HEADER CELL ADHESION 21-OCT-24 9H4R TITLE STRUCTURE OF FERTILIZATION-BLOCKING MONOCLONAL ANTIBODY IE-3 VHVL TITLE 2 BOUND TO THE ZP-N1 DOMAIN OF MOUSE ZP2 (CRYSTAL FORM I) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ZONA PELLUCIDA SPERM-BINDING PROTEIN 2; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP RESIDUES 35-138; COMPND 5 SYNONYM: ZONA PELLUCIDA GLYCOPROTEIN 2,ZP-2,ZONA PELLUCIDA PROTEIN A; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: DBREF 9H4R A 35 138 UNP P20239 ZP2_MOUSE 35 138 SEQADV COMPND 9 9H4R SER A 83 UNP P20239 ASN 83 ENGINEERED MUTATION SEQADV 9H4R LEU A COMPND 10 139 UNP P20239 EXPRESSION TAG SEQADV 9H4R GLU A 140 UNP P20239 COMPND 11 EXPRESSION TAG SEQADV 9H4R HIS A 141 UNP P20239 EXPRESSION TAG SEQADV COMPND 12 9H4R HIS A 142 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 143 UNP COMPND 13 P20239 EXPRESSION TAG SEQADV 9H4R HIS A 144 UNP P20239 EXPRESSION TAG COMPND 14 SEQADV 9H4R HIS A 145 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 146 COMPND 15 UNP P20239 EXPRESSION TAG; COMPND 16 MOL_ID: 2; COMPND 17 MOLECULE: HEAVY CHAIN VARIABLE (VH) DOMAIN OF ANTI-ZP2 MONOCLONAL COMPND 18 ANTIBODY IE-3; COMPND 19 CHAIN: H, X; COMPND 20 ENGINEERED: YES; COMPND 21 OTHER_DETAILS: THE CROSS-REFERENCE FOR 9H4R CHAINS H AND X ARE COMPND 22 RESIDUES 20-139 OF GENBANK ENTRY QCC30352 COMPND 23 (HTTPS://WWW.NCBI.NLM.NIH.GOV/PROTEIN/QCC30352), WITH THE PRECEDING 3 COMPND 24 RESIDUES (17-ETG-19) BEING AN EXPRESSION TAG.; COMPND 25 MOL_ID: 3; COMPND 26 MOLECULE: LIGHT CHAIN VARIABLE (VL) DOMAIN OF ANTI-ZP2 MONOCLONAL COMPND 27 ANTIBODY IE-3; COMPND 28 CHAIN: L, Y; COMPND 29 ENGINEERED: YES; COMPND 30 OTHER_DETAILS: THE CROSS-REFERENCE FOR 9H4R CHAINS L AND Y ARE COMPND 31 RESIDUES 21-134 OF GENBANK ENTRY QCC30353 COMPND 32 (HTTPS://WWW.NCBI.NLM.NIH.GOV/PROTEIN/QCC30353), WITH THE PRECEDING 3 COMPND 33 RESIDUES (18-ETG-20) BEING AN EXPRESSION TAG. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: ZP2, ZP-2, ZPA; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PHLSEC; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 14 ORGANISM_COMMON: NORWAY RAT; SOURCE 15 ORGANISM_TAXID: 10116; SOURCE 16 CELL_LINE: HYBRIDOMA; SOURCE 17 ATCC: CRL-2463; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PHLSEC3; SOURCE 24 MOL_ID: 3; SOURCE 25 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 26 ORGANISM_COMMON: NORWAY RAT; SOURCE 27 ORGANISM_TAXID: 10116; SOURCE 28 CELL_LINE: HYBRIDOMA; SOURCE 29 ATCC: CRL-2463; SOURCE 30 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 31 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 34 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 35 EXPRESSION_SYSTEM_PLASMID: PHLSEC3 KEYWDS ZONA PELLUCIDA, ZP2, ZP-N DOMAIN, ZP-N1 DOMAIN, ZP MODULE, ZP DOMAIN, KEYWDS 2 EGG-SPERM RECOGNITION, GAMETE INTERACTION, IMMUNOCONTRACEPTION, KEYWDS 3 MONOCLONAL ANTIBODY, IE-3, IE3, HEAVY CHAIN VARIABLE DOMAIN, LIGHT KEYWDS 4 CHAIN VARIABLE DOMAIN, CELL ADHESION EXPDTA X-RAY DIFFRACTION AUTHOR E.DIOGUARDI,D.DE SANCTIS,L.JOVINE REVDAT 1 12-MAR-25 9H4R 0 JRNL AUTH E.DIOGUARDI,A.STSIAPANAVA,E.FAHRENKAMP,L.HAN,D.DE SANCTIS, JRNL AUTH 2 J.INZUNZA,L.JOVINE JRNL TITL STRUCTURAL BASIS OF ZP2-TARGETED FEMALE NON-HORMONAL JRNL TITL 2 CONTRACEPTION JRNL REF PROC.NATL.ACAD.SCI.USA 2025 JRNL REFN ESSN 1091-6490 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.D.BLEIL,P.M.WASSARMAN REMARK 1 TITL SYNTHESIS OF ZONA PELLUCIDA PROTEINS BY DENUDED AND REMARK 1 TITL 2 FOLLICLE-ENCLOSED MOUSE OOCYTES DURING CULTURE IN VITRO. REMARK 1 REF PROC NATL ACAD SCI U S A V. 77 1029 1980 REMARK 1 REFN ISSN 0027-8424 REMARK 1 PMID 6928658 REMARK 1 DOI 10.1073/PNAS.77.2.1029 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.D.BLEIL,C.F.BEALL,P.M.WASSARMAN REMARK 1 TITL MAMMALIAN SPERM-EGG INTERACTION: FERTILIZATION OF MOUSE EGGS REMARK 1 TITL 2 TRIGGERS MODIFICATION OF THE MAJOR ZONA PELLUCIDA REMARK 1 TITL 3 GLYCOPROTEIN, ZP2. REMARK 1 REF DEV BIOL V. 86 189 1981 REMARK 1 REFN ISSN 0012-1606 REMARK 1 PMID 6793422 REMARK 1 DOI 10.1016/0012-1606(81)90329-8 REMARK 1 REFERENCE 3 REMARK 1 AUTH J.M.GREVE,G.S.SALZMANN,R.J.ROLLER,P.M.WASSARMAN REMARK 1 TITL BIOSYNTHESIS OF THE MAJOR ZONA PELLUCIDA GLYCOPROTEIN REMARK 1 TITL 2 SECRETED BY OOCYTES DURING MAMMALIAN OOGENESIS. REMARK 1 REF CELL V. 31 749 1982 REMARK 1 REFN ISSN 0092-8674 REMARK 1 PMID 6819087 REMARK 1 DOI 10.1016/0092-8674(82)90329-4 REMARK 1 REFERENCE 4 REMARK 1 AUTH L.F.LIANG,S.M.CHAMOW,J.DEAN REMARK 1 TITL OOCYTE-SPECIFIC EXPRESSION OF MOUSE ZP-2: DEVELOPMENTAL REMARK 1 TITL 2 REGULATION OF THE ZONA PELLUCIDA GENES. REMARK 1 REF MOL CELL BIOL V. 10 1507 1990 REMARK 1 REFN ISSN 0270-7306 REMARK 1 PMID 1690843 REMARK 1 DOI 10.1128/MCB.10.4.1507-1515.1990 REMARK 1 REFERENCE 5 REMARK 1 AUTH M.MONNE,L.HAN,T.SCHWEND,S.BURENDAHL,L.JOVINE REMARK 1 TITL CRYSTAL STRUCTURE OF THE ZP-N DOMAIN OF ZP3 REVEALS THE CORE REMARK 1 TITL 2 FOLD OF ANIMAL EGG COATS. REMARK 1 REF NATURE V. 456 653 2008 REMARK 1 REFN ESSN 1476-4687 REMARK 1 PMID 19052627 REMARK 1 DOI 10.1038/NATURE07599 REMARK 1 REFERENCE 6 REMARK 1 AUTH M.A.AVELLA,B.BAIBAKOV,J.DEAN REMARK 1 TITL A SINGLE DOMAIN OF THE ZP2 ZONA PELLUCIDA PROTEIN MEDIATES REMARK 1 TITL 2 GAMETE RECOGNITION IN MICE AND HUMANS. REMARK 1 REF J CELL BIOL V. 205 801 2014 REMARK 1 REFN ESSN 1540-8140 REMARK 1 PMID 24934154 REMARK 1 DOI 10.1128/MCB.22.9.3111-3120.2002 REMARK 1 REFERENCE 7 REMARK 1 AUTH I.J.EAST,B.J.GULYAS,J.DEAN REMARK 1 TITL MONOCLONAL ANTIBODIES TO THE MURINE ZONA PELLUCIDA PROTEIN REMARK 1 TITL 2 WITH SPERM RECEPTOR ACTIVITY: EFFECTS ON FERTILIZATION AND REMARK 1 TITL 3 EARLY DEVELOPMENT. REMARK 1 REF DEV BIOL V. 109 268 1985 REMARK 1 REFN ISSN 0012-1606 REMARK 1 PMID 3996750 REMARK 1 DOI 10.1016/0012-1606(85)90454-3 REMARK 1 REFERENCE 8 REMARK 1 AUTH I.J.EAST,D.R.MATTISON,J.DEAN REMARK 1 TITL MONOCLONAL ANTIBODIES TO THE MAJOR PROTEIN OF THE MURINE REMARK 1 TITL 2 ZONA PELLUCIDA: EFFECTS ON FERTILIZATION AND EARLY REMARK 1 TITL 3 DEVELOPMENT. REMARK 1 REF DEV BIOL V. 104 49 1984 REMARK 1 REFN ISSN 0012-1606 REMARK 1 PMID 6376213 REMARK 1 DOI 10.1016/0012-1606(84)90035-6 REMARK 1 REFERENCE 9 REMARK 1 AUTH J.LI,A.I.OLVERA,O.S.AKBARI,A.MORADIAN,M.J.SWEREDOSKI,S.HESS, REMARK 1 AUTH 2 B.A.HAY REMARK 1 TITL VECTORED ANTIBODY GENE DELIVERY MEDIATES LONG-TERM REMARK 1 TITL 2 CONTRACEPTION. REMARK 1 REF CURR BIOL V. 25 R820 2015 REMARK 1 REFN ISSN 1879-0445 REMARK 1 PMID 26439332 REMARK 1 DOI 10.1016/J.CUB.2015.08.002 REMARK 1 REFERENCE 10 REMARK 1 AUTH W.SUN,Y.H.LOU,J.DEAN,K.S.TUNG REMARK 1 TITL A CONTRACEPTIVE PEPTIDE VACCINE TARGETING SULFATED REMARK 1 TITL 2 GLYCOPROTEIN ZP2 OF THE MOUSE ZONA PELLUCIDA. REMARK 1 REF BIOL REPROD V. 60 900 1999 REMARK 1 REFN ISSN 0006-3363 REMARK 1 PMID 10084964 REMARK 1 DOI 10.1095/BIOLREPROD60.4.900 REMARK 1 REFERENCE 11 REMARK 1 AUTH I.RAJ,H.SADAT AL HOSSEINI,E.DIOGUARDI,K.NISHIMURA,L.HAN, REMARK 1 AUTH 2 A.VILLA,D.DE SANCTIS,L.JOVINE REMARK 1 TITL STRUCTURAL BASIS OF EGG COAT-SPERM RECOGNITION AT REMARK 1 TITL 2 FERTILIZATION. REMARK 1 REF CELL V. 169 1315 2017 REMARK 1 REFN ISSN 1097-4172 REMARK 1 PMID 28622512 REMARK 1 DOI 10.1016/J.CELL.2017.05.033 REMARK 1 REFERENCE 12 REMARK 1 AUTH S.NISHIO,C.EMORI,B.WISEMAN,D.FAHRENKAMP,E.DIOGUARDI, REMARK 1 AUTH 2 S.ZAMORA-CABALLERO,M.BOKHOVE,L.HAN,A.STSIAPANAVA,B.ALGARRA, REMARK 1 AUTH 3 Y.LU,M.KODANI,R.E.BAINBRIDGE,K.M.KOMONDOR,A.E.CARLSON, REMARK 1 AUTH 4 M.LANDREH,D.DE SANCTIS,S.YASUMASU,M.IKAWA,L.JOVINE REMARK 1 TITL ZP2 CLEAVAGE BLOCKS POLYSPERMY BY MODULATING THE REMARK 1 TITL 2 ARCHITECTURE OF THE EGG COAT. REMARK 1 REF CELL V. 187 1440 2024 REMARK 1 REFN ISSN 1097-4172 REMARK 1 PMID 38490181 REMARK 1 DOI 10.1016/J.CELL.2024.02.013 REMARK 2 REMARK 2 RESOLUTION. 1.53 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419+SVN 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) : 1.53 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.16 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.500 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4 REMARK 3 NUMBER OF REFLECTIONS : 109165 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.850 REMARK 3 FREE R VALUE TEST SET COUNT : 6384 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 29.1600 - 4.1500 0.90 5551 371 0.1388 0.1839 REMARK 3 2 4.1500 - 3.2900 0.91 5428 287 0.1578 0.1927 REMARK 3 3 3.2900 - 2.8800 0.93 5473 281 0.1956 0.2030 REMARK 3 4 2.8800 - 2.6200 0.91 5378 338 0.2186 0.2553 REMARK 3 5 2.6200 - 2.4300 0.92 5370 313 0.2434 0.2869 REMARK 3 6 2.4300 - 2.2900 0.93 5422 299 0.2413 0.2629 REMARK 3 7 2.2900 - 2.1700 0.93 5407 323 0.2603 0.2674 REMARK 3 8 2.1700 - 2.0800 0.93 5409 323 0.2622 0.3099 REMARK 3 9 2.0800 - 2.0000 0.92 5362 328 0.2708 0.2582 REMARK 3 10 2.0000 - 1.9300 0.92 5368 302 0.2835 0.3121 REMARK 3 11 1.9300 - 1.8700 0.91 5252 308 0.2838 0.2850 REMARK 3 12 1.8700 - 1.8100 0.88 5115 306 0.2970 0.2718 REMARK 3 13 1.8100 - 1.7700 0.88 5082 292 0.3058 0.3006 REMARK 3 14 1.7700 - 1.7200 0.87 5052 290 0.3145 0.2961 REMARK 3 15 1.7200 - 1.6800 0.87 5035 291 0.3241 0.3523 REMARK 3 16 1.6800 - 1.6500 0.84 4858 285 0.3313 0.3222 REMARK 3 17 1.6500 - 1.6200 0.82 4764 279 0.3396 0.3294 REMARK 3 18 1.6200 - 1.5800 0.81 4658 279 0.3437 0.3503 REMARK 3 19 1.5800 - 1.5600 0.81 4661 263 0.3392 0.3461 REMARK 3 20 1.5600 - 1.5300 0.78 4504 258 0.3627 0.3610 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.826 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.27 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.88 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: 0.3000 REMARK 3 OPERATOR: K,H,-L REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 5268 REMARK 3 ANGLE : 0.576 7146 REMARK 3 CHIRALITY : 0.045 784 REMARK 3 PLANARITY : 0.004 918 REMARK 3 DIHEDRAL : 11.644 1882 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 : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and resid 43 through 136) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and resid 43 through 136) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 21 through 77 or REMARK 3 resid 79 through 139)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "X" and (resid 21 through 77 or REMARK 3 resid 79 through 139)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 20 through 104 or REMARK 3 resid 106 through 132)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "Y" and (resid 20 through 104 or REMARK 3 resid 106 through 132)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9H4R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1292142646. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-SEP-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976251 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115130 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530 REMARK 200 RESOLUTION RANGE LOW (A) : 29.164 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 18.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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: P43-Q138 OF PDB ID 5II6; CHAIN H OF PDB ID 4AMK; REMARK 200 CHAIN L OF PDB ID 3MBX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (V/V) PEG 3350, 0.2 M SODIUM REMARK 280 TARTRATE, 0.1 M NA-HEPES PH 6.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 45.82000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.58500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.14500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.58500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.82000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.14500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 APPLY THE FOLLOWING TO CHAINS: A, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, X, Y 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 VAL A 35 REMARK 465 SER A 36 REMARK 465 LEU A 37 REMARK 465 PRO A 38 REMARK 465 GLN A 39 REMARK 465 SER A 40 REMARK 465 ILE A 137 REMARK 465 GLN A 138 REMARK 465 LEU A 139 REMARK 465 GLU A 140 REMARK 465 HIS A 141 REMARK 465 HIS A 142 REMARK 465 HIS A 143 REMARK 465 HIS A 144 REMARK 465 HIS A 145 REMARK 465 HIS A 146 REMARK 465 GLU H 17 REMARK 465 THR H 18 REMARK 465 GLY H 19 REMARK 465 LYS L 133 REMARK 465 ARG L 134 REMARK 465 VAL B 35 REMARK 465 SER B 36 REMARK 465 LEU B 37 REMARK 465 PRO B 38 REMARK 465 GLN B 39 REMARK 465 SER B 40 REMARK 465 GLU B 41 REMARK 465 GLN B 138 REMARK 465 LEU B 139 REMARK 465 GLU B 140 REMARK 465 HIS B 141 REMARK 465 HIS B 142 REMARK 465 HIS B 143 REMARK 465 HIS B 144 REMARK 465 HIS B 145 REMARK 465 HIS B 146 REMARK 465 GLU X 17 REMARK 465 THR X 18 REMARK 465 GLY X 19 REMARK 465 GLU Y 18 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 ILE H 67 -61.70 -95.00 REMARK 500 SER L 34 -130.73 -105.05 REMARK 500 TRP L 76 15.81 55.92 REMARK 500 ALA L 77 -10.44 71.58 REMARK 500 ILE X 67 -62.33 -94.66 REMARK 500 TRP Y 76 15.45 55.93 REMARK 500 ALA Y 77 -10.03 71.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9H4S RELATED DB: PDB REMARK 900 TETRAGONAL CRYSTAL FORM OF THE SAME COMPLEX REMARK 900 RELATED ID: 5II6 RELATED DB: PDB REMARK 900 HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE ZP2 ZP-N1 DOMAIN, IN THE REMARK 900 UNBOUND STATE REMARK 900 RELATED ID: 8RKE RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLETE N-TERMINAL REGION OF HUMAN ZP2 REMARK 900 (HZP2-N1N2N3) REMARK 900 RELATED ID: 8RKF RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE ZP-N1 AND ZP-N2 DOMAINS OF HUMAN ZP2 (HZP2- REMARK 900 N1N2) DBREF 9H4R A 35 138 UNP P20239 ZP2_MOUSE 35 138 DBREF 9H4R H 17 139 PDB 9H4R 9H4R 17 139 DBREF 9H4R L 18 134 PDB 9H4R 9H4R 18 134 DBREF 9H4R B 35 138 UNP P20239 ZP2_MOUSE 35 138 DBREF 9H4R X 17 139 PDB 9H4R 9H4R 17 139 DBREF 9H4R Y 18 134 PDB 9H4R 9H4R 18 134 SEQADV 9H4R SER A 83 UNP P20239 ASN 83 ENGINEERED MUTATION SEQADV 9H4R LEU A 139 UNP P20239 EXPRESSION TAG SEQADV 9H4R GLU A 140 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 141 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 142 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 143 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 144 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 145 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS A 146 UNP P20239 EXPRESSION TAG SEQADV 9H4R SER B 83 UNP P20239 ASN 83 ENGINEERED MUTATION SEQADV 9H4R LEU B 139 UNP P20239 EXPRESSION TAG SEQADV 9H4R GLU B 140 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS B 141 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS B 142 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS B 143 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS B 144 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS B 145 UNP P20239 EXPRESSION TAG SEQADV 9H4R HIS B 146 UNP P20239 EXPRESSION TAG SEQRES 1 A 112 VAL SER LEU PRO GLN SER GLU ASN PRO ALA PHE PRO GLY SEQRES 2 A 112 THR LEU ILE CYS ASP LYS ASP GLU VAL ARG ILE GLU PHE SEQRES 3 A 112 SER SER ARG PHE ASP MET GLU LYS TRP ASN PRO SER VAL SEQRES 4 A 112 VAL ASP THR LEU GLY SER GLU ILE LEU SER CYS THR TYR SEQRES 5 A 112 ALA LEU ASP LEU GLU ARG PHE VAL LEU LYS PHE PRO TYR SEQRES 6 A 112 GLU THR CYS THR ILE LYS VAL VAL GLY GLY TYR GLN VAL SEQRES 7 A 112 ASN ILE ARG VAL GLY ASP THR THR THR ASP VAL ARG TYR SEQRES 8 A 112 LYS ASP ASP MET TYR HIS PHE PHE CYS PRO ALA ILE GLN SEQRES 9 A 112 LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 H 123 GLU THR GLY GLN VAL GLN LEU GLN GLN SER GLY ALA GLU SEQRES 2 H 123 LEU VAL LYS PRO GLY SER SER VAL LYS ILE SER CYS LYS SEQRES 3 H 123 ALA SER GLY TYR THR PHE THR SER ASP ASP MET HIS TRP SEQRES 4 H 123 ILE LYS GLN GLN PRO GLY ASN GLY LEU GLU TRP ILE GLY SEQRES 5 H 123 TRP ILE TYR PRO GLY ASN ASP ASP THR LYS TYR ASN GLN SEQRES 6 H 123 LYS PHE ASN GLY LYS ALA THR LEU THR ALA ASP LYS SER SEQRES 7 H 123 SER SER THR VAL TYR MET GLN LEU SER SER LEU THR SER SEQRES 8 H 123 GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLY ASP LEU SEQRES 9 H 123 ASN TYR GLY GLY SER MET ASP ALA TRP GLY GLN GLY THR SEQRES 10 H 123 SER VAL THR VAL SER SER SEQRES 1 L 117 GLU THR GLY ASP THR VAL MET THR GLN SER PRO SER SER SEQRES 2 L 117 LEU ALA VAL SER ALA GLY GLU THR LEU THR ILE ASN CYS SEQRES 3 L 117 LYS SER SER GLN ASN LEU PHE SER SER ARG ASN GLN LYS SEQRES 4 L 117 ASN TYR LEU ALA TRP PHE GLN GLN LYS PRO GLY GLN SER SEQRES 5 L 117 PRO THR LEU LEU ILE HIS TRP ALA SER THR ARG GLN SER SEQRES 6 L 117 GLY VAL PRO ASP ARG PHE ILE GLY SER GLY SER GLY THR SEQRES 7 L 117 ASP PHE THR LEU THR ILE SER SER VAL GLN ALA GLU ASP SEQRES 8 L 117 LEU ALA ILE TYR TYR CYS GLN GLN TYR TYR ASN SER PRO SEQRES 9 L 117 LEU THR PHE GLY SER GLY THR LYS LEU GLU ILE LYS ARG SEQRES 1 B 112 VAL SER LEU PRO GLN SER GLU ASN PRO ALA PHE PRO GLY SEQRES 2 B 112 THR LEU ILE CYS ASP LYS ASP GLU VAL ARG ILE GLU PHE SEQRES 3 B 112 SER SER ARG PHE ASP MET GLU LYS TRP ASN PRO SER VAL SEQRES 4 B 112 VAL ASP THR LEU GLY SER GLU ILE LEU SER CYS THR TYR SEQRES 5 B 112 ALA LEU ASP LEU GLU ARG PHE VAL LEU LYS PHE PRO TYR SEQRES 6 B 112 GLU THR CYS THR ILE LYS VAL VAL GLY GLY TYR GLN VAL SEQRES 7 B 112 ASN ILE ARG VAL GLY ASP THR THR THR ASP VAL ARG TYR SEQRES 8 B 112 LYS ASP ASP MET TYR HIS PHE PHE CYS PRO ALA ILE GLN SEQRES 9 B 112 LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 X 123 GLU THR GLY GLN VAL GLN LEU GLN GLN SER GLY ALA GLU SEQRES 2 X 123 LEU VAL LYS PRO GLY SER SER VAL LYS ILE SER CYS LYS SEQRES 3 X 123 ALA SER GLY TYR THR PHE THR SER ASP ASP MET HIS TRP SEQRES 4 X 123 ILE LYS GLN GLN PRO GLY ASN GLY LEU GLU TRP ILE GLY SEQRES 5 X 123 TRP ILE TYR PRO GLY ASN ASP ASP THR LYS TYR ASN GLN SEQRES 6 X 123 LYS PHE ASN GLY LYS ALA THR LEU THR ALA ASP LYS SER SEQRES 7 X 123 SER SER THR VAL TYR MET GLN LEU SER SER LEU THR SER SEQRES 8 X 123 GLU ASP SER ALA VAL TYR PHE CYS ALA ARG GLY ASP LEU SEQRES 9 X 123 ASN TYR GLY GLY SER MET ASP ALA TRP GLY GLN GLY THR SEQRES 10 X 123 SER VAL THR VAL SER SER SEQRES 1 Y 117 GLU THR GLY ASP THR VAL MET THR GLN SER PRO SER SER SEQRES 2 Y 117 LEU ALA VAL SER ALA GLY GLU THR LEU THR ILE ASN CYS SEQRES 3 Y 117 LYS SER SER GLN ASN LEU PHE SER SER ARG ASN GLN LYS SEQRES 4 Y 117 ASN TYR LEU ALA TRP PHE GLN GLN LYS PRO GLY GLN SER SEQRES 5 Y 117 PRO THR LEU LEU ILE HIS TRP ALA SER THR ARG GLN SER SEQRES 6 Y 117 GLY VAL PRO ASP ARG PHE ILE GLY SER GLY SER GLY THR SEQRES 7 Y 117 ASP PHE THR LEU THR ILE SER SER VAL GLN ALA GLU ASP SEQRES 8 Y 117 LEU ALA ILE TYR TYR CYS GLN GLN TYR TYR ASN SER PRO SEQRES 9 Y 117 LEU THR PHE GLY SER GLY THR LYS LEU GLU ILE LYS ARG FORMUL 7 HOH *616(H2 O) HELIX 1 AA1 SER A 62 ASN A 70 1 9 HELIX 2 AA2 TYR A 99 THR A 103 1 5 HELIX 3 AA3 THR H 47 ASP H 51 5 5 HELIX 4 AA4 GLN H 81 ASN H 84 5 4 HELIX 5 AA5 THR H 106 SER H 110 5 5 HELIX 6 AA6 GLN L 105 LEU L 109 5 5 HELIX 7 AA7 SER B 62 ASN B 70 1 9 HELIX 8 AA8 TYR B 99 THR B 103 1 5 HELIX 9 AA9 THR X 47 ASP X 51 5 5 HELIX 10 AB1 GLN X 81 ASN X 84 5 4 HELIX 11 AB2 THR X 106 SER X 110 5 5 HELIX 12 AB3 GLN Y 105 LEU Y 109 5 5 SHEET 1 AA1 8 THR A 48 CYS A 51 0 SHEET 2 AA1 8 GLU A 55 GLU A 59 -1 O GLU A 59 N THR A 48 SHEET 3 AA1 8 VAL A 94 PRO A 98 -1 O PHE A 97 N VAL A 56 SHEET 4 AA1 8 ALA A 87 ASP A 89 -1 N ALA A 87 O LYS A 96 SHEET 5 AA1 8 ALA B 87 ASP B 89 -1 O LEU B 88 N LEU A 88 SHEET 6 AA1 8 VAL B 94 PRO B 98 -1 O VAL B 94 N ASP B 89 SHEET 7 AA1 8 GLU B 55 GLU B 59 -1 N VAL B 56 O PHE B 97 SHEET 8 AA1 8 THR B 48 CYS B 51 -1 N ILE B 50 O ARG B 57 SHEET 1 AA2 3 SER A 72 VAL A 74 0 SHEET 2 AA2 3 GLY A 109 VAL A 116 -1 O ARG A 115 N SER A 72 SHEET 3 AA2 3 ILE A 104 VAL A 106 -1 N VAL A 106 O GLY A 109 SHEET 1 AA3 3 SER A 72 VAL A 74 0 SHEET 2 AA3 3 GLY A 109 VAL A 116 -1 O ARG A 115 N SER A 72 SHEET 3 AA3 3 ASP A 128 PRO A 135 -1 O CYS A 134 N TYR A 110 SHEET 1 AA4 4 GLN H 22 GLN H 25 0 SHEET 2 AA4 4 VAL H 37 SER H 44 -1 O LYS H 42 N GLN H 24 SHEET 3 AA4 4 THR H 97 LEU H 102 -1 O MET H 100 N ILE H 39 SHEET 4 AA4 4 ALA H 87 ASP H 92 -1 N THR H 90 O TYR H 99 SHEET 1 AA5 6 GLU H 29 VAL H 31 0 SHEET 2 AA5 6 THR H 133 VAL H 137 1 O THR H 136 N GLU H 29 SHEET 3 AA5 6 ALA H 111 GLY H 118 -1 N ALA H 111 O VAL H 135 SHEET 4 AA5 6 ASP H 52 GLN H 58 -1 N HIS H 54 O ALA H 116 SHEET 5 AA5 6 LEU H 64 TYR H 71 -1 O GLU H 65 N LYS H 57 SHEET 6 AA5 6 ASP H 76 TYR H 79 -1 O ASP H 76 N TYR H 71 SHEET 1 AA6 4 GLU H 29 VAL H 31 0 SHEET 2 AA6 4 THR H 133 VAL H 137 1 O THR H 136 N GLU H 29 SHEET 3 AA6 4 ALA H 111 GLY H 118 -1 N ALA H 111 O VAL H 135 SHEET 4 AA6 4 MET H 126 TRP H 129 -1 O ALA H 128 N ARG H 117 SHEET 1 AA7 4 MET L 24 SER L 27 0 SHEET 2 AA7 4 LEU L 39 SER L 45 -1 O LYS L 44 N THR L 25 SHEET 3 AA7 4 ASP L 96 ILE L 101 -1 O LEU L 99 N ILE L 41 SHEET 4 AA7 4 PHE L 88 GLY L 92 -1 N ILE L 89 O THR L 100 SHEET 1 AA8 6 SER L 30 ALA L 32 0 SHEET 2 AA8 6 THR L 128 GLU L 131 1 O LYS L 129 N LEU L 31 SHEET 3 AA8 6 ILE L 111 GLN L 116 -1 N TYR L 112 O THR L 128 SHEET 4 AA8 6 LEU L 59 GLN L 64 -1 N PHE L 62 O TYR L 113 SHEET 5 AA8 6 THR L 71 HIS L 75 -1 O LEU L 73 N TRP L 61 SHEET 6 AA8 6 THR L 79 ARG L 80 -1 O THR L 79 N HIS L 75 SHEET 1 AA9 4 SER L 30 ALA L 32 0 SHEET 2 AA9 4 THR L 128 GLU L 131 1 O LYS L 129 N LEU L 31 SHEET 3 AA9 4 ILE L 111 GLN L 116 -1 N TYR L 112 O THR L 128 SHEET 4 AA9 4 THR L 123 PHE L 124 -1 O THR L 123 N GLN L 116 SHEET 1 AB1 2 PHE L 50 SER L 51 0 SHEET 2 AB1 2 LYS L 56 ASN L 57 -1 O LYS L 56 N SER L 51 SHEET 1 AB2 3 SER B 72 VAL B 74 0 SHEET 2 AB2 3 GLY B 109 VAL B 116 -1 O ARG B 115 N SER B 72 SHEET 3 AB2 3 ILE B 104 VAL B 106 -1 N ILE B 104 O GLN B 111 SHEET 1 AB3 3 SER B 72 VAL B 74 0 SHEET 2 AB3 3 GLY B 109 VAL B 116 -1 O ARG B 115 N SER B 72 SHEET 3 AB3 3 ASP B 128 PRO B 135 -1 O CYS B 134 N TYR B 110 SHEET 1 AB4 4 GLN X 22 GLN X 25 0 SHEET 2 AB4 4 VAL X 37 SER X 44 -1 O SER X 44 N GLN X 22 SHEET 3 AB4 4 THR X 97 LEU X 102 -1 O MET X 100 N ILE X 39 SHEET 4 AB4 4 ALA X 87 ASP X 92 -1 N ASP X 92 O THR X 97 SHEET 1 AB5 6 GLU X 29 VAL X 31 0 SHEET 2 AB5 6 THR X 133 VAL X 137 1 O SER X 134 N GLU X 29 SHEET 3 AB5 6 ALA X 111 GLY X 118 -1 N ALA X 111 O VAL X 135 SHEET 4 AB5 6 ASP X 52 GLN X 58 -1 N HIS X 54 O ALA X 116 SHEET 5 AB5 6 LEU X 64 TYR X 71 -1 O GLU X 65 N LYS X 57 SHEET 6 AB5 6 ASP X 76 TYR X 79 -1 O ASP X 76 N TYR X 71 SHEET 1 AB6 4 GLU X 29 VAL X 31 0 SHEET 2 AB6 4 THR X 133 VAL X 137 1 O SER X 134 N GLU X 29 SHEET 3 AB6 4 ALA X 111 GLY X 118 -1 N ALA X 111 O VAL X 135 SHEET 4 AB6 4 MET X 126 TRP X 129 -1 O ALA X 128 N ARG X 117 SHEET 1 AB7 4 MET Y 24 SER Y 27 0 SHEET 2 AB7 4 LEU Y 39 SER Y 45 -1 O LYS Y 44 N THR Y 25 SHEET 3 AB7 4 ASP Y 96 ILE Y 101 -1 O PHE Y 97 N CYS Y 43 SHEET 4 AB7 4 PHE Y 88 SER Y 93 -1 N ILE Y 89 O THR Y 100 SHEET 1 AB8 6 SER Y 30 VAL Y 33 0 SHEET 2 AB8 6 THR Y 128 ILE Y 132 1 O LYS Y 129 N LEU Y 31 SHEET 3 AB8 6 ALA Y 110 GLN Y 116 -1 N TYR Y 112 O THR Y 128 SHEET 4 AB8 6 LEU Y 59 GLN Y 64 -1 N PHE Y 62 O TYR Y 113 SHEET 5 AB8 6 PRO Y 70 HIS Y 75 -1 O THR Y 71 N GLN Y 63 SHEET 6 AB8 6 THR Y 79 ARG Y 80 -1 O THR Y 79 N HIS Y 75 SHEET 1 AB9 4 SER Y 30 VAL Y 33 0 SHEET 2 AB9 4 THR Y 128 ILE Y 132 1 O LYS Y 129 N LEU Y 31 SHEET 3 AB9 4 ALA Y 110 GLN Y 116 -1 N TYR Y 112 O THR Y 128 SHEET 4 AB9 4 THR Y 123 PHE Y 124 -1 O THR Y 123 N GLN Y 116 SHEET 1 AC1 2 PHE Y 50 SER Y 51 0 SHEET 2 AC1 2 LYS Y 56 ASN Y 57 -1 O LYS Y 56 N SER Y 51 SSBOND 1 CYS A 51 CYS A 134 1555 1555 2.03 SSBOND 2 CYS A 84 CYS A 102 1555 1555 2.03 SSBOND 3 CYS H 41 CYS H 115 1555 1555 2.03 SSBOND 4 CYS L 43 CYS L 114 1555 1555 2.03 SSBOND 5 CYS B 51 CYS B 134 1555 1555 2.03 SSBOND 6 CYS B 84 CYS B 102 1555 1555 2.03 SSBOND 7 CYS X 41 CYS X 115 1555 1555 2.03 SSBOND 8 CYS Y 43 CYS Y 114 1555 1555 2.03 CISPEP 1 SER L 27 PRO L 28 0 -1.60 CISPEP 2 SER L 120 PRO L 121 0 0.87 CISPEP 3 SER Y 27 PRO Y 28 0 -1.03 CISPEP 4 SER Y 120 PRO Y 121 0 1.99 CRYST1 91.640 92.290 91.170 90.00 90.00 90.00 P 21 21 21 8 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 0.010912 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010835 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010969 0.00000 MTRIX1 1 0.057928 0.998205 -0.015223 24.37735 1 MTRIX2 1 0.998315 -0.057871 0.004183 -25.75424 1 MTRIX3 1 0.003295 -0.015440 -0.999875 -23.28042 1 MTRIX1 2 0.057533 0.998169 -0.018674 24.18027 1 MTRIX2 2 0.998331 -0.057428 0.006141 -25.27227 1 MTRIX3 2 0.005057 -0.018996 -0.999807 -23.82157 1 MTRIX1 3 0.058294 0.998106 -0.019630 24.37258 1 MTRIX2 3 0.998059 -0.058700 -0.020802 -25.59329 1 MTRIX3 3 -0.021915 -0.018379 -0.999591 -23.83342 1