HEADER IMMUNE SYSTEM 12-DEC-24 9MI7 TITLE CRYSTAL STRUCTURE OF ADI-64597 ((HUMAN FAB, WITH SUBSTITUTED IGG1-CH1 TITLE 2 (HC-L128R AND K147R) AND SUBSTITUTED KAPPA CONSTANT DOMAIN (LC-Q124E, TITLE 3 V133Q, AND T178R)) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADI-64597 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: SUBSTITUTED IGG1-CH1 (HC-L128R AND K147R); COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ADI-64597 FAB LIGHT CHAIN; COMPND 8 CHAIN: L; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: KAPPA CONSTANT DOMAIN (LC-Q124E, V133Q, AND T178R)) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.B.BATTLES,M.WELIN,M.LAURSEN REVDAT 1 02-APR-25 9MI7 0 JRNL AUTH K.A.BARLOW,M.B.BATTLES,M.E.BROWN,K.CANFIELD,X.LU,H.LYNAUGH, JRNL AUTH 2 M.MORRILL,C.G.RAPPAZZO,S.P.REYES,C.SANDBERG,B.SHARKEY, JRNL AUTH 3 C.STRONG,J.ZHAO,A.SIVASUBRAMANIAN JRNL TITL DESIGN OF ORTHOGONAL CONSTANT DOMAIN INTERFACES TO AID JRNL TITL 2 PROPER HEAVY/LIGHT CHAIN PAIRING OF BISPECIFIC ANTIBODIES. JRNL REF MABS V. 17 79531 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40126074 JRNL DOI 10.1080/19420862.2025.2479531 REMARK 2 REMARK 2 RESOLUTION. 2.22 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2-4158 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 23297 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.180 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL 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 : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL 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 9MI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290851. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAY-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MAX IV REMARK 200 BEAMLINE : BIOMAX REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23297 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220 REMARK 200 RESOLUTION RANGE LOW (A) : 49.290 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 10.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6 REMARK 200 DATA REDUNDANCY IN SHELL : 10.50 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 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 (%): 52.76 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: ADI-64597 (HUMAN FAB) WAS RECEIVED AT REMARK 280 CONCENTRATION 16.5 MG/ML IN A BUFFER CONTAINING 2 MM TRIS-HCL PH REMARK 280 8.0 AND 150 MM NACL. PACT, BCS AND JCSG+ SCREENS (ALL FROM REMARK 280 MOLECULAR DIMENSIONS LTD.) WERE SET UP USING A MOSQUITO REMARK 280 CRYSTALLISATION ROBOT (STP LABTECH). SITTING DROPS OF 150 NL REMARK 280 PROTEIN AND 150 NL RESERVOIR SOLUTION WERE LEFT TO EQUILIBRATE REMARK 280 AGAINST A 40 UL RESERVOIR AT 20 C. AFTER A FEW DAYS, NEEDLE-LIKE REMARK 280 CRYSTALS WERE OBTAINED IN SEVERAL CONDITIONS. THE CRYSTAL USED REMARK 280 FOR DATA COLLECTION WAS OBTAINED IN THE BCS SCREEN, CONDITION REMARK 280 B10 (0.1 M HEPES PH 7.5, 22% W/V PEG SMEAR BROAD), VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 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 32.47700 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 64.95400 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: 18890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 135 REMARK 465 SER H 136 REMARK 465 THR H 137 REMARK 465 SER H 138 REMARK 465 GLY H 139 REMARK 465 LYS H 220 REMARK 465 SER H 221 REMARK 465 CYS H 222 REMARK 465 ASP L 1 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 SER H 15 -22.88 74.27 REMARK 500 SER L 30 -129.21 56.86 REMARK 500 ALA L 51 -39.71 67.88 REMARK 500 ASN L 138 71.18 54.31 REMARK 500 SER L 156 114.85 -161.64 REMARK 500 LYS L 190 -60.01 -109.14 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MI7 H 1 222 PDB 9MI7 9MI7 1 222 DBREF 9MI7 L 1 214 PDB 9MI7 9MI7 1 214 SEQRES 1 H 222 PCA VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 222 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 222 GLY SER VAL SER SER GLY ASP TYR TYR TRP THR TRP ILE SEQRES 4 H 222 ARG GLN SER PRO GLY LYS GLY LEU GLU TRP ILE GLY HIS SEQRES 5 H 222 ILE TYR TYR SER GLY ASN THR ASN TYR ASN PRO SER LEU SEQRES 6 H 222 LYS SER ARG LEU THR ILE SER ILE ASP THR SER LYS THR SEQRES 7 H 222 GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP SEQRES 8 H 222 THR ALA ILE TYR TYR CYS VAL ARG ASP ARG VAL THR GLY SEQRES 9 H 222 ALA PHE ASP ILE TRP GLY GLN GLY THR MET VAL THR VAL SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO ARG SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL ARG ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 H 222 CYS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER SEQRES 3 L 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 214 ASN LEU GLU THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP ILE ALA THR TYR PHE CYS GLN HIS PHE SEQRES 8 L 214 ASP HIS LEU PRO LEU ALA PHE GLY GLY GLY THR LYS VAL 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 GLU LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL GLN 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 GLU 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 GOL H 301 6 HET CL H 302 1 HET CL H 303 1 HET GOL L 301 6 HET CL L 302 1 HETNAM PCA PYROGLUTAMIC ACID HETNAM GOL GLYCEROL HETNAM CL CHLORIDE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 1 PCA C5 H7 N O3 FORMUL 3 GOL 2(C3 H8 O3) FORMUL 4 CL 3(CL 1-) FORMUL 8 HOH *51(H2 O) HELIX 1 AA1 LEU H 65 SER H 67 5 3 HELIX 2 AA2 THR H 88 THR H 92 5 5 HELIX 3 AA3 SER H 162 ALA H 164 5 3 HELIX 4 AA4 SER H 193 GLY H 196 5 4 HELIX 5 AA5 LYS H 207 ASN H 210 5 4 HELIX 6 AA6 GLN L 79 ILE L 83 5 5 HELIX 7 AA7 SER L 121 SER L 127 1 7 HELIX 8 AA8 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 79 LEU H 84 -1 O LEU H 84 N LEU H 18 SHEET 4 AA1 4 LEU H 69 ASP H 74 -1 N ASP H 74 O GLN H 79 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA2 6 ALA H 93 ARG H 101 -1 N TYR H 95 O THR H 113 SHEET 4 AA2 6 TYR H 34 SER H 42 -1 N ILE H 39 O TYR H 96 SHEET 5 AA2 6 GLY H 46 ILE H 53 -1 O GLU H 48 N ARG H 40 SHEET 6 AA2 6 THR H 59 TYR H 61 -1 O ASN H 60 N HIS H 52 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA3 4 ALA H 93 ARG H 101 -1 N TYR H 95 O THR H 113 SHEET 4 AA3 4 PHE H 106 TRP H 109 -1 O ILE H 108 N ARG H 99 SHEET 1 AA4 4 SER H 126 ARG H 130 0 SHEET 2 AA4 4 THR H 141 TYR H 151 -1 O LEU H 147 N PHE H 128 SHEET 3 AA4 4 TYR H 182 PRO H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 AA4 4 VAL H 169 THR H 171 -1 N HIS H 170 O VAL H 187 SHEET 1 AA5 4 SER H 126 ARG H 130 0 SHEET 2 AA5 4 THR H 141 TYR H 151 -1 O LEU H 147 N PHE H 128 SHEET 3 AA5 4 TYR H 182 PRO H 191 -1 O LEU H 184 N VAL H 148 SHEET 4 AA5 4 VAL H 175 LEU H 176 -1 N VAL H 175 O SER H 183 SHEET 1 AA6 3 THR H 157 TRP H 160 0 SHEET 2 AA6 3 TYR H 200 HIS H 206 -1 O ASN H 203 N SER H 159 SHEET 3 AA6 3 THR H 211 VAL H 217 -1 O VAL H 213 N VAL H 204 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O GLN 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 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA8 6 SER L 10 SER 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 HIS L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N ASN L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 ASN L 53 LEU L 54 -1 O ASN L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 SER 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 HIS L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA9 4 ALA L 97 PHE L 98 -1 O ALA L 97 N HIS 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 LEU L 179 N VAL L 132 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 ALA L 193 N LYS L 149 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 97 1555 1555 2.16 SSBOND 2 CYS H 146 CYS H 202 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.09 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 CISPEP 1 PHE H 152 PRO H 153 0 -2.57 CISPEP 2 GLU H 154 PRO H 155 0 -1.09 CISPEP 3 SER L 7 PRO L 8 0 -4.37 CISPEP 4 LEU L 94 PRO L 95 0 -1.90 CISPEP 5 TYR L 140 PRO L 141 0 4.56 CRYST1 65.983 65.983 97.431 90.00 90.00 120.00 P 31 3 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 0.015155 0.008750 0.000000 0.00000 SCALE2 0.000000 0.017500 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010264 0.00000