HEADER MEMBRANE PROTEIN 21-JAN-24 8XZI TITLE CRYO-EM STRUCTURE OF THE CMF-019-BOUND HUMAN APLNR-GI COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: APELIN RECEPTOR; COMPND 3 CHAIN: R; COMPND 4 SYNONYM: ANGIOTENSIN RECEPTOR-LIKE 1,G-PROTEIN COUPLED RECEPTOR APJ, COMPND 5 G-PROTEIN COUPLED RECEPTOR HG11; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 9 CHAIN: A; COMPND 10 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 14 BETA-1; COMPND 15 CHAIN: B; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 19 GAMMA-2; COMPND 20 CHAIN: G; COMPND 21 SYNONYM: G GAMMA-I; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: SCFV16; COMPND 25 CHAIN: S; COMPND 26 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: APLNR, AGTRL1, APJ; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GNAI1; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 16 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: GNB1; SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 24 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 GENE: GNG2; SOURCE 30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 32 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 33 MOL_ID: 5; SOURCE 34 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 35 ORGANISM_TAXID: 32630; SOURCE 36 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 38 EXPRESSION_SYSTEM_CELL: HI5 KEYWDS APLNR, CMF-019, CLASS A GPCR, G-PROTEIN-BIASED SMALL MOLECULE KEYWDS 2 AGONIST, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR W.WANG,S.JI,Y.ZHANG JRNL AUTH W.WANG,S.JI,Y.ZHANG JRNL TITL CRYO-EM STRUCTURE OF THE CMF-019-BOUND HUMAN APLNR-GI JRNL TITL 2 COMPLEX JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.70 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 75660 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 8XZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC. REMARK 100 THE DEPOSITION ID IS D_1300044321. 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 : CRYO-EM STRUCTURE OF THE CMF REMARK 245 -019-BOUND HUMAN APLNR-GI REMARK 245 COMPLEX REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 15.00 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 : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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 : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 50.00 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: R, A, B, G, S 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 R 1 REMARK 465 GLU R 2 REMARK 465 GLU R 3 REMARK 465 GLY R 4 REMARK 465 GLY R 5 REMARK 465 ASP R 6 REMARK 465 PHE R 7 REMARK 465 ASP R 8 REMARK 465 ASN R 9 REMARK 465 TYR R 10 REMARK 465 TYR R 11 REMARK 465 GLY R 12 REMARK 465 ALA R 13 REMARK 465 ASP R 14 REMARK 465 ASN R 15 REMARK 465 GLN R 16 REMARK 465 SER R 17 REMARK 465 GLU R 18 REMARK 465 GLN R 328 REMARK 465 SER R 329 REMARK 465 ARG R 330 REMARK 465 CYS R 331 REMARK 465 ALA R 332 REMARK 465 GLY R 333 REMARK 465 THR R 334 REMARK 465 SER R 335 REMARK 465 HIS R 336 REMARK 465 SER R 337 REMARK 465 SER R 338 REMARK 465 SER R 339 REMARK 465 GLY R 340 REMARK 465 GLU R 341 REMARK 465 LYS R 342 REMARK 465 SER R 343 REMARK 465 ALA R 344 REMARK 465 SER R 345 REMARK 465 TYR R 346 REMARK 465 SER R 347 REMARK 465 SER R 348 REMARK 465 GLY R 349 REMARK 465 HIS R 350 REMARK 465 SER R 351 REMARK 465 GLN R 352 REMARK 465 GLY R 353 REMARK 465 PRO R 354 REMARK 465 GLY R 355 REMARK 465 PRO R 356 REMARK 465 ASN R 357 REMARK 465 MET R 358 REMARK 465 GLY R 359 REMARK 465 LYS R 360 REMARK 465 GLY R 361 REMARK 465 GLY R 362 REMARK 465 GLU R 363 REMARK 465 GLN R 364 REMARK 465 MET R 365 REMARK 465 HIS R 366 REMARK 465 GLU R 367 REMARK 465 LYS R 368 REMARK 465 SER R 369 REMARK 465 ILE R 370 REMARK 465 PRO R 371 REMARK 465 TYR R 372 REMARK 465 SER R 373 REMARK 465 GLN R 374 REMARK 465 GLU R 375 REMARK 465 THR R 376 REMARK 465 LEU R 377 REMARK 465 VAL R 378 REMARK 465 VAL R 379 REMARK 465 ASP R 380 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 ILE A 55 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 VAL A 233 REMARK 465 LEU A 234 REMARK 465 ALA A 235 REMARK 465 GLU A 236 REMARK 465 ASP A 237 REMARK 465 GLU A 238 REMARK 465 GLU A 239 REMARK 465 ILE B 33 REMARK 465 THR B 34 REMARK 465 ASN B 35 REMARK 465 ASN B 36 REMARK 465 ILE B 37 REMARK 465 ASP B 38 REMARK 465 PRO B 39 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 465 ASP S 1 REMARK 465 GLY S 121A REMARK 465 GLY S 121B REMARK 465 GLY S 121C REMARK 465 GLY S 121D REMARK 465 SER S 121E REMARK 465 GLY S 121F REMARK 465 GLY S 121G REMARK 465 GLY S 121H REMARK 465 GLY S 121I REMARK 465 SER S 121J REMARK 465 GLY S 121K REMARK 465 GLY S 121L REMARK 465 GLY S 121M REMARK 465 GLY S 121N REMARK 465 LYS S 236 REMARK 465 GLY S 237 REMARK 465 SER S 238 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 O ASP R 23 N LYS R 25 1.23 REMARK 500 C ASP R 23 N LYS R 25 2.12 REMARK 500 O ASP R 23 CA LYS R 25 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PHE R 67 CB PHE R 67 CG -0.108 REMARK 500 GLU A 275 CD GLU A 275 OE1 -0.075 REMARK 500 CYS B 114 CB CYS B 114 SG -0.122 REMARK 500 TYR B 145 CZ TYR B 145 CE2 -0.080 REMARK 500 PHE B 199 CB PHE B 199 CG -0.129 REMARK 500 PHE B 241 CB PHE B 241 CG -0.130 REMARK 500 GLU B 260 CD GLU B 260 OE2 -0.066 REMARK 500 CYS B 271 CB CYS B 271 SG -0.124 REMARK 500 CYS S 96 CB CYS S 96 SG -0.138 REMARK 500 CYS S 217 CB CYS S 217 SG -0.108 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG R 62 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG R 62 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES REMARK 500 ARG R 127 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG R 233 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 ARG R 245 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ARG B 19 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 TYR B 105 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES REMARK 500 ARG B 137 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 PHE B 199 CB - CA - C ANGL. DEV. = -14.3 DEGREES REMARK 500 PHE B 241 CB - CA - C ANGL. DEV. = -14.9 DEGREES REMARK 500 PHE B 241 CB - CG - CD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 ASP B 258 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES REMARK 500 ARG G 27 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES REMARK 500 ARG S 72 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES REMARK 500 TYR S 103 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 PRO S 107 C - N - CA ANGL. DEV. = 9.4 DEGREES REMARK 500 ARG S 190 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES 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 GLU R 20 -162.42 71.24 REMARK 500 TRP R 24 1.60 4.24 REMARK 500 LYS R 25 -55.38 67.78 REMARK 500 ALA R 64 -22.88 -148.04 REMARK 500 PHE R 97 -44.00 81.30 REMARK 500 TYR R 185 -33.46 64.08 REMARK 500 PHE R 210 -53.67 -130.46 REMARK 500 ILE R 237 -66.63 -133.28 REMARK 500 THR A 4 -11.39 73.11 REMARK 500 SER A 44 -155.01 -117.75 REMARK 500 ALA A 203 -41.04 73.84 REMARK 500 TRP A 211 -15.55 -146.25 REMARK 500 THR B 164 -1.61 81.08 REMARK 500 THR B 196 -2.85 69.32 REMARK 500 SER S 21 -56.26 62.77 REMARK 500 CYS S 22 85.27 39.68 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38797 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE CMF-019-BOUND HUMAN APLNR-GI COMPLEX REMARK 900 RELATED ID: EMD-38971 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-38972 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-38973 RELATED DB: EMDB DBREF 8XZI R 1 380 UNP P35414 APJ_HUMAN 1 380 DBREF 8XZI A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 8XZI B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8XZI G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8XZI S 1 238 PDB 8XZI 8XZI 1 238 SEQADV 8XZI ASN A 47 UNP P63096 SER 47 CONFLICT SEQADV 8XZI ALA A 203 UNP P63096 GLY 203 CONFLICT SEQADV 8XZI ALA A 245 UNP P63096 GLU 245 CONFLICT SEQADV 8XZI SER A 326 UNP P63096 ALA 326 CONFLICT SEQRES 1 R 380 MET GLU GLU GLY GLY ASP PHE ASP ASN TYR TYR GLY ALA SEQRES 2 R 380 ASP ASN GLN SER GLU CYS GLU TYR THR ASP TRP LYS SER SEQRES 3 R 380 SER GLY ALA LEU ILE PRO ALA ILE TYR MET LEU VAL PHE SEQRES 4 R 380 LEU LEU GLY THR THR GLY ASN GLY LEU VAL LEU TRP THR SEQRES 5 R 380 VAL PHE ARG SER SER ARG GLU LYS ARG ARG SER ALA ASP SEQRES 6 R 380 ILE PHE ILE ALA SER LEU ALA VAL ALA ASP LEU THR PHE SEQRES 7 R 380 VAL VAL THR LEU PRO LEU TRP ALA THR TYR THR TYR ARG SEQRES 8 R 380 ASP TYR ASP TRP PRO PHE GLY THR PHE PHE CYS LYS LEU SEQRES 9 R 380 SER SER TYR LEU ILE PHE VAL ASN MET TYR ALA SER VAL SEQRES 10 R 380 PHE CYS LEU THR GLY LEU SER PHE ASP ARG TYR LEU ALA SEQRES 11 R 380 ILE VAL ARG PRO VAL ALA ASN ALA ARG LEU ARG LEU ARG SEQRES 12 R 380 VAL SER GLY ALA VAL ALA THR ALA VAL LEU TRP VAL LEU SEQRES 13 R 380 ALA ALA LEU LEU ALA MET PRO VAL MET VAL LEU ARG THR SEQRES 14 R 380 THR GLY ASP LEU GLU ASN THR THR LYS VAL GLN CYS TYR SEQRES 15 R 380 MET ASP TYR SER MET VAL ALA THR VAL SER SER GLU TRP SEQRES 16 R 380 ALA TRP GLU VAL GLY LEU GLY VAL SER SER THR THR VAL SEQRES 17 R 380 GLY PHE VAL VAL PRO PHE THR ILE MET LEU THR CYS TYR SEQRES 18 R 380 PHE PHE ILE ALA GLN THR ILE ALA GLY HIS PHE ARG LYS SEQRES 19 R 380 GLU ARG ILE GLU GLY LEU ARG LYS ARG ARG ARG LEU LEU SEQRES 20 R 380 SER ILE ILE VAL VAL LEU VAL VAL THR PHE ALA LEU CYS SEQRES 21 R 380 TRP MET PRO TYR HIS LEU VAL LYS THR LEU TYR MET LEU SEQRES 22 R 380 GLY SER LEU LEU HIS TRP PRO CYS ASP PHE ASP LEU PHE SEQRES 23 R 380 LEU MET ASN ILE PHE PRO TYR CYS THR CYS ILE SER TYR SEQRES 24 R 380 VAL ASN SER CYS LEU ASN PRO PHE LEU TYR ALA PHE PHE SEQRES 25 R 380 ASP PRO ARG PHE ARG GLN ALA CYS THR SER MET LEU CYS SEQRES 26 R 380 CYS GLY GLN SER ARG CYS ALA GLY THR SER HIS SER SER SEQRES 27 R 380 SER GLY GLU LYS SER ALA SER TYR SER SER GLY HIS SER SEQRES 28 R 380 GLN GLY PRO GLY PRO ASN MET GLY LYS GLY GLY GLU GLN SEQRES 29 R 380 MET HIS GLU LYS SER ILE PRO TYR SER GLN GLU THR LEU SEQRES 30 R 380 VAL VAL ASP SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS ASN THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS ALA SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 SER THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 B 339 SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU SEQRES 2 B 339 LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP SEQRES 3 B 339 ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL SEQRES 4 B 339 GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY SEQRES 5 B 339 HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SEQRES 6 B 339 SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU SEQRES 7 B 339 ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA SEQRES 8 B 339 ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR SEQRES 9 B 339 ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP SEQRES 10 B 339 ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY SEQRES 11 B 339 ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY SEQRES 12 B 339 TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE SEQRES 13 B 339 VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP SEQRES 14 B 339 ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS SEQRES 15 B 339 THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR SEQRES 16 B 339 ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS SEQRES 17 B 339 LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE SEQRES 18 B 339 THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE SEQRES 19 B 339 PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA SEQRES 20 B 339 THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU SEQRES 21 B 339 MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SEQRES 22 B 339 SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA SEQRES 23 B 339 GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU SEQRES 24 B 339 LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN SEQRES 25 B 339 ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA SEQRES 26 B 339 VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP SEQRES 27 B 339 ASN SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 S 250 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 250 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 250 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 250 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 250 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 250 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 250 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 250 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 250 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 250 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 250 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 250 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 250 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 250 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 250 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 250 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 250 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 250 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 250 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 S 250 LYS GLY SER HET D5N R 401 64 FORMUL 6 D5N HELIX 1 AA1 SER R 26 SER R 56 1 31 HELIX 2 AA2 ALA R 64 THR R 81 1 18 HELIX 3 AA3 THR R 81 ARG R 91 1 11 HELIX 4 AA4 GLY R 98 VAL R 132 1 35 HELIX 5 AA5 ASN R 137 SER R 145 1 9 HELIX 6 AA6 GLY R 146 ALA R 161 1 16 HELIX 7 AA7 ALA R 161 LEU R 167 1 7 HELIX 8 AA8 VAL R 191 SER R 193 5 3 HELIX 9 AA9 GLU R 194 PHE R 210 1 17 HELIX 10 AB1 PHE R 210 PHE R 232 1 23 HELIX 11 AB2 ILE R 237 LEU R 277 1 41 HELIX 12 AB3 PRO R 280 TYR R 299 1 20 HELIX 13 AB4 TYR R 299 ALA R 310 1 12 HELIX 14 AB5 ASP R 313 CYS R 325 1 13 HELIX 15 AB6 SER A 6 ALA A 31 1 26 HELIX 16 AB7 GLY A 45 LYS A 54 1 10 HELIX 17 AB8 GLU A 207 GLU A 216 5 10 HELIX 18 AB9 SER A 228 LEU A 232 5 5 HELIX 19 AC1 ASN A 241 ASN A 255 1 15 HELIX 20 AC2 ASN A 256 THR A 260 5 5 HELIX 21 AC3 LYS A 270 LYS A 279 1 10 HELIX 22 AC4 PRO A 282 CYS A 286 5 5 HELIX 23 AC5 THR A 295 ASP A 309 1 15 HELIX 24 AC6 LYS A 330 CYS A 351 1 22 HELIX 25 AC7 GLU B 3 ALA B 24 1 22 HELIX 26 AC8 THR G 6 ASN G 24 1 19 HELIX 27 AC9 LYS G 29 HIS G 44 1 16 HELIX 28 AD1 ALA G 45 ASP G 48 5 4 HELIX 29 AD2 PRO G 55 ASN G 59 5 5 HELIX 30 AD3 ALA S 28 PHE S 32 5 5 HELIX 31 AD4 SER S 53 GLY S 56 5 4 HELIX 32 AD5 ASP S 74 ASN S 77 5 4 HELIX 33 AD6 ARG S 87 THR S 91 5 5 HELIX 34 AD7 GLU S 208 VAL S 212 5 5 SHEET 1 AA1 2 ARG R 168 GLY R 171 0 SHEET 2 AA1 2 GLN R 180 MET R 183 -1 O TYR R 182 N THR R 169 SHEET 1 AA2 6 VAL A 185 PHE A 191 0 SHEET 2 AA2 6 LEU A 194 ASP A 200 -1 O ASP A 200 N VAL A 185 SHEET 3 AA2 6 VAL A 34 GLY A 40 1 N LEU A 38 O PHE A 199 SHEET 4 AA2 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 37 SHEET 5 AA2 6 SER A 263 ASN A 269 1 O ILE A 265 N ILE A 221 SHEET 6 AA2 6 ILE A 319 PHE A 323 1 O TYR A 320 N LEU A 266 SHEET 1 AA3 4 ARG B 46 LEU B 51 0 SHEET 2 AA3 4 LEU B 336 ASN B 340 -1 O ILE B 338 N ARG B 48 SHEET 3 AA3 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA3 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA4 4 ILE B 58 TRP B 63 0 SHEET 2 AA4 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AA4 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA4 4 LYS B 89 PRO B 94 -1 O VAL B 90 N ILE B 81 SHEET 1 AA5 4 VAL B 100 TYR B 105 0 SHEET 2 AA5 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 SHEET 3 AA5 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA5 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA6 4 LEU B 146 ASP B 153 0 SHEET 2 AA6 4 GLN B 156 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA6 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA6 4 GLN B 175 PHE B 180 -1 O THR B 177 N LEU B 168 SHEET 1 AA7 4 VAL B 187 LEU B 192 0 SHEET 2 AA7 4 LEU B 198 ALA B 203 -1 O VAL B 200 N SER B 191 SHEET 3 AA7 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA7 4 CYS B 218 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA8 4 ILE B 229 PHE B 234 0 SHEET 2 AA8 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA8 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA8 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA9 4 ILE B 273 PHE B 278 0 SHEET 2 AA9 4 LEU B 284 TYR B 289 -1 O LEU B 286 N SER B 277 SHEET 3 AA9 4 ASN B 293 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA9 4 ARG B 304 ALA B 309 -1 O ALA B 305 N VAL B 296 SHEET 1 AB1 2 GLN S 3 VAL S 5 0 SHEET 2 AB1 2 SER S 23 SER S 25 -1 O SER S 25 N GLN S 3 SHEET 1 AB2 6 GLY S 10 VAL S 12 0 SHEET 2 AB2 6 THR S 115 VAL S 119 1 O THR S 116 N GLY S 10 SHEET 3 AB2 6 ALA S 92 SER S 99 -1 N TYR S 94 O THR S 115 SHEET 4 AB2 6 GLY S 33 GLN S 39 -1 N VAL S 37 O TYR S 95 SHEET 5 AB2 6 LEU S 45 ILE S 51 -1 O GLU S 46 N ARG S 38 SHEET 6 AB2 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB3 4 GLY S 10 VAL S 12 0 SHEET 2 AB3 4 THR S 115 VAL S 119 1 O THR S 116 N GLY S 10 SHEET 3 AB3 4 ALA S 92 SER S 99 -1 N TYR S 94 O THR S 115 SHEET 4 AB3 4 PHE S 110 TRP S 111 -1 O PHE S 110 N ARG S 98 SHEET 1 AB4 3 ARG S 18 LYS S 19 0 SHEET 2 AB4 3 THR S 78 MET S 83 -1 O MET S 83 N ARG S 18 SHEET 3 AB4 3 PHE S 68 ASP S 73 -1 N THR S 69 O GLN S 82 SHEET 1 AB5 4 MET S 128 THR S 129 0 SHEET 2 AB5 4 VAL S 143 SER S 149 -1 O ARG S 148 N THR S 129 SHEET 3 AB5 4 ALA S 199 ILE S 204 -1 O PHE S 200 N CYS S 147 SHEET 4 AB5 4 PHE S 191 GLY S 195 -1 N SER S 192 O THR S 203 SHEET 1 AB6 6 SER S 134 PRO S 136 0 SHEET 2 AB6 6 THR S 231 GLU S 234 1 O LYS S 232 N VAL S 135 SHEET 3 AB6 6 VAL S 214 GLN S 219 -1 N TYR S 215 O THR S 231 SHEET 4 AB6 6 LEU S 162 GLN S 167 -1 N TYR S 163 O MET S 218 SHEET 5 AB6 6 GLN S 174 ARG S 179 -1 O LEU S 176 N TRP S 164 SHEET 6 AB6 6 ASN S 182 LEU S 183 -1 O ASN S 182 N TYR S 178 SHEET 1 AB7 4 SER S 134 PRO S 136 0 SHEET 2 AB7 4 THR S 231 GLU S 234 1 O LYS S 232 N VAL S 135 SHEET 3 AB7 4 VAL S 214 GLN S 219 -1 N TYR S 215 O THR S 231 SHEET 4 AB7 4 THR S 226 PHE S 227 -1 O THR S 226 N GLN S 219 SSBOND 1 CYS R 19 CYS R 281 1555 1555 2.08 SSBOND 2 CYS R 102 CYS R 181 1555 1555 2.12 SSBOND 3 CYS S 22 CYS S 96 1555 1555 2.03 SSBOND 4 CYS S 147 CYS S 217 1555 1555 2.03 CISPEP 1 TYR S 223 PRO S 224 0 0.65 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