HEADER SIGNALING PROTEIN 26-JAN-24 8VTI TITLE LATROPHILIN-3 (ADGRL3) HORMR AND GAIN DOMAINS IN THE CONTEXT OF THE TITLE 2 HOLORECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: ISOFORM 4 OF ADHESION G PROTEIN-COUPLED RECEPTOR L3; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CALCIUM-INDEPENDENT ALPHA-LATROTOXIN RECEPTOR 3,CIRL-3, COMPND 5 LATROPHILIN-3,LECTOMEDIN-3; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ISOFORM 4 OF ADHESION G PROTEIN-COUPLED RECEPTOR L3; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: CALCIUM-INDEPENDENT ALPHA-LATROTOXIN RECEPTOR 3,CIRL-3, COMPND 11 LATROPHILIN-3,LECTOMEDIN-3; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: SAB LIGHT CHAIN; COMPND 15 CHAIN: C; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: SAB HEAVY CHAIN; COMPND 19 CHAIN: D; COMPND 20 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADGRL3, KIAA0768, LEC3, LPHN3; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 GENE: ADGRL3, KIAA0768, LEC3, LPHN3; SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 21 ORGANISM_TAXID: 32630; SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 24 MOL_ID: 4; SOURCE 25 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 26 ORGANISM_TAXID: 32630; SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ADHESION GPCR, GAIN DOMAIN, CELL-CELL ADHESION, SYNAPSE, SIGNALING KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.P.KORDON,S.J.BANDEKAR,D.ARAC REVDAT 1 11-DEC-24 8VTI 0 JRNL AUTH S.P.KORDON,K.CECHOVA,S.J.BANDEKAR,K.LEON,P.DUTKA,G.SIFFER, JRNL AUTH 2 A.A.KOSSIAKOFF,R.VAFABAKHSH,D.ARAC JRNL TITL CONFORMATIONAL COUPLING BETWEEN EXTRACELLULAR AND JRNL TITL 2 TRANSMEMBRANE DOMAINS MODULATES HOLO-ADHESION GPCR FUNCTION. JRNL REF NAT COMMUN V. 15 10545 2024 JRNL REFN ESSN 2041-1723 JRNL PMID 39627215 JRNL DOI 10.1038/S41467-024-54836-4 REMARK 2 REMARK 2 RESOLUTION. 3.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.900 REMARK 3 NUMBER OF PARTICLES : 96958 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8VTI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1000281213. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : LATROPHILIN3/ADGRL3 REMARK 245 HORMR+GAIN/7TM HOLORECEPTOR IN REMARK 245 COMPLEX WITH SYNTHETIC ANTIBODY REMARK 245 FRAGMENT; LATROPHILIN3/ADGRL3; REMARK 245 SYNTHETIC ANTIBODY FRAGMENT REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 110.00 REMARK 245 ILLUMINATION MODE : OTHER REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E 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 ASP A 480 REMARK 465 TYR A 481 REMARK 465 LYS A 482 REMARK 465 ASP A 483 REMARK 465 ASP A 484 REMARK 465 ASP A 485 REMARK 465 ASP A 486 REMARK 465 ALA A 487 REMARK 465 MET A 488 REMARK 465 ALA A 489 REMARK 465 GLN A 490 REMARK 465 ILE A 491 REMARK 465 PRO A 492 REMARK 465 ALA A 493 REMARK 465 LEU A 494 REMARK 465 GLU A 495 REMARK 465 GLU A 496 REMARK 465 VAL B 866 REMARK 465 LYS B 867 REMARK 465 HIS B 868 REMARK 465 SER B 869 REMARK 465 ASP B 870 REMARK 465 ALA B 871 REMARK 465 VAL B 872 REMARK 465 HIS B 873 REMARK 465 ASP B 874 REMARK 465 LEU B 875 REMARK 465 LEU B 876 REMARK 465 LEU B 877 REMARK 465 ASP B 878 REMARK 465 VAL B 879 REMARK 465 ILE B 880 REMARK 465 THR B 881 REMARK 465 TRP B 882 REMARK 465 VAL B 883 REMARK 465 GLY B 884 REMARK 465 ILE B 885 REMARK 465 LEU B 886 REMARK 465 LEU B 887 REMARK 465 SER B 888 REMARK 465 LEU B 889 REMARK 465 VAL B 890 REMARK 465 CYS B 891 REMARK 465 LEU B 892 REMARK 465 LEU B 893 REMARK 465 ILE B 894 REMARK 465 CYS B 895 REMARK 465 ILE B 896 REMARK 465 PHE B 897 REMARK 465 THR B 898 REMARK 465 PHE B 899 REMARK 465 CYS B 900 REMARK 465 PHE B 901 REMARK 465 PHE B 902 REMARK 465 ARG B 903 REMARK 465 GLY B 904 REMARK 465 LEU B 905 REMARK 465 GLN B 906 REMARK 465 SER B 907 REMARK 465 ASP B 908 REMARK 465 ARG B 909 REMARK 465 ASN B 910 REMARK 465 THR B 911 REMARK 465 ILE B 912 REMARK 465 HIS B 913 REMARK 465 LYS B 914 REMARK 465 ASN B 915 REMARK 465 LEU B 916 REMARK 465 CYS B 917 REMARK 465 ILE B 918 REMARK 465 SER B 919 REMARK 465 LEU B 920 REMARK 465 PHE B 921 REMARK 465 VAL B 922 REMARK 465 ALA B 923 REMARK 465 GLU B 924 REMARK 465 LEU B 925 REMARK 465 LEU B 926 REMARK 465 PHE B 927 REMARK 465 LEU B 928 REMARK 465 ILE B 929 REMARK 465 GLY B 930 REMARK 465 ILE B 931 REMARK 465 ASN B 932 REMARK 465 ARG B 933 REMARK 465 THR B 934 REMARK 465 ASP B 935 REMARK 465 GLN B 936 REMARK 465 PRO B 937 REMARK 465 ILE B 938 REMARK 465 ALA B 939 REMARK 465 CYS B 940 REMARK 465 ALA B 941 REMARK 465 VAL B 942 REMARK 465 PHE B 943 REMARK 465 ALA B 944 REMARK 465 ALA B 945 REMARK 465 LEU B 946 REMARK 465 LEU B 947 REMARK 465 HIS B 948 REMARK 465 PHE B 949 REMARK 465 PHE B 950 REMARK 465 PHE B 951 REMARK 465 LEU B 952 REMARK 465 ALA B 953 REMARK 465 ALA B 954 REMARK 465 PHE B 955 REMARK 465 THR B 956 REMARK 465 TRP B 957 REMARK 465 MET B 958 REMARK 465 PHE B 959 REMARK 465 LEU B 960 REMARK 465 GLU B 961 REMARK 465 GLY B 962 REMARK 465 VAL B 963 REMARK 465 GLN B 964 REMARK 465 LEU B 965 REMARK 465 TYR B 966 REMARK 465 ILE B 967 REMARK 465 MET B 968 REMARK 465 LEU B 969 REMARK 465 VAL B 970 REMARK 465 GLU B 971 REMARK 465 VAL B 972 REMARK 465 PHE B 973 REMARK 465 GLU B 974 REMARK 465 SER B 975 REMARK 465 GLU B 976 REMARK 465 HIS B 977 REMARK 465 SER B 978 REMARK 465 ARG B 979 REMARK 465 ARG B 980 REMARK 465 LYS B 981 REMARK 465 TYR B 982 REMARK 465 PHE B 983 REMARK 465 TYR B 984 REMARK 465 LEU B 985 REMARK 465 VAL B 986 REMARK 465 GLY B 987 REMARK 465 TYR B 988 REMARK 465 GLY B 989 REMARK 465 MET B 990 REMARK 465 PRO B 991 REMARK 465 ALA B 992 REMARK 465 LEU B 993 REMARK 465 ILE B 994 REMARK 465 VAL B 995 REMARK 465 ALA B 996 REMARK 465 VAL B 997 REMARK 465 SER B 998 REMARK 465 ALA B 999 REMARK 465 ALA B 1000 REMARK 465 VAL B 1001 REMARK 465 ASP B 1002 REMARK 465 TYR B 1003 REMARK 465 ARG B 1004 REMARK 465 SER B 1005 REMARK 465 TYR B 1006 REMARK 465 GLY B 1007 REMARK 465 THR B 1008 REMARK 465 ASP B 1009 REMARK 465 LYS B 1010 REMARK 465 VAL B 1011 REMARK 465 CYS B 1012 REMARK 465 TRP B 1013 REMARK 465 LEU B 1014 REMARK 465 ARG B 1015 REMARK 465 LEU B 1016 REMARK 465 ASP B 1017 REMARK 465 THR B 1018 REMARK 465 TYR B 1019 REMARK 465 PHE B 1020 REMARK 465 ILE B 1021 REMARK 465 TRP B 1022 REMARK 465 SER B 1023 REMARK 465 PHE B 1024 REMARK 465 ILE B 1025 REMARK 465 GLY B 1026 REMARK 465 PRO B 1027 REMARK 465 ALA B 1028 REMARK 465 THR B 1029 REMARK 465 LEU B 1030 REMARK 465 ILE B 1031 REMARK 465 ILE B 1032 REMARK 465 MET B 1033 REMARK 465 LEU B 1034 REMARK 465 ASN B 1035 REMARK 465 VAL B 1036 REMARK 465 ILE B 1037 REMARK 465 PHE B 1038 REMARK 465 LEU B 1039 REMARK 465 GLY B 1040 REMARK 465 ILE B 1041 REMARK 465 ALA B 1042 REMARK 465 LEU B 1043 REMARK 465 TYR B 1044 REMARK 465 LYS B 1045 REMARK 465 MET B 1046 REMARK 465 PHE B 1047 REMARK 465 HIS B 1048 REMARK 465 HIS B 1049 REMARK 465 THR B 1050 REMARK 465 ALA B 1051 REMARK 465 ILE B 1052 REMARK 465 LEU B 1053 REMARK 465 LYS B 1054 REMARK 465 PRO B 1055 REMARK 465 GLU B 1056 REMARK 465 SER B 1057 REMARK 465 GLY B 1058 REMARK 465 CYS B 1059 REMARK 465 LEU B 1060 REMARK 465 ASP B 1061 REMARK 465 ASN B 1062 REMARK 465 ILE B 1063 REMARK 465 ASN B 1064 REMARK 465 TYR B 1065 REMARK 465 GLU B 1066 REMARK 465 ASP B 1067 REMARK 465 ASN B 1068 REMARK 465 ARG B 1069 REMARK 465 PRO B 1070 REMARK 465 PHE B 1071 REMARK 465 ILE B 1072 REMARK 465 LYS B 1073 REMARK 465 SER B 1074 REMARK 465 TRP B 1075 REMARK 465 VAL B 1076 REMARK 465 ILE B 1077 REMARK 465 GLY B 1078 REMARK 465 ALA B 1079 REMARK 465 ILE B 1080 REMARK 465 ALA B 1081 REMARK 465 LEU B 1082 REMARK 465 LEU B 1083 REMARK 465 CYS B 1084 REMARK 465 LEU B 1085 REMARK 465 LEU B 1086 REMARK 465 GLY B 1087 REMARK 465 LEU B 1088 REMARK 465 THR B 1089 REMARK 465 TRP B 1090 REMARK 465 ALA B 1091 REMARK 465 PHE B 1092 REMARK 465 GLY B 1093 REMARK 465 LEU B 1094 REMARK 465 MET B 1095 REMARK 465 TYR B 1096 REMARK 465 ILE B 1097 REMARK 465 ASN B 1098 REMARK 465 GLU B 1099 REMARK 465 SER B 1100 REMARK 465 THR B 1101 REMARK 465 VAL B 1102 REMARK 465 ILE B 1103 REMARK 465 MET B 1104 REMARK 465 ALA B 1105 REMARK 465 TYR B 1106 REMARK 465 LEU B 1107 REMARK 465 PHE B 1108 REMARK 465 THR B 1109 REMARK 465 ILE B 1110 REMARK 465 PHE B 1111 REMARK 465 ASN B 1112 REMARK 465 SER B 1113 REMARK 465 LEU B 1114 REMARK 465 GLN B 1115 REMARK 465 GLY B 1116 REMARK 465 MET B 1117 REMARK 465 PHE B 1118 REMARK 465 ILE B 1119 REMARK 465 PHE B 1120 REMARK 465 ILE B 1121 REMARK 465 PHE B 1122 REMARK 465 HIS B 1123 REMARK 465 CYS B 1124 REMARK 465 VAL B 1125 REMARK 465 LEU B 1126 REMARK 465 GLN B 1127 REMARK 465 LYS B 1128 REMARK 465 LYS B 1129 REMARK 465 VAL B 1130 REMARK 465 ARG B 1131 REMARK 465 LYS B 1132 REMARK 465 GLU B 1133 REMARK 465 TYR B 1134 REMARK 465 GLY B 1135 REMARK 465 LYS B 1136 REMARK 465 CYS B 1137 REMARK 465 LEU B 1138 REMARK 465 ARG B 1139 REMARK 465 THR B 1140 REMARK 465 HIS B 1141 REMARK 465 CYS B 1142 REMARK 465 CYS B 1143 REMARK 465 SER B 1144 REMARK 465 GLY B 1145 REMARK 465 LYS B 1146 REMARK 465 SER B 1147 REMARK 465 THR B 1148 REMARK 465 GLU B 1149 REMARK 465 SER B 1150 REMARK 465 SER B 1151 REMARK 465 ILE B 1152 REMARK 465 GLY B 1153 REMARK 465 SER B 1154 REMARK 465 GLY B 1155 REMARK 465 LYS B 1156 REMARK 465 THR B 1157 REMARK 465 SER B 1158 REMARK 465 GLY B 1159 REMARK 465 SER B 1160 REMARK 465 HIS B 1161 REMARK 465 HIS B 1162 REMARK 465 HIS B 1163 REMARK 465 HIS B 1164 REMARK 465 HIS B 1165 REMARK 465 HIS B 1166 REMARK 465 HIS B 1167 REMARK 465 HIS B 1168 REMARK 465 SER C 1 REMARK 465 ASP C 2 REMARK 465 LYS C 108 REMARK 465 ARG C 109 REMARK 465 THR C 110 REMARK 465 VAL C 111 REMARK 465 ALA C 112 REMARK 465 ALA C 113 REMARK 465 PRO C 114 REMARK 465 SER C 115 REMARK 465 VAL C 116 REMARK 465 PHE C 117 REMARK 465 ILE C 118 REMARK 465 PHE C 119 REMARK 465 PRO C 120 REMARK 465 PRO C 121 REMARK 465 SER C 122 REMARK 465 ASP C 123 REMARK 465 SER C 124 REMARK 465 GLN C 125 REMARK 465 LEU C 126 REMARK 465 LYS C 127 REMARK 465 SER C 128 REMARK 465 GLY C 129 REMARK 465 THR C 130 REMARK 465 ALA C 131 REMARK 465 SER C 132 REMARK 465 VAL C 133 REMARK 465 VAL C 134 REMARK 465 CYS C 135 REMARK 465 LEU C 136 REMARK 465 LEU C 137 REMARK 465 ASN C 138 REMARK 465 ASN C 139 REMARK 465 PHE C 140 REMARK 465 TYR C 141 REMARK 465 PRO C 142 REMARK 465 ARG C 143 REMARK 465 GLU C 144 REMARK 465 ALA C 145 REMARK 465 LYS C 146 REMARK 465 VAL C 147 REMARK 465 GLN C 148 REMARK 465 TRP C 149 REMARK 465 LYS C 150 REMARK 465 VAL C 151 REMARK 465 ASP C 152 REMARK 465 ASN C 153 REMARK 465 ALA C 154 REMARK 465 LEU C 155 REMARK 465 GLN C 156 REMARK 465 SER C 157 REMARK 465 GLY C 158 REMARK 465 ASN C 159 REMARK 465 SER C 160 REMARK 465 GLN C 161 REMARK 465 GLU C 162 REMARK 465 SER C 163 REMARK 465 VAL C 164 REMARK 465 THR C 165 REMARK 465 GLU C 166 REMARK 465 GLN C 167 REMARK 465 ASP C 168 REMARK 465 SER C 169 REMARK 465 LYS C 170 REMARK 465 ASP C 171 REMARK 465 SER C 172 REMARK 465 THR C 173 REMARK 465 TYR C 174 REMARK 465 SER C 175 REMARK 465 LEU C 176 REMARK 465 SER C 177 REMARK 465 SER C 178 REMARK 465 THR C 179 REMARK 465 LEU C 180 REMARK 465 THR C 181 REMARK 465 LEU C 182 REMARK 465 SER C 183 REMARK 465 LYS C 184 REMARK 465 ALA C 185 REMARK 465 ASP C 186 REMARK 465 TYR C 187 REMARK 465 GLU C 188 REMARK 465 LYS C 189 REMARK 465 HIS C 190 REMARK 465 LYS C 191 REMARK 465 VAL C 192 REMARK 465 TYR C 193 REMARK 465 ALA C 194 REMARK 465 CYS C 195 REMARK 465 GLU C 196 REMARK 465 VAL C 197 REMARK 465 THR C 198 REMARK 465 HIS C 199 REMARK 465 GLN C 200 REMARK 465 GLY C 201 REMARK 465 LEU C 202 REMARK 465 SER C 203 REMARK 465 SER C 204 REMARK 465 PRO C 205 REMARK 465 VAL C 206 REMARK 465 THR C 207 REMARK 465 LYS C 208 REMARK 465 SER C 209 REMARK 465 PHE C 210 REMARK 465 ASN C 211 REMARK 465 ARG C 212 REMARK 465 GLY C 213 REMARK 465 GLU C 214 REMARK 465 CYS C 215 REMARK 465 GLU D 1 REMARK 465 ILE D 2 REMARK 465 SER D 3 REMARK 465 GLU D 4 REMARK 465 SER D 127 REMARK 465 ALA D 128 REMARK 465 SER D 129 REMARK 465 THR D 130 REMARK 465 LYS D 131 REMARK 465 GLY D 132 REMARK 465 PRO D 133 REMARK 465 SER D 134 REMARK 465 VAL D 135 REMARK 465 PHE D 136 REMARK 465 PRO D 137 REMARK 465 LEU D 138 REMARK 465 ALA D 139 REMARK 465 PRO D 140 REMARK 465 SER D 141 REMARK 465 SER D 142 REMARK 465 LYS D 143 REMARK 465 SER D 144 REMARK 465 THR D 145 REMARK 465 SER D 146 REMARK 465 GLY D 147 REMARK 465 GLY D 148 REMARK 465 THR D 149 REMARK 465 ALA D 150 REMARK 465 ALA D 151 REMARK 465 LEU D 152 REMARK 465 GLY D 153 REMARK 465 CYS D 154 REMARK 465 LEU D 155 REMARK 465 VAL D 156 REMARK 465 LYS D 157 REMARK 465 ASP D 158 REMARK 465 TYR D 159 REMARK 465 PHE D 160 REMARK 465 PRO D 161 REMARK 465 GLU D 162 REMARK 465 PRO D 163 REMARK 465 VAL D 164 REMARK 465 THR D 165 REMARK 465 VAL D 166 REMARK 465 SER D 167 REMARK 465 TRP D 168 REMARK 465 ASN D 169 REMARK 465 SER D 170 REMARK 465 GLY D 171 REMARK 465 ALA D 172 REMARK 465 LEU D 173 REMARK 465 THR D 174 REMARK 465 SER D 175 REMARK 465 GLY D 176 REMARK 465 VAL D 177 REMARK 465 HIS D 178 REMARK 465 THR D 179 REMARK 465 PHE D 180 REMARK 465 PRO D 181 REMARK 465 ALA D 182 REMARK 465 VAL D 183 REMARK 465 LEU D 184 REMARK 465 GLN D 185 REMARK 465 SER D 186 REMARK 465 SER D 187 REMARK 465 GLY D 188 REMARK 465 LEU D 189 REMARK 465 TYR D 190 REMARK 465 SER D 191 REMARK 465 LEU D 192 REMARK 465 SER D 193 REMARK 465 SER D 194 REMARK 465 VAL D 195 REMARK 465 VAL D 196 REMARK 465 THR D 197 REMARK 465 VAL D 198 REMARK 465 PRO D 199 REMARK 465 SER D 200 REMARK 465 SER D 201 REMARK 465 SER D 202 REMARK 465 LEU D 203 REMARK 465 GLY D 204 REMARK 465 THR D 205 REMARK 465 GLN D 206 REMARK 465 THR D 207 REMARK 465 TYR D 208 REMARK 465 ILE D 209 REMARK 465 CYS D 210 REMARK 465 ASN D 211 REMARK 465 VAL D 212 REMARK 465 ASN D 213 REMARK 465 HIS D 214 REMARK 465 LYS D 215 REMARK 465 PRO D 216 REMARK 465 SER D 217 REMARK 465 ASN D 218 REMARK 465 THR D 219 REMARK 465 LYS D 220 REMARK 465 VAL D 221 REMARK 465 ASP D 222 REMARK 465 LYS D 223 REMARK 465 LYS D 224 REMARK 465 VAL D 225 REMARK 465 GLU D 226 REMARK 465 PRO D 227 REMARK 465 LYS D 228 REMARK 465 SER D 229 REMARK 465 CYS D 230 REMARK 465 ASP D 231 REMARK 465 LYS D 232 REMARK 465 THR D 233 REMARK 465 HIS D 234 REMARK 465 THR D 235 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 ARG A 504 39.18 -85.02 REMARK 500 GLN A 513 53.81 -150.26 REMARK 500 TYR A 531 99.73 -168.77 REMARK 500 THR A 579 0.69 -67.31 REMARK 500 ALA A 618 31.21 -145.35 REMARK 500 THR A 687 62.92 39.13 REMARK 500 THR A 706 66.79 -101.44 REMARK 500 ASN A 718 -10.96 -141.56 REMARK 500 ASN A 750 38.04 70.98 REMARK 500 THR A 757 55.54 -91.59 REMARK 500 GLU A 811 54.94 -92.44 REMARK 500 MET A 828 19.52 52.84 REMARK 500 LEU A 840 -75.72 -93.85 REMARK 500 HIS B 863 64.22 -158.81 REMARK 500 CYS C 24 81.67 -161.61 REMARK 500 SER C 32 -129.12 49.36 REMARK 500 LYS C 43 -167.22 -128.14 REMARK 500 SER C 53 -68.78 -138.39 REMARK 500 PRO C 81 -3.31 -51.54 REMARK 500 GLU C 82 34.76 -99.87 REMARK 500 ASP C 83 29.38 -143.39 REMARK 500 PHE C 99 -165.55 -115.70 REMARK 500 CYS D 25 87.22 -151.01 REMARK 500 LYS D 46 -158.02 -140.82 REMARK 500 MET D 86 79.72 -118.27 REMARK 500 ALA D 91 0.95 -66.26 REMARK 500 TYR D 112 48.44 39.43 REMARK 500 TRP D 117 -143.62 -115.39 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PHE A 715 PRO A 716 -38.08 REMARK 500 TYR C 95 PRO C 96 31.99 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-43523 RELATED DB: EMDB REMARK 900 LATROPHILIN3/ADGRL3 HORMR AND GAIN DOMAINS IN COMPLEX WITH A REMARK 900 SYNTHETIC ANTIBODY FRAGMENT DBREF 8VTI A 490 854 UNP Q9HAR2 AGRL3_HUMAN 490 854 DBREF 8VTI B 855 1160 UNP Q9HAR2 AGRL3_HUMAN 855 1160 DBREF 8VTI C 1 215 PDB 8VTI 8VTI 1 215 DBREF 8VTI D 1 235 PDB 8VTI 8VTI 1 235 SEQADV 8VTI ASP A 480 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI TYR A 481 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI LYS A 482 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI ASP A 483 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI ASP A 484 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI ASP A 485 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI ASP A 486 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI ALA A 487 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI MET A 488 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI ALA A 489 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1161 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1162 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1163 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1164 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1165 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1166 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1167 UNP Q9HAR2 EXPRESSION TAG SEQADV 8VTI HIS B 1168 UNP Q9HAR2 EXPRESSION TAG SEQRES 1 A 375 ASP TYR LYS ASP ASP ASP ASP ALA MET ALA GLN ILE PRO SEQRES 2 A 375 ALA LEU GLU GLU SER CYS GLU ALA VAL GLU ALA ARG GLU SEQRES 3 A 375 ILE MET TRP PHE LYS THR ARG GLN GLY GLN ILE ALA LYS SEQRES 4 A 375 GLN PRO CYS PRO ALA GLY THR ILE GLY VAL SER THR TYR SEQRES 5 A 375 LEU CYS LEU ALA PRO ASP GLY ILE TRP ASP PRO GLN GLY SEQRES 6 A 375 PRO ASP LEU SER ASN CYS SER SER PRO TRP VAL ASN HIS SEQRES 7 A 375 ILE THR GLN LYS LEU LYS SER GLY GLU THR ALA ALA ASN SEQRES 8 A 375 ILE ALA ARG GLU LEU ALA GLU GLN THR ARG ASN HIS LEU SEQRES 9 A 375 ASN ALA GLY ASP ILE THR TYR SER VAL ARG ALA MET ASP SEQRES 10 A 375 GLN LEU VAL GLY LEU LEU ASP VAL GLN LEU ARG ASN LEU SEQRES 11 A 375 THR PRO GLY GLY LYS ASP SER ALA ALA ARG SER LEU ASN SEQRES 12 A 375 LYS LEU GLN LYS ARG GLU ARG SER CYS ARG ALA TYR VAL SEQRES 13 A 375 GLN ALA MET VAL GLU THR VAL ASN ASN LEU LEU GLN PRO SEQRES 14 A 375 GLN ALA LEU ASN ALA TRP ARG ASP LEU THR THR SER ASP SEQRES 15 A 375 GLN LEU ARG ALA ALA THR MET LEU LEU HIS THR VAL GLU SEQRES 16 A 375 GLU SER ALA PHE VAL LEU ALA ASP ASN LEU LEU LYS THR SEQRES 17 A 375 ASP ILE VAL ARG GLU ASN THR ASP ASN ILE LYS LEU GLU SEQRES 18 A 375 VAL ALA ARG LEU SER THR GLU GLY ASN LEU GLU ASP LEU SEQRES 19 A 375 LYS PHE PRO GLU ASN MET GLY HIS GLY SER THR ILE GLN SEQRES 20 A 375 LEU SER ALA ASN THR LEU LYS GLN ASN GLY ARG ASN GLY SEQRES 21 A 375 GLU ILE ARG VAL ALA PHE VAL LEU TYR ASN ASN LEU GLY SEQRES 22 A 375 PRO TYR LEU SER THR GLU ASN ALA SER MET LYS LEU GLY SEQRES 23 A 375 THR GLU ALA LEU SER THR ASN HIS SER VAL ILE VAL ASN SEQRES 24 A 375 SER PRO VAL ILE THR ALA ALA ILE ASN LYS GLU PHE SER SEQRES 25 A 375 ASN LYS VAL TYR LEU ALA ASP PRO VAL VAL PHE THR VAL SEQRES 26 A 375 LYS HIS ILE LYS GLN SER GLU GLU ASN PHE ASN PRO ASN SEQRES 27 A 375 CYS SER PHE TRP SER TYR SER LYS ARG THR MET THR GLY SEQRES 28 A 375 TYR TRP SER THR GLN GLY CYS ARG LEU LEU THR THR ASN SEQRES 29 A 375 LYS THR HIS THR THR CYS SER CYS ASN HIS LEU SEQRES 1 B 314 THR ASN PHE ALA VAL LEU MET ALA HIS VAL GLU VAL LYS SEQRES 2 B 314 HIS SER ASP ALA VAL HIS ASP LEU LEU LEU ASP VAL ILE SEQRES 3 B 314 THR TRP VAL GLY ILE LEU LEU SER LEU VAL CYS LEU LEU SEQRES 4 B 314 ILE CYS ILE PHE THR PHE CYS PHE PHE ARG GLY LEU GLN SEQRES 5 B 314 SER ASP ARG ASN THR ILE HIS LYS ASN LEU CYS ILE SER SEQRES 6 B 314 LEU PHE VAL ALA GLU LEU LEU PHE LEU ILE GLY ILE ASN SEQRES 7 B 314 ARG THR ASP GLN PRO ILE ALA CYS ALA VAL PHE ALA ALA SEQRES 8 B 314 LEU LEU HIS PHE PHE PHE LEU ALA ALA PHE THR TRP MET SEQRES 9 B 314 PHE LEU GLU GLY VAL GLN LEU TYR ILE MET LEU VAL GLU SEQRES 10 B 314 VAL PHE GLU SER GLU HIS SER ARG ARG LYS TYR PHE TYR SEQRES 11 B 314 LEU VAL GLY TYR GLY MET PRO ALA LEU ILE VAL ALA VAL SEQRES 12 B 314 SER ALA ALA VAL ASP TYR ARG SER TYR GLY THR ASP LYS SEQRES 13 B 314 VAL CYS TRP LEU ARG LEU ASP THR TYR PHE ILE TRP SER SEQRES 14 B 314 PHE ILE GLY PRO ALA THR LEU ILE ILE MET LEU ASN VAL SEQRES 15 B 314 ILE PHE LEU GLY ILE ALA LEU TYR LYS MET PHE HIS HIS SEQRES 16 B 314 THR ALA ILE LEU LYS PRO GLU SER GLY CYS LEU ASP ASN SEQRES 17 B 314 ILE ASN TYR GLU ASP ASN ARG PRO PHE ILE LYS SER TRP SEQRES 18 B 314 VAL ILE GLY ALA ILE ALA LEU LEU CYS LEU LEU GLY LEU SEQRES 19 B 314 THR TRP ALA PHE GLY LEU MET TYR ILE ASN GLU SER THR SEQRES 20 B 314 VAL ILE MET ALA TYR LEU PHE THR ILE PHE ASN SER LEU SEQRES 21 B 314 GLN GLY MET PHE ILE PHE ILE PHE HIS CYS VAL LEU GLN SEQRES 22 B 314 LYS LYS VAL ARG LYS GLU TYR GLY LYS CYS LEU ARG THR SEQRES 23 B 314 HIS CYS CYS SER GLY LYS SER THR GLU SER SER ILE GLY SEQRES 24 B 314 SER GLY LYS THR SER GLY SER HIS HIS HIS HIS HIS HIS SEQRES 25 B 314 HIS HIS SEQRES 1 C 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 C 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 C 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 C 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 C 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 C 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 C 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 C 215 SER GLY GLN TYR PRO LEU THR PHE GLY GLN GLY THR LYS SEQRES 9 C 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 C 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 C 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 C 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 C 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 C 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 C 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 C 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 C 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 235 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 D 235 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 D 235 ALA SER GLY PHE ASN ILE SER SER SER TYR ILE HIS TRP SEQRES 4 D 235 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 D 235 SER ILE SER PRO TYR SER GLY TYR THR SER TYR ALA ASP SEQRES 6 D 235 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 D 235 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 D 235 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG HIS ASN TYR SEQRES 9 D 235 TRP GLN TRP TRP GLU TYR SER TYR ALA LEU ASP TYR TRP SEQRES 10 D 235 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 D 235 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 D 235 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 D 235 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 D 235 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 D 235 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 D 235 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 D 235 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 D 235 ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS SEQRES 19 D 235 THR HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET NAG A 901 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 3(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 HELIX 1 AA1 PRO A 553 GLY A 565 1 13 HELIX 2 AA2 THR A 567 THR A 579 1 13 HELIX 3 AA3 ASN A 584 LEU A 609 1 26 HELIX 4 AA4 ALA A 618 LEU A 646 1 29 HELIX 5 AA5 GLN A 647 GLN A 649 5 3 HELIX 6 AA6 ALA A 650 LEU A 657 1 8 HELIX 7 AA7 THR A 658 ASN A 683 1 26 HELIX 8 AA8 SER A 728 ASN A 735 1 8 HELIX 9 AA9 LEU A 751 LEU A 755 5 5 HELIX 10 AB1 ALA D 64 LYS D 68 5 5 HELIX 11 AB2 THR D 77 LYS D 79 5 3 SHEET 1 AA1 2 VAL A 501 GLU A 502 0 SHEET 2 AA1 2 ILE A 506 MET A 507 -1 O ILE A 506 N GLU A 502 SHEET 1 AA2 2 LYS A 518 PRO A 520 0 SHEET 2 AA2 2 VAL A 528 THR A 530 -1 O SER A 529 N GLN A 519 SHEET 1 AA3 6 ILE A 689 VAL A 690 0 SHEET 2 AA3 6 ILE A 697 LEU A 704 -1 O VAL A 701 N VAL A 690 SHEET 3 AA3 6 ILE A 741 TYR A 748 -1 O PHE A 745 N GLU A 700 SHEET 4 AA3 6 VAL A 781 ILE A 786 -1 O VAL A 781 N TYR A 748 SHEET 5 AA3 6 ASN B 856 ALA B 862 -1 O PHE B 857 N ILE A 782 SHEET 6 AA3 6 VAL A 775 ILE A 776 -1 N ILE A 776 O MET B 861 SHEET 1 AA4 7 ILE A 689 VAL A 690 0 SHEET 2 AA4 7 ILE A 697 LEU A 704 -1 O VAL A 701 N VAL A 690 SHEET 3 AA4 7 ILE A 741 TYR A 748 -1 O PHE A 745 N GLU A 700 SHEET 4 AA4 7 VAL A 781 ILE A 786 -1 O VAL A 781 N TYR A 748 SHEET 5 AA4 7 ASN B 856 ALA B 862 -1 O PHE B 857 N ILE A 782 SHEET 6 AA4 7 ASN A 817 SER A 824 -1 N SER A 819 O ALA B 858 SHEET 7 AA4 7 THR A 829 SER A 833 -1 O SER A 833 N PHE A 820 SHEET 1 AA5 5 LYS A 714 PHE A 715 0 SHEET 2 AA5 5 ILE A 725 GLN A 726 -1 O ILE A 725 N PHE A 715 SHEET 3 AA5 5 VAL A 794 LYS A 805 -1 O VAL A 801 N GLN A 726 SHEET 4 AA5 5 HIS A 846 LEU A 854 -1 O ASN A 852 N LEU A 796 SHEET 5 AA5 5 CYS A 837 THR A 842 -1 N ARG A 838 O SER A 850 SHEET 1 AA6 6 SER C 11 LEU C 12 0 SHEET 2 AA6 6 THR C 103 VAL C 105 1 O LYS C 104 N LEU C 12 SHEET 3 AA6 6 THR C 86 TYR C 87 -1 N TYR C 87 O THR C 103 SHEET 4 AA6 6 VAL C 34 GLN C 39 -1 N GLN C 39 O THR C 86 SHEET 5 AA6 6 PRO C 45 TYR C 50 -1 O LYS C 46 N GLN C 38 SHEET 6 AA6 6 SER C 54 LEU C 55 -1 O SER C 54 N TYR C 50 SHEET 1 AA7 5 SER C 11 LEU C 12 0 SHEET 2 AA7 5 THR C 103 VAL C 105 1 O LYS C 104 N LEU C 12 SHEET 3 AA7 5 THR C 86 TYR C 87 -1 N TYR C 87 O THR C 103 SHEET 4 AA7 5 VAL C 34 GLN C 39 -1 N GLN C 39 O THR C 86 SHEET 5 AA7 5 GLN C 90 GLN C 91 -1 O GLN C 90 N ALA C 35 SHEET 1 AA8 3 VAL C 20 ILE C 22 0 SHEET 2 AA8 3 PHE C 72 ILE C 76 -1 O LEU C 74 N ILE C 22 SHEET 3 AA8 3 PHE C 63 ARG C 67 -1 N SER C 66 O THR C 73 SHEET 1 AA9 4 GLN D 6 SER D 10 0 SHEET 2 AA9 4 SER D 20 SER D 28 -1 O SER D 24 N SER D 10 SHEET 3 AA9 4 THR D 81 ASN D 87 -1 O MET D 86 N LEU D 21 SHEET 4 AA9 4 PHE D 71 ASP D 76 -1 N SER D 74 O TYR D 83 SHEET 1 AB1 5 GLY D 13 LEU D 14 0 SHEET 2 AB1 5 THR D 121 THR D 124 1 O THR D 124 N GLY D 13 SHEET 3 AB1 5 ALA D 95 ALA D 100 -1 N TYR D 97 O THR D 121 SHEET 4 AB1 5 ILE D 37 GLN D 42 -1 N HIS D 38 O ALA D 100 SHEET 5 AB1 5 LEU D 48 ILE D 54 -1 O GLU D 49 N ARG D 41 SSBOND 1 CYS A 498 CYS A 533 1555 1555 2.00 SSBOND 2 CYS A 521 CYS A 550 1555 1555 2.05 SSBOND 3 CYS A 818 CYS A 849 1555 1555 2.03 SSBOND 4 CYS A 837 CYS A 851 1555 1555 2.03 SSBOND 5 CYS C 24 CYS C 89 1555 1555 2.01 SSBOND 6 CYS D 25 CYS D 99 1555 1555 2.04 LINK ND2 ASN A 817 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN A 843 C1 NAG A 901 1555 1555 1.43 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44 CISPEP 1 SER C 8 PRO C 9 0 -11.81 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000