER D 159 VAL D 163 -1 N SER D 162 O SER D 176 SHEET 1 AA5 4 ALA D 153 LEU D 154 0 SHEET 2 AA5 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AA5 4 VAL D 191 THR D 197 -1 O ALA D 193 N LYS D 149 SHEET 4 AA5 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AA6 4 GLN C 3 SER C 7 0 SHEET 2 AA6 4 LEU C 18 SER C 25 -1 O SER C 21 N SER C 7 SHEET 3 AA6 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA6 4 PHE C 67 ASP C 72 -1 N ASP C 72 O THR C 77 SHEET 1 AA7 6 VAL C 11 VAL C 12 0 SHEET 2 AA7 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AA7 6 ALA C 88 VAL C 95 -1 N TYR C 90 O THR C 107 SHEET 4 AA7 6 MET C 34 GLN C 39 -1 N VAL C 37 O PHE C 91 SHEET 5 AA7 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AA7 6 LYS C 57 TYR C 59 -1 O TYR C 58 N ILE C 50 SHEET 1 AA8 4 VAL C 11 VAL C 12 0 SHEET 2 AA8 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AA8 4 ALA C 88 VAL C 95 -1 N TYR C 90 O THR C 107 SHEET 4 AA8 4 PHE C 100F TRP C 103 -1 O LEU C 102 N ARG C 94 SHEET 1 AA9 4 SER C 120 LEU C 124 0 SHEET 2 AA9 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124 SHEET 3 AA9 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142 SHEET 4 AA9 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AB1 4 SER C 120 LEU C 124 0 SHEET 2 AB1 4 THR C 135 TYR C 145 -1 O GLY C 139 N LEU C 124 SHEET 3 AB1 4 TYR C 176 PRO C 185 -1 O LEU C 178 N VAL C 142 SHEET 4 AB1 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AB2 3 THR C 151 TRP C 154 0 SHEET 2 AB2 3 TYR C 194 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AB2 3 THR C 205 VAL C 211 -1 O THR C 205 N HIS C 200 SSBOND 1 CYS D 23 CYS D 88 1555 1555 2.09 SSBOND 2 CYS D 134 CYS D 194 1555 1555 2.02 SSBOND 3 CYS C 22 CYS C 92 1555 1555 2.07 SSBOND 4 CYS C 140 CYS C 196 1555 1555 2.04 CISPEP 1 SER D 7 PRO D 8 0 -12.10 CISPEP 2 TYR D 140 PRO D 141 0 4.15 CISPEP 3 PHE C 146 PRO C 147 0 -2.63 CISPEP 4 GLU C 148 PRO C 149 0 -2.85 CRYST1 42.325 76.744 74.453 90.00 88.38 90.00 P 1 21 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 0.023627 0.000000 -0.000668 0.00000 SCALE2 0.000000 0.013030 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013437 0.00000