HEADER MEMBRANE PROTEIN 10-JUN-22 7Y3G TITLE CRYO-EM STRUCTURE OF A CLASS A ORPHAN GPCR COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 10 BETA-1; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 16 GAMMA-2; COMPND 17 CHAIN: G; COMPND 18 SYNONYM: G GAMMA-I; COMPND 19 ENGINEERED: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: NANOBODY 35; COMPND 22 CHAIN: N; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: G-PROTEIN COUPLED RECEPTOR 12; COMPND 26 CHAIN: R; COMPND 27 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: GNAS, GNAS1, GSP; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 24 ORGANISM_TAXID: 9844; SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: GPR12; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS ORPHAN G PROTEIN COUPLED-RECEPTOR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Z.J.LIU,T.HUA,H.LI,J.Y.ZHANG,F.LUO REVDAT 1 07-JUN-23 7Y3G 0 JRNL AUTH H.LI,J.ZHANG,Y.YU,F.LUO,L.WU,J.LIU,N.CHEN,Z.LIU,T.HUA JRNL TITL STRUCTURAL INSIGHT INTO THE CONSTITUTIVE ACTIVITY OF HUMAN JRNL TITL 2 ORPHAN RECEPTOR GPR12. JRNL REF SCI BULL (BEIJING) V. 68 95 2023 JRNL REFN ESSN 2095-9281 JRNL PMID 36593162 JRNL DOI 10.1016/J.SCIB.2022.12.023 REMARK 2 REMARK 2 RESOLUTION. 2.77 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : EPU, CRYOSPARC, COOT, COOT, PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6KPG 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) : 2.770 REMARK 3 NUMBER OF PARTICLES : 75313 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 7Y3G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-22. REMARK 100 THE DEPOSITION ID IS D_1300030141. 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 : COMPLEX OF GPCR AND G PROTEIN; REMARK 245 ISOFORM GNAS-2 OF GUANINE REMARK 245 NUCLEOTIDE-BINDING PROTEIN G(S) REMARK 245 SUBUNIT ALPHA ISOFORMS SHORT; REMARK 245 GUANINE NUCLEOTIDE-BINDING REMARK 245 PROTEIN G(I)/G(S)/G(T) SUBUNIT REMARK 245 BETA-1; GUANINE NUCLEOTIDE- REMARK 245 BINDING PROTEIN G(I)/G(S)/G(O) REMARK 245 SUBUNIT GAMMA-2; NANOBODY 35; G- REMARK 245 PROTEIN COUPLED RECEPTOR 12 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 : 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 : 10156 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) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 165000 REMARK 245 CALIBRATED MAGNIFICATION : 165000 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: A, B, G, N, R 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 1 REMARK 465 GLY A 2 REMARK 465 CYS A 3 REMARK 465 LEU A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 LYS A 8 REMARK 465 THR A 9 REMARK 465 GLU A 10 REMARK 465 ALA A 48 REMARK 465 GLY A 49 REMARK 465 GLU A 50 REMARK 465 SER A 51 REMARK 465 MET A 60 REMARK 465 ARG A 61 REMARK 465 ILE A 62 REMARK 465 LEU A 63 REMARK 465 HIS A 64 REMARK 465 VAL A 65 REMARK 465 ASN A 66 REMARK 465 GLY A 67 REMARK 465 PHE A 68 REMARK 465 ASN A 69 REMARK 465 GLY A 70 REMARK 465 GLU A 71 REMARK 465 GLY A 72 REMARK 465 GLY A 73 REMARK 465 GLU A 74 REMARK 465 GLU A 75 REMARK 465 ASP A 76 REMARK 465 PRO A 77 REMARK 465 GLN A 78 REMARK 465 ALA A 79 REMARK 465 ALA A 80 REMARK 465 ARG A 81 REMARK 465 SER A 82 REMARK 465 ASN A 83 REMARK 465 SER A 84 REMARK 465 ASP A 85 REMARK 465 GLY A 86 REMARK 465 GLU A 87 REMARK 465 LYS A 88 REMARK 465 ALA A 89 REMARK 465 THR A 90 REMARK 465 LYS A 91 REMARK 465 VAL A 92 REMARK 465 GLN A 93 REMARK 465 ASP A 94 REMARK 465 ILE A 95 REMARK 465 LYS A 96 REMARK 465 ASN A 97 REMARK 465 ASN A 98 REMARK 465 LEU A 99 REMARK 465 LYS A 100 REMARK 465 GLU A 101 REMARK 465 ALA A 102 REMARK 465 ILE A 103 REMARK 465 GLU A 104 REMARK 465 THR A 105 REMARK 465 ILE A 106 REMARK 465 VAL A 107 REMARK 465 ALA A 108 REMARK 465 ALA A 109 REMARK 465 MET A 110 REMARK 465 SER A 111 REMARK 465 ASN A 112 REMARK 465 LEU A 113 REMARK 465 VAL A 114 REMARK 465 PRO A 115 REMARK 465 PRO A 116 REMARK 465 VAL A 117 REMARK 465 GLU A 118 REMARK 465 LEU A 119 REMARK 465 ALA A 120 REMARK 465 ASN A 121 REMARK 465 PRO A 122 REMARK 465 GLU A 123 REMARK 465 ASN A 124 REMARK 465 GLN A 125 REMARK 465 PHE A 126 REMARK 465 ARG A 127 REMARK 465 VAL A 128 REMARK 465 ASP A 129 REMARK 465 TYR A 130 REMARK 465 ILE A 131 REMARK 465 LEU A 132 REMARK 465 SER A 133 REMARK 465 VAL A 134 REMARK 465 MET A 135 REMARK 465 ASN A 136 REMARK 465 VAL A 137 REMARK 465 PRO A 138 REMARK 465 ASP A 139 REMARK 465 PHE A 140 REMARK 465 ASP A 141 REMARK 465 PHE A 142 REMARK 465 PRO A 143 REMARK 465 PRO A 144 REMARK 465 GLU A 145 REMARK 465 PHE A 146 REMARK 465 TYR A 147 REMARK 465 GLU A 148 REMARK 465 HIS A 149 REMARK 465 ALA A 150 REMARK 465 LYS A 151 REMARK 465 ALA A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 GLU A 155 REMARK 465 ASP A 156 REMARK 465 GLU A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 ARG A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 TYR A 163 REMARK 465 GLU A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ASN A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ILE A 172 REMARK 465 ASP A 173 REMARK 465 CYS A 174 REMARK 465 ALA A 175 REMARK 465 GLN A 176 REMARK 465 TYR A 177 REMARK 465 PHE A 178 REMARK 465 LEU A 179 REMARK 465 ASP A 180 REMARK 465 LYS A 181 REMARK 465 ILE A 182 REMARK 465 ASP A 183 REMARK 465 VAL A 184 REMARK 465 ILE A 185 REMARK 465 LYS A 186 REMARK 465 GLN A 187 REMARK 465 ALA A 188 REMARK 465 ASP A 189 REMARK 465 TYR A 190 REMARK 465 VAL A 191 REMARK 465 PRO A 192 REMARK 465 SER A 193 REMARK 465 ASP A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 LEU A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 CYS A 200 REMARK 465 ARG A 201 REMARK 465 VAL A 202 REMARK 465 LEU A 203 REMARK 465 THR A 204 REMARK 465 SER A 252 REMARK 465 TYR A 253 REMARK 465 ASN A 254 REMARK 465 MET A 255 REMARK 465 VAL A 256 REMARK 465 ILE A 257 REMARK 465 ARG A 258 REMARK 465 GLU A 259 REMARK 465 ASP A 260 REMARK 465 ASN A 261 REMARK 465 GLN A 262 REMARK 465 THR A 263 REMARK 465 LYS A 305 REMARK 465 SER A 306 REMARK 465 GLU A 330 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 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 MET N -22 REMARK 465 LYS N -21 REMARK 465 TYR N -20 REMARK 465 LEU N -19 REMARK 465 LEU N -18 REMARK 465 PRO N -17 REMARK 465 THR N -16 REMARK 465 ALA N -15 REMARK 465 ALA N -14 REMARK 465 ALA N -13 REMARK 465 GLY N -12 REMARK 465 LEU N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 ALA N -7 REMARK 465 ALA N -6 REMARK 465 GLN N -5 REMARK 465 PRO N -4 REMARK 465 ALA N -3 REMARK 465 MET N -2 REMARK 465 ALA N -1 REMARK 465 MET N 0 REMARK 465 SER N 127 REMARK 465 SER N 128 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 HIS N 131 REMARK 465 HIS N 132 REMARK 465 HIS N 133 REMARK 465 HIS N 134 REMARK 465 MET R -43 REMARK 465 LYS R -42 REMARK 465 THR R -41 REMARK 465 ILE R -40 REMARK 465 ILE R -39 REMARK 465 ALA R -38 REMARK 465 LEU R -37 REMARK 465 SER R -36 REMARK 465 TYR R -35 REMARK 465 ILE R -34 REMARK 465 PHE R -33 REMARK 465 CYS R -32 REMARK 465 LEU R -31 REMARK 465 VAL R -30 REMARK 465 PHE R -29 REMARK 465 ALA R -28 REMARK 465 HIS R -27 REMARK 465 HIS R -26 REMARK 465 HIS R -25 REMARK 465 HIS R -24 REMARK 465 HIS R -23 REMARK 465 HIS R -22 REMARK 465 HIS R -21 REMARK 465 HIS R -20 REMARK 465 HIS R -19 REMARK 465 HIS R -18 REMARK 465 ASP R -17 REMARK 465 TYR R -16 REMARK 465 LYS R -15 REMARK 465 ASP R -14 REMARK 465 ASP R -13 REMARK 465 ASP R -12 REMARK 465 ASP R -11 REMARK 465 LYS R -10 REMARK 465 GLU R -9 REMARK 465 ASN R -8 REMARK 465 LEU R -7 REMARK 465 TYR R -6 REMARK 465 PHE R -5 REMARK 465 GLN R -4 REMARK 465 SER R -3 REMARK 465 GLY R -2 REMARK 465 ALA R -1 REMARK 465 PRO R 0 REMARK 465 MET R 1 REMARK 465 ASN R 2 REMARK 465 GLU R 3 REMARK 465 ASP R 4 REMARK 465 LEU R 5 REMARK 465 LYS R 6 REMARK 465 VAL R 7 REMARK 465 ASN R 8 REMARK 465 LEU R 9 REMARK 465 SER R 10 REMARK 465 GLY R 11 REMARK 465 LEU R 12 REMARK 465 PRO R 13 REMARK 465 ARG R 14 REMARK 465 ASP R 15 REMARK 465 TYR R 16 REMARK 465 LEU R 17 REMARK 465 ASP R 18 REMARK 465 ALA R 19 REMARK 465 ALA R 20 REMARK 465 ALA R 21 REMARK 465 ALA R 22 REMARK 465 GLU R 23 REMARK 465 ASN R 24 REMARK 465 ILE R 25 REMARK 465 SER R 26 REMARK 465 ALA R 27 REMARK 465 ALA R 28 REMARK 465 VAL R 29 REMARK 465 SER R 30 REMARK 465 SER R 31 REMARK 465 ARG R 32 REMARK 465 VAL R 33 REMARK 465 PRO R 34 REMARK 465 ALA R 35 REMARK 465 VAL R 36 REMARK 465 GLU R 37 REMARK 465 PRO R 38 REMARK 465 GLU R 39 REMARK 465 PRO R 40 REMARK 465 GLU R 41 REMARK 465 LEU R 42 REMARK 465 VAL R 43 REMARK 465 LEU R 238 REMARK 465 ALA R 239 REMARK 465 THR R 240 REMARK 465 SER R 241 REMARK 465 HIS R 242 REMARK 465 TYR R 243 REMARK 465 VAL R 244 REMARK 465 THR R 245 REMARK 465 LEU R 312 REMARK 465 CYS R 313 REMARK 465 LEU R 314 REMARK 465 ILE R 315 REMARK 465 CYS R 316 REMARK 465 CYS R 317 REMARK 465 GLY R 318 REMARK 465 CYS R 319 REMARK 465 ILE R 320 REMARK 465 PRO R 321 REMARK 465 SER R 322 REMARK 465 SER R 323 REMARK 465 LEU R 324 REMARK 465 ALA R 325 REMARK 465 GLN R 326 REMARK 465 ARG R 327 REMARK 465 ALA R 328 REMARK 465 ARG R 329 REMARK 465 SER R 330 REMARK 465 PRO R 331 REMARK 465 SER R 332 REMARK 465 ASP R 333 REMARK 465 VAL R 334 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 OG SER B 331 OD1 ASP B 333 2.03 REMARK 500 OG SER B 161 OD1 ASP B 163 2.05 REMARK 500 OD1 ASN R 198 OG SER R 271 2.15 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 LYS A 58 35.28 -83.52 REMARK 500 LEU A 302 51.44 -93.40 REMARK 500 ALA A 337 -20.84 74.24 REMARK 500 ASP A 354 -168.55 -77.29 REMARK 500 ASP B 205 21.78 -144.54 REMARK 500 ASN G 24 79.60 -106.75 REMARK 500 SER R 109 11.08 56.61 REMARK 500 VAL R 190 -65.90 -106.55 REMARK 500 VAL R 191 -65.80 -133.73 REMARK 500 ILE R 273 -57.61 -121.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-33594 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF A CLASS A ORPHAN GPCR DBREF 7Y3G A 1 394 UNP P63092 GNAS2_HUMAN 1 394 DBREF 7Y3G B 1 340 UNP P62873 GBB1_HUMAN 1 340 DBREF 7Y3G G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 7Y3G N -22 134 PDB 7Y3G 7Y3G -22 134 DBREF 7Y3G R 1 334 UNP P47775 GPR12_HUMAN 1 334 SEQADV 7Y3G ASN A 54 UNP P63092 SER 54 ENGINEERED MUTATION SEQADV 7Y3G ALA A 226 UNP P63092 GLY 226 ENGINEERED MUTATION SEQADV 7Y3G ALA A 268 UNP P63092 GLU 268 ENGINEERED MUTATION SEQADV 7Y3G LYS A 271 UNP P63092 ASN 271 ENGINEERED MUTATION SEQADV 7Y3G ASP A 274 UNP P63092 LYS 274 ENGINEERED MUTATION SEQADV 7Y3G LYS A 280 UNP P63092 ARG 280 ENGINEERED MUTATION SEQADV 7Y3G ASP A 284 UNP P63092 THR 284 ENGINEERED MUTATION SEQADV 7Y3G THR A 285 UNP P63092 ILE 285 ENGINEERED MUTATION SEQADV 7Y3G MET R -43 UNP P47775 INITIATING METHIONINE SEQADV 7Y3G LYS R -42 UNP P47775 EXPRESSION TAG SEQADV 7Y3G THR R -41 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ILE R -40 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ILE R -39 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ALA R -38 UNP P47775 EXPRESSION TAG SEQADV 7Y3G LEU R -37 UNP P47775 EXPRESSION TAG SEQADV 7Y3G SER R -36 UNP P47775 EXPRESSION TAG SEQADV 7Y3G TYR R -35 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ILE R -34 UNP P47775 EXPRESSION TAG SEQADV 7Y3G PHE R -33 UNP P47775 EXPRESSION TAG SEQADV 7Y3G CYS R -32 UNP P47775 EXPRESSION TAG SEQADV 7Y3G LEU R -31 UNP P47775 EXPRESSION TAG SEQADV 7Y3G VAL R -30 UNP P47775 EXPRESSION TAG SEQADV 7Y3G PHE R -29 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ALA R -28 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -27 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -26 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -25 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -24 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -23 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -22 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -21 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -20 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -19 UNP P47775 EXPRESSION TAG SEQADV 7Y3G HIS R -18 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ASP R -17 UNP P47775 EXPRESSION TAG SEQADV 7Y3G TYR R -16 UNP P47775 EXPRESSION TAG SEQADV 7Y3G LYS R -15 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ASP R -14 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ASP R -13 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ASP R -12 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ASP R -11 UNP P47775 EXPRESSION TAG SEQADV 7Y3G LYS R -10 UNP P47775 EXPRESSION TAG SEQADV 7Y3G GLU R -9 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ASN R -8 UNP P47775 EXPRESSION TAG SEQADV 7Y3G LEU R -7 UNP P47775 EXPRESSION TAG SEQADV 7Y3G TYR R -6 UNP P47775 EXPRESSION TAG SEQADV 7Y3G PHE R -5 UNP P47775 EXPRESSION TAG SEQADV 7Y3G GLN R -4 UNP P47775 EXPRESSION TAG SEQADV 7Y3G SER R -3 UNP P47775 EXPRESSION TAG SEQADV 7Y3G GLY R -2 UNP P47775 EXPRESSION TAG SEQADV 7Y3G ALA R -1 UNP P47775 EXPRESSION TAG SEQADV 7Y3G PRO R 0 UNP P47775 EXPRESSION TAG SEQRES 1 A 394 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2 A 394 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3 A 394 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4 A 394 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5 A 394 LYS ASN THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6 A 394 ASN GLY PHE ASN GLY GLU GLY GLY GLU GLU ASP PRO GLN SEQRES 7 A 394 ALA ALA ARG SER ASN SER ASP GLY GLU LYS ALA THR LYS SEQRES 8 A 394 VAL GLN ASP ILE LYS ASN ASN LEU LYS GLU ALA ILE GLU SEQRES 9 A 394 THR ILE VAL ALA ALA MET SER ASN LEU VAL PRO PRO VAL SEQRES 10 A 394 GLU LEU ALA ASN PRO GLU ASN GLN PHE ARG VAL ASP TYR SEQRES 11 A 394 ILE LEU SER VAL MET ASN VAL PRO ASP PHE ASP PHE PRO SEQRES 12 A 394 PRO GLU PHE TYR GLU HIS ALA LYS ALA LEU TRP GLU ASP SEQRES 13 A 394 GLU GLY VAL ARG ALA CYS TYR GLU ARG SER ASN GLU TYR SEQRES 14 A 394 GLN LEU ILE ASP CYS ALA GLN TYR PHE LEU ASP LYS ILE SEQRES 15 A 394 ASP VAL ILE LYS GLN ALA ASP TYR VAL PRO SER ASP GLN SEQRES 16 A 394 ASP LEU LEU ARG CYS ARG VAL LEU THR SER GLY ILE PHE SEQRES 17 A 394 GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS MET SEQRES 18 A 394 PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG ARG LYS TRP SEQRES 19 A 394 ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE VAL SEQRES 20 A 394 VAL ALA SER SER SER TYR ASN MET VAL ILE ARG GLU ASP SEQRES 21 A 394 ASN GLN THR ASN ARG LEU GLN ALA ALA LEU LYS LEU PHE SEQRES 22 A 394 ASP SER ILE TRP ASN ASN LYS TRP LEU ARG ASP THR SER SEQRES 23 A 394 VAL ILE LEU PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU SEQRES 24 A 394 LYS VAL LEU ALA GLY LYS SER LYS ILE GLU ASP TYR PHE SEQRES 25 A 394 PRO GLU PHE ALA ARG TYR THR THR PRO GLU ASP ALA THR SEQRES 26 A 394 PRO GLU PRO GLY GLU ASP PRO ARG VAL THR ARG ALA LYS SEQRES 27 A 394 TYR PHE ILE ARG ASP GLU PHE LEU ARG ILE SER THR ALA SEQRES 28 A 394 SER GLY ASP GLY ARG HIS TYR CYS TYR PRO HIS PHE THR SEQRES 29 A 394 CYS ALA VAL ASP THR GLU ASN ILE ARG ARG VAL PHE ASN SEQRES 30 A 394 ASP CYS ARG ASP ILE ILE GLN ARG MET HIS LEU ARG GLN SEQRES 31 A 394 TYR GLU LEU LEU SEQRES 1 B 340 MET SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN SEQRES 2 B 340 LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA SEQRES 3 B 340 ASP ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO SEQRES 4 B 340 VAL GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG SEQRES 5 B 340 GLY HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR SEQRES 6 B 340 ASP SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS SEQRES 7 B 340 LEU ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS SEQRES 8 B 340 ALA ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA SEQRES 9 B 340 TYR ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU SEQRES 10 B 340 ASP ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU SEQRES 11 B 340 GLY ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR SEQRES 12 B 340 GLY TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN SEQRES 13 B 340 ILE VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP SEQRES 14 B 340 ASP ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY SEQRES 15 B 340 HIS THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP SEQRES 16 B 340 THR ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA SEQRES 17 B 340 LYS LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR SEQRES 18 B 340 PHE THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE SEQRES 19 B 340 PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP SEQRES 20 B 340 ALA THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU SEQRES 21 B 340 LEU MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE SEQRES 22 B 340 THR SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU SEQRES 23 B 340 ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA SEQRES 24 B 340 LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP SEQRES 25 B 340 ASN ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET SEQRES 26 B 340 ALA VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE SEQRES 27 B 340 TRP 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 N 157 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 N 157 LEU LEU ALA ALA GLN PRO ALA MET ALA MET GLN VAL GLN SEQRES 3 N 157 LEU GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SEQRES 4 N 157 SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SEQRES 5 N 157 SER ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY SEQRES 6 N 157 LYS GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY SEQRES 7 N 157 ALA SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE SEQRES 8 N 157 THR ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU SEQRES 9 N 157 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR SEQRES 10 N 157 TYR CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS SEQRES 11 N 157 PHE ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN SEQRES 12 N 157 GLY THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS SEQRES 13 N 157 HIS SEQRES 1 R 378 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 378 VAL PHE ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 3 R 378 ASP TYR LYS ASP ASP ASP ASP LYS GLU ASN LEU TYR PHE SEQRES 4 R 378 GLN SER GLY ALA PRO MET ASN GLU ASP LEU LYS VAL ASN SEQRES 5 R 378 LEU SER GLY LEU PRO ARG ASP TYR LEU ASP ALA ALA ALA SEQRES 6 R 378 ALA GLU ASN ILE SER ALA ALA VAL SER SER ARG VAL PRO SEQRES 7 R 378 ALA VAL GLU PRO GLU PRO GLU LEU VAL VAL ASN PRO TRP SEQRES 8 R 378 ASP ILE VAL LEU CYS THR SER GLY THR LEU ILE SER CYS SEQRES 9 R 378 GLU ASN ALA ILE VAL VAL LEU ILE ILE PHE HIS ASN PRO SEQRES 10 R 378 SER LEU ARG ALA PRO MET PHE LEU LEU ILE GLY SER LEU SEQRES 11 R 378 ALA LEU ALA ASP LEU LEU ALA GLY ILE GLY LEU ILE THR SEQRES 12 R 378 ASN PHE VAL PHE ALA TYR LEU LEU GLN SER GLU ALA THR SEQRES 13 R 378 LYS LEU VAL THR ILE GLY LEU ILE VAL ALA SER PHE SER SEQRES 14 R 378 ALA SER VAL CYS SER LEU LEU ALA ILE THR VAL ASP ARG SEQRES 15 R 378 TYR LEU SER LEU TYR TYR ALA LEU THR TYR HIS SER GLU SEQRES 16 R 378 ARG THR VAL THR PHE THR TYR VAL MET LEU VAL MET LEU SEQRES 17 R 378 TRP GLY THR SER ILE CYS LEU GLY LEU LEU PRO VAL MET SEQRES 18 R 378 GLY TRP ASN CYS LEU ARG ASP GLU SER THR CYS SER VAL SEQRES 19 R 378 VAL ARG PRO LEU THR LYS ASN ASN ALA ALA ILE LEU SER SEQRES 20 R 378 VAL SER PHE LEU PHE MET PHE ALA LEU MET LEU GLN LEU SEQRES 21 R 378 TYR ILE GLN ILE CYS LYS ILE VAL MET ARG HIS ALA HIS SEQRES 22 R 378 GLN ILE ALA LEU GLN HIS HIS PHE LEU ALA THR SER HIS SEQRES 23 R 378 TYR VAL THR THR ARG LYS GLY VAL SER THR LEU ALA ILE SEQRES 24 R 378 ILE LEU GLY THR PHE ALA ALA CYS TRP MET PRO PHE THR SEQRES 25 R 378 LEU TYR SER LEU ILE ALA ASP TYR THR TYR PRO SER ILE SEQRES 26 R 378 TYR THR TYR ALA THR LEU LEU PRO ALA THR TYR ASN SER SEQRES 27 R 378 ILE ILE ASN PRO VAL ILE TYR ALA PHE ARG ASN GLN GLU SEQRES 28 R 378 ILE GLN LYS ALA LEU CYS LEU ILE CYS CYS GLY CYS ILE SEQRES 29 R 378 PRO SER SER LEU ALA GLN ARG ALA ARG SER PRO SER ASP SEQRES 30 R 378 VAL HELIX 1 AA1 ASP A 11 ARG A 38 1 28 HELIX 2 AA2 LYS A 53 LYS A 58 1 6 HELIX 3 AA3 TRP A 234 PHE A 238 5 5 HELIX 4 AA4 ARG A 265 ASN A 278 1 14 HELIX 5 AA5 ASN A 279 ARG A 283 5 5 HELIX 6 AA6 LYS A 293 LEU A 302 1 10 HELIX 7 AA7 GLU A 314 TYR A 318 5 5 HELIX 8 AA8 VAL A 334 THR A 350 1 17 HELIX 9 AA9 GLU A 370 TYR A 391 1 22 HELIX 10 AB1 LEU B 4 ALA B 24 1 21 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 ASN B 35 ILE B 37 5 3 HELIX 13 AB4 ALA G 7 ASN G 24 1 18 HELIX 14 AB5 LYS G 29 HIS G 44 1 16 HELIX 15 AB6 PRO G 55 ASN G 59 5 5 HELIX 16 AB7 THR N 28 TYR N 32 5 5 HELIX 17 AB8 GLY N 62 LYS N 65 5 4 HELIX 18 AB9 LYS N 87 THR N 91 5 5 HELIX 19 AC1 ASN R 45 ASN R 72 1 28 HELIX 20 AC2 ALA R 77 PHE R 103 1 27 HELIX 21 AC3 LYS R 113 TYR R 144 1 32 HELIX 22 AC4 ALA R 145 TYR R 148 5 4 HELIX 23 AC5 THR R 153 LEU R 174 1 22 HELIX 24 AC6 PRO R 175 MET R 177 5 3 HELIX 25 AC7 ASN R 180 ASP R 184 5 5 HELIX 26 AC8 LEU R 194 PHE R 206 1 13 HELIX 27 AC9 MET R 209 HIS R 236 1 28 HELIX 28 AD1 ARG R 247 CYS R 263 1 17 HELIX 29 AD2 TRP R 264 LEU R 272 1 9 HELIX 30 AD3 SER R 280 PHE R 303 1 24 HELIX 31 AD4 ASN R 305 ALA R 311 1 7 SHEET 1 AA1 6 ILE A 207 VAL A 214 0 SHEET 2 AA1 6 VAL A 217 VAL A 224 -1 O ASP A 223 N PHE A 208 SHEET 3 AA1 6 THR A 40 LEU A 46 1 N LEU A 43 O HIS A 220 SHEET 4 AA1 6 ALA A 243 VAL A 248 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 LEU A 291 1 O PHE A 290 N PHE A 246 SHEET 6 AA1 6 CYS A 359 PHE A 363 1 O HIS A 362 N LEU A 289 SHEET 1 AA2 4 ARG B 46 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 ASN B 340 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 HIS B 62 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O VAL B 71 N HIS B 62 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 ASN B 88 PRO B 94 -1 O VAL B 90 N ILE B 81 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA5 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 175 PHE B 180 -1 O THR B 177 N LEU B 168 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O GLY B 244 N ASN B 230 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLU B 260 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O GLY B 288 N THR B 274 SHEET 3 AA8 4 ASN B 293 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 ALA B 309 -1 O LEU B 308 N CYS B 294 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 SER N 17 SER N 25 -1 O ALA N 23 N GLN N 5 SHEET 3 AA9 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB1 5 ILE N 58 TYR N 60 0 SHEET 2 AB1 5 LEU N 45 ILE N 51 -1 N ASP N 50 O SER N 59 SHEET 3 AB1 5 MET N 34 GLN N 39 -1 N ARG N 38 O GLU N 46 SHEET 4 AB1 5 ALA N 92 ARG N 98 -1 O TYR N 95 N VAL N 37 SHEET 5 AB1 5 THR N 122 VAL N 124 -1 O VAL N 124 N ALA N 92 SSBOND 1 CYS R 181 CYS R 188 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