HEADER CELL ADHESION 24-JUN-25 9P97 TITLE CRYOEM STRUCTURE OF THE CLOSED INTEGRIN ALPHAEBETA7 BOUND TO FAB LF61 CAVEAT 9P97 NAG B 2003 HAS WRONG CHIRALITY AT ATOM C2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTEGRIN ALPHA-E; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HML-1 ANTIGEN,INTEGRIN ALPHA-IEL,MUCOSAL LYMPHOCYTE 1 COMPND 5 ANTIGEN; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: ECTODOMAIN; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: INTEGRIN BETA-7; COMPND 10 CHAIN: B; COMPND 11 SYNONYM: GUT HOMING RECEPTOR BETA SUBUNIT; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: FAB LF61 HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: FAB LF61 LIGHT CHAIN; COMPND 19 CHAIN: L; 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: ITGAE; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: ITGB7; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_TAXID: 10090; SOURCE 18 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 22 ORGANISM_TAXID: 10090; SOURCE 23 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS AEB7, GUT ADHESION, TISSUE RESIDENCE, MEMBRANE RECEPTOR, CELL KEYWDS 2 ADHESION EXPDTA ELECTRON MICROSCOPY AUTHOR J.A.HOLLIS,M.G.CAMPBELL REVDAT 1 24-SEP-25 9P97 0 JRNL AUTH J.A.HOLLIS,M.C.CHAN,H.S.MALIK,M.G.CAMPBELL JRNL TITL MOLECULAR EXAPTATION BY THE INTEGRIN ALPHA I DOMAIN. JRNL REF SCI ADV V. 11 X9567 2025 JRNL REFN ESSN 2375-2548 JRNL PMID 40929264 JRNL DOI 10.1126/SCIADV.ADX9567 REMARK 2 REMARK 2 RESOLUTION. 2.92 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, 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) : 2.920 REMARK 3 NUMBER OF PARTICLES : 402099 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 9P97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-25. REMARK 100 THE DEPOSITION ID IS D_1000297365. 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 : PROTEIN COMPLEX OF OPEN REMARK 245 INTEGRIN ALPHAEBETA7 WITH FAB REMARK 245 LF61 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.15 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 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 : TFS GLACIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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, H, L, C, D, E, F 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 MET A -17 REMARK 465 TRP A -16 REMARK 465 LEU A -15 REMARK 465 PHE A -14 REMARK 465 HIS A -13 REMARK 465 THR A -12 REMARK 465 LEU A -11 REMARK 465 LEU A -10 REMARK 465 CYS A -9 REMARK 465 ILE A -8 REMARK 465 ALA A -7 REMARK 465 SER A -6 REMARK 465 LEU A -5 REMARK 465 ALA A -4 REMARK 465 LEU A -3 REMARK 465 LEU A -2 REMARK 465 ALA A -1 REMARK 465 ALA A 0 REMARK 465 TYR A 142 REMARK 465 SER A 143 REMARK 465 ASN A 144 REMARK 465 LYS A 145 REMARK 465 GLU A 146 REMARK 465 GLY A 147 REMARK 465 GLY A 148 REMARK 465 GLY A 149 REMARK 465 GLU A 150 REMARK 465 ASP A 151 REMARK 465 ASP A 152 REMARK 465 VAL A 153 REMARK 465 ASN A 154 REMARK 465 THR A 155 REMARK 465 ALA A 156 REMARK 465 ARG A 157 REMARK 465 GLN A 158 REMARK 465 ARG A 159 REMARK 465 ARG A 160 REMARK 465 ALA A 161 REMARK 465 LEU A 162 REMARK 465 GLU A 163 REMARK 465 LYS A 164 REMARK 465 GLU A 165 REMARK 465 GLU A 166 REMARK 465 GLU A 167 REMARK 465 GLU A 168 REMARK 465 ASP A 169 REMARK 465 LYS A 170 REMARK 465 GLU A 171 REMARK 465 GLU A 172 REMARK 465 GLU A 173 REMARK 465 GLU A 174 REMARK 465 ASP A 175 REMARK 465 GLU A 176 REMARK 465 GLU A 177 REMARK 465 GLU A 178 REMARK 465 GLU A 179 REMARK 465 GLU A 180 REMARK 465 PRO A 800 REMARK 465 TYR A 801 REMARK 465 GLU A 802 REMARK 465 LYS A 803 REMARK 465 ALA A 804 REMARK 465 CYS A 805 REMARK 465 LYS A 806 REMARK 465 ASN A 807 REMARK 465 LYS A 808 REMARK 465 LEU A 809 REMARK 465 PHE A 810 REMARK 465 CYS A 811 REMARK 465 VAL A 812 REMARK 465 ALA A 813 REMARK 465 GLU A 814 REMARK 465 LEU A 815 REMARK 465 GLN A 816 REMARK 465 LEU A 817 REMARK 465 ALA A 818 REMARK 465 THR A 819 REMARK 465 THR A 820 REMARK 465 VAL A 821 REMARK 465 SER A 822 REMARK 465 GLN A 823 REMARK 465 GLN A 824 REMARK 465 GLU A 825 REMARK 465 LEU A 826 REMARK 465 VAL A 827 REMARK 465 VAL A 828 REMARK 465 GLY A 829 REMARK 465 LEU A 830 REMARK 465 THR A 831 REMARK 465 LYS A 832 REMARK 465 GLU A 833 REMARK 465 LEU A 834 REMARK 465 THR A 835 REMARK 465 LEU A 836 REMARK 465 ASN A 837 REMARK 465 ILE A 838 REMARK 465 ASN A 839 REMARK 465 LEU A 840 REMARK 465 THR A 841 REMARK 465 ASN A 842 REMARK 465 SER A 843 REMARK 465 GLY A 844 REMARK 465 GLU A 845 REMARK 465 ASP A 846 REMARK 465 SER A 847 REMARK 465 TYR A 848 REMARK 465 MET A 849 REMARK 465 THR A 850 REMARK 465 SER A 851 REMARK 465 MET A 852 REMARK 465 ALA A 853 REMARK 465 LEU A 854 REMARK 465 ASN A 855 REMARK 465 TYR A 856 REMARK 465 PRO A 857 REMARK 465 ARG A 858 REMARK 465 ASN A 859 REMARK 465 LEU A 860 REMARK 465 GLN A 861 REMARK 465 LEU A 862 REMARK 465 LYS A 863 REMARK 465 ARG A 864 REMARK 465 MET A 865 REMARK 465 GLN A 866 REMARK 465 LYS A 867 REMARK 465 PRO A 868 REMARK 465 PRO A 869 REMARK 465 SER A 870 REMARK 465 PRO A 871 REMARK 465 ASN A 872 REMARK 465 ILE A 873 REMARK 465 GLN A 874 REMARK 465 CYS A 875 REMARK 465 ASP A 876 REMARK 465 ASP A 877 REMARK 465 PRO A 878 REMARK 465 GLN A 879 REMARK 465 PRO A 880 REMARK 465 VAL A 881 REMARK 465 ALA A 882 REMARK 465 SER A 883 REMARK 465 VAL A 884 REMARK 465 LEU A 885 REMARK 465 ILE A 886 REMARK 465 MET A 887 REMARK 465 ASN A 888 REMARK 465 CYS A 889 REMARK 465 ARG A 890 REMARK 465 ILE A 891 REMARK 465 GLY A 892 REMARK 465 HIS A 893 REMARK 465 PRO A 894 REMARK 465 VAL A 895 REMARK 465 LEU A 896 REMARK 465 LYS A 897 REMARK 465 ARG A 898 REMARK 465 SER A 899 REMARK 465 SER A 900 REMARK 465 ALA A 901 REMARK 465 HIS A 902 REMARK 465 VAL A 903 REMARK 465 SER A 904 REMARK 465 VAL A 905 REMARK 465 VAL A 906 REMARK 465 TRP A 907 REMARK 465 GLN A 908 REMARK 465 LEU A 909 REMARK 465 GLU A 910 REMARK 465 GLU A 911 REMARK 465 ASN A 912 REMARK 465 ALA A 913 REMARK 465 PHE A 914 REMARK 465 PRO A 915 REMARK 465 ASN A 916 REMARK 465 ARG A 917 REMARK 465 THR A 918 REMARK 465 ALA A 919 REMARK 465 ASP A 920 REMARK 465 ILE A 921 REMARK 465 THR A 922 REMARK 465 VAL A 923 REMARK 465 THR A 924 REMARK 465 VAL A 925 REMARK 465 THR A 926 REMARK 465 ASN A 927 REMARK 465 SER A 928 REMARK 465 ASN A 929 REMARK 465 GLU A 930 REMARK 465 ARG A 931 REMARK 465 ARG A 932 REMARK 465 SER A 933 REMARK 465 LEU A 934 REMARK 465 ALA A 935 REMARK 465 ASN A 936 REMARK 465 GLU A 937 REMARK 465 THR A 938 REMARK 465 HIS A 939 REMARK 465 THR A 940 REMARK 465 LEU A 941 REMARK 465 GLN A 942 REMARK 465 PHE A 943 REMARK 465 ARG A 944 REMARK 465 HIS A 945 REMARK 465 GLY A 946 REMARK 465 PHE A 947 REMARK 465 VAL A 948 REMARK 465 ALA A 949 REMARK 465 VAL A 950 REMARK 465 LEU A 951 REMARK 465 SER A 952 REMARK 465 LYS A 953 REMARK 465 PRO A 954 REMARK 465 SER A 955 REMARK 465 ILE A 956 REMARK 465 MET A 957 REMARK 465 TYR A 958 REMARK 465 VAL A 959 REMARK 465 ASN A 960 REMARK 465 THR A 961 REMARK 465 GLY A 962 REMARK 465 GLN A 963 REMARK 465 GLY A 964 REMARK 465 LEU A 965 REMARK 465 SER A 966 REMARK 465 HIS A 967 REMARK 465 HIS A 968 REMARK 465 LYS A 969 REMARK 465 GLU A 970 REMARK 465 PHE A 971 REMARK 465 LEU A 972 REMARK 465 PHE A 973 REMARK 465 HIS A 974 REMARK 465 VAL A 975 REMARK 465 HIS A 976 REMARK 465 GLY A 977 REMARK 465 GLU A 978 REMARK 465 ASN A 979 REMARK 465 LEU A 980 REMARK 465 PHE A 981 REMARK 465 GLY A 982 REMARK 465 ALA A 983 REMARK 465 GLU A 984 REMARK 465 TYR A 985 REMARK 465 GLN A 986 REMARK 465 LEU A 987 REMARK 465 GLN A 988 REMARK 465 ILE A 989 REMARK 465 CYS A 990 REMARK 465 VAL A 991 REMARK 465 PRO A 992 REMARK 465 THR A 993 REMARK 465 LYS A 994 REMARK 465 LEU A 995 REMARK 465 ARG A 996 REMARK 465 GLY A 997 REMARK 465 LEU A 998 REMARK 465 GLN A 999 REMARK 465 VAL A 1000 REMARK 465 VAL A 1001 REMARK 465 ALA A 1002 REMARK 465 VAL A 1003 REMARK 465 LYS A 1004 REMARK 465 LYS A 1005 REMARK 465 LEU A 1006 REMARK 465 THR A 1007 REMARK 465 ARG A 1008 REMARK 465 THR A 1009 REMARK 465 GLN A 1010 REMARK 465 ALA A 1011 REMARK 465 SER A 1012 REMARK 465 THR A 1013 REMARK 465 VAL A 1014 REMARK 465 CYS A 1015 REMARK 465 THR A 1016 REMARK 465 TRP A 1017 REMARK 465 SER A 1018 REMARK 465 GLN A 1019 REMARK 465 GLU A 1020 REMARK 465 ARG A 1021 REMARK 465 ALA A 1022 REMARK 465 CYS A 1023 REMARK 465 ALA A 1024 REMARK 465 TYR A 1025 REMARK 465 SER A 1026 REMARK 465 SER A 1027 REMARK 465 VAL A 1028 REMARK 465 GLN A 1029 REMARK 465 HIS A 1030 REMARK 465 VAL A 1031 REMARK 465 GLU A 1032 REMARK 465 GLU A 1033 REMARK 465 TRP A 1034 REMARK 465 HIS A 1035 REMARK 465 SER A 1036 REMARK 465 VAL A 1037 REMARK 465 SER A 1038 REMARK 465 CYS A 1039 REMARK 465 VAL A 1040 REMARK 465 ILE A 1041 REMARK 465 ALA A 1042 REMARK 465 SER A 1043 REMARK 465 ASP A 1044 REMARK 465 LYS A 1045 REMARK 465 GLU A 1046 REMARK 465 ASN A 1047 REMARK 465 VAL A 1048 REMARK 465 THR A 1049 REMARK 465 VAL A 1050 REMARK 465 ALA A 1051 REMARK 465 ALA A 1052 REMARK 465 GLU A 1053 REMARK 465 ILE A 1054 REMARK 465 SER A 1055 REMARK 465 TRP A 1056 REMARK 465 ASP A 1057 REMARK 465 HIS A 1058 REMARK 465 SER A 1059 REMARK 465 GLU A 1060 REMARK 465 GLU A 1061 REMARK 465 LEU A 1062 REMARK 465 LEU A 1063 REMARK 465 LYS A 1064 REMARK 465 ASP A 1065 REMARK 465 VAL A 1066 REMARK 465 THR A 1067 REMARK 465 GLU A 1068 REMARK 465 LEU A 1069 REMARK 465 GLN A 1070 REMARK 465 ILE A 1071 REMARK 465 LEU A 1072 REMARK 465 GLY A 1073 REMARK 465 GLU A 1074 REMARK 465 ILE A 1075 REMARK 465 SER A 1076 REMARK 465 PHE A 1077 REMARK 465 ASN A 1078 REMARK 465 LYS A 1079 REMARK 465 SER A 1080 REMARK 465 LEU A 1081 REMARK 465 TYR A 1082 REMARK 465 GLU A 1083 REMARK 465 GLY A 1084 REMARK 465 LEU A 1085 REMARK 465 ASN A 1086 REMARK 465 ALA A 1087 REMARK 465 GLU A 1088 REMARK 465 ASN A 1089 REMARK 465 HIS A 1090 REMARK 465 ARG A 1091 REMARK 465 THR A 1092 REMARK 465 LYS A 1093 REMARK 465 ILE A 1094 REMARK 465 THR A 1095 REMARK 465 VAL A 1096 REMARK 465 VAL A 1097 REMARK 465 PHE A 1098 REMARK 465 LEU A 1099 REMARK 465 LYS A 1100 REMARK 465 ASP A 1101 REMARK 465 GLU A 1102 REMARK 465 LYS A 1103 REMARK 465 TYR A 1104 REMARK 465 HIS A 1105 REMARK 465 GLY A 1106 REMARK 465 THR A 1107 REMARK 465 GLY A 1108 REMARK 465 GLY A 1109 REMARK 465 LEU A 1110 REMARK 465 GLU A 1111 REMARK 465 VAL A 1112 REMARK 465 LEU A 1113 REMARK 465 PHE A 1114 REMARK 465 GLN A 1115 REMARK 465 GLY A 1116 REMARK 465 PRO A 1117 REMARK 465 GLY A 1118 REMARK 465 GLU A 1119 REMARK 465 ASN A 1120 REMARK 465 ALA A 1121 REMARK 465 GLN A 1122 REMARK 465 CYS A 1123 REMARK 465 GLU A 1124 REMARK 465 LYS A 1125 REMARK 465 GLU A 1126 REMARK 465 LEU A 1127 REMARK 465 GLN A 1128 REMARK 465 ALA A 1129 REMARK 465 LEU A 1130 REMARK 465 GLU A 1131 REMARK 465 LYS A 1132 REMARK 465 GLU A 1133 REMARK 465 ASN A 1134 REMARK 465 ALA A 1135 REMARK 465 GLN A 1136 REMARK 465 LEU A 1137 REMARK 465 GLU A 1138 REMARK 465 TRP A 1139 REMARK 465 GLU A 1140 REMARK 465 LEU A 1141 REMARK 465 GLN A 1142 REMARK 465 ALA A 1143 REMARK 465 LEU A 1144 REMARK 465 GLU A 1145 REMARK 465 LYS A 1146 REMARK 465 GLU A 1147 REMARK 465 LEU A 1148 REMARK 465 ALA A 1149 REMARK 465 GLN A 1150 REMARK 465 TRP A 1151 REMARK 465 SER A 1152 REMARK 465 HIS A 1153 REMARK 465 PRO A 1154 REMARK 465 GLN A 1155 REMARK 465 PHE A 1156 REMARK 465 GLU A 1157 REMARK 465 LYS A 1158 REMARK 465 MET B -18 REMARK 465 VAL B -17 REMARK 465 ALA B -16 REMARK 465 LEU B -15 REMARK 465 PRO B -14 REMARK 465 MET B -13 REMARK 465 VAL B -12 REMARK 465 LEU B -11 REMARK 465 VAL B -10 REMARK 465 LEU B -9 REMARK 465 LEU B -8 REMARK 465 LEU B -7 REMARK 465 VAL B -6 REMARK 465 LEU B -5 REMARK 465 SER B -4 REMARK 465 ARG B -3 REMARK 465 GLY B -2 REMARK 465 GLU B -1 REMARK 465 SER B 0 REMARK 465 GLU B 1 REMARK 465 LEU B 2 REMARK 465 ASP B 3 REMARK 465 ALA B 4 REMARK 465 LYS B 5 REMARK 465 ILE B 6 REMARK 465 PRO B 7 REMARK 465 SER B 8 REMARK 465 THR B 9 REMARK 465 GLY B 10 REMARK 465 ASP B 11 REMARK 465 ALA B 12 REMARK 465 THR B 13 REMARK 465 GLU B 14 REMARK 465 TRP B 15 REMARK 465 ARG B 16 REMARK 465 ASN B 17 REMARK 465 PRO B 18 REMARK 465 HIS B 19 REMARK 465 LEU B 20 REMARK 465 SER B 21 REMARK 465 MET B 22 REMARK 465 LEU B 23 REMARK 465 GLY B 24 REMARK 465 SER B 25 REMARK 465 CYS B 26 REMARK 465 GLN B 27 REMARK 465 PRO B 28 REMARK 465 ALA B 29 REMARK 465 PRO B 30 REMARK 465 SER B 31 REMARK 465 CYS B 32 REMARK 465 GLN B 33 REMARK 465 LYS B 34 REMARK 465 CYS B 35 REMARK 465 ILE B 36 REMARK 465 LEU B 37 REMARK 465 SER B 38 REMARK 465 HIS B 39 REMARK 465 PRO B 40 REMARK 465 SER B 41 REMARK 465 CYS B 42 REMARK 465 ALA B 43 REMARK 465 TRP B 44 REMARK 465 CYS B 45 REMARK 465 LYS B 46 REMARK 465 GLN B 47 REMARK 465 LEU B 48 REMARK 465 ASN B 49 REMARK 465 PHE B 50 REMARK 465 THR B 51 REMARK 465 ALA B 52 REMARK 465 SER B 53 REMARK 465 GLY B 54 REMARK 465 GLU B 55 REMARK 465 ALA B 56 REMARK 465 GLU B 57 REMARK 465 ALA B 58 REMARK 465 ARG B 59 REMARK 465 ARG B 60 REMARK 465 CYS B 61 REMARK 465 ALA B 62 REMARK 465 ARG B 63 REMARK 465 ARG B 64 REMARK 465 GLU B 65 REMARK 465 GLU B 66 REMARK 465 LEU B 67 REMARK 465 LEU B 68 REMARK 465 ALA B 69 REMARK 465 ARG B 70 REMARK 465 GLY B 71 REMARK 465 CYS B 72 REMARK 465 PRO B 73 REMARK 465 LEU B 74 REMARK 465 GLU B 75 REMARK 465 GLU B 76 REMARK 465 LEU B 77 REMARK 465 GLU B 78 REMARK 465 GLU B 79 REMARK 465 PRO B 80 REMARK 465 ASP B 456 REMARK 465 CYS B 457 REMARK 465 ASN B 458 REMARK 465 CYS B 459 REMARK 465 SER B 460 REMARK 465 ASP B 461 REMARK 465 THR B 462 REMARK 465 GLN B 463 REMARK 465 PRO B 464 REMARK 465 GLN B 465 REMARK 465 ALA B 466 REMARK 465 PRO B 467 REMARK 465 HIS B 468 REMARK 465 CYS B 469 REMARK 465 SER B 470 REMARK 465 ASP B 471 REMARK 465 GLY B 472 REMARK 465 GLN B 473 REMARK 465 GLY B 474 REMARK 465 HIS B 475 REMARK 465 LEU B 476 REMARK 465 GLN B 477 REMARK 465 CYS B 478 REMARK 465 GLY B 479 REMARK 465 VAL B 480 REMARK 465 CYS B 481 REMARK 465 SER B 482 REMARK 465 CYS B 483 REMARK 465 ALA B 484 REMARK 465 PRO B 485 REMARK 465 GLY B 486 REMARK 465 ARG B 487 REMARK 465 LEU B 488 REMARK 465 GLY B 489 REMARK 465 ARG B 490 REMARK 465 LEU B 491 REMARK 465 CYS B 492 REMARK 465 GLU B 493 REMARK 465 CYS B 494 REMARK 465 SER B 495 REMARK 465 VAL B 496 REMARK 465 ALA B 497 REMARK 465 GLU B 498 REMARK 465 LEU B 499 REMARK 465 SER B 500 REMARK 465 SER B 501 REMARK 465 PRO B 502 REMARK 465 ASP B 503 REMARK 465 LEU B 504 REMARK 465 GLU B 505 REMARK 465 SER B 506 REMARK 465 GLY B 507 REMARK 465 CYS B 508 REMARK 465 ARG B 509 REMARK 465 ALA B 510 REMARK 465 PRO B 511 REMARK 465 ASN B 512 REMARK 465 GLY B 513 REMARK 465 THR B 514 REMARK 465 GLY B 515 REMARK 465 PRO B 516 REMARK 465 LEU B 517 REMARK 465 CYS B 518 REMARK 465 SER B 519 REMARK 465 GLY B 520 REMARK 465 LYS B 521 REMARK 465 GLY B 522 REMARK 465 HIS B 523 REMARK 465 CYS B 524 REMARK 465 GLN B 525 REMARK 465 CYS B 526 REMARK 465 GLY B 527 REMARK 465 ARG B 528 REMARK 465 CYS B 529 REMARK 465 SER B 530 REMARK 465 CYS B 531 REMARK 465 SER B 532 REMARK 465 GLY B 533 REMARK 465 GLN B 534 REMARK 465 SER B 535 REMARK 465 SER B 536 REMARK 465 GLY B 537 REMARK 465 HIS B 538 REMARK 465 LEU B 539 REMARK 465 CYS B 540 REMARK 465 GLU B 541 REMARK 465 CYS B 542 REMARK 465 ASP B 543 REMARK 465 ASP B 544 REMARK 465 ALA B 545 REMARK 465 SER B 546 REMARK 465 CYS B 547 REMARK 465 GLU B 548 REMARK 465 ARG B 549 REMARK 465 HIS B 550 REMARK 465 GLU B 551 REMARK 465 GLY B 552 REMARK 465 ILE B 553 REMARK 465 LEU B 554 REMARK 465 CYS B 555 REMARK 465 GLY B 556 REMARK 465 GLY B 557 REMARK 465 PHE B 558 REMARK 465 GLY B 559 REMARK 465 ARG B 560 REMARK 465 CYS B 561 REMARK 465 GLN B 562 REMARK 465 CYS B 563 REMARK 465 GLY B 564 REMARK 465 VAL B 565 REMARK 465 CYS B 566 REMARK 465 HIS B 567 REMARK 465 CYS B 568 REMARK 465 HIS B 569 REMARK 465 ALA B 570 REMARK 465 ASN B 571 REMARK 465 ARG B 572 REMARK 465 THR B 573 REMARK 465 GLY B 574 REMARK 465 ARG B 575 REMARK 465 ALA B 576 REMARK 465 CYS B 577 REMARK 465 GLU B 578 REMARK 465 CYS B 579 REMARK 465 SER B 580 REMARK 465 GLY B 581 REMARK 465 ASP B 582 REMARK 465 MET B 583 REMARK 465 ASP B 584 REMARK 465 SER B 585 REMARK 465 CYS B 586 REMARK 465 ILE B 587 REMARK 465 SER B 588 REMARK 465 PRO B 589 REMARK 465 GLU B 590 REMARK 465 GLY B 591 REMARK 465 GLY B 592 REMARK 465 LEU B 593 REMARK 465 CYS B 594 REMARK 465 SER B 595 REMARK 465 GLY B 596 REMARK 465 HIS B 597 REMARK 465 GLY B 598 REMARK 465 ARG B 599 REMARK 465 CYS B 600 REMARK 465 LYS B 601 REMARK 465 CYS B 602 REMARK 465 ASN B 603 REMARK 465 ARG B 604 REMARK 465 CYS B 605 REMARK 465 GLN B 606 REMARK 465 CYS B 607 REMARK 465 LEU B 608 REMARK 465 ASP B 609 REMARK 465 GLY B 610 REMARK 465 TYR B 611 REMARK 465 TYR B 612 REMARK 465 GLY B 613 REMARK 465 ALA B 614 REMARK 465 LEU B 615 REMARK 465 CYS B 616 REMARK 465 ASP B 617 REMARK 465 GLN B 618 REMARK 465 CYS B 619 REMARK 465 PRO B 620 REMARK 465 GLY B 621 REMARK 465 CYS B 622 REMARK 465 LYS B 623 REMARK 465 THR B 624 REMARK 465 PRO B 625 REMARK 465 CYS B 626 REMARK 465 GLU B 627 REMARK 465 ARG B 628 REMARK 465 HIS B 629 REMARK 465 ARG B 630 REMARK 465 ASP B 631 REMARK 465 CYS B 632 REMARK 465 ALA B 633 REMARK 465 GLU B 634 REMARK 465 CYS B 635 REMARK 465 GLY B 636 REMARK 465 ALA B 637 REMARK 465 PHE B 638 REMARK 465 ARG B 639 REMARK 465 THR B 640 REMARK 465 GLY B 641 REMARK 465 PRO B 642 REMARK 465 LEU B 643 REMARK 465 ALA B 644 REMARK 465 THR B 645 REMARK 465 ASN B 646 REMARK 465 CYS B 647 REMARK 465 SER B 648 REMARK 465 THR B 649 REMARK 465 ALA B 650 REMARK 465 CYS B 651 REMARK 465 ALA B 652 REMARK 465 HIS B 653 REMARK 465 THR B 654 REMARK 465 ASN B 655 REMARK 465 VAL B 656 REMARK 465 THR B 657 REMARK 465 LEU B 658 REMARK 465 ALA B 659 REMARK 465 LEU B 660 REMARK 465 ALA B 661 REMARK 465 PRO B 662 REMARK 465 ILE B 663 REMARK 465 LEU B 664 REMARK 465 ASP B 665 REMARK 465 ASP B 666 REMARK 465 GLY B 667 REMARK 465 TRP B 668 REMARK 465 CYS B 669 REMARK 465 LYS B 670 REMARK 465 GLU B 671 REMARK 465 ARG B 672 REMARK 465 THR B 673 REMARK 465 LEU B 674 REMARK 465 ASP B 675 REMARK 465 ASN B 676 REMARK 465 GLN B 677 REMARK 465 LEU B 678 REMARK 465 PHE B 679 REMARK 465 PHE B 680 REMARK 465 PHE B 681 REMARK 465 LEU B 682 REMARK 465 VAL B 683 REMARK 465 GLU B 684 REMARK 465 ASP B 685 REMARK 465 ASP B 686 REMARK 465 ALA B 687 REMARK 465 ARG B 688 REMARK 465 GLY B 689 REMARK 465 THR B 690 REMARK 465 VAL B 691 REMARK 465 VAL B 692 REMARK 465 LEU B 693 REMARK 465 ARG B 694 REMARK 465 VAL B 695 REMARK 465 ARG B 696 REMARK 465 PRO B 697 REMARK 465 GLN B 698 REMARK 465 GLU B 699 REMARK 465 LYS B 700 REMARK 465 GLY B 701 REMARK 465 ALA B 702 REMARK 465 ASP B 703 REMARK 465 HIS B 704 REMARK 465 ASP B 705 REMARK 465 THR B 706 REMARK 465 SER B 707 REMARK 465 GLY B 708 REMARK 465 LEU B 709 REMARK 465 GLU B 710 REMARK 465 VAL B 711 REMARK 465 LEU B 712 REMARK 465 PHE B 713 REMARK 465 GLN B 714 REMARK 465 GLY B 715 REMARK 465 PRO B 716 REMARK 465 GLY B 717 REMARK 465 LYS B 718 REMARK 465 ASN B 719 REMARK 465 ALA B 720 REMARK 465 GLN B 721 REMARK 465 CYS B 722 REMARK 465 LYS B 723 REMARK 465 LYS B 724 REMARK 465 LYS B 725 REMARK 465 LEU B 726 REMARK 465 GLN B 727 REMARK 465 ALA B 728 REMARK 465 LEU B 729 REMARK 465 LYS B 730 REMARK 465 LYS B 731 REMARK 465 LYS B 732 REMARK 465 ASN B 733 REMARK 465 ALA B 734 REMARK 465 GLN B 735 REMARK 465 LEU B 736 REMARK 465 LYS B 737 REMARK 465 TRP B 738 REMARK 465 LYS B 739 REMARK 465 LEU B 740 REMARK 465 GLN B 741 REMARK 465 ALA B 742 REMARK 465 LEU B 743 REMARK 465 LYS B 744 REMARK 465 LYS B 745 REMARK 465 LYS B 746 REMARK 465 LEU B 747 REMARK 465 ALA B 748 REMARK 465 GLN B 749 REMARK 465 GLY B 750 REMARK 465 GLY B 751 REMARK 465 HIS B 752 REMARK 465 HIS B 753 REMARK 465 HIS B 754 REMARK 465 HIS B 755 REMARK 465 HIS B 756 REMARK 465 HIS B 757 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 HD22 ASN B 415 C1 NAG B 2003 0.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 56 60.26 60.47 REMARK 500 ASP A 57 29.84 49.99 REMARK 500 LEU A 100 54.68 -93.41 REMARK 500 PRO A 132 9.40 -69.58 REMARK 500 PHE A 236 135.96 -171.70 REMARK 500 LYS A 262 78.04 -103.94 REMARK 500 HIS A 380 -137.73 57.41 REMARK 500 ALA A 430 -142.89 60.58 REMARK 500 CYS A 501 85.98 -150.94 REMARK 500 VAL A 523 -60.87 -124.36 REMARK 500 MET A 566 33.88 -95.88 REMARK 500 GLN A 571 31.01 72.22 REMARK 500 ASP A 589 -139.78 55.32 REMARK 500 ARG A 703 -123.00 58.18 REMARK 500 VAL B 178 -64.10 -124.94 REMARK 500 HIS B 195 78.16 -154.09 REMARK 500 VAL B 213 -62.57 -107.76 REMARK 500 ASN B 260 59.00 -94.90 REMARK 500 ALA B 403 59.36 -93.67 REMARK 500 ARG B 406 118.39 -160.48 REMARK 500 SER H 180 -99.79 53.35 REMARK 500 PRO L 51 171.06 -57.39 REMARK 500 SER L 72 -138.93 48.05 REMARK 500 PRO L 150 -170.03 -69.81 REMARK 500 ASN L 179 42.11 70.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1203 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 504 OD1 REMARK 620 2 ASP A 506 OD1 98.2 REMARK 620 3 ASP A 508 OD1 85.6 72.7 REMARK 620 4 SER A 510 O 66.5 160.0 92.6 REMARK 620 5 ASP A 512 OD1 125.7 115.1 143.2 84.8 REMARK 620 6 ASP A 512 OD2 82.5 116.1 166.1 76.1 45.1 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1204 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 568 OD1 REMARK 620 2 SER A 570 OG 104.4 REMARK 620 3 ASP A 572 OD1 78.0 86.9 REMARK 620 4 LEU A 574 O 73.8 167.4 80.6 REMARK 620 5 ASP A 576 OD1 144.0 98.3 131.4 89.6 REMARK 620 6 ASP A 576 OD2 92.7 98.0 170.3 94.5 56.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1205 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 636 OD2 REMARK 620 2 SER A 638 OG 83.7 REMARK 620 3 ASP A 640 OD1 66.3 78.1 REMARK 620 4 ASP A 640 OD2 114.9 69.7 51.0 REMARK 620 5 LEU A 642 O 86.2 168.9 93.7 111.0 REMARK 620 6 ASP A 644 OD1 136.7 114.1 152.6 108.3 76.5 REMARK 620 7 ASP A 644 OD2 89.8 80.7 149.5 137.9 103.8 57.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER B 144 OG REMARK 620 2 ASP B 271 OD2 139.1 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER B 144 O REMARK 620 2 ASP B 147 OD1 80.5 REMARK 620 3 ASP B 147 OD2 118.6 48.9 REMARK 620 4 ASP B 148 OD1 97.9 68.7 93.6 REMARK 620 5 GLU B 354 O 168.3 98.8 67.6 71.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B2004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 179 OD2 REMARK 620 2 ASN B 235 OD1 113.0 REMARK 620 3 ASP B 237 O 174.4 70.1 REMARK 620 4 ASP B 237 OD1 103.0 97.0 71.7 REMARK 620 5 PRO B 239 O 88.8 151.4 89.8 95.6 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-71401 RELATED DB: EMDB REMARK 900 CRYOEM STRUCTURE OF THE CLOSED INTEGRIN ALPHAEBETA7 BOUND TO FAB REMARK 900 LF61 DBREF 9P97 A -17 1105 UNP P38570 ITAE_HUMAN 1 1123 DBREF 9P97 B -18 704 UNP P26010 ITB7_HUMAN 1 723 DBREF 9P97 H 1 220 PDB 9P97 9P97 1 220 DBREF 9P97 L 1 216 PDB 9P97 9P97 1 216 SEQADV 9P97 GLY A 1106 UNP P38570 EXPRESSION TAG SEQADV 9P97 THR A 1107 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLY A 1108 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLY A 1109 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1110 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1111 UNP P38570 EXPRESSION TAG SEQADV 9P97 VAL A 1112 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1113 UNP P38570 EXPRESSION TAG SEQADV 9P97 PHE A 1114 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1115 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLY A 1116 UNP P38570 EXPRESSION TAG SEQADV 9P97 PRO A 1117 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLY A 1118 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1119 UNP P38570 EXPRESSION TAG SEQADV 9P97 ASN A 1120 UNP P38570 EXPRESSION TAG SEQADV 9P97 ALA A 1121 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1122 UNP P38570 EXPRESSION TAG SEQADV 9P97 CYS A 1123 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1124 UNP P38570 EXPRESSION TAG SEQADV 9P97 LYS A 1125 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1126 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1127 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1128 UNP P38570 EXPRESSION TAG SEQADV 9P97 ALA A 1129 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1130 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1131 UNP P38570 EXPRESSION TAG SEQADV 9P97 LYS A 1132 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1133 UNP P38570 EXPRESSION TAG SEQADV 9P97 ASN A 1134 UNP P38570 EXPRESSION TAG SEQADV 9P97 ALA A 1135 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1136 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1137 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1138 UNP P38570 EXPRESSION TAG SEQADV 9P97 TRP A 1139 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1140 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1141 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1142 UNP P38570 EXPRESSION TAG SEQADV 9P97 ALA A 1143 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1144 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1145 UNP P38570 EXPRESSION TAG SEQADV 9P97 LYS A 1146 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1147 UNP P38570 EXPRESSION TAG SEQADV 9P97 LEU A 1148 UNP P38570 EXPRESSION TAG SEQADV 9P97 ALA A 1149 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1150 UNP P38570 EXPRESSION TAG SEQADV 9P97 TRP A 1151 UNP P38570 EXPRESSION TAG SEQADV 9P97 SER A 1152 UNP P38570 EXPRESSION TAG SEQADV 9P97 HIS A 1153 UNP P38570 EXPRESSION TAG SEQADV 9P97 PRO A 1154 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLN A 1155 UNP P38570 EXPRESSION TAG SEQADV 9P97 PHE A 1156 UNP P38570 EXPRESSION TAG SEQADV 9P97 GLU A 1157 UNP P38570 EXPRESSION TAG SEQADV 9P97 LYS A 1158 UNP P38570 EXPRESSION TAG SEQADV 9P97 ASP B 705 UNP P26010 EXPRESSION TAG SEQADV 9P97 THR B 706 UNP P26010 EXPRESSION TAG SEQADV 9P97 SER B 707 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLY B 708 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 709 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLU B 710 UNP P26010 EXPRESSION TAG SEQADV 9P97 VAL B 711 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 712 UNP P26010 EXPRESSION TAG SEQADV 9P97 PHE B 713 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLN B 714 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLY B 715 UNP P26010 EXPRESSION TAG SEQADV 9P97 PRO B 716 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLY B 717 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 718 UNP P26010 EXPRESSION TAG SEQADV 9P97 ASN B 719 UNP P26010 EXPRESSION TAG SEQADV 9P97 ALA B 720 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLN B 721 UNP P26010 EXPRESSION TAG SEQADV 9P97 CYS B 722 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 723 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 724 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 725 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 726 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLN B 727 UNP P26010 EXPRESSION TAG SEQADV 9P97 ALA B 728 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 729 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 730 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 731 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 732 UNP P26010 EXPRESSION TAG SEQADV 9P97 ASN B 733 UNP P26010 EXPRESSION TAG SEQADV 9P97 ALA B 734 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLN B 735 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 736 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 737 UNP P26010 EXPRESSION TAG SEQADV 9P97 TRP B 738 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 739 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 740 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLN B 741 UNP P26010 EXPRESSION TAG SEQADV 9P97 ALA B 742 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 743 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 744 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 745 UNP P26010 EXPRESSION TAG SEQADV 9P97 LYS B 746 UNP P26010 EXPRESSION TAG SEQADV 9P97 LEU B 747 UNP P26010 EXPRESSION TAG SEQADV 9P97 ALA B 748 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLN B 749 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLY B 750 UNP P26010 EXPRESSION TAG SEQADV 9P97 GLY B 751 UNP P26010 EXPRESSION TAG SEQADV 9P97 HIS B 752 UNP P26010 EXPRESSION TAG SEQADV 9P97 HIS B 753 UNP P26010 EXPRESSION TAG SEQADV 9P97 HIS B 754 UNP P26010 EXPRESSION TAG SEQADV 9P97 HIS B 755 UNP P26010 EXPRESSION TAG SEQADV 9P97 HIS B 756 UNP P26010 EXPRESSION TAG SEQADV 9P97 HIS B 757 UNP P26010 EXPRESSION TAG SEQRES 1 A 1176 MET TRP LEU PHE HIS THR LEU LEU CYS ILE ALA SER LEU SEQRES 2 A 1176 ALA LEU LEU ALA ALA PHE ASN VAL ASP VAL ALA ARG PRO SEQRES 3 A 1176 TRP LEU THR PRO LYS GLY GLY ALA PRO PHE VAL LEU SER SEQRES 4 A 1176 SER LEU LEU HIS GLN ASP PRO SER THR ASN GLN THR TRP SEQRES 5 A 1176 LEU LEU VAL THR SER PRO ARG THR LYS ARG THR PRO GLY SEQRES 6 A 1176 PRO LEU HIS ARG CYS SER LEU VAL GLN ASP GLU ILE LEU SEQRES 7 A 1176 CYS HIS PRO VAL GLU HIS VAL PRO ILE PRO LYS GLY ARG SEQRES 8 A 1176 HIS ARG GLY VAL THR VAL VAL ARG SER HIS HIS GLY VAL SEQRES 9 A 1176 LEU ILE CYS ILE GLN VAL LEU VAL ARG ARG PRO HIS SER SEQRES 10 A 1176 LEU SER SER GLU LEU THR GLY THR CYS SER LEU LEU GLY SEQRES 11 A 1176 PRO ASP LEU ARG PRO GLN ALA GLN ALA ASN PHE PHE ASP SEQRES 12 A 1176 LEU GLU ASN LEU LEU ASP PRO ASP ALA ARG VAL ASP THR SEQRES 13 A 1176 GLY ASP CYS TYR SER ASN LYS GLU GLY GLY GLY GLU ASP SEQRES 14 A 1176 ASP VAL ASN THR ALA ARG GLN ARG ARG ALA LEU GLU LYS SEQRES 15 A 1176 GLU GLU GLU GLU ASP LYS GLU GLU GLU GLU ASP GLU GLU SEQRES 16 A 1176 GLU GLU GLU ALA GLY THR GLU ILE ALA ILE ILE LEU ASP SEQRES 17 A 1176 GLY SER GLY SER ILE ASP PRO PRO ASP PHE GLN ARG ALA SEQRES 18 A 1176 LYS ASP PHE ILE SER ASN MET MET ARG ASN PHE TYR GLU SEQRES 19 A 1176 LYS CYS PHE GLU CYS ASN PHE ALA LEU VAL GLN TYR GLY SEQRES 20 A 1176 GLY VAL ILE GLN THR GLU PHE ASP LEU ARG ASP SER GLN SEQRES 21 A 1176 ASP VAL MET ALA SER LEU ALA ARG VAL GLN ASN ILE THR SEQRES 22 A 1176 GLN VAL GLY SER VAL THR LYS THR ALA SER ALA MET GLN SEQRES 23 A 1176 HIS VAL LEU ASP SER ILE PHE THR SER SER HIS GLY SER SEQRES 24 A 1176 ARG ARG LYS ALA SER LYS VAL MET VAL VAL LEU THR ASP SEQRES 25 A 1176 GLY GLY ILE PHE GLU ASP PRO LEU ASN LEU THR THR VAL SEQRES 26 A 1176 ILE ASN SER PRO LYS MET GLN GLY VAL GLU ARG PHE ALA SEQRES 27 A 1176 ILE GLY VAL GLY GLU GLU PHE LYS SER ALA ARG THR ALA SEQRES 28 A 1176 ARG GLU LEU ASN LEU ILE ALA SER ASP PRO ASP GLU THR SEQRES 29 A 1176 HIS ALA PHE LYS VAL THR ASN TYR MET ALA LEU ASP GLY SEQRES 30 A 1176 LEU LEU SER LYS LEU ARG TYR ASN ILE ILE SER MET GLU SEQRES 31 A 1176 GLY THR VAL GLY ASP ALA LEU HIS TYR GLN LEU ALA GLN SEQRES 32 A 1176 ILE GLY PHE SER ALA GLN ILE LEU ASP GLU ARG GLN VAL SEQRES 33 A 1176 LEU LEU GLY ALA VAL GLY ALA PHE ASP TRP SER GLY GLY SEQRES 34 A 1176 ALA LEU LEU TYR ASP THR ARG SER ARG ARG GLY ARG PHE SEQRES 35 A 1176 LEU ASN GLN THR ALA ALA ALA ALA ALA ASP ALA GLU ALA SEQRES 36 A 1176 ALA GLN TYR SER TYR LEU GLY TYR ALA VAL ALA VAL LEU SEQRES 37 A 1176 HIS LYS THR CYS SER LEU SER TYR ILE ALA GLY ALA PRO SEQRES 38 A 1176 ARG TYR LYS HIS HIS GLY ALA VAL PHE GLU LEU GLN LYS SEQRES 39 A 1176 GLU GLY ARG GLU ALA SER PHE LEU PRO VAL LEU GLU GLY SEQRES 40 A 1176 GLU GLN MET GLY SER TYR PHE GLY SER GLU LEU CYS PRO SEQRES 41 A 1176 VAL ASP ILE ASP MET ASP GLY SER THR ASP PHE LEU LEU SEQRES 42 A 1176 VAL ALA ALA PRO PHE TYR HIS VAL HIS GLY GLU GLU GLY SEQRES 43 A 1176 ARG VAL TYR VAL TYR ARG LEU SER GLU GLN ASP GLY SER SEQRES 44 A 1176 PHE SER LEU ALA ARG ILE LEU SER GLY HIS PRO GLY PHE SEQRES 45 A 1176 THR ASN ALA ARG PHE GLY PHE ALA MET ALA ALA MET GLY SEQRES 46 A 1176 ASP LEU SER GLN ASP LYS LEU THR ASP VAL ALA ILE GLY SEQRES 47 A 1176 ALA PRO LEU GLU GLY PHE GLY ALA ASP ASP GLY ALA SER SEQRES 48 A 1176 PHE GLY SER VAL TYR ILE TYR ASN GLY HIS TRP ASP GLY SEQRES 49 A 1176 LEU SER ALA SER PRO SER GLN ARG ILE ARG ALA SER THR SEQRES 50 A 1176 VAL ALA PRO GLY LEU GLN TYR PHE GLY MET SER MET ALA SEQRES 51 A 1176 GLY GLY PHE ASP ILE SER GLY ASP GLY LEU ALA ASP ILE SEQRES 52 A 1176 THR VAL GLY THR LEU GLY GLN ALA VAL VAL PHE ARG SER SEQRES 53 A 1176 ARG PRO VAL VAL ARG LEU LYS VAL SER MET ALA PHE THR SEQRES 54 A 1176 PRO SER ALA LEU PRO ILE GLY PHE ASN GLY VAL VAL ASN SEQRES 55 A 1176 VAL ARG LEU CYS PHE GLU ILE SER SER VAL THR THR ALA SEQRES 56 A 1176 SER GLU SER GLY LEU ARG GLU ALA LEU LEU ASN PHE THR SEQRES 57 A 1176 LEU ASP VAL ASP VAL GLY LYS GLN ARG ARG ARG LEU GLN SEQRES 58 A 1176 CYS SER ASP VAL ARG SER CYS LEU GLY CYS LEU ARG GLU SEQRES 59 A 1176 TRP SER SER GLY SER GLN LEU CYS GLU ASP LEU LEU LEU SEQRES 60 A 1176 MET PRO THR GLU GLY GLU LEU CYS GLU GLU ASP CYS PHE SEQRES 61 A 1176 SER ASN ALA SER VAL LYS VAL SER TYR GLN LEU GLN THR SEQRES 62 A 1176 PRO GLU GLY GLN THR ASP HIS PRO GLN PRO ILE LEU ASP SEQRES 63 A 1176 ARG TYR THR GLU PRO PHE ALA ILE PHE GLN LEU PRO TYR SEQRES 64 A 1176 GLU LYS ALA CYS LYS ASN LYS LEU PHE CYS VAL ALA GLU SEQRES 65 A 1176 LEU GLN LEU ALA THR THR VAL SER GLN GLN GLU LEU VAL SEQRES 66 A 1176 VAL GLY LEU THR LYS GLU LEU THR LEU ASN ILE ASN LEU SEQRES 67 A 1176 THR ASN SER GLY GLU ASP SER TYR MET THR SER MET ALA SEQRES 68 A 1176 LEU ASN TYR PRO ARG ASN LEU GLN LEU LYS ARG MET GLN SEQRES 69 A 1176 LYS PRO PRO SER PRO ASN ILE GLN CYS ASP ASP PRO GLN SEQRES 70 A 1176 PRO VAL ALA SER VAL LEU ILE MET ASN CYS ARG ILE GLY SEQRES 71 A 1176 HIS PRO VAL LEU LYS ARG SER SER ALA HIS VAL SER VAL SEQRES 72 A 1176 VAL TRP GLN LEU GLU GLU ASN ALA PHE PRO ASN ARG THR SEQRES 73 A 1176 ALA ASP ILE THR VAL THR VAL THR ASN SER ASN GLU ARG SEQRES 74 A 1176 ARG SER LEU ALA ASN GLU THR HIS THR LEU GLN PHE ARG SEQRES 75 A 1176 HIS GLY PHE VAL ALA VAL LEU SER LYS PRO SER ILE MET SEQRES 76 A 1176 TYR VAL ASN THR GLY GLN GLY LEU SER HIS HIS LYS GLU SEQRES 77 A 1176 PHE LEU PHE HIS VAL HIS GLY GLU ASN LEU PHE GLY ALA SEQRES 78 A 1176 GLU TYR GLN LEU GLN ILE CYS VAL PRO THR LYS LEU ARG SEQRES 79 A 1176 GLY LEU GLN VAL VAL ALA VAL LYS LYS LEU THR ARG THR SEQRES 80 A 1176 GLN ALA SER THR VAL CYS THR TRP SER GLN GLU ARG ALA SEQRES 81 A 1176 CYS ALA TYR SER SER VAL GLN HIS VAL GLU GLU TRP HIS SEQRES 82 A 1176 SER VAL SER CYS VAL ILE ALA SER ASP LYS GLU ASN VAL SEQRES 83 A 1176 THR VAL ALA ALA GLU ILE SER TRP ASP HIS SER GLU GLU SEQRES 84 A 1176 LEU LEU LYS ASP VAL THR GLU LEU GLN ILE LEU GLY GLU SEQRES 85 A 1176 ILE SER PHE ASN LYS SER LEU TYR GLU GLY LEU ASN ALA SEQRES 86 A 1176 GLU ASN HIS ARG THR LYS ILE THR VAL VAL PHE LEU LYS SEQRES 87 A 1176 ASP GLU LYS TYR HIS GLY THR GLY GLY LEU GLU VAL LEU SEQRES 88 A 1176 PHE GLN GLY PRO GLY GLU ASN ALA GLN CYS GLU LYS GLU SEQRES 89 A 1176 LEU GLN ALA LEU GLU LYS GLU ASN ALA GLN LEU GLU TRP SEQRES 90 A 1176 GLU LEU GLN ALA LEU GLU LYS GLU LEU ALA GLN TRP SER SEQRES 91 A 1176 HIS PRO GLN PHE GLU LYS SEQRES 1 B 776 MET VAL ALA LEU PRO MET VAL LEU VAL LEU LEU LEU VAL SEQRES 2 B 776 LEU SER ARG GLY GLU SER GLU LEU ASP ALA LYS ILE PRO SEQRES 3 B 776 SER THR GLY ASP ALA THR GLU TRP ARG ASN PRO HIS LEU SEQRES 4 B 776 SER MET LEU GLY SER CYS GLN PRO ALA PRO SER CYS GLN SEQRES 5 B 776 LYS CYS ILE LEU SER HIS PRO SER CYS ALA TRP CYS LYS SEQRES 6 B 776 GLN LEU ASN PHE THR ALA SER GLY GLU ALA GLU ALA ARG SEQRES 7 B 776 ARG CYS ALA ARG ARG GLU GLU LEU LEU ALA ARG GLY CYS SEQRES 8 B 776 PRO LEU GLU GLU LEU GLU GLU PRO ARG GLY GLN GLN GLU SEQRES 9 B 776 VAL LEU GLN ASP GLN PRO LEU SER GLN GLY ALA ARG GLY SEQRES 10 B 776 GLU GLY ALA THR GLN LEU ALA PRO GLN ARG VAL ARG VAL SEQRES 11 B 776 THR LEU ARG PRO GLY GLU PRO GLN GLN LEU GLN VAL ARG SEQRES 12 B 776 PHE LEU ARG ALA GLU GLY TYR PRO VAL ASP LEU TYR TYR SEQRES 13 B 776 LEU MET ASP LEU SER TYR SER MET LYS ASP ASP LEU GLU SEQRES 14 B 776 ARG VAL ARG GLN LEU GLY HIS ALA LEU LEU VAL ARG LEU SEQRES 15 B 776 GLN GLU VAL THR HIS SER VAL ARG ILE GLY PHE GLY SER SEQRES 16 B 776 PHE VAL ASP LYS THR VAL LEU PRO PHE VAL SER THR VAL SEQRES 17 B 776 PRO SER LYS LEU ARG HIS PRO CYS PRO THR ARG LEU GLU SEQRES 18 B 776 ARG CYS GLN SER PRO PHE SER PHE HIS HIS VAL LEU SER SEQRES 19 B 776 LEU THR GLY ASP ALA GLN ALA PHE GLU ARG GLU VAL GLY SEQRES 20 B 776 ARG GLN SER VAL SER GLY ASN LEU ASP SER PRO GLU GLY SEQRES 21 B 776 GLY PHE ASP ALA ILE LEU GLN ALA ALA LEU CYS GLN GLU SEQRES 22 B 776 GLN ILE GLY TRP ARG ASN VAL SER ARG LEU LEU VAL PHE SEQRES 23 B 776 THR SER ASP ASP THR PHE HIS THR ALA GLY ASP GLY LYS SEQRES 24 B 776 LEU GLY GLY ILE PHE MET PRO SER ASP GLY HIS CYS HIS SEQRES 25 B 776 LEU ASP SER ASN GLY LEU TYR SER ARG SER THR GLU PHE SEQRES 26 B 776 ASP TYR PRO SER VAL GLY GLN VAL ALA GLN ALA LEU SER SEQRES 27 B 776 ALA ALA ASN ILE GLN PRO ILE PHE ALA VAL THR SER ALA SEQRES 28 B 776 ALA LEU PRO VAL TYR GLN GLU LEU SER LYS LEU ILE PRO SEQRES 29 B 776 LYS SER ALA VAL GLY GLU LEU SER GLU ASP SER SER ASN SEQRES 30 B 776 VAL VAL GLN LEU ILE MET ASP ALA TYR ASN SER LEU SER SEQRES 31 B 776 SER THR VAL THR LEU GLU HIS SER SER LEU PRO PRO GLY SEQRES 32 B 776 VAL HIS ILE SER TYR GLU SER GLN CYS GLU GLY PRO GLU SEQRES 33 B 776 LYS ARG GLU GLY LYS ALA GLU ASP ARG GLY GLN CYS ASN SEQRES 34 B 776 HIS VAL ARG ILE ASN GLN THR VAL THR PHE TRP VAL SER SEQRES 35 B 776 LEU GLN ALA THR HIS CYS LEU PRO GLU PRO HIS LEU LEU SEQRES 36 B 776 ARG LEU ARG ALA LEU GLY PHE SER GLU GLU LEU ILE VAL SEQRES 37 B 776 GLU LEU HIS THR LEU CYS ASP CYS ASN CYS SER ASP THR SEQRES 38 B 776 GLN PRO GLN ALA PRO HIS CYS SER ASP GLY GLN GLY HIS SEQRES 39 B 776 LEU GLN CYS GLY VAL CYS SER CYS ALA PRO GLY ARG LEU SEQRES 40 B 776 GLY ARG LEU CYS GLU CYS SER VAL ALA GLU LEU SER SER SEQRES 41 B 776 PRO ASP LEU GLU SER GLY CYS ARG ALA PRO ASN GLY THR SEQRES 42 B 776 GLY PRO LEU CYS SER GLY LYS GLY HIS CYS GLN CYS GLY SEQRES 43 B 776 ARG CYS SER CYS SER GLY GLN SER SER GLY HIS LEU CYS SEQRES 44 B 776 GLU CYS ASP ASP ALA SER CYS GLU ARG HIS GLU GLY ILE SEQRES 45 B 776 LEU CYS GLY GLY PHE GLY ARG CYS GLN CYS GLY VAL CYS SEQRES 46 B 776 HIS CYS HIS ALA ASN ARG THR GLY ARG ALA CYS GLU CYS SEQRES 47 B 776 SER GLY ASP MET ASP SER CYS ILE SER PRO GLU GLY GLY SEQRES 48 B 776 LEU CYS SER GLY HIS GLY ARG CYS LYS CYS ASN ARG CYS SEQRES 49 B 776 GLN CYS LEU ASP GLY TYR TYR GLY ALA LEU CYS ASP GLN SEQRES 50 B 776 CYS PRO GLY CYS LYS THR PRO CYS GLU ARG HIS ARG ASP SEQRES 51 B 776 CYS ALA GLU CYS GLY ALA PHE ARG THR GLY PRO LEU ALA SEQRES 52 B 776 THR ASN CYS SER THR ALA CYS ALA HIS THR ASN VAL THR SEQRES 53 B 776 LEU ALA LEU ALA PRO ILE LEU ASP ASP GLY TRP CYS LYS SEQRES 54 B 776 GLU ARG THR LEU ASP ASN GLN LEU PHE PHE PHE LEU VAL SEQRES 55 B 776 GLU ASP ASP ALA ARG GLY THR VAL VAL LEU ARG VAL ARG SEQRES 56 B 776 PRO GLN GLU LYS GLY ALA ASP HIS ASP THR SER GLY LEU SEQRES 57 B 776 GLU VAL LEU PHE GLN GLY PRO GLY LYS ASN ALA GLN CYS SEQRES 58 B 776 LYS LYS LYS LEU GLN ALA LEU LYS LYS LYS ASN ALA GLN SEQRES 59 B 776 LEU LYS TRP LYS LEU GLN ALA LEU LYS LYS LYS LEU ALA SEQRES 60 B 776 GLN GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 H 220 MET VAL GLN LEU GLN ARG ALA GLY PRO THR ILE VAL LYS SEQRES 2 H 220 PRO GLY SER ALA VAL LYS LEU SER CYS LYS ALA THR GLY SEQRES 3 H 220 PHE ALA TYR GLU ASP TYR TYR ILE PHE TRP VAL ARG GLN SEQRES 4 H 220 ARG GLU GLY GLY ASN GLY GLN LYS TRP ILE GLY ARG ILE SEQRES 5 H 220 HIS PRO GLY SER GLY GLU THR LYS TYR ASN ASP LYS PHE SEQRES 6 H 220 LYS GLY LYS ALA THR LEU THR ALA ASP THR GLU ALA SER SEQRES 7 H 220 SER ALA TYR MET ARG LEU THR SER LEU THR SER GLU ASP SEQRES 8 H 220 THR ALA VAL TRP TYR CYS GLY TRP GLU ARG SER VAL GLY SEQRES 9 H 220 ARG ALA THR PHE ALA TYR TRP GLY GLN GLY THR SER VAL SEQRES 10 H 220 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR SEQRES 11 H 220 PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET SEQRES 12 H 220 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 13 H 220 PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SEQRES 14 H 220 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU SEQRES 15 H 220 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER THR SEQRES 16 H 220 TRP PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO SEQRES 17 H 220 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO SEQRES 1 L 215 ALA ALA ILE THR PHE ASN LEU ALA PRO GLU SER LEU VAL SEQRES 2 L 215 VAL THR ALA GLY SER LYS VAL THR PHE SER CYS LYS ALA SEQRES 3 L 215 SER GLN ASP PHE LEU ASN SER ALA THR LYS ARG ASN TYR SEQRES 4 L 215 LEU THR TRP TYR GLN GLN ARG ASP GLY LYS PRO PRO LYS SEQRES 5 L 215 LEU LEU ILE TYR TRP ALA SER ALA ARG LEU SER GLY VAL SEQRES 6 L 215 PRO ALA ARG PHE THR GLY SER GLY GLY GLY GLY THR GLU SEQRES 7 L 215 PHE THR LEU THR ILE SER SER VAL LYS ALA ALA ASP ILE SEQRES 8 L 215 GLY THR TYR TYR CYS ARG GLN LEU ARG SER ARG PRO LEU SEQRES 9 L 215 THR PHE GLY GLY GLY THR LYS LEU THR VAL LYS GLN PRO SEQRES 10 L 215 LYS SER SER PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11 L 215 GLU GLU LEU GLU THR ASN LYS ALA THR LEU VAL CYS THR SEQRES 12 L 215 ILE THR ASP PHE TYR PRO GLY VAL VAL THR VAL ASP TRP SEQRES 13 L 215 LYS VAL ASP GLY THR PRO VAL THR GLN GLY MET GLU THR SEQRES 14 L 215 THR GLN PRO SER LYS GLN SER ASN ASN LYS TYR MET ALA SEQRES 15 L 215 SER SER TYR LEU THR LEU THR ALA ARG ALA TRP GLU ARG SEQRES 16 L 215 HIS SER SER TYR SER CYS GLN VAL THR HIS GLU GLY HIS SEQRES 17 L 215 THR VAL GLU LYS SER LEU SER HET NAG C 1 27 HET NAG C 2 27 HET BMA C 3 20 HET MAN C 4 22 HET MAN C 5 22 HET NAG D 1 27 HET NAG D 2 28 HET NAG E 1 27 HET NAG E 2 27 HET BMA E 3 22 HET NAG F 1 27 HET NAG F 2 28 HET NAG A1201 28 HET NAG A1202 28 HET CA A1203 1 HET CA A1204 1 HET CA A1205 1 HET CA B2001 1 HET CA B2002 1 HET NAG B2003 28 HET CA B2004 1 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM CA CALCIUM ION 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 HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 5 NAG 11(C8 H15 N O6) FORMUL 5 BMA 2(C6 H12 O6) FORMUL 5 MAN 2(C6 H12 O6) FORMUL 11 CA 6(CA 2+) HELIX 1 AA1 ASP A 125 LEU A 129 5 5 HELIX 2 AA2 ASP A 196 CYS A 218 1 23 HELIX 3 AA3 ARG A 239 GLN A 242 5 4 HELIX 4 AA4 ASP A 243 ASN A 253 1 11 HELIX 5 AA5 LYS A 262 ILE A 274 1 13 HELIX 6 AA6 THR A 276 GLY A 280 5 5 HELIX 7 AA7 ASN A 303 ASN A 309 1 7 HELIX 8 AA8 SER A 310 GLN A 314 5 5 HELIX 9 AA9 GLU A 325 LYS A 328 5 4 HELIX 10 AB1 SER A 329 ALA A 340 1 12 HELIX 11 AB2 PRO A 343 HIS A 347 1 5 HELIX 12 AB3 MET A 355 GLY A 359 5 5 HELIX 13 AB4 LEU A 360 ILE A 369 1 10 HELIX 14 AB5 LEU A 379 ALA A 384 5 6 HELIX 15 AB6 ALA A 431 ALA A 438 1 8 HELIX 16 AB7 ARG A 464 HIS A 468 5 5 HELIX 17 AB8 SER A 618 VAL A 620 5 3 HELIX 18 AB9 ALA A 697 GLY A 701 5 5 HELIX 19 AC1 ASP A 726 LEU A 731 1 6 HELIX 20 AC2 SER B 142 SER B 144 5 3 HELIX 21 AC3 MET B 145 ARG B 153 1 9 HELIX 22 AC4 LEU B 155 GLN B 164 1 10 HELIX 23 AC5 VAL B 189 HIS B 195 1 7 HELIX 24 AC6 ASP B 219 ARG B 229 1 11 HELIX 25 AC7 GLY B 241 CYS B 252 1 12 HELIX 26 AC8 CYS B 252 GLY B 257 1 6 HELIX 27 AC9 GLY B 277 GLY B 283 5 7 HELIX 28 AD1 TYR B 300 PHE B 306 5 7 HELIX 29 AD2 SER B 310 ASN B 322 1 13 HELIX 30 AD3 ALA B 333 ILE B 344 1 12 HELIX 31 AD4 ASN B 358 SER B 372 1 15 HELIX 32 AD5 ASP H 63 LYS H 66 5 4 HELIX 33 AD6 THR H 88 THR H 92 5 5 HELIX 34 AD7 GLY H 135 ASN H 141 5 7 HELIX 35 AD8 SER H 164 SER H 166 5 3 HELIX 36 AD9 PRO H 208 SER H 211 5 4 HELIX 37 AE1 LYS L 87 ILE L 91 5 5 HELIX 38 AE2 SER L 130 THR L 136 1 7 HELIX 39 AE3 ALA L 191 ARG L 196 1 6 SHEET 1 AA1 4 VAL A 3 LEU A 10 0 SHEET 2 AA1 4 ALA A 653 SER A 658 -1 O ARG A 657 N ASP A 4 SHEET 3 AA1 4 ILE A 645 GLY A 648 -1 N VAL A 647 O VAL A 654 SHEET 4 AA1 4 MET A 631 GLY A 633 -1 N ALA A 632 O THR A 646 SHEET 1 AA2 4 SER A 22 GLN A 26 0 SHEET 2 AA2 4 THR A 33 THR A 38 -1 O LEU A 36 N LEU A 23 SHEET 3 AA2 4 LEU A 49 LEU A 54 -1 O HIS A 50 N VAL A 37 SHEET 4 AA2 4 ILE A 59 PRO A 63 -1 O HIS A 62 N ARG A 51 SHEET 1 AA3 4 VAL A 77 SER A 82 0 SHEET 2 AA3 4 GLY A 85 VAL A 94 -1 O CYS A 89 N THR A 78 SHEET 3 AA3 4 GLU A 103 LEU A 111 -1 O LEU A 111 N VAL A 86 SHEET 4 AA3 4 PRO A 117 ASN A 122 -1 O ALA A 121 N CYS A 108 SHEET 1 AA4 6 GLN A 233 PHE A 236 0 SHEET 2 AA4 6 CYS A 221 TYR A 228 -1 N GLN A 227 O GLN A 233 SHEET 3 AA4 6 THR A 183 ASP A 190 1 N ILE A 187 O VAL A 226 SHEET 4 AA4 6 SER A 286 THR A 293 1 O VAL A 290 N ILE A 188 SHEET 5 AA4 6 VAL A 316 VAL A 323 1 O PHE A 319 N VAL A 291 SHEET 6 AA4 6 ALA A 348 VAL A 351 1 O VAL A 351 N GLY A 322 SHEET 1 AA5 4 ILE A 386 ILE A 392 0 SHEET 2 AA5 4 GLN A 397 ALA A 402 -1 O LEU A 399 N GLN A 391 SHEET 3 AA5 4 ALA A 412 ASP A 416 -1 O TYR A 415 N VAL A 398 SHEET 4 AA5 4 ARG A 421 LEU A 425 -1 O LEU A 425 N ALA A 412 SHEET 1 AA6 4 VAL A 447 HIS A 451 0 SHEET 2 AA6 4 LEU A 456 GLY A 461 -1 O SER A 457 N LEU A 450 SHEET 3 AA6 4 ALA A 470 GLU A 477 -1 O PHE A 472 N ALA A 460 SHEET 4 AA6 4 GLU A 480 GLU A 488 -1 O GLU A 480 N GLU A 477 SHEET 1 AA7 4 LEU A 500 VAL A 503 0 SHEET 2 AA7 4 PHE A 513 ALA A 518 -1 O PHE A 513 N VAL A 503 SHEET 3 AA7 4 ARG A 529 LEU A 535 -1 O TYR A 531 N VAL A 516 SHEET 4 AA7 4 PHE A 542 LEU A 548 -1 O LEU A 548 N VAL A 530 SHEET 1 AA8 4 MET A 563 ALA A 565 0 SHEET 2 AA8 4 ASP A 576 ALA A 581 -1 O ALA A 578 N ALA A 564 SHEET 3 AA8 4 SER A 596 HIS A 603 -1 O TYR A 598 N ILE A 579 SHEET 4 AA8 4 GLY A 606 LEU A 607 -1 O GLY A 606 N HIS A 603 SHEET 1 AA9 4 MET A 563 ALA A 565 0 SHEET 2 AA9 4 ASP A 576 ALA A 581 -1 O ALA A 578 N ALA A 564 SHEET 3 AA9 4 SER A 596 HIS A 603 -1 O TYR A 598 N ILE A 579 SHEET 4 AA9 4 GLN A 613 ARG A 616 -1 O ILE A 615 N VAL A 597 SHEET 1 AB1 2 VAL A 661 VAL A 662 0 SHEET 2 AB1 2 ILE A 786 LEU A 787 1 O ILE A 786 N VAL A 662 SHEET 1 AB2 4 LEU A 664 THR A 671 0 SHEET 2 AB2 4 VAL A 683 ILE A 691 -1 O ASN A 684 N THR A 671 SHEET 3 AB2 4 GLN A 742 PRO A 751 -1 O LEU A 749 N VAL A 683 SHEET 4 AB2 4 LEU A 722 CYS A 724 -1 N GLN A 723 O MET A 750 SHEET 1 AB3 4 CYS A 733 ARG A 735 0 SHEET 2 AB3 4 LEU A 706 VAL A 713 -1 N LEU A 707 O ARG A 735 SHEET 3 AB3 4 ALA A 765 GLN A 774 -1 O GLN A 772 N ASN A 708 SHEET 4 AB3 4 PHE A 794 LEU A 799 -1 O PHE A 797 N VAL A 767 SHEET 1 AB4 6 GLN B 83 GLN B 88 0 SHEET 2 AB4 6 ARG B 108 LEU B 113 -1 O ARG B 110 N GLU B 85 SHEET 3 AB4 6 LEU B 447 THR B 453 1 O HIS B 452 N VAL B 111 SHEET 4 AB4 6 HIS B 434 ALA B 440 -1 N HIS B 434 O LEU B 451 SHEET 5 AB4 6 THR B 373 HIS B 378 -1 N GLU B 377 O ARG B 439 SHEET 6 AB4 6 GLY B 407 ASN B 410 -1 O CYS B 409 N VAL B 374 SHEET 1 AB5 4 LEU B 104 ALA B 105 0 SHEET 2 AB5 4 GLN B 119 LEU B 126 -1 O ARG B 124 N ALA B 105 SHEET 3 AB5 4 THR B 417 ALA B 426 -1 O VAL B 422 N LEU B 121 SHEET 4 AB5 4 VAL B 385 SER B 388 -1 N HIS B 386 O GLN B 425 SHEET 1 AB6 4 LEU B 104 ALA B 105 0 SHEET 2 AB6 4 GLN B 119 LEU B 126 -1 O ARG B 124 N ALA B 105 SHEET 3 AB6 4 THR B 417 ALA B 426 -1 O VAL B 422 N LEU B 121 SHEET 4 AB6 4 SER B 391 GLN B 392 -1 N GLN B 392 O THR B 419 SHEET 1 AB7 6 HIS B 211 THR B 217 0 SHEET 2 AB7 6 VAL B 170 PHE B 177 -1 N ILE B 172 O THR B 217 SHEET 3 AB7 6 VAL B 133 ASP B 140 1 N LEU B 135 O ARG B 171 SHEET 4 AB7 6 SER B 262 SER B 269 1 O LEU B 264 N ASP B 134 SHEET 5 AB7 6 ILE B 323 VAL B 329 1 O ILE B 326 N LEU B 265 SHEET 6 AB7 6 ALA B 348 GLU B 351 1 O GLY B 350 N PHE B 327 SHEET 1 AB8 4 GLN H 3 ARG H 6 0 SHEET 2 AB8 4 VAL H 18 THR H 25 -1 O LYS H 23 N GLN H 5 SHEET 3 AB8 4 SER H 79 LEU H 84 -1 O LEU H 84 N VAL H 18 SHEET 4 AB8 4 ALA H 69 ASP H 74 -1 N THR H 72 O TYR H 81 SHEET 1 AB9 6 THR H 10 VAL H 12 0 SHEET 2 AB9 6 THR H 115 VAL H 119 1 O SER H 116 N THR H 10 SHEET 3 AB9 6 ALA H 93 TRP H 99 -1 N ALA H 93 O VAL H 117 SHEET 4 AB9 6 ILE H 34 GLN H 39 -1 N GLN H 39 O VAL H 94 SHEET 5 AB9 6 GLN H 46 ILE H 52 -1 O ILE H 49 N TRP H 36 SHEET 6 AB9 6 THR H 59 TYR H 61 -1 O LYS H 60 N ARG H 51 SHEET 1 AC1 4 THR H 10 VAL H 12 0 SHEET 2 AC1 4 THR H 115 VAL H 119 1 O SER H 116 N THR H 10 SHEET 3 AC1 4 ALA H 93 TRP H 99 -1 N ALA H 93 O VAL H 117 SHEET 4 AC1 4 TYR H 110 TRP H 111 -1 O TYR H 110 N TRP H 99 SHEET 1 AC2 4 SER H 128 PRO H 131 0 SHEET 2 AC2 4 MET H 143 TYR H 153 -1 O LYS H 151 N SER H 128 SHEET 3 AC2 4 LEU H 182 PRO H 192 -1 O VAL H 189 N LEU H 146 SHEET 4 AC2 4 HIS H 172 THR H 173 -1 N HIS H 172 O SER H 188 SHEET 1 AC3 4 SER H 128 PRO H 131 0 SHEET 2 AC3 4 MET H 143 TYR H 153 -1 O LYS H 151 N SER H 128 SHEET 3 AC3 4 LEU H 182 PRO H 192 -1 O VAL H 189 N LEU H 146 SHEET 4 AC3 4 VAL H 177 GLN H 179 -1 N GLN H 179 O LEU H 182 SHEET 1 AC4 3 THR H 159 TRP H 162 0 SHEET 2 AC4 3 THR H 202 HIS H 207 -1 O ALA H 206 N THR H 159 SHEET 3 AC4 3 THR H 212 LYS H 217 -1 O THR H 212 N HIS H 207 SHEET 1 AC5 3 PHE L 5 LEU L 7 0 SHEET 2 AC5 3 CYS L 24 ALA L 26 -1 O LYS L 25 N ASN L 6 SHEET 3 AC5 3 GLU L 78 PHE L 79 -1 O PHE L 79 N CYS L 24 SHEET 1 AC6 5 SER L 11 VAL L 14 0 SHEET 2 AC6 5 THR L 111 VAL L 115 1 O THR L 114 N VAL L 14 SHEET 3 AC6 5 THR L 93 GLN L 98 -1 N TYR L 94 O THR L 111 SHEET 4 AC6 5 LEU L 40 GLN L 45 -1 N TYR L 43 O TYR L 95 SHEET 5 AC6 5 LYS L 52 ILE L 55 -1 O LEU L 54 N TRP L 42 SHEET 1 AC7 3 VAL L 20 THR L 21 0 SHEET 2 AC7 3 THR L 82 ILE L 83 -1 O ILE L 83 N VAL L 20 SHEET 3 AC7 3 PHE L 69 THR L 70 -1 N THR L 70 O THR L 82 SHEET 1 AC8 4 SER L 123 PHE L 127 0 SHEET 2 AC8 4 LYS L 138 PHE L 148 -1 O THR L 146 N SER L 123 SHEET 3 AC8 4 TYR L 181 THR L 190 -1 O ALA L 183 N ILE L 145 SHEET 4 AC8 4 THR L 170 THR L 171 -1 N THR L 171 O SER L 184 SHEET 1 AC9 4 THR L 162 VAL L 164 0 SHEET 2 AC9 4 THR L 154 VAL L 159 -1 N VAL L 159 O THR L 162 SHEET 3 AC9 4 TYR L 200 THR L 205 -1 O SER L 201 N LYS L 158 SHEET 4 AC9 4 VAL L 211 LEU L 215 -1 O LEU L 215 N TYR L 200 SSBOND 1 CYS A 52 CYS A 61 1555 1555 2.03 SSBOND 2 CYS A 688 CYS A 744 1555 1555 2.03 SSBOND 3 CYS B 252 CYS B 292 1555 1555 2.03 SSBOND 4 CYS H 22 CYS H 97 1555 1555 2.03 SSBOND 5 CYS L 24 CYS L 96 1555 1555 2.03 LINK ND2 ASN A 31 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 253 C1 NAG A1201 1555 1555 1.45 LINK ND2 ASN A 303 C1 NAG A1202 1555 1555 1.44 LINK ND2 ASN A 426 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 708 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN B 260 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN B 415 C1 NAG B2003 1555 1555 1.46 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.45 LINK O6 BMA C 3 C1 MAN C 5 1555 1555 1.45 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.45 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK OD1 ASP A 504 CA CA A1203 1555 1555 2.19 LINK OD1 ASP A 506 CA CA A1203 1555 1555 2.57 LINK OD1 ASP A 508 CA CA A1203 1555 1555 2.21 LINK O SER A 510 CA CA A1203 1555 1555 2.44 LINK OD1 ASP A 512 CA CA A1203 1555 1555 3.09 LINK OD2 ASP A 512 CA CA A1203 1555 1555 2.21 LINK OD1 ASP A 568 CA CA A1204 1555 1555 2.49 LINK OG SER A 570 CA CA A1204 1555 1555 2.23 LINK OD1 ASP A 572 CA CA A1204 1555 1555 2.40 LINK O LEU A 574 CA CA A1204 1555 1555 2.52 LINK OD1 ASP A 576 CA CA A1204 1555 1555 2.43 LINK OD2 ASP A 576 CA CA A1204 1555 1555 2.15 LINK OD2 ASP A 636 CA CA A1205 1555 1555 3.20 LINK OG SER A 638 CA CA A1205 1555 1555 2.48 LINK OD1 ASP A 640 CA CA A1205 1555 1555 2.06 LINK OD2 ASP A 640 CA CA A1205 1555 1555 2.79 LINK O LEU A 642 CA CA A1205 1555 1555 2.30 LINK OD1 ASP A 644 CA CA A1205 1555 1555 2.16 LINK OD2 ASP A 644 CA CA A1205 1555 1555 2.35 LINK OG SER B 144 CA CA B2001 1555 1555 2.81 LINK O SER B 144 CA CA B2002 1555 1555 2.53 LINK OD1 ASP B 147 CA CA B2002 1555 1555 2.28 LINK OD2 ASP B 147 CA CA B2002 1555 1555 2.84 LINK OD1 ASP B 148 CA CA B2002 1555 1555 2.31 LINK OD2 ASP B 179 CA CA B2004 1555 1555 2.11 LINK OD1 ASN B 235 CA CA B2004 1555 1555 2.06 LINK O ASP B 237 CA CA B2004 1555 1555 2.29 LINK OD1 ASP B 237 CA CA B2004 1555 1555 2.12 LINK O PRO B 239 CA CA B2004 1555 1555 2.27 LINK OD2 ASP B 271 CA CA B2001 1555 1555 2.42 LINK O GLU B 354 CA CA B2002 1555 1555 2.74 CISPEP 1 GLY A 47 PRO A 48 0 -6.11 CISPEP 2 ASP A 342 PRO A 343 0 1.34 CISPEP 3 THR A 671 PRO A 672 0 3.59 CISPEP 4 ALA B 105 PRO B 106 0 -1.68 CISPEP 5 LEU B 183 PRO B 184 0 0.39 CISPEP 6 PHE H 154 PRO H 155 0 -5.35 CISPEP 7 GLU H 156 PRO H 157 0 -4.38 CISPEP 8 TRP H 196 PRO H 197 0 -1.71 CISPEP 9 ALA L 8 PRO L 9 0 -1.82 CISPEP 10 ARG L 102 PRO L 104 0 -4.83 CISPEP 11 TYR L 149 PRO L 150 0 -1.37 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