HEADER MEMBRANE PROTEIN 20-MAR-25 9U4W TITLE CRYO-EM STRUCTURE OF PIG GNRHR BOUND WITH MAMMAL GNRH COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 7 BETA-1; COMPND 8 CHAIN: B; COMPND 9 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GONADOLIBERIN-1; COMPND 13 CHAIN: F; COMPND 14 SYNONYM: GONADOLIBERIN I,GONADORELIN,GONADOTROPIN-RELEASING HORMONE COMPND 15 I,GNRH-I,LULIBERIN I,LUTEINIZING HORMONE-RELEASING HORMONE I,LH-RH I; 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: BETA-2 ADRENERGIC RECEPTOR,GONADOTROPIN-RELEASING HORMONE COMPND 25 RECEPTOR; COMPND 26 CHAIN: R; COMPND 27 SYNONYM: GNRH RECEPTOR,GNRH-R,LUTEINIZING HORMONE-RELEASING HORMONE COMPND 28 RECEPTOR,LHRH; COMPND 29 ENGINEERED: YES; COMPND 30 MOL_ID: 6; COMPND 31 MOLECULE: SCFV16; COMPND 32 CHAIN: S; COMPND 33 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 GENE: GNB1; SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 14 MOL_ID: 3; SOURCE 15 SYNTHETIC: YES; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 GENE: GNG2; SOURCE 24 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SUS SCROFA; SOURCE 28 ORGANISM_COMMON: HUMAN, PIG; SOURCE 29 ORGANISM_TAXID: 9606, 9823; SOURCE 30 GENE: ADRB2, ADRB2R, B2AR, GNRHR; SOURCE 31 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 33 MOL_ID: 6; SOURCE 34 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 35 ORGANISM_COMMON: HUMAN; SOURCE 36 ORGANISM_TAXID: 9606; SOURCE 37 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS CRYO-EM, GONADOTROPIN RELEASING HORMONE RECEPTOR, GNRHR, MEMBRANE KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.SHEN,H.E.XU REVDAT 1 11-JUN-25 9U4W 0 JRNL AUTH S.SHEN,H.E.XU JRNL TITL CRYO-EM STRUCTURES OF GNRHR: FOUNDATIONS FOR NEXT-GENERATION JRNL TITL 2 THERAPEUTICS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.18 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.180 REMARK 3 NUMBER OF PARTICLES : 118050 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9U4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 25-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1300057698. 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 PIG GNRHR REMARK 245 BOUND WITH MAMMAL GNRH 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 : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 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 : NULL REMARK 245 IMAGING MODE : DARK 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, G, R, 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 A 1 REMARK 465 GLY A 2 REMARK 465 SER A 3 REMARK 465 THR A 4 REMARK 465 VAL A 5 REMARK 465 GLN A 165 REMARK 465 MET A 166 REMARK 465 ARG A 167 REMARK 465 ILE A 168 REMARK 465 LEU A 169 REMARK 465 HIS A 170 REMARK 465 GLY A 171 REMARK 465 GLY A 172 REMARK 465 SER A 173 REMARK 465 GLY A 174 REMARK 465 GLY A 175 REMARK 465 SER A 176 REMARK 465 GLY A 177 REMARK 465 GLY A 178 REMARK 465 THR A 179 REMARK 465 SER A 180 REMARK 465 GLY A 181 REMARK 465 LEU A 267 REMARK 465 ALA A 268 REMARK 465 GLY A 269 REMARK 465 LYS A 270 REMARK 465 VAL A 359 REMARK 465 GLY B 2 REMARK 465 SER B 3 REMARK 465 LEU B 4 REMARK 465 LEU B 5 REMARK 465 GLN B 6 REMARK 465 SER B 7 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 R -85 REMARK 465 ASP R -84 REMARK 465 SER R -83 REMARK 465 LYS R -82 REMARK 465 GLY R -81 REMARK 465 SER R -80 REMARK 465 SER R -79 REMARK 465 GLN R -78 REMARK 465 LYS R -77 REMARK 465 GLY R -76 REMARK 465 SER R -75 REMARK 465 ARG R -74 REMARK 465 LEU R -73 REMARK 465 LEU R -72 REMARK 465 LEU R -71 REMARK 465 LEU R -70 REMARK 465 LEU R -69 REMARK 465 VAL R -68 REMARK 465 VAL R -67 REMARK 465 SER R -66 REMARK 465 ASN R -65 REMARK 465 LEU R -64 REMARK 465 LEU R -63 REMARK 465 LEU R -62 REMARK 465 CYS R -61 REMARK 465 GLN R -60 REMARK 465 GLY R -59 REMARK 465 VAL R -58 REMARK 465 VAL R -57 REMARK 465 SER R -56 REMARK 465 ASP R -55 REMARK 465 TYR R -54 REMARK 465 LYS R -53 REMARK 465 ASP R -52 REMARK 465 ASP R -51 REMARK 465 ASP R -50 REMARK 465 ASP R -49 REMARK 465 VAL R -48 REMARK 465 HIS R -47 REMARK 465 HIS R -46 REMARK 465 HIS R -45 REMARK 465 HIS R -44 REMARK 465 HIS R -43 REMARK 465 HIS R -42 REMARK 465 HIS R -41 REMARK 465 HIS R -40 REMARK 465 ASP R -39 REMARK 465 MET R -38 REMARK 465 GLY R -37 REMARK 465 GLN R -36 REMARK 465 PRO R -35 REMARK 465 GLY R -34 REMARK 465 ASN R -33 REMARK 465 GLY R -32 REMARK 465 SER R -31 REMARK 465 ALA R -30 REMARK 465 PHE R -29 REMARK 465 LEU R -28 REMARK 465 LEU R -27 REMARK 465 ALA R -26 REMARK 465 PRO R -25 REMARK 465 ASN R -24 REMARK 465 GLY R -23 REMARK 465 SER R -22 REMARK 465 HIS R -21 REMARK 465 ALA R -20 REMARK 465 PRO R -19 REMARK 465 ASP R -18 REMARK 465 HIS R -17 REMARK 465 ASP R -16 REMARK 465 VAL R -15 REMARK 465 THR R -14 REMARK 465 GLN R -13 REMARK 465 GLN R -12 REMARK 465 ARG R -11 REMARK 465 ASP R -10 REMARK 465 GLU R -9 REMARK 465 GLU R -8 REMARK 465 ASN R -7 REMARK 465 LEU R -6 REMARK 465 TYR R -5 REMARK 465 PHE R -4 REMARK 465 GLN R -3 REMARK 465 GLY R -2 REMARK 465 ALA R -1 REMARK 465 SER R 0 REMARK 465 MET R 1 REMARK 465 ALA R 2 REMARK 465 ASN R 3 REMARK 465 SER R 4 REMARK 465 ALA R 5 REMARK 465 SER R 6 REMARK 465 PRO R 7 REMARK 465 GLU R 8 REMARK 465 GLN R 9 REMARK 465 ASN R 10 REMARK 465 GLN R 11 REMARK 465 ASN R 12 REMARK 465 HIS R 13 REMARK 465 CYS R 14 REMARK 465 SER R 15 REMARK 465 ALA R 16 REMARK 465 ILE R 17 REMARK 465 ASN R 18 REMARK 465 SER R 19 REMARK 465 SER R 20 REMARK 465 ILE R 21 REMARK 465 LEU R 22 REMARK 465 LEU R 23 REMARK 465 THR R 24 REMARK 465 GLN R 25 REMARK 465 GLY R 26 REMARK 465 TRP R 63 REMARK 465 THR R 64 REMARK 465 GLN R 65 REMARK 465 ARG R 66 REMARK 465 LYS R 67 REMARK 465 GLU R 68 REMARK 465 LYS R 69 REMARK 465 GLY R 70 REMARK 465 LYS R 71 REMARK 465 LYS R 72 REMARK 465 LEU R 73 REMARK 465 ALA R 184 REMARK 465 ASP R 185 REMARK 465 SER R 186 REMARK 465 SER R 187 REMARK 465 GLY R 188 REMARK 465 GLN R 189 REMARK 465 THR R 190 REMARK 465 GLU R 191 REMARK 465 GLN R 244 REMARK 465 ASP R 245 REMARK 465 PRO R 246 REMARK 465 HIS R 247 REMARK 465 ASN R 248 REMARK 465 LEU R 249 REMARK 465 GLN R 250 REMARK 465 LEU R 251 REMARK 465 ASN R 252 REMARK 465 GLN R 253 REMARK 465 SER R 254 REMARK 465 LYS R 255 REMARK 465 MET S -37 REMARK 465 LEU S -36 REMARK 465 LEU S -35 REMARK 465 VAL S -34 REMARK 465 ASN S -33 REMARK 465 GLN S -32 REMARK 465 SER S -31 REMARK 465 HIS S -30 REMARK 465 GLN S -29 REMARK 465 GLY S -28 REMARK 465 PHE S -27 REMARK 465 ASN S -26 REMARK 465 LYS S -25 REMARK 465 GLU S -24 REMARK 465 HIS S -23 REMARK 465 THR S -22 REMARK 465 SER S -21 REMARK 465 LYS S -20 REMARK 465 MET S -19 REMARK 465 VAL S -18 REMARK 465 SER S -17 REMARK 465 ALA S -16 REMARK 465 ILE S -15 REMARK 465 VAL S -14 REMARK 465 LEU S -13 REMARK 465 TYR S -12 REMARK 465 VAL S -11 REMARK 465 LEU S -10 REMARK 465 LEU S -9 REMARK 465 ALA S -8 REMARK 465 ALA S -7 REMARK 465 ALA S -6 REMARK 465 ALA S -5 REMARK 465 HIS S -4 REMARK 465 SER S -3 REMARK 465 ALA S -2 REMARK 465 PHE S -1 REMARK 465 ALA S 0 REMARK 465 ALA S 120 REMARK 465 GLY S 121 REMARK 465 GLY S 122 REMARK 465 GLY S 123 REMARK 465 GLY S 124 REMARK 465 SER S 125 REMARK 465 GLY S 126 REMARK 465 GLY S 127 REMARK 465 GLY S 128 REMARK 465 GLY S 129 REMARK 465 SER S 130 REMARK 465 GLY S 131 REMARK 465 GLY S 132 REMARK 465 GLY S 133 REMARK 465 GLY S 134 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A 203 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 204 CG OD1 OD2 REMARK 470 ARG A 207 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 272 CG CD CE NZ REMARK 470 GLU A 274 CG CD OE1 OE2 REMARK 470 ASP A 333 CG OD1 OD2 REMARK 470 LYS A 345 CG CD CE NZ REMARK 470 GLU A 355 CG CD OE1 OE2 REMARK 470 GLU B 17 CG CD OE1 OE2 REMARK 470 LYS B 20 CG CD CE NZ REMARK 470 GLN B 80 CG CD OE1 NE2 REMARK 470 ARG B 219 CG CD NE CZ NH1 NH2 REMARK 470 MET B 222 CG SD CE REMARK 470 LYS G 20 CG CD CE NZ REMARK 470 MET G 21 CG SD CE REMARK 470 GLU G 22 CG CD OE1 OE2 REMARK 470 ASN G 24 CG OD1 ND2 REMARK 470 ASP G 26 CG OD1 OD2 REMARK 470 MET G 38 CG SD CE REMARK 470 LYS R 62 CG CD CE NZ REMARK 470 VAL R 149 CG1 CG2 REMARK 470 LYS R 150 CG CD CE NZ REMARK 470 ARG R 299 CG CD NE CZ NH1 NH2 REMARK 470 ARG S 86 CG CD NE CZ NH1 NH2 REMARK 470 MET S 192 CG SD CE REMARK 470 GLN S 231 CG CD OE1 NE2 REMARK 470 LEU S 233 CG CD1 CD2 REMARK 470 GLU S 234 CG CD OE1 OE2 REMARK 470 TYR S 235 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR S 238 OG1 CG2 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 ASP A 204 -168.76 -163.29 REMARK 500 ASN A 243 35.25 -99.75 REMARK 500 GLU A 274 53.22 -119.00 REMARK 500 ASP A 319 51.58 -92.28 REMARK 500 ASP B 252 50.03 -93.10 REMARK 500 PHE B 297 -3.48 68.53 REMARK 500 ALA B 307 -4.91 76.63 REMARK 500 ASN B 318 -179.37 -172.29 REMARK 500 LEU F 7 48.93 -81.74 REMARK 500 PRO F 9 71.76 -68.93 REMARK 500 SER R 34 0.93 -69.75 REMARK 500 GLN R 106 133.69 75.67 REMARK 500 PRO R 173 -18.43 -49.16 REMARK 500 ARG S 17 147.38 -173.24 REMARK 500 SER S 24 115.96 -161.33 REMARK 500 ARG S 191 39.15 -140.35 REMARK 500 MET S 192 -10.11 72.85 REMARK 500 SER S 193 -35.41 -131.02 REMARK 500 HIS S 232 34.27 -97.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63857 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF PIG GNRHR BOUND WITH MAMMAL GNRH DBREF 9U4W A 1 359 PDB 9U4W 9U4W 1 359 DBREF 9U4W B 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 9U4W F 1 10 UNP P01148 GON1_HUMAN 24 33 DBREF 9U4W G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9U4W R -85 0 PDB 9U4W 9U4W -85 0 DBREF 9U4W R 9 328 UNP P49922 GNRHR_PIG 9 328 DBREF 9U4W S -37 247 PDB 9U4W 9U4W -37 247 SEQADV 9U4W GLY B 2 UNP P62873 EXPRESSION TAG SEQADV 9U4W SER B 3 UNP P62873 EXPRESSION TAG SEQADV 9U4W LEU B 4 UNP P62873 EXPRESSION TAG SEQADV 9U4W LEU B 5 UNP P62873 EXPRESSION TAG SEQADV 9U4W GLN B 6 UNP P62873 EXPRESSION TAG SEQADV 9U4W NH2 F 11 UNP P01148 AMIDATION SEQADV 9U4W MET R 1 PDB LINKER SEQADV 9U4W ALA R 2 PDB LINKER SEQADV 9U4W ASN R 3 PDB LINKER SEQADV 9U4W SER R 4 PDB LINKER SEQADV 9U4W ALA R 5 PDB LINKER SEQADV 9U4W SER R 6 PDB LINKER SEQADV 9U4W PRO R 7 PDB LINKER SEQADV 9U4W GLU R 8 PDB LINKER SEQRES 1 A 246 MET GLY SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA SEQRES 2 A 246 GLU ARG SER LYS MET ILE ASP LYS ASN LEU ARG GLU ASP SEQRES 3 A 246 GLY GLU LYS ALA ARG ARG THR LEU ARG LEU LEU LEU LEU SEQRES 4 A 246 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 246 MET ARG ILE LEU HIS GLY GLY SER GLY GLY SER GLY GLY SEQRES 6 A 246 THR SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS SEQRES 7 A 246 VAL ASN PHE HIS MET PHE ASP VAL GLY GLY GLN ARG ASP SEQRES 8 A 246 GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR SEQRES 9 A 246 ALA ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG SEQRES 10 A 246 LEU GLN GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN SEQRES 11 A 246 ASN ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU SEQRES 12 A 246 ASN LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY SEQRES 13 A 246 LYS SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG SEQRES 14 A 246 TYR THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU SEQRES 15 A 246 ASP PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG LYS SEQRES 16 A 246 GLU PHE VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG SEQRES 17 A 246 HIS ILE CYS TYR PRO HIS PHE THR CYS ALA VAL ASP THR SEQRES 18 A 246 GLU ASN ALA ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE SEQRES 19 A 246 ILE LEU GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 B 344 GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG GLN SEQRES 2 B 344 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 3 B 344 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 4 B 344 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 5 B 344 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 6 B 344 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 7 B 344 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 8 B 344 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 9 B 344 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 10 B 344 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 11 B 344 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 12 B 344 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 13 B 344 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 14 B 344 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 15 B 344 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 16 B 344 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 17 B 344 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 18 B 344 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 19 B 344 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 20 B 344 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 21 B 344 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 22 B 344 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 23 B 344 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 24 B 344 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 25 B 344 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 26 B 344 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 27 B 344 PHE LEU LYS ILE TRP ASN SEQRES 1 F 11 PCA HIS TRP SER TYR GLY LEU ARG PRO GLY NH2 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 R 414 MET ASP SER LYS GLY SER SER GLN LYS GLY SER ARG LEU SEQRES 2 R 414 LEU LEU LEU LEU VAL VAL SER ASN LEU LEU LEU CYS GLN SEQRES 3 R 414 GLY VAL VAL SER ASP TYR LYS ASP ASP ASP ASP VAL HIS SEQRES 4 R 414 HIS HIS HIS HIS HIS HIS HIS ASP MET GLY GLN PRO GLY SEQRES 5 R 414 ASN GLY SER ALA PHE LEU LEU ALA PRO ASN GLY SER HIS SEQRES 6 R 414 ALA PRO ASP HIS ASP VAL THR GLN GLN ARG ASP GLU GLU SEQRES 7 R 414 ASN LEU TYR PHE GLN GLY ALA SER MET ALA ASN SER ALA SEQRES 8 R 414 SER PRO GLU GLN ASN GLN ASN HIS CYS SER ALA ILE ASN SEQRES 9 R 414 SER SER ILE LEU LEU THR GLN GLY ASN LEU PRO THR LEU SEQRES 10 R 414 THR LEU SER GLY LYS ILE ARG VAL THR VAL THR PHE PHE SEQRES 11 R 414 LEU PHE LEU LEU SER THR ALA PHE ASN ALA SER PHE LEU SEQRES 12 R 414 LEU LYS LEU GLN LYS TRP THR GLN ARG LYS GLU LYS GLY SEQRES 13 R 414 LYS LYS LEU SER ARG MET LYS VAL LEU LEU LYS HIS LEU SEQRES 14 R 414 THR LEU ALA ASN LEU LEU GLU THR LEU ILE VAL MET PRO SEQRES 15 R 414 LEU ASP GLY MET TRP ASN ILE THR VAL GLN TRP TYR ALA SEQRES 16 R 414 GLY GLU PHE LEU CYS LYS VAL LEU SER TYR LEU LYS LEU SEQRES 17 R 414 PHE SER MET TYR ALA PRO ALA PHE MET MET VAL VAL ILE SEQRES 18 R 414 SER LEU ASP ARG SER LEU ALA ILE THR ARG PRO LEU ALA SEQRES 19 R 414 VAL LYS SER ASN SER ARG LEU GLY ARG PHE MET ILE GLY SEQRES 20 R 414 LEU ALA TRP LEU LEU SER SER ILE PHE ALA GLY PRO GLN SEQRES 21 R 414 LEU TYR ILE PHE ARG MET ILE HIS LEU ALA ASP SER SER SEQRES 22 R 414 GLY GLN THR GLU GLY PHE SER GLN CYS VAL THR HIS GLY SEQRES 23 R 414 SER PHE PRO GLN TRP TRP HIS GLN ALA PHE TYR ASN PHE SEQRES 24 R 414 PHE THR PHE SER CYS LEU PHE ILE ILE PRO LEU LEU ILE SEQRES 25 R 414 MET LEU ILE CYS ASN ALA LYS ILE MET PHE THR LEU THR SEQRES 26 R 414 ARG VAL LEU GLN GLN ASP PRO HIS ASN LEU GLN LEU ASN SEQRES 27 R 414 GLN SER LYS ASN ASN ILE PRO ARG ALA ARG LEU ARG THR SEQRES 28 R 414 LEU LYS MET THR VAL ALA PHE ALA ALA SER PHE ILE VAL SEQRES 29 R 414 CYS TRP THR PRO TYR TYR VAL LEU GLY ILE TRP TYR TRP SEQRES 30 R 414 PHE ASP PRO GLU MET VAL ASN ARG VAL SER ASP PRO VAL SEQRES 31 R 414 ASN HIS PHE PHE PHE LEU PHE ALA PHE LEU ASN PRO CYS SEQRES 32 R 414 PHE ASP PRO LEU ILE TYR GLY TYR PHE SER LEU SEQRES 1 S 285 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS SEQRES 2 S 285 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR SEQRES 3 S 285 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA VAL SEQRES 4 S 285 GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN PRO GLY SEQRES 5 S 285 GLY SER ARG LYS LEU SER CYS SER ALA SER GLY PHE ALA SEQRES 6 S 285 PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN ALA PRO SEQRES 7 S 285 GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SER GLY SEQRES 8 S 285 SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS GLY ARG SEQRES 9 S 285 PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR LEU PHE SEQRES 10 S 285 LEU GLN MET THR SER LEU ARG SER GLU ASP THR ALA MET SEQRES 11 S 285 TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SER SER SEQRES 12 S 285 PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 13 S 285 SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY SEQRES 14 S 285 GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN ALA THR SEQRES 15 S 285 SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER ILE SEQRES 16 S 285 SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN GLY SEQRES 17 S 285 ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY GLN SEQRES 18 S 285 SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU ALA SEQRES 19 S 285 SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY SEQRES 20 S 285 THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA GLU SEQRES 21 S 285 ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU TYR SEQRES 22 S 285 PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU MODRES 9U4W PCA F 1 GLN MODIFIED RESIDUE HET PCA F 1 14 HET NH2 F 11 1 HETNAM PCA PYROGLUTAMIC ACID HETNAM NH2 AMINO GROUP FORMUL 3 PCA C5 H7 N O3 FORMUL 3 NH2 H2 N HELIX 1 AA1 GLU A 8 ARG A 32 1 25 HELIX 2 AA2 ILE A 210 ASN A 214 5 5 HELIX 3 AA3 ASP A 227 ARG A 230 5 4 HELIX 4 AA4 LEU A 231 ASN A 243 1 13 HELIX 5 AA5 ASN A 244 ARG A 248 5 5 HELIX 6 AA6 LYS A 258 LYS A 265 1 8 HELIX 7 AA7 ASP A 296 ALA A 316 1 21 HELIX 8 AA8 GLU A 335 ASN A 357 1 23 HELIX 9 AA9 LEU B 9 CYS B 30 1 22 HELIX 10 AB1 THR B 34 THR B 39 1 6 HELIX 11 AB2 ASN B 40 ILE B 42 5 3 HELIX 12 AB3 ALA G 7 ASN G 24 1 18 HELIX 13 AB4 LYS G 29 HIS G 44 1 16 HELIX 14 AB5 ALA G 45 ASP G 48 5 4 HELIX 15 AB6 THR R 32 LYS R 62 1 31 HELIX 16 AB7 ARG R 75 THR R 104 1 30 HELIX 17 AB8 GLY R 110 ARG R 145 1 36 HELIX 18 AB9 ARG R 145 LYS R 150 1 6 HELIX 19 AC1 SER R 151 SER R 153 5 3 HELIX 20 AC2 ARG R 154 GLY R 172 1 19 HELIX 21 AC3 PRO R 173 PHE R 178 1 6 HELIX 22 AC4 GLN R 204 PHE R 220 1 17 HELIX 23 AC5 PHE R 220 GLN R 243 1 24 HELIX 24 AC6 ASN R 257 ASP R 293 1 37 HELIX 25 AC7 PRO R 294 ASN R 298 5 5 HELIX 26 AC8 SER R 301 PHE R 308 1 8 HELIX 27 AC9 PHE R 309 ALA R 312 5 4 HELIX 28 AD1 PHE R 313 SER R 327 1 15 HELIX 29 AD2 ALA S 27 PHE S 31 5 5 HELIX 30 AD3 SER S 52 GLY S 55 5 4 HELIX 31 AD4 ARG S 86 THR S 90 5 5 HELIX 32 AD5 GLU S 220 VAL S 224 5 5 SHEET 1 AA1 6 PHE A 183 VAL A 189 0 SHEET 2 AA1 6 VAL A 192 ASP A 198 -1 O PHE A 194 N PHE A 187 SHEET 3 AA1 6 LEU A 34 GLY A 40 1 N LEU A 36 O HIS A 195 SHEET 4 AA1 6 ALA A 218 ASP A 224 1 O ILE A 220 N LEU A 37 SHEET 5 AA1 6 SER A 251 ASN A 257 1 O ILE A 253 N ILE A 219 SHEET 6 AA1 6 CYS A 324 PHE A 328 1 O HIS A 327 N LEU A 256 SHEET 1 AA2 4 ARG B 51 LEU B 56 0 SHEET 2 AA2 4 LEU B 341 ASN B 345 -1 O LEU B 341 N LEU B 56 SHEET 3 AA2 4 VAL B 332 SER B 336 -1 N VAL B 332 O TRP B 344 SHEET 4 AA2 4 VAL B 320 VAL B 325 -1 N SER B 321 O GLY B 335 SHEET 1 AA3 4 ILE B 63 TRP B 68 0 SHEET 2 AA3 4 LEU B 74 SER B 79 -1 O ALA B 78 N ALA B 65 SHEET 3 AA3 4 LYS B 83 ASP B 88 -1 O TRP B 87 N LEU B 75 SHEET 4 AA3 4 HIS B 96 PRO B 99 -1 O ILE B 98 N LEU B 84 SHEET 1 AA4 4 THR B 107 TYR B 110 0 SHEET 2 AA4 4 TYR B 116 GLY B 120 -1 O ALA B 118 N ALA B 109 SHEET 3 AA4 4 CYS B 126 ASN B 130 -1 O TYR B 129 N VAL B 117 SHEET 4 AA4 4 ARG B 139 LEU B 144 -1 O LEU B 144 N CYS B 126 SHEET 1 AA5 4 LEU B 151 ASP B 158 0 SHEET 2 AA5 4 GLN B 161 SER B 166 -1 O SER B 165 N SER B 152 SHEET 3 AA5 4 THR B 170 ASP B 175 -1 O TRP B 174 N ILE B 162 SHEET 4 AA5 4 GLN B 180 GLN B 181 -1 O GLN B 180 N ASP B 175 SHEET 1 AA6 4 VAL B 192 LEU B 197 0 SHEET 2 AA6 4 LEU B 203 ALA B 208 -1 O GLY B 207 N MET B 193 SHEET 3 AA6 4 SER B 212 ASP B 217 -1 O TRP B 216 N PHE B 204 SHEET 4 AA6 4 CYS B 223 PHE B 227 -1 O PHE B 227 N ALA B 213 SHEET 1 AA7 4 ILE B 234 ILE B 237 0 SHEET 2 AA7 4 ALA B 245 SER B 250 -1 O GLY B 249 N ALA B 236 SHEET 3 AA7 4 CYS B 255 ASP B 259 -1 O ARG B 256 N THR B 248 SHEET 4 AA7 4 GLN B 264 TYR B 269 -1 O TYR B 269 N CYS B 255 SHEET 1 AA8 4 VAL B 281 PHE B 283 0 SHEET 2 AA8 4 LEU B 289 GLY B 293 -1 O LEU B 291 N SER B 282 SHEET 3 AA8 4 CYS B 299 ASP B 303 -1 O TRP B 302 N LEU B 290 SHEET 4 AA8 4 ARG B 309 LEU B 313 -1 O LEU B 313 N CYS B 299 SHEET 1 AA9 2 MET R 180 HIS R 182 0 SHEET 2 AA9 2 SER R 194 CYS R 196 -1 O GLN R 195 N ILE R 181 SHEET 1 AB1 4 GLN S 2 SER S 6 0 SHEET 2 AB1 4 LEU S 19 SER S 24 -1 O SER S 20 N SER S 6 SHEET 3 AB1 4 THR S 77 GLN S 81 -1 O LEU S 78 N CYS S 21 SHEET 4 AB1 4 THR S 68 ASP S 72 -1 N SER S 70 O PHE S 79 SHEET 1 AB2 6 GLY S 9 VAL S 11 0 SHEET 2 AB2 6 THR S 114 VAL S 118 1 O THR S 117 N VAL S 11 SHEET 3 AB2 6 MET S 92 SER S 98 -1 N TYR S 93 O THR S 114 SHEET 4 AB2 6 GLY S 32 GLN S 38 -1 N VAL S 36 O TYR S 94 SHEET 5 AB2 6 LEU S 44 ILE S 50 -1 O VAL S 47 N TRP S 35 SHEET 6 AB2 6 ILE S 57 TYR S 59 -1 O TYR S 58 N TYR S 49 SHEET 1 AB3 4 MET S 140 GLN S 142 0 SHEET 2 AB3 4 ILE S 157 SER S 161 -1 O ARG S 160 N THR S 141 SHEET 3 AB3 4 ALA S 211 THR S 215 -1 O LEU S 214 N ILE S 157 SHEET 4 AB3 4 SER S 204 GLY S 207 -1 N SER S 204 O THR S 215 SHEET 1 AB4 5 SER S 146 PRO S 148 0 SHEET 2 AB4 5 THR S 243 GLU S 246 1 O LYS S 244 N VAL S 147 SHEET 3 AB4 5 GLY S 225 CYS S 229 -1 N GLY S 225 O LEU S 245 SHEET 4 AB4 5 TRP S 176 GLN S 179 -1 N GLN S 179 O VAL S 226 SHEET 5 AB4 5 GLN S 186 LEU S 187 -1 O GLN S 186 N LEU S 178 SSBOND 1 CYS R 114 CYS R 196 1555 1555 2.03 LINK C PCA F 1 N HIS F 2 1555 1555 1.33 LINK C GLY F 10 N NH2 F 11 1555 1555 1.33 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