HEADER CELL ADHESION,SUGAR BINDING PROTEIN 15-AUG-24 9D6F TITLE CRYO-EM STRUCTURE OF E. COLI FIMH LECTIN DOMAIN BOUND TO FABS 440-2 TITLE 2 AND 454-3 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 440-2 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 440-2 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: 445-3 FAB HEAVY CHAIN; COMPND 11 CHAIN: A; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: 445-3 FAB LIGHT CHAIN; COMPND 15 CHAIN: C; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: TYPE 1 FIMBRIN D-MANNOSE SPECIFIC ADHESIN FIMH, DONOR COMPND 19 STRAND COMPLEMENTED WITH FIMG PEPTIDE 'TRIPLE MUTANT'; COMPND 20 CHAIN: D; COMPND 21 ENGINEERED: YES; COMPND 22 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_ATCC_NUMBER: 9606; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 20 ORGANISM_TAXID: 10090; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 25 ORGANISM_TAXID: 562; SOURCE 26 GENE: FIMH, B4320, JW4283, FIMG, B4319, JW4282; SOURCE 27 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIGEN, COMPLEX, ADHESION, STRUCTURAL PROTEIN, CELL ADHESION, SUGAR KEYWDS 2 BINDING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.A.LEES,S.HAN REVDAT 1 05-FEB-25 9D6F 0 JRNL AUTH N.C.SILMON DE MONERRI,Y.CHE,J.A.LEES,J.JASTI,H.WU, JRNL AUTH 2 M.C.GRIFFOR,S.KODALI,J.C.HAWKINS,J.LYPOWY,C.PONCE,K.CURLEY, JRNL AUTH 3 A.ESADZE,J.CARCAMO,D.KEENEY,A.ILLENBERGER,Y.V.MATSUKA, JRNL AUTH 4 S.SHANKER,L.CHORRO,A.V.GRIBENKO,S.HAN,A.S.ANDERSON, JRNL AUTH 5 R.G.K.DONALD JRNL TITL STRUCTURE-BASED DESIGN OF A HIGHLY IMMUNOGENIC, JRNL TITL 2 CONFORMATIONALLY STABILIZED FIMH ANTIGEN FOR A URINARY TRACT JRNL TITL 3 INFECTION VACCINE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.24 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 4.240 REMARK 3 NUMBER OF PARTICLES : 185595 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 9D6F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000287398. 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 : FIMH-DSG TM IN COMPLEX WITH REMARK 245 FABS 440-2 AND 445-3; FIMH-DSG REMARK 245 TM; FAB 440-2; FAB 445-3 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL 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 K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 3200.00 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) : 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A, C, D 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 SER L -1 REMARK 465 PRO L 0 REMARK 465 ASP L 1 REMARK 465 ALA L 7 REMARK 465 ALA L 8 REMARK 465 LYS L 112 REMARK 465 ARG L 113 REMARK 465 ALA L 114 REMARK 465 ASP L 115 REMARK 465 ALA L 116 REMARK 465 ALA L 117 REMARK 465 PRO L 118 REMARK 465 THR L 119 REMARK 465 VAL L 120 REMARK 465 SER L 121 REMARK 465 ILE L 122 REMARK 465 PHE L 123 REMARK 465 PRO L 124 REMARK 465 PRO L 125 REMARK 465 SER L 126 REMARK 465 SER L 127 REMARK 465 GLU L 128 REMARK 465 GLN L 129 REMARK 465 LEU L 130 REMARK 465 THR L 131 REMARK 465 SER L 132 REMARK 465 GLY L 133 REMARK 465 GLY L 134 REMARK 465 ALA L 135 REMARK 465 SER L 136 REMARK 465 VAL L 137 REMARK 465 VAL L 138 REMARK 465 CYS L 139 REMARK 465 PHE L 140 REMARK 465 LEU L 141 REMARK 465 ASN L 142 REMARK 465 ASN L 143 REMARK 465 PHE L 144 REMARK 465 TYR L 145 REMARK 465 PRO L 146 REMARK 465 LYS L 147 REMARK 465 ASP L 148 REMARK 465 ILE L 149 REMARK 465 ASN L 150 REMARK 465 VAL L 151 REMARK 465 LYS L 152 REMARK 465 TRP L 153 REMARK 465 LYS L 154 REMARK 465 ILE L 155 REMARK 465 ASP L 156 REMARK 465 GLY L 157 REMARK 465 SER L 158 REMARK 465 GLU L 159 REMARK 465 ARG L 160 REMARK 465 GLN L 161 REMARK 465 ASN L 162 REMARK 465 GLY L 163 REMARK 465 VAL L 164 REMARK 465 LEU L 165 REMARK 465 ASN L 166 REMARK 465 SER L 167 REMARK 465 TRP L 168 REMARK 465 THR L 169 REMARK 465 ASP L 170 REMARK 465 GLN L 171 REMARK 465 ASP L 172 REMARK 465 SER L 173 REMARK 465 LYS L 174 REMARK 465 ASP L 175 REMARK 465 SER L 176 REMARK 465 THR L 177 REMARK 465 TYR L 178 REMARK 465 SER L 179 REMARK 465 MET L 180 REMARK 465 SER L 181 REMARK 465 SER L 182 REMARK 465 THR L 183 REMARK 465 LEU L 184 REMARK 465 THR L 185 REMARK 465 LEU L 186 REMARK 465 THR L 187 REMARK 465 LYS L 188 REMARK 465 ASP L 189 REMARK 465 GLU L 190 REMARK 465 TYR L 191 REMARK 465 GLU L 192 REMARK 465 ARG L 193 REMARK 465 HIS L 194 REMARK 465 ASN L 195 REMARK 465 SER L 196 REMARK 465 TYR L 197 REMARK 465 THR L 198 REMARK 465 CYS L 199 REMARK 465 GLU L 200 REMARK 465 ALA L 201 REMARK 465 THR L 202 REMARK 465 HIS L 203 REMARK 465 LYS L 204 REMARK 465 THR L 205 REMARK 465 SER L 206 REMARK 465 THR L 207 REMARK 465 SER L 208 REMARK 465 PRO L 209 REMARK 465 ILE L 210 REMARK 465 VAL L 211 REMARK 465 LYS L 212 REMARK 465 SER L 213 REMARK 465 PHE L 214 REMARK 465 ASN L 215 REMARK 465 ARG L 216 REMARK 465 ASN L 217 REMARK 465 GLU L 218 REMARK 465 CYS L 219 REMARK 465 SER H -1 REMARK 465 PRO H 0 REMARK 465 THR H 87 REMARK 465 SER H 122 REMARK 465 ALA H 123 REMARK 465 LYS H 124 REMARK 465 THR H 125 REMARK 465 THR H 126 REMARK 465 ALA H 127 REMARK 465 PRO H 128 REMARK 465 SER H 129 REMARK 465 VAL H 130 REMARK 465 TYR H 131 REMARK 465 PRO H 132 REMARK 465 LEU H 133 REMARK 465 ALA H 134 REMARK 465 PRO H 135 REMARK 465 VAL H 136 REMARK 465 CYS H 137 REMARK 465 GLY H 138 REMARK 465 ASP H 139 REMARK 465 THR H 140 REMARK 465 THR H 141 REMARK 465 GLY H 142 REMARK 465 SER H 143 REMARK 465 SER H 144 REMARK 465 VAL H 145 REMARK 465 THR H 146 REMARK 465 LEU H 147 REMARK 465 GLY H 148 REMARK 465 CYS H 149 REMARK 465 LEU H 150 REMARK 465 VAL H 151 REMARK 465 LYS H 152 REMARK 465 GLY H 153 REMARK 465 TYR H 154 REMARK 465 PHE H 155 REMARK 465 PRO H 156 REMARK 465 GLU H 157 REMARK 465 PRO H 158 REMARK 465 VAL H 159 REMARK 465 THR H 160 REMARK 465 LEU H 161 REMARK 465 THR H 162 REMARK 465 TRP H 163 REMARK 465 ASN H 164 REMARK 465 SER H 165 REMARK 465 GLY H 166 REMARK 465 SER H 167 REMARK 465 LEU H 168 REMARK 465 SER H 169 REMARK 465 SER H 170 REMARK 465 GLY H 171 REMARK 465 VAL H 172 REMARK 465 HIS H 173 REMARK 465 THR H 174 REMARK 465 PHE H 175 REMARK 465 PRO H 176 REMARK 465 ALA H 177 REMARK 465 VAL H 178 REMARK 465 LEU H 179 REMARK 465 GLN H 180 REMARK 465 SER H 181 REMARK 465 ASP H 182 REMARK 465 LEU H 183 REMARK 465 TYR H 184 REMARK 465 THR H 185 REMARK 465 LEU H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 SER H 189 REMARK 465 VAL H 190 REMARK 465 THR H 191 REMARK 465 VAL H 192 REMARK 465 THR H 193 REMARK 465 SER H 194 REMARK 465 SER H 195 REMARK 465 THR H 196 REMARK 465 TRP H 197 REMARK 465 PRO H 198 REMARK 465 SER H 199 REMARK 465 GLN H 200 REMARK 465 SER H 201 REMARK 465 ILE H 202 REMARK 465 THR H 203 REMARK 465 CYS H 204 REMARK 465 ASN H 205 REMARK 465 VAL H 206 REMARK 465 ALA H 207 REMARK 465 HIS H 208 REMARK 465 PRO H 209 REMARK 465 ALA H 210 REMARK 465 SER H 211 REMARK 465 SER H 212 REMARK 465 THR H 213 REMARK 465 LYS H 214 REMARK 465 VAL H 215 REMARK 465 ASP H 216 REMARK 465 LYS H 217 REMARK 465 LYS H 218 REMARK 465 ILE H 219 REMARK 465 GLY H 220 REMARK 465 GLY H 221 REMARK 465 GLY H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 SER A -1 REMARK 465 PRO A 0 REMARK 465 GLY A 100 REMARK 465 ASP A 101 REMARK 465 SER A 116 REMARK 465 ALA A 117 REMARK 465 ALA A 118 REMARK 465 LYS A 119 REMARK 465 THR A 120 REMARK 465 THR A 121 REMARK 465 ALA A 122 REMARK 465 PRO A 123 REMARK 465 SER A 124 REMARK 465 VAL A 125 REMARK 465 TYR A 126 REMARK 465 PRO A 127 REMARK 465 LEU A 128 REMARK 465 ALA A 129 REMARK 465 PRO A 130 REMARK 465 VAL A 131 REMARK 465 CYS A 132 REMARK 465 GLY A 133 REMARK 465 ASP A 134 REMARK 465 THR A 135 REMARK 465 THR A 136 REMARK 465 GLY A 137 REMARK 465 SER A 138 REMARK 465 SER A 139 REMARK 465 VAL A 140 REMARK 465 THR A 141 REMARK 465 LEU A 142 REMARK 465 GLY A 143 REMARK 465 CYS A 144 REMARK 465 LEU A 145 REMARK 465 VAL A 146 REMARK 465 LYS A 147 REMARK 465 GLY A 148 REMARK 465 TYR A 149 REMARK 465 PHE A 150 REMARK 465 PRO A 151 REMARK 465 GLU A 152 REMARK 465 PRO A 153 REMARK 465 VAL A 154 REMARK 465 THR A 155 REMARK 465 LEU A 156 REMARK 465 THR A 157 REMARK 465 TRP A 158 REMARK 465 ASN A 159 REMARK 465 SER A 160 REMARK 465 GLY A 161 REMARK 465 SER A 162 REMARK 465 LEU A 163 REMARK 465 SER A 164 REMARK 465 SER A 165 REMARK 465 GLY A 166 REMARK 465 VAL A 167 REMARK 465 HIS A 168 REMARK 465 THR A 169 REMARK 465 PHE A 170 REMARK 465 PRO A 171 REMARK 465 ALA A 172 REMARK 465 VAL A 173 REMARK 465 LEU A 174 REMARK 465 GLN A 175 REMARK 465 SER A 176 REMARK 465 ASP A 177 REMARK 465 LEU A 178 REMARK 465 TYR A 179 REMARK 465 THR A 180 REMARK 465 LEU A 181 REMARK 465 SER A 182 REMARK 465 SER A 183 REMARK 465 SER A 184 REMARK 465 VAL A 185 REMARK 465 THR A 186 REMARK 465 VAL A 187 REMARK 465 THR A 188 REMARK 465 SER A 189 REMARK 465 SER A 190 REMARK 465 THR A 191 REMARK 465 TRP A 192 REMARK 465 PRO A 193 REMARK 465 SER A 194 REMARK 465 GLN A 195 REMARK 465 SER A 196 REMARK 465 ILE A 197 REMARK 465 THR A 198 REMARK 465 CYS A 199 REMARK 465 ASN A 200 REMARK 465 VAL A 201 REMARK 465 ALA A 202 REMARK 465 HIS A 203 REMARK 465 PRO A 204 REMARK 465 ALA A 205 REMARK 465 SER A 206 REMARK 465 SER A 207 REMARK 465 THR A 208 REMARK 465 LYS A 209 REMARK 465 VAL A 210 REMARK 465 ASP A 211 REMARK 465 LYS A 212 REMARK 465 LYS A 213 REMARK 465 ILE A 214 REMARK 465 GLY A 215 REMARK 465 GLY A 216 REMARK 465 GLY A 217 REMARK 465 HIS A 218 REMARK 465 HIS A 219 REMARK 465 HIS A 220 REMARK 465 HIS A 221 REMARK 465 HIS A 222 REMARK 465 HIS A 223 REMARK 465 SER C -1 REMARK 465 PRO C 0 REMARK 465 ASP C 1 REMARK 465 LYS C 107 REMARK 465 ARG C 108 REMARK 465 ALA C 109 REMARK 465 ASP C 110 REMARK 465 ALA C 111 REMARK 465 ALA C 112 REMARK 465 PRO C 113 REMARK 465 THR C 114 REMARK 465 VAL C 115 REMARK 465 SER C 116 REMARK 465 ILE C 117 REMARK 465 PHE C 118 REMARK 465 PRO C 119 REMARK 465 PRO C 120 REMARK 465 SER C 121 REMARK 465 SER C 122 REMARK 465 GLU C 123 REMARK 465 GLN C 124 REMARK 465 LEU C 125 REMARK 465 THR C 126 REMARK 465 SER C 127 REMARK 465 GLY C 128 REMARK 465 GLY C 129 REMARK 465 ALA C 130 REMARK 465 SER C 131 REMARK 465 VAL C 132 REMARK 465 VAL C 133 REMARK 465 CYS C 134 REMARK 465 PHE C 135 REMARK 465 LEU C 136 REMARK 465 ASN C 137 REMARK 465 ASN C 138 REMARK 465 PHE C 139 REMARK 465 TYR C 140 REMARK 465 PRO C 141 REMARK 465 LYS C 142 REMARK 465 ASP C 143 REMARK 465 ILE C 144 REMARK 465 ASN C 145 REMARK 465 VAL C 146 REMARK 465 LYS C 147 REMARK 465 TRP C 148 REMARK 465 LYS C 149 REMARK 465 ILE C 150 REMARK 465 ASP C 151 REMARK 465 GLY C 152 REMARK 465 SER C 153 REMARK 465 GLU C 154 REMARK 465 ARG C 155 REMARK 465 GLN C 156 REMARK 465 ASN C 157 REMARK 465 GLY C 158 REMARK 465 VAL C 159 REMARK 465 LEU C 160 REMARK 465 ASN C 161 REMARK 465 SER C 162 REMARK 465 TRP C 163 REMARK 465 THR C 164 REMARK 465 ASP C 165 REMARK 465 GLN C 166 REMARK 465 ASP C 167 REMARK 465 SER C 168 REMARK 465 LYS C 169 REMARK 465 ASP C 170 REMARK 465 SER C 171 REMARK 465 THR C 172 REMARK 465 TYR C 173 REMARK 465 SER C 174 REMARK 465 MET C 175 REMARK 465 SER C 176 REMARK 465 SER C 177 REMARK 465 THR C 178 REMARK 465 LEU C 179 REMARK 465 THR C 180 REMARK 465 LEU C 181 REMARK 465 THR C 182 REMARK 465 LYS C 183 REMARK 465 ASP C 184 REMARK 465 GLU C 185 REMARK 465 TYR C 186 REMARK 465 GLU C 187 REMARK 465 ARG C 188 REMARK 465 HIS C 189 REMARK 465 ASN C 190 REMARK 465 SER C 191 REMARK 465 TYR C 192 REMARK 465 THR C 193 REMARK 465 CYS C 194 REMARK 465 GLU C 195 REMARK 465 ALA C 196 REMARK 465 THR C 197 REMARK 465 HIS C 198 REMARK 465 LYS C 199 REMARK 465 THR C 200 REMARK 465 SER C 201 REMARK 465 THR C 202 REMARK 465 SER C 203 REMARK 465 PRO C 204 REMARK 465 ILE C 205 REMARK 465 VAL C 206 REMARK 465 LYS C 207 REMARK 465 SER C 208 REMARK 465 PHE C 209 REMARK 465 ASN C 210 REMARK 465 ARG C 211 REMARK 465 ASN C 212 REMARK 465 GLU C 213 REMARK 465 CYS C 214 REMARK 465 ALA D 165 REMARK 465 ARG D 166 REMARK 465 ASP D 167 REMARK 465 VAL D 168 REMARK 465 THR D 169 REMARK 465 VAL D 170 REMARK 465 THR D 171 REMARK 465 LEU D 172 REMARK 465 PRO D 173 REMARK 465 ASP D 174 REMARK 465 TYR D 175 REMARK 465 PRO D 176 REMARK 465 GLY D 177 REMARK 465 SER D 178 REMARK 465 VAL D 179 REMARK 465 PRO D 180 REMARK 465 ILE D 181 REMARK 465 PRO D 182 REMARK 465 LEU D 183 REMARK 465 THR D 184 REMARK 465 VAL D 185 REMARK 465 TYR D 186 REMARK 465 CYS D 187 REMARK 465 ALA D 188 REMARK 465 LYS D 189 REMARK 465 SER D 190 REMARK 465 GLN D 191 REMARK 465 ASN D 192 REMARK 465 LEU D 193 REMARK 465 GLY D 194 REMARK 465 TYR D 195 REMARK 465 TYR D 196 REMARK 465 LEU D 197 REMARK 465 SER D 198 REMARK 465 GLY D 199 REMARK 465 THR D 200 REMARK 465 THR D 201 REMARK 465 ALA D 202 REMARK 465 ASP D 203 REMARK 465 ALA D 204 REMARK 465 GLY D 205 REMARK 465 ASN D 206 REMARK 465 SER D 207 REMARK 465 ILE D 208 REMARK 465 PHE D 209 REMARK 465 THR D 210 REMARK 465 ASN D 211 REMARK 465 THR D 212 REMARK 465 ALA D 213 REMARK 465 SER D 214 REMARK 465 PHE D 215 REMARK 465 SER D 216 REMARK 465 PRO D 217 REMARK 465 ALA D 218 REMARK 465 GLN D 219 REMARK 465 GLY D 220 REMARK 465 VAL D 221 REMARK 465 GLY D 222 REMARK 465 VAL D 223 REMARK 465 GLN D 224 REMARK 465 LEU D 225 REMARK 465 THR D 226 REMARK 465 ARG D 227 REMARK 465 GLN D 228 REMARK 465 GLY D 229 REMARK 465 THR D 230 REMARK 465 ILE D 231 REMARK 465 ILE D 232 REMARK 465 PRO D 233 REMARK 465 ALA D 234 REMARK 465 ASN D 235 REMARK 465 ASN D 236 REMARK 465 THR D 237 REMARK 465 VAL D 238 REMARK 465 SER D 239 REMARK 465 LEU D 240 REMARK 465 GLY D 241 REMARK 465 ALA D 242 REMARK 465 VAL D 243 REMARK 465 GLY D 244 REMARK 465 THR D 245 REMARK 465 SER D 246 REMARK 465 ALA D 247 REMARK 465 VAL D 248 REMARK 465 SER D 249 REMARK 465 LEU D 250 REMARK 465 GLY D 251 REMARK 465 LEU D 252 REMARK 465 THR D 253 REMARK 465 ALA D 254 REMARK 465 ASN D 255 REMARK 465 TYR D 256 REMARK 465 ALA D 257 REMARK 465 ARG D 258 REMARK 465 THR D 259 REMARK 465 GLY D 260 REMARK 465 GLY D 261 REMARK 465 GLN D 262 REMARK 465 VAL D 263 REMARK 465 THR D 264 REMARK 465 ALA D 265 REMARK 465 GLY D 266 REMARK 465 ASN D 267 REMARK 465 VAL D 268 REMARK 465 GLN D 269 REMARK 465 SER D 270 REMARK 465 ILE D 271 REMARK 465 ILE D 272 REMARK 465 GLY D 273 REMARK 465 VAL D 274 REMARK 465 THR D 275 REMARK 465 PHE D 276 REMARK 465 VAL D 277 REMARK 465 TYR D 278 REMARK 465 GLN D 279 REMARK 465 GLY D 280 REMARK 465 GLY D 281 REMARK 465 SER D 282 REMARK 465 SER D 283 REMARK 465 GLY D 284 REMARK 465 GLY D 285 REMARK 465 GLY D 286 REMARK 465 ALA D 287 REMARK 465 ASP D 288 REMARK 465 VAL D 289 REMARK 465 THR D 290 REMARK 465 ILE D 291 REMARK 465 THR D 292 REMARK 465 VAL D 293 REMARK 465 ASN D 294 REMARK 465 GLY D 295 REMARK 465 LYS D 296 REMARK 465 VAL D 297 REMARK 465 VAL D 298 REMARK 465 ALA D 299 REMARK 465 LYS D 300 REMARK 465 GLY D 301 REMARK 465 GLY D 302 REMARK 465 HIS D 303 REMARK 465 HIS D 304 REMARK 465 HIS D 305 REMARK 465 HIS D 306 REMARK 465 HIS D 307 REMARK 465 HIS D 308 REMARK 465 HIS D 309 REMARK 465 HIS D 310 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 PHE A 88 CG CD1 CD2 CE1 CE2 CZ 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 THR L 17 -74.80 -125.46 REMARK 500 SER L 32 -73.90 65.34 REMARK 500 LEU L 52 -62.97 -128.33 REMARK 500 ARG L 55 -100.57 56.68 REMARK 500 SER L 61 -138.99 58.76 REMARK 500 GLU L 98 -140.85 55.02 REMARK 500 GLN H 6 -101.65 -119.98 REMARK 500 ALA H 92 -149.54 -149.14 REMARK 500 TRP H 103 -50.34 -143.95 REMARK 500 SER H 104 63.65 -159.61 REMARK 500 THR H 105 -156.82 -109.80 REMARK 500 TYR H 111 90.59 57.43 REMARK 500 PRO A 41 80.17 -66.98 REMARK 500 ILE A 48 -75.59 -123.32 REMARK 500 TYR A 50 93.55 -166.53 REMARK 500 SER A 55 -140.20 -125.89 REMARK 500 LEU A 70 60.29 61.05 REMARK 500 PRO A 103 -132.29 -80.03 REMARK 500 ALA C 9 -105.27 57.41 REMARK 500 LEU C 11 -97.95 -114.73 REMARK 500 ASN C 28 75.29 55.77 REMARK 500 TYR C 30 -161.25 -100.82 REMARK 500 ASN C 32 57.25 -157.29 REMARK 500 ALA C 51 -127.26 56.93 REMARK 500 ASN C 53 101.71 -167.86 REMARK 500 GLU C 81 -159.55 -96.09 REMARK 500 TYR C 92 -62.62 -124.99 REMARK 500 THR C 100 -153.14 -81.16 REMARK 500 GLN D 32 -155.73 -112.95 REMARK 500 TYR D 48 80.67 58.73 REMARK 500 PRO D 85 85.06 -67.75 REMARK 500 ASN D 96 -45.82 -145.30 REMARK 500 TYR D 137 -67.00 -107.69 REMARK 500 THR D 158 -126.32 55.80 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46596 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF E. COLI FIMH LECTIN DOMAIN BOUND TO FABS 440-2 REMARK 900 AND 454-3 DBREF 9D6F L -1 219 PDB 9D6F 9D6F -1 219 DBREF 9D6F H -1 228 PDB 9D6F 9D6F -1 228 DBREF 9D6F A -1 223 PDB 9D6F 9D6F -1 223 DBREF 9D6F C -1 214 PDB 9D6F 9D6F -1 214 DBREF 9D6F D 1 279 UNP P08191 FIMH_ECOLI 22 300 DBREF 9D6F D 287 300 UNP P08190 FIMG_ECOLI 24 37 SEQADV 9D6F SER D 7 UNP P08191 ASN 28 ENGINEERED MUTATION SEQADV 9D6F ALA D 15 UNP P08191 GLY 36 ENGINEERED MUTATION SEQADV 9D6F ALA D 16 UNP P08191 GLY 37 ENGINEERED MUTATION SEQADV 9D6F ALA D 27 UNP P08191 VAL 48 ENGINEERED MUTATION SEQADV 9D6F SER D 70 UNP P08191 ASN 91 ENGINEERED MUTATION SEQADV 9D6F GLN D 228 UNP P08191 ASN 249 ENGINEERED MUTATION SEQADV 9D6F GLY D 280 UNP P08191 LINKER SEQADV 9D6F GLY D 281 UNP P08191 LINKER SEQADV 9D6F SER D 282 UNP P08191 LINKER SEQADV 9D6F SER D 283 UNP P08191 LINKER SEQADV 9D6F GLY D 284 UNP P08191 LINKER SEQADV 9D6F GLY D 285 UNP P08191 LINKER SEQADV 9D6F GLY D 286 UNP P08191 LINKER SEQADV 9D6F GLY D 301 UNP P08190 EXPRESSION TAG SEQADV 9D6F GLY D 302 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 303 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 304 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 305 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 306 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 307 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 308 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 309 UNP P08190 EXPRESSION TAG SEQADV 9D6F HIS D 310 UNP P08190 EXPRESSION TAG SEQRES 1 L 221 SER PRO ASP ILE VAL MET THR GLN ALA ALA PHE SER ASN SEQRES 2 L 221 PRO VAL THR LEU GLY THR SER ALA SER ILE SER CYS SER SEQRES 3 L 221 SER SER LYS SER LEU LEU HIS SER ASN GLY ILE THR TYR SEQRES 4 L 221 LEU TYR TRP TYR LEU GLN ARG PRO GLY GLN SER PRO GLN SEQRES 5 L 221 LEU LEU ILE TYR ARG MET SER ASN LEU ALA SER GLY VAL SEQRES 6 L 221 PRO ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE SEQRES 7 L 221 ALA LEU ARG ILE SER ARG VAL GLU THR GLU ASP VAL GLY SEQRES 8 L 221 VAL TYR TYR CYS ALA GLN MET LEU GLU ARG PRO TYR THR SEQRES 9 L 221 PHE GLY SER GLY THR LYS LEU GLU ILE LYS ARG ALA ASP SEQRES 10 L 221 ALA ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU SEQRES 11 L 221 GLN LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU SEQRES 12 L 221 ASN ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS SEQRES 13 L 221 ILE ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER SEQRES 14 L 221 TRP THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SEQRES 15 L 221 SER SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG SEQRES 16 L 221 HIS ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER SEQRES 17 L 221 THR SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 H 230 SER PRO GLN VAL GLN LEU THR GLN SER GLY ALA GLU LEU SEQRES 2 H 230 VAL LYS PRO GLY ALA SER VAL LYS ILE SER CYS LYS ALA SEQRES 3 H 230 SER GLY TYR THR PHE THR ASP TYR TYR ILE ASN TRP VAL SEQRES 4 H 230 LYS GLN ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY LYS SEQRES 5 H 230 ILE GLY PRO GLY ASN ASN SER THR TYR TYR LYS GLU ASN SEQRES 6 H 230 PHE GLU GLY LYS ALA THR LEU THR ALA ASP LYS SER PHE SEQRES 7 H 230 SER THR ALA TYR MET GLN LEU SER SER LEU THR SER GLU SEQRES 8 H 230 ASP SER ALA VAL TYR PHE CYS ALA ARG TRP GLY TYR LEU SEQRES 9 H 230 TRP SER THR GLY GLY GLY PHE ASP TYR TRP GLY HIS GLY SEQRES 10 H 230 THR THR LEU THR VAL SER SER ALA LYS THR THR ALA PRO SEQRES 11 H 230 SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR THR SEQRES 12 H 230 GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 13 H 230 PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER SEQRES 14 H 230 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 230 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR SEQRES 16 H 230 SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN VAL SEQRES 17 H 230 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 H 230 GLY GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 A 225 SER PRO GLN VAL GLN LEU GLN GLN SER GLY SER GLU LEU SEQRES 2 A 225 ALA LYS PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SEQRES 3 A 225 SER GLY TYR THR PHE THR ARG TYR TRP MET HIS TRP VAL SEQRES 4 A 225 LYS GLN ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR SEQRES 5 A 225 SER ASN PRO SER SER GLY TYR THR ASN PHE ASN GLN LYS SEQRES 6 A 225 PHE LYS ASP LYS ALA ALA LEU THR ALA ASP THR SER SER SEQRES 7 A 225 ASN THR ALA TYR ILE GLN LEU ASN GLY LEU THR PHE GLU SEQRES 8 A 225 ASP SER ALA VAL TYR PHE CYS ALA ARG ASP GLY ASP PRO SEQRES 9 A 225 PRO PHE VAL TYR TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 A 225 SER ALA ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU SEQRES 11 A 225 ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR SEQRES 12 A 225 LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL SEQRES 13 A 225 THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL SEQRES 14 A 225 HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR SEQRES 15 A 225 LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO SEQRES 16 A 225 SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER SEQRES 17 A 225 SER THR LYS VAL ASP LYS LYS ILE GLY GLY GLY HIS HIS SEQRES 18 A 225 HIS HIS HIS HIS SEQRES 1 C 216 SER PRO ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SEQRES 2 C 216 SER ALA SER VAL GLY GLU THR VAL THR ILE THR CYS ARG SEQRES 3 C 216 ALA SER GLU ASN ILE TYR SER ASN LEU ALA TRP TYR GLN SEQRES 4 C 216 GLN LYS GLN GLY LYS SER PRO GLN LEU LEU VAL ASP GLY SEQRES 5 C 216 ALA THR ASN LEU ALA ASP GLY VAL PRO SER ARG PHE SER SEQRES 6 C 216 GLY SER GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN SEQRES 7 C 216 SER VAL GLN SER GLU ASP PHE GLY ASN TYR TYR CYS GLN SEQRES 8 C 216 HIS PHE TYR GLY THR PRO PHE THR PHE GLY THR GLY THR SEQRES 9 C 216 LYS LEU GLU MET LYS ARG ALA ASP ALA ALA PRO THR VAL SEQRES 10 C 216 SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SER GLY SEQRES 11 C 216 GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO SEQRES 12 C 216 LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU SEQRES 13 C 216 ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SEQRES 14 C 216 SER LYS ASP SER THR TYR SER MET SER SER THR LEU THR SEQRES 15 C 216 LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR SEQRES 16 C 216 CYS GLU ALA THR HIS LYS THR SER THR SER PRO ILE VAL SEQRES 17 C 216 LYS SER PHE ASN ARG ASN GLU CYS SEQRES 1 D 310 PHE ALA CYS LYS THR ALA SER GLY THR ALA ILE PRO ILE SEQRES 2 D 310 GLY ALA ALA SER ALA ASN VAL TYR VAL ASN LEU ALA PRO SEQRES 3 D 310 ALA VAL ASN VAL GLY GLN ASN LEU VAL VAL ASP LEU SER SEQRES 4 D 310 THR GLN ILE PHE CYS HIS ASN ASP TYR PRO GLU THR ILE SEQRES 5 D 310 THR ASP TYR VAL THR LEU GLN ARG GLY SER ALA TYR GLY SEQRES 6 D 310 GLY VAL LEU SER SER PHE SER GLY THR VAL LYS TYR SER SEQRES 7 D 310 GLY SER SER TYR PRO PHE PRO THR THR SER GLU THR PRO SEQRES 8 D 310 ARG VAL VAL TYR ASN SER ARG THR ASP LYS PRO TRP PRO SEQRES 9 D 310 VAL ALA LEU TYR LEU THR PRO VAL SER SER ALA GLY GLY SEQRES 10 D 310 VAL ALA ILE LYS ALA GLY SER LEU ILE ALA VAL LEU ILE SEQRES 11 D 310 LEU ARG GLN THR ASN ASN TYR ASN SER ASP ASP PHE GLN SEQRES 12 D 310 PHE VAL TRP ASN ILE TYR ALA ASN ASN ASP VAL VAL VAL SEQRES 13 D 310 PRO THR GLY GLY CYS ASP VAL SER ALA ARG ASP VAL THR SEQRES 14 D 310 VAL THR LEU PRO ASP TYR PRO GLY SER VAL PRO ILE PRO SEQRES 15 D 310 LEU THR VAL TYR CYS ALA LYS SER GLN ASN LEU GLY TYR SEQRES 16 D 310 TYR LEU SER GLY THR THR ALA ASP ALA GLY ASN SER ILE SEQRES 17 D 310 PHE THR ASN THR ALA SER PHE SER PRO ALA GLN GLY VAL SEQRES 18 D 310 GLY VAL GLN LEU THR ARG GLN GLY THR ILE ILE PRO ALA SEQRES 19 D 310 ASN ASN THR VAL SER LEU GLY ALA VAL GLY THR SER ALA SEQRES 20 D 310 VAL SER LEU GLY LEU THR ALA ASN TYR ALA ARG THR GLY SEQRES 21 D 310 GLY GLN VAL THR ALA GLY ASN VAL GLN SER ILE ILE GLY SEQRES 22 D 310 VAL THR PHE VAL TYR GLN GLY GLY SER SER GLY GLY GLY SEQRES 23 D 310 ALA ASP VAL THR ILE THR VAL ASN GLY LYS VAL VAL ALA SEQRES 24 D 310 LYS GLY GLY HIS HIS HIS HIS HIS HIS HIS HIS HELIX 1 AA1 GLU L 84 VAL L 88 5 5 HELIX 2 AA2 THR A 87 SER A 91 5 5 SHEET 1 AA1 2 MET L 4 THR L 5 0 SHEET 2 AA1 2 SER L 24 SER L 25 -1 O SER L 24 N THR L 5 SHEET 1 AA2 5 ASN L 58 LEU L 59 0 SHEET 2 AA2 5 GLN L 50 ARG L 55 -1 N TYR L 54 O ASN L 58 SHEET 3 AA2 5 LEU L 38 GLN L 43 -1 N LEU L 42 O GLN L 50 SHEET 4 AA2 5 ALA L 94 GLN L 95 -1 O ALA L 94 N TYR L 39 SHEET 5 AA2 5 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 AA3 5 ASN L 58 LEU L 59 0 SHEET 2 AA3 5 GLN L 50 ARG L 55 -1 N TYR L 54 O ASN L 58 SHEET 3 AA3 5 LEU L 38 GLN L 43 -1 N LEU L 42 O GLN L 50 SHEET 4 AA3 5 VAL L 90 TYR L 91 -1 O VAL L 90 N GLN L 43 SHEET 5 AA3 5 THR L 107 LYS L 108 -1 O THR L 107 N TYR L 91 SHEET 1 AA4 2 SER L 68 GLY L 71 0 SHEET 2 AA4 2 PHE L 76 ARG L 79 -1 O ARG L 79 N SER L 68 SHEET 1 AA5 2 GLU H 10 VAL H 12 0 SHEET 2 AA5 2 LEU H 118 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 1 AA6 3 CYS H 22 LYS H 23 0 SHEET 2 AA6 3 THR H 78 MET H 81 -1 O ALA H 79 N CYS H 22 SHEET 3 AA6 3 LEU H 70 ALA H 72 -1 N THR H 71 O TYR H 80 SHEET 1 AA7 4 THR H 58 TYR H 60 0 SHEET 2 AA7 4 GLN H 43 ILE H 51 -1 N LYS H 50 O TYR H 59 SHEET 3 AA7 4 ILE H 34 ARG H 40 -1 N ILE H 34 O ILE H 51 SHEET 4 AA7 4 VAL H 93 TYR H 94 -1 O VAL H 93 N GLN H 39 SHEET 1 AA8 4 THR H 58 TYR H 60 0 SHEET 2 AA8 4 GLN H 43 ILE H 51 -1 N LYS H 50 O TYR H 59 SHEET 3 AA8 4 ILE H 34 ARG H 40 -1 N ILE H 34 O ILE H 51 SHEET 4 AA8 4 ALA H 97 ARG H 98 -1 O ALA H 97 N ASN H 35 SHEET 1 AA9 3 LEU A 4 GLN A 6 0 SHEET 2 AA9 3 CYS A 22 ALA A 24 -1 O LYS A 23 N GLN A 5 SHEET 3 AA9 3 THR A 78 ALA A 79 -1 O ALA A 79 N CYS A 22 SHEET 1 AB1 2 SER A 17 LYS A 19 0 SHEET 2 AB1 2 GLN A 82 ASN A 84 -1 O LEU A 83 N VAL A 18 SHEET 1 AB2 3 LEU A 45 SER A 51 0 SHEET 2 AB2 3 MET A 34 GLN A 39 -1 N LYS A 38 O GLU A 46 SHEET 3 AB2 3 VAL A 93 ARG A 98 -1 O VAL A 93 N GLN A 39 SHEET 1 AB3 4 MET C 4 THR C 5 0 SHEET 2 AB3 4 VAL C 19 ALA C 25 -1 O ARG C 24 N THR C 5 SHEET 3 AB3 4 GLN C 70 ILE C 75 -1 O LEU C 73 N ILE C 21 SHEET 4 AB3 4 SER C 63 SER C 65 -1 N SER C 65 O SER C 72 SHEET 1 AB4 3 GLN C 45 VAL C 48 0 SHEET 2 AB4 3 LEU C 33 GLN C 38 -1 N TRP C 35 O VAL C 48 SHEET 3 AB4 3 ASN C 85 HIS C 90 -1 O GLN C 89 N ALA C 34 SHEET 1 AB5 3 LYS D 4 THR D 5 0 SHEET 2 AB5 3 ILE D 42 CYS D 44 -1 O PHE D 43 N LYS D 4 SHEET 3 AB5 3 LYS D 101 PRO D 102 -1 O LYS D 101 N CYS D 44 SHEET 1 AB6 5 SER D 17 VAL D 22 0 SHEET 2 AB6 5 PHE D 142 ALA D 150 1 O TYR D 149 N VAL D 20 SHEET 3 AB6 5 LEU D 125 ASN D 135 -1 N LEU D 129 O TRP D 146 SHEET 4 AB6 5 ASP D 54 LEU D 58 -1 N THR D 57 O ARG D 132 SHEET 5 AB6 5 VAL D 93 TYR D 95 -1 O TYR D 95 N ASP D 54 SHEET 1 AB7 2 VAL D 36 ASP D 37 0 SHEET 2 AB7 2 ALA D 106 LEU D 107 -1 O LEU D 107 N VAL D 36 SHEET 1 AB8 2 VAL D 75 LYS D 76 0 SHEET 2 AB8 2 SER D 81 TYR D 82 -1 O TYR D 82 N VAL D 75 SSBOND 1 CYS L 23 CYS L 93 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 3 CYS A 22 CYS A 96 1555 1555 2.03 SSBOND 4 CYS C 23 CYS C 88 1555 1555 2.04 SSBOND 5 CYS D 3 CYS D 44 1555 1555 2.03 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