HEADER CELL ADHESION 21-OCT-24 9H4S TITLE STRUCTURE OF FERTILIZATION-BLOCKING MONOCLONAL ANTIBODY IE-3 VHVL TITLE 2 BOUND TO THE ZP-N1 DOMAIN OF MOUSE ZP2 (CRYSTAL FORM II) 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_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHLSEC; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_TAXID: 10116; SOURCE 14 CELL_LINE: HYBRIDOMA; SOURCE 15 ATCC: CRL-2463; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PHLSEC3; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 23 ORGANISM_TAXID: 10116; SOURCE 24 CELL_LINE: HYBRIDOMA; SOURCE 25 ATCC: CRL-2463; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 EXPRESSION_SYSTEM_CELL_LINE: HEK293T; SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 30 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 9H4S 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. 2.02 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) : 2.02 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.31 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.510 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 66919 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.190 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.240 REMARK 3 FREE R VALUE TEST SET COUNT : 1498 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 43.3100 - 4.4900 1.00 6250 143 0.1499 0.1662 REMARK 3 2 4.4900 - 3.5700 1.00 6133 144 0.1475 0.1500 REMARK 3 3 3.5700 - 3.1100 1.00 6114 136 0.1871 0.1979 REMARK 3 4 3.1100 - 2.8300 0.99 6069 136 0.2189 0.2581 REMARK 3 5 2.8300 - 2.6300 0.99 6028 138 0.2285 0.2345 REMARK 3 6 2.6300 - 2.4700 0.98 5988 136 0.2281 0.2607 REMARK 3 7 2.4700 - 2.3500 0.97 5913 136 0.2519 0.2959 REMARK 3 8 2.3500 - 2.2500 0.96 5865 137 0.2543 0.2848 REMARK 3 9 2.2500 - 2.1600 0.95 5760 130 0.2654 0.2716 REMARK 3 10 2.1600 - 2.0900 0.94 5694 131 0.2854 0.2953 REMARK 3 11 2.0900 - 2.0200 0.92 5607 131 0.3081 0.3196 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) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.311 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 49.56 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.81 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 : 0.003 5369 REMARK 3 ANGLE : 0.612 7284 REMARK 3 CHIRALITY : 0.045 800 REMARK 3 PLANARITY : 0.003 937 REMARK 3 DIHEDRAL : 11.954 1924 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 37 THROUGH 138) REMARK 3 ORIGIN FOR THE GROUP (A): 63.3973 71.5640 -2.1645 REMARK 3 T TENSOR REMARK 3 T11: 0.3060 T22: 0.3298 REMARK 3 T33: 0.1615 T12: -0.0068 REMARK 3 T13: 0.0340 T23: -0.0071 REMARK 3 L TENSOR REMARK 3 L11: 2.8925 L22: 2.9535 REMARK 3 L33: 1.0800 L12: -0.5146 REMARK 3 L13: 0.8765 L23: -0.6673 REMARK 3 S TENSOR REMARK 3 S11: 0.0852 S12: 0.0197 S13: 0.1049 REMARK 3 S21: -0.0909 S22: -0.0444 S23: -0.0700 REMARK 3 S31: 0.1449 S32: 0.0869 S33: -0.0328 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 20 THROUGH 139) REMARK 3 ORIGIN FOR THE GROUP (A): 47.8206 97.9648 11.4923 REMARK 3 T TENSOR REMARK 3 T11: 0.7269 T22: 0.6877 REMARK 3 T33: 0.8010 T12: -0.1585 REMARK 3 T13: 0.3899 T23: -0.1842 REMARK 3 L TENSOR REMARK 3 L11: 2.4500 L22: 3.0634 REMARK 3 L33: 2.7040 L12: -0.2725 REMARK 3 L13: -1.0172 L23: 0.3648 REMARK 3 S TENSOR REMARK 3 S11: 0.4876 S12: -0.8541 S13: 0.4986 REMARK 3 S21: 0.8800 S22: -0.2703 S23: 0.9638 REMARK 3 S31: -0.2952 S32: -0.0856 S33: 0.0155 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 18 THROUGH 133) REMARK 3 ORIGIN FOR THE GROUP (A): 62.4711 103.5483 -3.6329 REMARK 3 T TENSOR REMARK 3 T11: 0.3209 T22: 0.2637 REMARK 3 T33: 0.4953 T12: -0.0054 REMARK 3 T13: 0.1213 T23: -0.0251 REMARK 3 L TENSOR REMARK 3 L11: 4.2854 L22: 2.4740 REMARK 3 L33: 2.2518 L12: 1.3657 REMARK 3 L13: -0.0942 L23: 0.0700 REMARK 3 S TENSOR REMARK 3 S11: 0.2229 S12: -0.1194 S13: 0.9258 REMARK 3 S21: 0.2246 S22: -0.2052 S23: 0.4013 REMARK 3 S31: -0.1917 S32: 0.0670 S33: 0.0105 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 36 THROUGH 137) REMARK 3 ORIGIN FOR THE GROUP (A): 110.5970 122.4880 -27.0130 REMARK 3 T TENSOR REMARK 3 T11: 0.3940 T22: 0.3353 REMARK 3 T33: 0.2080 T12: -0.0076 REMARK 3 T13: 0.0245 T23: 0.0215 REMARK 3 L TENSOR REMARK 3 L11: 3.2669 L22: 2.6875 REMARK 3 L33: 1.2994 L12: 0.8245 REMARK 3 L13: 0.4674 L23: 1.2066 REMARK 3 S TENSOR REMARK 3 S11: -0.0753 S12: 0.0425 S13: 0.1231 REMARK 3 S21: 0.1763 S22: 0.0683 S23: 0.1677 REMARK 3 S31: -0.0173 S32: 0.1423 S33: 0.0144 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'X' AND RESID 20 THROUGH 139) REMARK 3 ORIGIN FOR THE GROUP (A): 87.6271 103.8597 -12.4283 REMARK 3 T TENSOR REMARK 3 T11: 0.3740 T22: 0.3412 REMARK 3 T33: 0.3845 T12: 0.0284 REMARK 3 T13: 0.0046 T23: 0.0781 REMARK 3 L TENSOR REMARK 3 L11: 4.3638 L22: 2.5536 REMARK 3 L33: 4.3168 L12: 1.6729 REMARK 3 L13: -1.4502 L23: -1.0926 REMARK 3 S TENSOR REMARK 3 S11: 0.0696 S12: -0.4595 S13: -0.3614 REMARK 3 S21: 0.1047 S22: -0.1148 S23: -0.2143 REMARK 3 S31: 0.2727 S32: 0.3177 S33: 0.0217 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'Y' AND RESID 18 THROUGH 133) REMARK 3 ORIGIN FOR THE GROUP (A): 79.1720 117.0996 -27.2824 REMARK 3 T TENSOR REMARK 3 T11: 0.3559 T22: 0.3604 REMARK 3 T33: 0.5027 T12: -0.0395 REMARK 3 T13: -0.0281 T23: 0.1417 REMARK 3 L TENSOR REMARK 3 L11: 3.6001 L22: 3.6863 REMARK 3 L33: 2.8364 L12: 0.6185 REMARK 3 L13: -1.1151 L23: -1.2190 REMARK 3 S TENSOR REMARK 3 S11: -0.0541 S12: 0.5230 S13: 0.5513 REMARK 3 S21: -0.3757 S22: 0.4222 S23: 0.8420 REMARK 3 S31: 0.0050 S32: -0.3714 S33: -0.2813 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 37 through 137) 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 37 through 137) 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" 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" 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" 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" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9H4S 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_1292142648. 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 : 5.6 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 : 68723 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020 REMARK 200 RESOLUTION RANGE LOW (A) : 43.314 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.10 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: PARTIALLY REFINED MODEL OF PDB ID 6GF4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.95 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M LITHIUM SULFATE, 0.2 M AMMONIUM REMARK 280 SULFATE, 0.1 TRI-SODIUM CITRATE PH 5.6, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y,X,Z+3/4 REMARK 290 4555 Y,-X,Z+1/4 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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.74000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.61000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 17.87000 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 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 ARG L 134 REMARK 465 VAL B 35 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 ARG Y 134 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 ALA L 77 -16.23 70.63 REMARK 500 SER L 78 -3.57 -143.95 REMARK 500 PHE B 93 68.23 60.04 REMARK 500 ALA Y 77 -15.95 70.51 REMARK 500 SER Y 78 -3.69 -143.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9H4R RELATED DB: PDB REMARK 900 ORTHORHOMBIC 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 9H4S A 35 138 UNP P20239 ZP2_MOUSE 35 138 DBREF 9H4S H 17 139 PDB 9H4S 9H4S 17 139 DBREF 9H4S L 18 134 PDB 9H4S 9H4S 18 134 DBREF 9H4S B 35 138 UNP P20239 ZP2_MOUSE 35 138 DBREF 9H4S X 17 139 PDB 9H4S 9H4S 17 139 DBREF 9H4S Y 18 134 PDB 9H4S 9H4S 18 134 SEQADV 9H4S SER A 83 UNP P20239 ASN 83 ENGINEERED MUTATION SEQADV 9H4S LEU A 139 UNP P20239 EXPRESSION TAG SEQADV 9H4S GLU A 140 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS A 141 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS A 142 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS A 143 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS A 144 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS A 145 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS A 146 UNP P20239 EXPRESSION TAG SEQADV 9H4S SER B 83 UNP P20239 ASN 83 ENGINEERED MUTATION SEQADV 9H4S LEU B 139 UNP P20239 EXPRESSION TAG SEQADV 9H4S GLU B 140 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS B 141 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS B 142 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS B 143 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS B 144 UNP P20239 EXPRESSION TAG SEQADV 9H4S HIS B 145 UNP P20239 EXPRESSION TAG SEQADV 9H4S 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 *308(H2 O) HELIX 1 AA1 PRO A 98 THR A 103 1 6 HELIX 2 AA2 THR H 47 ASP H 51 5 5 HELIX 3 AA3 GLN H 81 ASN H 84 5 4 HELIX 4 AA4 THR H 106 SER H 110 5 5 HELIX 5 AA5 LEU H 120 GLY H 123 5 4 HELIX 6 AA6 GLN L 105 LEU L 109 5 5 HELIX 7 AA7 TYR B 99 THR B 103 1 5 HELIX 8 AA8 THR X 47 ASP X 51 5 5 HELIX 9 AA9 GLN X 81 ASN X 84 5 4 HELIX 10 AB1 THR X 106 SER X 110 5 5 HELIX 11 AB2 LEU X 120 GLY X 123 5 4 HELIX 12 AB3 GLN Y 105 LEU Y 109 5 5 SHEET 1 AA1 4 GLY A 47 CYS A 51 0 SHEET 2 AA1 4 VAL A 56 PHE A 60 -1 O ARG A 57 N ILE A 50 SHEET 3 AA1 4 VAL A 94 PHE A 97 -1 O PHE A 97 N VAL A 56 SHEET 4 AA1 4 ALA A 87 ASP A 89 -1 N ASP A 89 O VAL A 94 SHEET 1 AA2 3 ASN A 70 VAL A 74 0 SHEET 2 AA2 3 GLY A 109 GLY A 117 -1 O GLY A 117 N ASN A 70 SHEET 3 AA2 3 ILE A 104 VAL A 106 -1 N VAL A 106 O GLY A 109 SHEET 1 AA3 3 ASN A 70 VAL A 74 0 SHEET 2 AA3 3 GLY A 109 GLY A 117 -1 O GLY A 117 N ASN A 70 SHEET 3 AA3 3 ASP A 128 PRO A 135 -1 O PHE A 132 N VAL A 112 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 VAL H 98 N CYS H 41 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 TYR H 113 O THR H 133 SHEET 4 AA5 6 ASP H 52 GLN H 58 -1 N HIS H 54 O ALA H 116 SHEET 5 AA5 6 GLU H 65 ILE H 70 -1 O GLU H 65 N LYS H 57 SHEET 6 AA5 6 THR H 77 TYR H 79 -1 O LYS H 78 N TRP H 69 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 TYR H 113 O THR H 133 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 ASN L 42 N SER L 27 SHEET 3 AA7 4 ASP L 96 ILE L 101 -1 O PHE L 97 N CYS L 43 SHEET 4 AA7 4 PHE L 88 SER L 93 -1 N ILE L 89 O THR L 100 SHEET 1 AA8 6 SER L 30 VAL L 33 0 SHEET 2 AA8 6 THR L 128 ILE L 132 1 O GLU L 131 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 ALA L 60 O GLN L 115 SHEET 5 AA8 6 THR L 71 HIS L 75 -1 O THR L 71 N GLN L 63 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 VAL L 33 0 SHEET 2 AA9 4 THR L 128 ILE L 132 1 O GLU L 131 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 4 GLY B 47 CYS B 51 0 SHEET 2 AB2 4 GLU B 55 PHE B 60 -1 O ARG B 57 N ILE B 50 SHEET 3 AB2 4 VAL B 94 PRO B 98 -1 O PHE B 97 N VAL B 56 SHEET 4 AB2 4 ALA B 87 ASP B 89 -1 N ASP B 89 O VAL B 94 SHEET 1 AB3 3 ASN B 70 VAL B 74 0 SHEET 2 AB3 3 GLY B 109 GLY B 117 -1 O GLY B 117 N ASN B 70 SHEET 3 AB3 3 ILE B 104 VAL B 106 -1 N VAL B 106 O GLY B 109 SHEET 1 AB4 3 ASN B 70 VAL B 74 0 SHEET 2 AB4 3 GLY B 109 GLY B 117 -1 O GLY B 117 N ASN B 70 SHEET 3 AB4 3 ASP B 128 PRO B 135 -1 O PHE B 132 N VAL B 112 SHEET 1 AB5 4 GLN X 22 GLN X 25 0 SHEET 2 AB5 4 VAL X 37 SER X 44 -1 O LYS X 42 N GLN X 24 SHEET 3 AB5 4 THR X 97 LEU X 102 -1 O VAL X 98 N CYS X 41 SHEET 4 AB5 4 ALA X 87 ASP X 92 -1 N THR X 90 O TYR X 99 SHEET 1 AB6 6 GLU X 29 VAL X 31 0 SHEET 2 AB6 6 THR X 133 VAL X 137 1 O THR X 136 N VAL X 31 SHEET 3 AB6 6 ALA X 111 GLY X 118 -1 N TYR X 113 O THR X 133 SHEET 4 AB6 6 ASP X 52 GLN X 58 -1 N HIS X 54 O ALA X 116 SHEET 5 AB6 6 GLU X 65 ILE X 70 -1 O GLU X 65 N LYS X 57 SHEET 6 AB6 6 THR X 77 TYR X 79 -1 O LYS X 78 N TRP X 69 SHEET 1 AB7 4 GLU X 29 VAL X 31 0 SHEET 2 AB7 4 THR X 133 VAL X 137 1 O THR X 136 N VAL X 31 SHEET 3 AB7 4 ALA X 111 GLY X 118 -1 N TYR X 113 O THR X 133 SHEET 4 AB7 4 MET X 126 TRP X 129 -1 O ALA X 128 N ARG X 117 SHEET 1 AB8 4 MET Y 24 SER Y 27 0 SHEET 2 AB8 4 LEU Y 39 SER Y 45 -1 O ASN Y 42 N SER Y 27 SHEET 3 AB8 4 ASP Y 96 ILE Y 101 -1 O PHE Y 97 N CYS Y 43 SHEET 4 AB8 4 PHE Y 88 SER Y 93 -1 N ILE Y 89 O THR Y 100 SHEET 1 AB9 6 SER Y 30 SER Y 34 0 SHEET 2 AB9 6 THR Y 128 LYS Y 133 1 O LYS Y 129 N LEU Y 31 SHEET 3 AB9 6 ALA Y 110 GLN Y 116 -1 N ALA Y 110 O LEU Y 130 SHEET 4 AB9 6 LEU Y 59 GLN Y 64 -1 N PHE Y 62 O TYR Y 113 SHEET 5 AB9 6 THR Y 71 HIS Y 75 -1 O THR Y 71 N GLN Y 63 SHEET 6 AB9 6 THR Y 79 ARG Y 80 -1 O THR Y 79 N HIS Y 75 SHEET 1 AC1 4 SER Y 30 SER Y 34 0 SHEET 2 AC1 4 THR Y 128 LYS Y 133 1 O LYS Y 129 N LEU Y 31 SHEET 3 AC1 4 ALA Y 110 GLN Y 116 -1 N ALA Y 110 O LEU Y 130 SHEET 4 AC1 4 THR Y 123 PHE Y 124 -1 O THR Y 123 N GLN Y 116 SHEET 1 AC2 2 PHE Y 50 SER Y 51 0 SHEET 2 AC2 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 -5.05 CISPEP 2 SER L 120 PRO L 121 0 -0.56 CISPEP 3 SER Y 27 PRO Y 28 0 -5.41 CISPEP 4 SER Y 120 PRO Y 121 0 -0.12 CRYST1 121.750 121.750 71.480 90.00 90.00 90.00 P 43 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 0.008214 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008214 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013990 0.00000 MTRIX1 1 -0.145344 -0.989372 0.004188 190.75855 1 MTRIX2 1 0.989380 -0.145336 0.002264 70.33894 1 MTRIX3 1 -0.001631 0.004472 0.999989 -25.24318 1 MTRIX1 2 -0.102353 -0.991501 0.080305 188.73198 1 MTRIX2 2 0.994716 -0.101370 0.016233 66.03653 1 MTRIX3 2 -0.007954 0.081542 0.996638 -31.48981 1 MTRIX1 3 -0.150529 -0.985530 0.077920 190.91024 1 MTRIX2 3 0.987804 -0.146765 0.051994 70.77559 1 MTRIX3 3 -0.039806 0.084797 0.995603 -29.96127 1