HEADER MEMBRANE PROTEIN 27-MAR-24 9EUO TITLE OUTWARD-OPEN STRUCTURE OF DROSOPHILA DOPAMINE TRANSPORTER BOUND TO AN TITLE 2 ATYPICAL NON-COMPETITIVE INHIBITOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: SODIUM-DEPENDENT DOPAMINE TRANSPORTER; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PROTEIN FUMIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 9D5 ANTIBODY, LIGHT CHAIN; COMPND 9 CHAIN: L; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 9D5 ANTIBODY, HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 GENE: DAT, FMN, CG8380; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS SLC6A3, DOPAMINE TRANSPORTER, ATYPICAL INHIBITORS, NEUROTRANSMITTER KEYWDS 2 SODIUM SYMPORTERS, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.N.PEDERSEN,F.YANG,S.ITA,Y.XU,R.AKUNURI,S.TRAMPARI,C.M.T.NEUMANN, AUTHOR 2 L.M.DESDORF,B.SCHIOETT,J.M.SALVINO,O.V.MORTENSEN,P.NISSEN, AUTHOR 3 A.SHAHSAVAR JRNL AUTH C.N.PEDERSEN,F.YANG,S.ITA,Y.XU,R.AKUNURI,S.TRAMPARI, JRNL AUTH 2 C.M.T.NEUMANN,L.M.DESDORF,B.SCHIOTT,J.M.SALVINO, JRNL AUTH 3 O.V.MORTENSEN,P.NISSEN,A.SHAHSAVAR JRNL TITL CRYO-EM STRUCTURE OF THE DOPAMINE TRANSPORTER WITH A NOVEL JRNL TITL 2 ATYPICAL NON-COMPETITIVE INHIBITOR BOUND TO THE ORTHOSTERIC JRNL TITL 3 SITE. JRNL REF J.NEUROCHEM. 2024 JRNL REFN ESSN 1471-4159 JRNL PMID 39010681 JRNL DOI 10.1111/JNC.16179 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERAX, COOT, CRYOSPARC, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 4M48 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 147413 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 9EUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292137592. 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 : DROSOPHILA MELANOGASTER REMARK 245 DOPAMINE TRANSPORTER BOUND TO REMARK 245 ATYPICAL INHIBITOR AC-4-248 AND REMARK 245 IN COMPLEX WITH FAB 9D5 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 8.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 14624 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) : 800.00 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 : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 61.30 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, H 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 20 REMARK 465 ASN A 21 REMARK 465 SER A 22 REMARK 465 ILE A 23 REMARK 465 SER A 24 REMARK 465 GLN A 600 REMARK 465 GLN A 601 REMARK 465 LEU A 602 REMARK 465 VAL A 603 REMARK 465 PRO A 604 REMARK 465 ARG A 605 REMARK 465 MET L -21 REMARK 465 ASP L -20 REMARK 465 PHE L -19 REMARK 465 GLN L -18 REMARK 465 VAL L -17 REMARK 465 GLN L -16 REMARK 465 ILE L -15 REMARK 465 PHE L -14 REMARK 465 SER L -13 REMARK 465 PHE L -12 REMARK 465 LEU L -11 REMARK 465 LEU L -10 REMARK 465 ILE L -9 REMARK 465 SER L -8 REMARK 465 ALA L -7 REMARK 465 SER L -6 REMARK 465 VAL L -5 REMARK 465 ALA L -4 REMARK 465 MET L -3 REMARK 465 SER L -2 REMARK 465 ARG L -1 REMARK 465 GLY L 0 REMARK 465 ARG L 109 REMARK 465 ALA L 110 REMARK 465 ASP L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 THR L 115 REMARK 465 VAL L 116 REMARK 465 SER L 117 REMARK 465 ILE L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLN L 125 REMARK 465 LEU L 126 REMARK 465 THR L 127 REMARK 465 SER L 128 REMARK 465 GLY L 129 REMARK 465 GLY L 130 REMARK 465 ALA L 131 REMARK 465 SER L 132 REMARK 465 VAL L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 PHE L 136 REMARK 465 LEU L 137 REMARK 465 ASN L 138 REMARK 465 ASN L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 LYS L 143 REMARK 465 ASP L 144 REMARK 465 ILE L 145 REMARK 465 ASN L 146 REMARK 465 VAL L 147 REMARK 465 LYS L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ILE L 151 REMARK 465 ASP L 152 REMARK 465 GLY L 153 REMARK 465 SER L 154 REMARK 465 GLU L 155 REMARK 465 ARG L 156 REMARK 465 GLN L 157 REMARK 465 ASN L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 LEU L 161 REMARK 465 ASN L 162 REMARK 465 SER L 163 REMARK 465 TRP L 164 REMARK 465 THR L 165 REMARK 465 ASP L 166 REMARK 465 GLN L 167 REMARK 465 ASP L 168 REMARK 465 SER L 169 REMARK 465 LYS L 170 REMARK 465 ASP L 171 REMARK 465 SER L 172 REMARK 465 THR L 173 REMARK 465 TYR L 174 REMARK 465 SER L 175 REMARK 465 MET L 176 REMARK 465 SER L 177 REMARK 465 SER L 178 REMARK 465 THR L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 LEU L 182 REMARK 465 THR L 183 REMARK 465 LYS L 184 REMARK 465 ASP L 185 REMARK 465 GLU L 186 REMARK 465 TYR L 187 REMARK 465 GLU L 188 REMARK 465 ARG L 189 REMARK 465 HIS L 190 REMARK 465 ASN L 191 REMARK 465 SER L 192 REMARK 465 TYR L 193 REMARK 465 THR L 194 REMARK 465 CYS L 195 REMARK 465 GLU L 196 REMARK 465 ALA L 197 REMARK 465 THR L 198 REMARK 465 HIS L 199 REMARK 465 LYS L 200 REMARK 465 THR L 201 REMARK 465 SER L 202 REMARK 465 THR L 203 REMARK 465 SER L 204 REMARK 465 PRO L 205 REMARK 465 ILE L 206 REMARK 465 VAL L 207 REMARK 465 LYS L 208 REMARK 465 SER L 209 REMARK 465 PHE L 210 REMARK 465 ASN L 211 REMARK 465 ARG L 212 REMARK 465 ASN L 213 REMARK 465 GLU L 214 REMARK 465 CYS L 215 REMARK 465 MET H -18 REMARK 465 ASN H -17 REMARK 465 PHE H -16 REMARK 465 GLY H -15 REMARK 465 LEU H -14 REMARK 465 ARG H -13 REMARK 465 LEU H -12 REMARK 465 VAL H -11 REMARK 465 PHE H -10 REMARK 465 LEU H -9 REMARK 465 VAL H -8 REMARK 465 LEU H -7 REMARK 465 ILE H -6 REMARK 465 LEU H -5 REMARK 465 LYS H -4 REMARK 465 GLY H -3 REMARK 465 VAL H -2 REMARK 465 GLN H -1 REMARK 465 CYS H 0 REMARK 465 GLU H 1 REMARK 465 LYS H 121 REMARK 465 THR H 122 REMARK 465 THR H 123 REMARK 465 ALA H 124 REMARK 465 PRO H 125 REMARK 465 SER H 126 REMARK 465 VAL H 127 REMARK 465 TYR H 128 REMARK 465 PRO H 129 REMARK 465 LEU H 130 REMARK 465 ALA H 131 REMARK 465 PRO H 132 REMARK 465 VAL H 133 REMARK 465 CYS H 134 REMARK 465 GLY H 135 REMARK 465 ASP H 136 REMARK 465 THR H 137 REMARK 465 THR H 138 REMARK 465 GLY H 139 REMARK 465 SER H 140 REMARK 465 SER H 141 REMARK 465 VAL H 142 REMARK 465 THR H 143 REMARK 465 LEU H 144 REMARK 465 GLY H 145 REMARK 465 CYS H 146 REMARK 465 LEU H 147 REMARK 465 VAL H 148 REMARK 465 LYS H 149 REMARK 465 GLY H 150 REMARK 465 TYR H 151 REMARK 465 PHE H 152 REMARK 465 PRO H 153 REMARK 465 GLU H 154 REMARK 465 PRO H 155 REMARK 465 VAL H 156 REMARK 465 THR H 157 REMARK 465 LEU H 158 REMARK 465 THR H 159 REMARK 465 TRP H 160 REMARK 465 ASN H 161 REMARK 465 SER H 162 REMARK 465 GLY H 163 REMARK 465 SER H 164 REMARK 465 LEU H 165 REMARK 465 SER H 166 REMARK 465 SER H 167 REMARK 465 GLY H 168 REMARK 465 VAL H 169 REMARK 465 HIS H 170 REMARK 465 THR H 171 REMARK 465 PHE H 172 REMARK 465 PRO H 173 REMARK 465 ALA H 174 REMARK 465 VAL H 175 REMARK 465 LEU H 176 REMARK 465 GLN H 177 REMARK 465 SER H 178 REMARK 465 ASP H 179 REMARK 465 LEU H 180 REMARK 465 TYR H 181 REMARK 465 THR H 182 REMARK 465 LEU H 183 REMARK 465 SER H 184 REMARK 465 SER H 185 REMARK 465 SER H 186 REMARK 465 VAL H 187 REMARK 465 THR H 188 REMARK 465 VAL H 189 REMARK 465 THR H 190 REMARK 465 SER H 191 REMARK 465 SER H 192 REMARK 465 THR H 193 REMARK 465 TRP H 194 REMARK 465 PRO H 195 REMARK 465 SER H 196 REMARK 465 GLN H 197 REMARK 465 SER H 198 REMARK 465 ILE H 199 REMARK 465 THR H 200 REMARK 465 CYS H 201 REMARK 465 ASN H 202 REMARK 465 VAL H 203 REMARK 465 ALA H 204 REMARK 465 HIS H 205 REMARK 465 PRO H 206 REMARK 465 ALA H 207 REMARK 465 SER H 208 REMARK 465 SER H 209 REMARK 465 THR H 210 REMARK 465 LYS H 211 REMARK 465 VAL H 212 REMARK 465 ASP H 213 REMARK 465 LYS H 214 REMARK 465 LYS H 215 REMARK 465 ILE H 216 REMARK 465 GLU H 217 REMARK 465 PRO H 218 REMARK 465 ARG H 219 REMARK 465 GLY H 220 REMARK 465 PRO H 221 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 OD1 ASP L 83 H ALA L 84 1.48 REMARK 500 O TYR H 32 HH22 ARG H 72 1.55 REMARK 500 O VAL H 37 H TYR H 95 1.58 REMARK 500 HH11 ARG A 27 O ARG A 92 1.59 REMARK 500 OD1 ASP A 506 HH22 ARG H 56 1.59 REMARK 500 OD1 ASP A 506 NH2 ARG H 56 2.19 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 ARG A 52 -56.08 -124.43 REMARK 500 ASN A 60 48.96 -106.11 REMARK 500 VAL A 391 -66.07 -120.07 REMARK 500 ALA A 479 -29.59 -140.68 REMARK 500 SER L 51 -157.62 -165.64 REMARK 500 ASP L 83 -80.15 -99.25 REMARK 500 THR H 28 90.74 -69.79 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 NA A 705 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 44 O REMARK 620 2 ASN A 49 OD1 99.4 REMARK 620 3 SER A 320 O 70.8 141.7 REMARK 620 4 SER A 320 OG 131.6 128.7 73.6 REMARK 620 5 ASN A 352 OD1 57.3 142.4 63.5 78.0 REMARK 620 N 1 2 3 4 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-19978 RELATED DB: EMDB REMARK 900 OUTWARD-OPEN STRUCTURE OF DROSOPHILA DOPAMINE TRANSPORTER BOUND TO REMARK 900 AN ATYPICAL NON-COMPETITIVE INHIBITOR REMARK 900 RELATED ID: EMD-19979 RELATED DB: EMDB REMARK 900 INHIBITOR-FREE OUTWARD-OPEN STRUCTURE OF DROSOPHILA DOPAMINE REMARK 900 TRANSPORTER REMARK 900 RELATED ID: 9EUP RELATED DB: PDB REMARK 900 INHIBITOR-FREE OUTWARD-OPEN STRUCTURE OF DROSOPHILA DOPAMINE REMARK 900 TRANSPORTER DBREF 9EUO A 21 601 UNP Q7K4Y6 DAT_DROME 21 601 DBREF 9EUO L -21 215 PDB 9EUO 9EUO -21 215 DBREF 9EUO H -18 221 PDB 9EUO 9EUO -18 221 SEQADV 9EUO MET A 20 UNP Q7K4Y6 INITIATING METHIONINE SEQADV 9EUO ALA A 74 UNP Q7K4Y6 VAL 74 ENGINEERED MUTATION SEQADV 9EUO A UNP Q7K4Y6 ASN 164 DELETION SEQADV 9EUO A UNP Q7K4Y6 ALA 165 DELETION SEQADV 9EUO A UNP Q7K4Y6 SER 166 DELETION SEQADV 9EUO A UNP Q7K4Y6 ARG 167 DELETION SEQADV 9EUO A UNP Q7K4Y6 VAL 168 DELETION SEQADV 9EUO A UNP Q7K4Y6 PRO 169 DELETION SEQADV 9EUO A UNP Q7K4Y6 VAL 170 DELETION SEQADV 9EUO A UNP Q7K4Y6 ILE 171 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLY 172 DELETION SEQADV 9EUO A UNP Q7K4Y6 ASN 173 DELETION SEQADV 9EUO A UNP Q7K4Y6 TYR 174 DELETION SEQADV 9EUO A UNP Q7K4Y6 SER 175 DELETION SEQADV 9EUO A UNP Q7K4Y6 ASP 176 DELETION SEQADV 9EUO A UNP Q7K4Y6 LEU 177 DELETION SEQADV 9EUO A UNP Q7K4Y6 TYR 178 DELETION SEQADV 9EUO A UNP Q7K4Y6 ALA 179 DELETION SEQADV 9EUO A UNP Q7K4Y6 MET 180 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLY 181 DELETION SEQADV 9EUO A UNP Q7K4Y6 ASN 182 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLN 183 DELETION SEQADV 9EUO A UNP Q7K4Y6 SER 184 DELETION SEQADV 9EUO A UNP Q7K4Y6 LEU 185 DELETION SEQADV 9EUO A UNP Q7K4Y6 LEU 186 DELETION SEQADV 9EUO A UNP Q7K4Y6 TYR 187 DELETION SEQADV 9EUO A UNP Q7K4Y6 ASN 188 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLU 189 DELETION SEQADV 9EUO A UNP Q7K4Y6 THR 190 DELETION SEQADV 9EUO A UNP Q7K4Y6 TYR 191 DELETION SEQADV 9EUO A UNP Q7K4Y6 MET 192 DELETION SEQADV 9EUO A UNP Q7K4Y6 ASN 193 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLY 194 DELETION SEQADV 9EUO A UNP Q7K4Y6 SER 195 DELETION SEQADV 9EUO A UNP Q7K4Y6 SER 196 DELETION SEQADV 9EUO A UNP Q7K4Y6 LEU 197 DELETION SEQADV 9EUO A UNP Q7K4Y6 ASP 198 DELETION SEQADV 9EUO A UNP Q7K4Y6 THR 199 DELETION SEQADV 9EUO A UNP Q7K4Y6 SER 200 DELETION SEQADV 9EUO A UNP Q7K4Y6 ALA 201 DELETION SEQADV 9EUO A UNP Q7K4Y6 VAL 202 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLY 203 DELETION SEQADV 9EUO A UNP Q7K4Y6 HIS 204 DELETION SEQADV 9EUO A UNP Q7K4Y6 VAL 205 DELETION SEQADV 9EUO A UNP Q7K4Y6 GLU 206 DELETION SEQADV 9EUO ALA A 275 UNP Q7K4Y6 VAL 275 ENGINEERED MUTATION SEQADV 9EUO ALA A 311 UNP Q7K4Y6 VAL 311 ENGINEERED MUTATION SEQADV 9EUO ALA A 415 UNP Q7K4Y6 LEU 415 ENGINEERED MUTATION SEQADV 9EUO LEU A 538 UNP Q7K4Y6 GLY 538 ENGINEERED MUTATION SEQADV 9EUO LEU A 602 UNP Q7K4Y6 EXPRESSION TAG SEQADV 9EUO VAL A 603 UNP Q7K4Y6 EXPRESSION TAG SEQADV 9EUO PRO A 604 UNP Q7K4Y6 EXPRESSION TAG SEQADV 9EUO ARG A 605 UNP Q7K4Y6 EXPRESSION TAG SEQRES 1 A 543 MET ASN SER ILE SER ASP GLU ARG GLU THR TRP SER GLY SEQRES 2 A 543 LYS VAL ASP PHE LEU LEU SER VAL ILE GLY PHE ALA VAL SEQRES 3 A 543 ASP LEU ALA ASN VAL TRP ARG PHE PRO TYR LEU CYS TYR SEQRES 4 A 543 LYS ASN GLY GLY GLY ALA PHE LEU VAL PRO TYR GLY ILE SEQRES 5 A 543 MET LEU ALA VAL GLY GLY ILE PRO LEU PHE TYR MET GLU SEQRES 6 A 543 LEU ALA LEU GLY GLN HIS ASN ARG LYS GLY ALA ILE THR SEQRES 7 A 543 CYS TRP GLY ARG LEU VAL PRO LEU PHE LYS GLY ILE GLY SEQRES 8 A 543 TYR ALA VAL VAL LEU ILE ALA PHE TYR VAL ASP PHE TYR SEQRES 9 A 543 TYR ASN VAL ILE ILE ALA TRP SER LEU ARG PHE PHE PHE SEQRES 10 A 543 ALA SER PHE THR ASN SER LEU PRO TRP THR SER CYS ASN SEQRES 11 A 543 ASN ILE TRP ASN THR PRO ASN CYS ARG PRO PHE GLU SER SEQRES 12 A 543 GLN GLY PHE GLN SER ALA ALA SER GLU TYR PHE ASN ARG SEQRES 13 A 543 TYR ILE LEU GLU LEU ASN ARG SER GLU GLY ILE HIS ASP SEQRES 14 A 543 LEU GLY ALA ILE LYS TRP ASP MET ALA LEU CYS LEU LEU SEQRES 15 A 543 ILE VAL TYR LEU ILE CYS TYR PHE SER LEU TRP LYS GLY SEQRES 16 A 543 ILE SER THR SER GLY LYS VAL VAL TRP PHE THR ALA LEU SEQRES 17 A 543 PHE PRO TYR ALA ALA LEU LEU ILE LEU LEU ILE ARG GLY SEQRES 18 A 543 LEU THR LEU PRO GLY SER PHE LEU GLY ILE GLN TYR TYR SEQRES 19 A 543 LEU THR PRO ASN PHE SER ALA ILE TYR LYS ALA GLU VAL SEQRES 20 A 543 TRP ALA ASP ALA ALA THR GLN VAL PHE PHE SER LEU GLY SEQRES 21 A 543 PRO GLY PHE GLY VAL LEU LEU ALA TYR ALA SER TYR ASN SEQRES 22 A 543 LYS TYR HIS ASN ASN VAL TYR LYS ASP ALA LEU LEU THR SEQRES 23 A 543 SER PHE ILE ASN SER ALA THR SER PHE ILE ALA GLY PHE SEQRES 24 A 543 VAL ILE PHE SER VAL LEU GLY TYR MET ALA HIS THR LEU SEQRES 25 A 543 GLY VAL ARG ILE GLU ASP VAL ALA THR GLU GLY PRO GLY SEQRES 26 A 543 LEU VAL PHE VAL VAL TYR PRO ALA ALA ILE ALA THR MET SEQRES 27 A 543 PRO ALA SER THR PHE TRP ALA LEU ILE PHE PHE MET MET SEQRES 28 A 543 LEU ALA THR LEU GLY LEU ASP SER SER PHE GLY GLY SER SEQRES 29 A 543 GLU ALA ILE ILE THR ALA LEU SER ASP GLU PHE PRO LYS SEQRES 30 A 543 ILE LYS ARG ASN ARG GLU LEU PHE VAL ALA GLY LEU PHE SEQRES 31 A 543 SER LEU TYR PHE VAL VAL GLY LEU ALA SER CYS THR GLN SEQRES 32 A 543 GLY GLY PHE TYR PHE PHE HIS LEU LEU ASP ARG TYR ALA SEQRES 33 A 543 ALA GLY TYR SER ILE LEU VAL ALA VAL PHE PHE GLU ALA SEQRES 34 A 543 ILE ALA VAL SER TRP ILE TYR GLY THR ASN ARG PHE SER SEQRES 35 A 543 GLU ASP ILE ARG ASP MET ILE GLY PHE PRO PRO GLY ARG SEQRES 36 A 543 TYR TRP GLN VAL CYS TRP ARG PHE VAL ALA PRO ILE PHE SEQRES 37 A 543 LEU LEU PHE ILE THR VAL TYR LEU LEU ILE GLY TYR GLU SEQRES 38 A 543 PRO LEU THR TYR ALA ASP TYR VAL TYR PRO SER TRP ALA SEQRES 39 A 543 ASN ALA LEU GLY TRP CYS ILE ALA GLY SER SER VAL VAL SEQRES 40 A 543 MET ILE PRO ALA VAL ALA ILE PHE LYS LEU LEU SER THR SEQRES 41 A 543 PRO GLY SER LEU ARG GLN ARG PHE THR ILE LEU THR THR SEQRES 42 A 543 PRO TRP ARG ASP GLN GLN LEU VAL PRO ARG SEQRES 1 L 237 MET ASP PHE GLN VAL GLN ILE PHE SER PHE LEU LEU ILE SEQRES 2 L 237 SER ALA SER VAL ALA MET SER ARG GLY GLU ASN VAL LEU SEQRES 3 L 237 THR GLN SER PRO ALA ILE MET SER THR SER PRO GLY GLU SEQRES 4 L 237 LYS VAL THR MET THR CYS ARG ALA SER SER SER VAL GLY SEQRES 5 L 237 SER SER TYR LEU HIS TRP TYR GLN GLN LYS SER GLY ALA SEQRES 6 L 237 SER PRO LYS LEU TRP ILE TYR SER THR SER ASN LEU ALA SEQRES 7 L 237 SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SER GLY SEQRES 8 L 237 THR SER TYR SER LEU THR ILE SER SER VAL GLU ALA GLU SEQRES 9 L 237 ASP ALA ALA THR TYR TYR CYS GLN GLN PHE SER GLY TYR SEQRES 10 L 237 PRO LEU THR PHE GLY SER GLY THR LYS LEU GLU MET LYS SEQRES 11 L 237 ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO PRO SEQRES 12 L 237 SER SER GLU GLN LEU THR SER GLY GLY ALA SER VAL VAL SEQRES 13 L 237 CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN VAL SEQRES 14 L 237 LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY VAL SEQRES 15 L 237 LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP SER THR SEQRES 16 L 237 TYR SER MET SER SER THR LEU THR LEU THR LYS ASP GLU SEQRES 17 L 237 TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR HIS SEQRES 18 L 237 LYS THR SER THR SER PRO ILE VAL LYS SER PHE ASN ARG SEQRES 19 L 237 ASN GLU CYS SEQRES 1 H 240 MET ASN PHE GLY LEU ARG LEU VAL PHE LEU VAL LEU ILE SEQRES 2 H 240 LEU LYS GLY VAL GLN CYS GLU VAL GLN LEU VAL GLU SER SEQRES 3 H 240 GLY GLY GLY LEU VAL LYS PRO GLY GLY SER LEU LYS LEU SEQRES 4 H 240 SER CYS ALA ALA SER GLY PHE THR PHE SER SER TYR ALA SEQRES 5 H 240 MET SER TRP VAL ARG GLN SER PRO GLU LYS ARG LEU GLU SEQRES 6 H 240 TRP VAL ALA GLU ILE SER SER GLY GLY ARG TYR ILE TYR SEQRES 7 H 240 TYR SER ASP THR VAL THR GLY ARG PHE THR ILE SER ARG SEQRES 8 H 240 ASP ASN ALA ARG ASN ILE LEU HIS LEU GLU MET SER SER SEQRES 9 H 240 LEU ARG SER GLU ASP THR ALA MET TYR TYR CYS ALA ARG SEQRES 10 H 240 GLY GLU VAL ARG GLN ARG GLY PHE ASP TYR TRP GLY GLN SEQRES 11 H 240 GLY THR THR LEU THR VAL SER SER ALA LYS THR THR ALA SEQRES 12 H 240 PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR SEQRES 13 H 240 THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY SEQRES 14 H 240 TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SEQRES 15 H 240 SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 16 H 240 GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL SEQRES 17 H 240 THR SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN SEQRES 18 H 240 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS SEQRES 19 H 240 ILE GLU PRO ARG GLY PRO HET H8F A 701 48 HET Y01 A 702 84 HET 144 A 703 20 HET CLR A 704 74 HET NA A 705 1 HET CL A 706 1 HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM 144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM HETNAM CLR CHOLESTEROL HETNAM NA SODIUM ION HETNAM CL CHLORIDE ION FORMUL 4 H8F FORMUL 5 Y01 C31 H50 O4 FORMUL 6 144 C4 H12 N O3 1+ FORMUL 7 CLR C27 H46 O FORMUL 8 NA NA 1+ FORMUL 9 CL CL 1- HELIX 1 AA1 GLY A 32 VAL A 45 1 14 HELIX 2 AA2 LEU A 47 ARG A 52 1 6 HELIX 3 AA3 ARG A 52 ASN A 60 1 9 HELIX 4 AA4 GLY A 61 ALA A 64 5 4 HELIX 5 AA5 PHE A 65 VAL A 75 1 11 HELIX 6 AA6 GLY A 76 ARG A 92 1 17 HELIX 7 AA7 GLY A 94 VAL A 103 1 10 HELIX 8 AA8 PRO A 104 PHE A 106 5 3 HELIX 9 AA9 LYS A 107 SER A 138 1 32 HELIX 10 AB1 LEU A 143 SER A 147 5 5 HELIX 11 AB2 ALA A 211 TYR A 219 1 9 HELIX 12 AB3 GLU A 222 SER A 226 5 5 HELIX 13 AB4 LYS A 236 TRP A 255 1 20 HELIX 14 AB5 GLY A 257 ALA A 269 1 13 HELIX 15 AB6 LEU A 270 LEU A 286 1 17 HELIX 16 AB7 GLY A 288 THR A 298 1 11 HELIX 17 AB8 SER A 302 TYR A 305 5 4 HELIX 18 AB9 LYS A 306 GLY A 322 1 17 HELIX 19 AC1 GLY A 326 TYR A 334 1 9 HELIX 20 AC2 ASN A 340 LEU A 374 1 35 HELIX 21 AC3 ARG A 377 ALA A 382 1 6 HELIX 22 AC4 GLY A 385 VAL A 391 1 7 HELIX 23 AC5 VAL A 391 ALA A 398 1 8 HELIX 24 AC6 ALA A 402 PHE A 437 1 36 HELIX 25 AC7 PRO A 438 LYS A 441 5 4 HELIX 26 AC8 ASN A 443 CYS A 463 1 21 HELIX 27 AC9 GLY A 466 ALA A 478 1 13 HELIX 28 AD1 ALA A 479 TRP A 496 1 18 HELIX 29 AD2 GLY A 499 GLY A 512 1 14 HELIX 30 AD3 GLY A 516 PHE A 525 1 10 HELIX 31 AD4 PHE A 525 GLY A 541 1 17 HELIX 32 AD5 PRO A 553 VAL A 569 1 17 HELIX 33 AD6 VAL A 569 THR A 582 1 14 HELIX 34 AD7 SER A 585 THR A 595 1 11 HELIX 35 AD8 THR H 28 TYR H 32 5 5 HELIX 36 AD9 ARG H 87 THR H 91 5 5 SHEET 1 AA1 2 CYS A 157 ARG A 158 0 SHEET 2 AA1 2 GLN A 209 SER A 210 1 O GLN A 209 N ARG A 158 SHEET 1 AA2 2 THR A 546 TYR A 547 0 SHEET 2 AA2 2 TYR A 550 VAL A 551 -1 O TYR A 550 N TYR A 547 SHEET 1 AA3 3 LEU L 4 SER L 7 0 SHEET 2 AA3 3 VAL L 19 VAL L 29 -1 O THR L 22 N SER L 7 SHEET 3 AA3 3 PHE L 63 ILE L 76 -1 O TYR L 72 N CYS L 23 SHEET 1 AA4 5 MET L 11 THR L 13 0 SHEET 2 AA4 5 THR L 103 MET L 107 1 O GLU L 106 N MET L 11 SHEET 3 AA4 5 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA4 5 LEU L 34 GLN L 39 -1 N GLN L 39 O THR L 86 SHEET 5 AA4 5 LYS L 46 ILE L 49 -1 O ILE L 49 N TRP L 36 SHEET 1 AA5 4 MET L 11 THR L 13 0 SHEET 2 AA5 4 THR L 103 MET L 107 1 O GLU L 106 N MET L 11 SHEET 3 AA5 4 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA5 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AA6 4 GLN H 3 SER H 7 0 SHEET 2 AA6 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA6 4 ILE H 78 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AA6 4 PHE H 68 ASP H 73 -1 N SER H 71 O HIS H 80 SHEET 1 AA7 6 GLY H 10 VAL H 12 0 SHEET 2 AA7 6 THR H 113 VAL H 117 1 O THR H 116 N GLY H 10 SHEET 3 AA7 6 ALA H 92 ALA H 97 -1 N ALA H 92 O LEU H 115 SHEET 4 AA7 6 SER H 35 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA7 6 LEU H 45 ILE H 51 -1 O ALA H 49 N TRP H 36 SHEET 6 AA7 6 ILE H 58 TYR H 60 -1 O TYR H 59 N GLU H 50 SSBOND 1 CYS A 148 CYS A 157 1555 1555 2.03 SSBOND 2 CYS L 23 CYS L 89 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 96 1555 1555 2.04 LINK O ALA A 44 NA NA A 705 1555 1555 2.56 LINK OD1 ASN A 49 NA NA A 705 1555 1555 2.35 LINK O SER A 320 NA NA A 705 1555 1555 2.95 LINK OG SER A 320 NA NA A 705 1555 1555 2.47 LINK OD1 ASN A 352 NA NA A 705 1555 1555 3.11 CISPEP 1 SER L 7 PRO L 8 0 -2.75 CISPEP 2 TYR L 95 PRO L 96 0 -0.55 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