HEADER MEMBRANE PROTEIN 20-MAR-25 9U4Y TITLE CRYO-EM STRUCTURE OF XENOPUS LAEVIS GNRHR BOUND WITH MAMMAL GNRH COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 3 BETA-1; COMPND 4 CHAIN: B; COMPND 5 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 9 GAMMA-2; COMPND 10 CHAIN: G; COMPND 11 SYNONYM: G GAMMA-I; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: GONADOLIBERIN-1; COMPND 15 CHAIN: C; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA-1; COMPND 19 CHAIN: A; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: SCFV16; COMPND 23 CHAIN: S; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 6; COMPND 26 MOLECULE: BETA-2 ADRENERGIC RECEPTOR,GONADOTROPIN-RELEASING HORMONE COMPND 27 RECEPTOR; COMPND 28 CHAIN: R; COMPND 29 SYNONYM: BETA-2 ADRENORECEPTOR,BETA-2 ADRENOCEPTOR; COMPND 30 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: GNB1; 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: GNG2; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 18 ORGANISM_TAXID: 32630; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 25 MOL_ID: 5; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 31 MOL_ID: 6; SOURCE 32 ORGANISM_SCIENTIFIC: ATELES, XENOPUS LAEVIS; SOURCE 33 ORGANISM_COMMON: AFRICAN CLAWED FROG; SOURCE 34 ORGANISM_TAXID: 9506, 8355; SOURCE 35 GENE: ADRB2, ADRB2R, B2AR, GNRHR.L, GNRHR, GNRHR1, GNRHR2-A, XGNRHR; SOURCE 36 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 37 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS CRYO-EM, GNRHR, GONADOTROPIN-RELEASING HORMONE RECEPTOR, MEMBRANE KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR S.SHEN,H.E.XU REVDAT 1 11-JUN-25 9U4Y 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. 2.67 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) : 2.670 REMARK 3 NUMBER OF PARTICLES : 255764 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 9U4Y 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_1300057679. 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 XENOPUS REMARK 245 LAEVIS GNRHR BOUND WITH MAMMAL REMARK 245 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: B, G, C, A, S, 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 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 A 1 REMARK 465 GLY A 2 REMARK 465 SER A 3 REMARK 465 THR A 4 REMARK 465 VAL A 5 REMARK 465 SER A 6 REMARK 465 ALA A 7 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 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 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 LEU R 2 REMARK 465 THR R 3 REMARK 465 MET R 4 REMARK 465 SER R 5 REMARK 465 TYR R 6 REMARK 465 GLN R 7 REMARK 465 GLY R 8 REMARK 465 ILE R 9 REMARK 465 MET R 10 REMARK 465 ASP R 11 REMARK 465 SER R 12 REMARK 465 GLN R 13 REMARK 465 ASP R 14 REMARK 465 LEU R 15 REMARK 465 CYS R 16 REMARK 465 ALA R 17 REMARK 465 LEU R 18 REMARK 465 ASN R 19 REMARK 465 ARG R 20 REMARK 465 SER R 21 REMARK 465 CYS R 22 REMARK 465 PHE R 23 REMARK 465 HIS R 24 REMARK 465 LEU R 25 REMARK 465 LYS R 26 REMARK 465 GLU R 27 REMARK 465 GLN R 28 REMARK 465 GLU R 29 REMARK 465 LYS R 30 REMARK 465 THR R 31 REMARK 465 TYR R 32 REMARK 465 GLY R 33 REMARK 465 PRO R 34 REMARK 465 ASN R 35 REMARK 465 ILE R 36 REMARK 465 THR R 37 REMARK 465 VAL R 38 REMARK 465 LEU R 39 REMARK 465 ASN R 40 REMARK 465 ASP R 41 REMARK 465 LYS R 42 REMARK 465 ALA R 43 REMARK 465 PHE R 44 REMARK 465 ILE R 45 REMARK 465 LEU R 46 REMARK 465 PRO R 47 REMARK 465 THR R 48 REMARK 465 PHE R 49 REMARK 465 SER R 196 REMARK 465 GLU R 197 REMARK 465 PRO R 198 REMARK 465 ILE R 199 REMARK 465 HIS R 200 REMARK 465 PHE R 201 REMARK 465 VAL R 202 REMARK 465 MET R 250 REMARK 465 LYS R 251 REMARK 465 ALA R 252 REMARK 465 THR R 253 REMARK 465 CYS R 254 REMARK 465 VAL R 255 REMARK 465 SER R 256 REMARK 465 SER R 257 REMARK 465 LYS R 258 REMARK 465 GLU R 259 REMARK 465 ILE R 260 REMARK 465 ASP R 261 REMARK 465 LEU R 262 REMARK 465 ARG R 263 REMARK 465 ARG R 264 REMARK 465 SER R 265 REMARK 465 SER R 266 REMARK 465 ASN R 267 REMARK 465 PHE R 339 REMARK 465 THR R 340 REMARK 465 ILE R 341 REMARK 465 HIS R 342 REMARK 465 PHE R 343 REMARK 465 ARG R 344 REMARK 465 ARG R 345 REMARK 465 GLU R 346 REMARK 465 ILE R 347 REMARK 465 ARG R 348 REMARK 465 ARG R 349 REMARK 465 VAL R 350 REMARK 465 CYS R 351 REMARK 465 ARG R 352 REMARK 465 CYS R 353 REMARK 465 ALA R 354 REMARK 465 ALA R 355 REMARK 465 GLN R 356 REMARK 465 GLY R 357 REMARK 465 LYS R 358 REMARK 465 ASP R 359 REMARK 465 HIS R 360 REMARK 465 ASP R 361 REMARK 465 THR R 362 REMARK 465 ALA R 363 REMARK 465 SER R 364 REMARK 465 VAL R 365 REMARK 465 GLY R 366 REMARK 465 THR R 367 REMARK 465 GLY R 368 REMARK 465 SER R 369 REMARK 465 PHE R 370 REMARK 465 ARG R 371 REMARK 465 ILE R 372 REMARK 465 THR R 373 REMARK 465 THR R 374 REMARK 465 THR R 375 REMARK 465 PRO R 376 REMARK 465 ALA R 377 REMARK 465 PRO R 378 REMARK 465 ILE R 379 REMARK 465 LYS R 380 REMARK 465 ARG R 381 REMARK 465 THR R 382 REMARK 465 VAL R 383 REMARK 465 GLY R 384 REMARK 465 VAL R 385 REMARK 465 LEU R 386 REMARK 465 GLY R 387 REMARK 465 GLY R 388 REMARK 465 SER R 389 REMARK 465 GLY R 390 REMARK 465 LYS R 391 REMARK 465 PHE R 392 REMARK 465 GLU R 393 REMARK 465 LEU R 394 REMARK 465 GLU R 395 REMARK 465 VAL R 396 REMARK 465 THR R 397 REMARK 465 GLY R 398 REMARK 465 HIS R 399 REMARK 465 GLY R 400 REMARK 465 LEU R 401 REMARK 465 HIS R 402 REMARK 465 SER R 403 REMARK 465 GLY R 404 REMARK 465 LYS R 405 REMARK 465 CYS R 406 REMARK 465 ASP R 407 REMARK 465 GLN R 408 REMARK 465 CYS R 409 REMARK 465 GLN R 410 REMARK 465 GLY R 411 REMARK 465 ARG R 412 REMARK 465 ILE R 413 REMARK 465 VAL R 414 REMARK 465 GLU R 415 REMARK 465 SER R 416 REMARK 465 PHE R 417 REMARK 465 MET R 418 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 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 ARG A 203 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 207 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 272 CG CD CE NZ REMARK 470 ILE A 273 CG1 CG2 CD1 REMARK 470 GLU A 274 CG CD OE1 OE2 REMARK 470 LYS A 345 CG CD CE NZ REMARK 470 GLU A 355 CG CD OE1 OE2 REMARK 470 GLN R 203 CG CD OE1 NE2 REMARK 470 ASN R 268 CG OD1 ND2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR B 92 9.41 57.52 REMARK 500 THR B 201 -2.75 72.56 REMARK 500 ASP B 252 46.29 -85.54 REMARK 500 ALA B 253 49.78 38.77 REMARK 500 ASP B 296 47.67 -85.85 REMARK 500 PHE B 297 16.44 53.25 REMARK 500 ALA B 307 -4.39 71.97 REMARK 500 SER C 4 71.40 -102.79 REMARK 500 ARG C 8 105.00 -28.34 REMARK 500 ARG A 206 14.26 56.31 REMARK 500 ARG S 191 45.23 -140.55 REMARK 500 MET S 192 -11.16 74.55 REMARK 500 PRO S 236 75.61 -65.54 REMARK 500 TYR R 120 -9.02 -59.85 REMARK 500 SER R 304 78.02 -151.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63858 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF XENOPUS LAEVIS GNRHR BOUND WITH MAMMAL GNRH REMARK 900 RELATED ID: 9U4W RELATED DB: PDB DBREF 9U4Y B 7 345 UNP P62873 GBB1_HUMAN 2 340 DBREF 9U4Y G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9U4Y C 1 10 UNP Q28588 GON1_SHEEP 1 10 DBREF 9U4Y A 1 359 PDB 9U4Y 9U4Y 1 359 DBREF 9U4Y S -37 247 PDB 9U4Y 9U4Y -37 247 DBREF 9U4Y R -38 -9 UNP P07550 ADRB2_HUMAN 1 30 DBREF 9U4Y R 1 418 UNP Q90WJ2 Q90WJ2_XENLA 1 418 SEQADV 9U4Y GLY B 2 UNP P62873 EXPRESSION TAG SEQADV 9U4Y SER B 3 UNP P62873 EXPRESSION TAG SEQADV 9U4Y LEU B 4 UNP P62873 EXPRESSION TAG SEQADV 9U4Y LEU B 5 UNP P62873 EXPRESSION TAG SEQADV 9U4Y GLN B 6 UNP P62873 EXPRESSION TAG SEQADV 9U4Y NH2 C 11 UNP Q28588 AMIDATION SEQADV 9U4Y MET R -85 UNP P07550 INITIATING METHIONINE SEQADV 9U4Y ASP R -84 UNP P07550 EXPRESSION TAG SEQADV 9U4Y SER R -83 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LYS R -82 UNP P07550 EXPRESSION TAG SEQADV 9U4Y GLY R -81 UNP P07550 EXPRESSION TAG SEQADV 9U4Y SER R -80 UNP P07550 EXPRESSION TAG SEQADV 9U4Y SER R -79 UNP P07550 EXPRESSION TAG SEQADV 9U4Y GLN R -78 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LYS R -77 UNP P07550 EXPRESSION TAG SEQADV 9U4Y GLY R -76 UNP P07550 EXPRESSION TAG SEQADV 9U4Y SER R -75 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ARG R -74 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -73 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -72 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -71 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -70 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -69 UNP P07550 EXPRESSION TAG SEQADV 9U4Y VAL R -68 UNP P07550 EXPRESSION TAG SEQADV 9U4Y VAL R -67 UNP P07550 EXPRESSION TAG SEQADV 9U4Y SER R -66 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASN R -65 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -64 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -63 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LEU R -62 UNP P07550 EXPRESSION TAG SEQADV 9U4Y CYS R -61 UNP P07550 EXPRESSION TAG SEQADV 9U4Y GLN R -60 UNP P07550 EXPRESSION TAG SEQADV 9U4Y GLY R -59 UNP P07550 EXPRESSION TAG SEQADV 9U4Y VAL R -58 UNP P07550 EXPRESSION TAG SEQADV 9U4Y VAL R -57 UNP P07550 EXPRESSION TAG SEQADV 9U4Y SER R -56 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASP R -55 UNP P07550 EXPRESSION TAG SEQADV 9U4Y TYR R -54 UNP P07550 EXPRESSION TAG SEQADV 9U4Y LYS R -53 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASP R -52 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASP R -51 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASP R -50 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASP R -49 UNP P07550 EXPRESSION TAG SEQADV 9U4Y VAL R -48 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -47 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -46 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -45 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -44 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -43 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -42 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -41 UNP P07550 EXPRESSION TAG SEQADV 9U4Y HIS R -40 UNP P07550 EXPRESSION TAG SEQADV 9U4Y ASP R -39 UNP P07550 EXPRESSION TAG SEQADV 9U4Y GLN R -12 UNP P07550 GLU 27 CONFLICT SEQADV 9U4Y GLU R -8 UNP P07550 LINKER SEQADV 9U4Y ASN R -7 UNP P07550 LINKER SEQADV 9U4Y LEU R -6 UNP P07550 LINKER SEQADV 9U4Y TYR R -5 UNP P07550 LINKER SEQADV 9U4Y PHE R -4 UNP P07550 LINKER SEQADV 9U4Y GLN R -3 UNP P07550 LINKER SEQADV 9U4Y GLY R -2 UNP P07550 LINKER SEQADV 9U4Y ALA R -1 UNP P07550 LINKER SEQADV 9U4Y SER R 0 UNP P07550 LINKER 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 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 C 11 PCA HIS TRP SER TYR GLY LEU ARG PRO GLY NH2 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 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 SEQRES 1 R 504 MET ASP SER LYS GLY SER SER GLN LYS GLY SER ARG LEU SEQRES 2 R 504 LEU LEU LEU LEU VAL VAL SER ASN LEU LEU LEU CYS GLN SEQRES 3 R 504 GLY VAL VAL SER ASP TYR LYS ASP ASP ASP ASP VAL HIS SEQRES 4 R 504 HIS HIS HIS HIS HIS HIS HIS ASP MET GLY GLN PRO GLY SEQRES 5 R 504 ASN GLY SER ALA PHE LEU LEU ALA PRO ASN GLY SER HIS SEQRES 6 R 504 ALA PRO ASP HIS ASP VAL THR GLN GLN ARG ASP GLU GLU SEQRES 7 R 504 ASN LEU TYR PHE GLN GLY ALA SER MET LEU THR MET SER SEQRES 8 R 504 TYR GLN GLY ILE MET ASP SER GLN ASP LEU CYS ALA LEU SEQRES 9 R 504 ASN ARG SER CYS PHE HIS LEU LYS GLU GLN GLU LYS THR SEQRES 10 R 504 TYR GLY PRO ASN ILE THR VAL LEU ASN ASP LYS ALA PHE SEQRES 11 R 504 ILE LEU PRO THR PHE SER THR ALA ALA LYS ILE ARG VAL SEQRES 12 R 504 ALA ILE THR CYS VAL LEU PHE ILE PHE SER ALA CYS PHE SEQRES 13 R 504 ASN ILE ALA ALA LEU TRP THR ILE THR TYR LYS TYR LYS SEQRES 14 R 504 LYS LYS SER HIS ILE ARG ILE LEU ILE ILE ASN LEU VAL SEQRES 15 R 504 ALA ALA ASP LEU PHE ILE THR LEU VAL VAL MET PRO LEU SEQRES 16 R 504 ASP ALA VAL TRP ASN VAL THR LEU GLN TRP TYR ALA GLY SEQRES 17 R 504 ASP LEU ALA CYS ARG VAL LEU MET PHE LEU LYS LEU ALA SEQRES 18 R 504 ALA MET TYR SER SER ALA PHE VAL THR VAL VAL ILE SER SEQRES 19 R 504 LEU ASP ARG GLN ALA ALA ILE LEU ASN PRO LEU GLY ILE SEQRES 20 R 504 GLY ASP ALA LYS LYS LYS ASN LYS ILE MET LEU CYS VAL SEQRES 21 R 504 ALA TRP PHE LEU SER TYR LEU LEU ALA ILE PRO GLN LEU SEQRES 22 R 504 PHE VAL PHE HIS THR VAL SER ARG SER GLU PRO ILE HIS SEQRES 23 R 504 PHE VAL GLN CYS ALA THR VAL GLY SER PHE GLN ALA HIS SEQRES 24 R 504 TRP GLN GLU THR ILE TYR ASN MET PHE THR PHE PHE CYS SEQRES 25 R 504 LEU PHE LEU LEU PRO LEU LEU ILE MET VAL SER CYS TYR SEQRES 26 R 504 THR ARG ILE LEU MET GLU ILE SER HIS LYS MET LYS ALA SEQRES 27 R 504 THR CYS VAL SER SER LYS GLU ILE ASP LEU ARG ARG SER SEQRES 28 R 504 SER ASN ASN ILE PRO ARG ALA ARG MET ARG THR LEU LYS SEQRES 29 R 504 MET SER LEU VAL ILE VAL LEU THR PHE ILE VAL CYS TRP SEQRES 30 R 504 THR PRO TYR TYR LEU LEU GLY ILE TRP TYR TRP PHE SER SEQRES 31 R 504 PRO GLU MET LEU THR GLU GLU LYS VAL PRO PRO SER LEU SEQRES 32 R 504 SER HIS ILE LEU PHE LEU PHE GLY LEU LEU ASN THR CYS SEQRES 33 R 504 LEU ASP PRO ILE ILE TYR GLY LEU PHE THR ILE HIS PHE SEQRES 34 R 504 ARG ARG GLU ILE ARG ARG VAL CYS ARG CYS ALA ALA GLN SEQRES 35 R 504 GLY LYS ASP HIS ASP THR ALA SER VAL GLY THR GLY SER SEQRES 36 R 504 PHE ARG ILE THR THR THR PRO ALA PRO ILE LYS ARG THR SEQRES 37 R 504 VAL GLY VAL LEU GLY GLY SER GLY LYS PHE GLU LEU GLU SEQRES 38 R 504 VAL THR GLY HIS GLY LEU HIS SER GLY LYS CYS ASP GLN SEQRES 39 R 504 CYS GLN GLY ARG ILE VAL GLU SER PHE MET MODRES 9U4Y PCA C 1 GLN MODIFIED RESIDUE HET PCA C 1 14 HET NH2 C 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 B 8 ALA B 31 1 24 HELIX 2 AA2 THR B 34 THR B 39 1 6 HELIX 3 AA3 ALA G 7 ASN G 24 1 18 HELIX 4 AA4 LYS G 29 HIS G 44 1 16 HELIX 5 AA5 ASP A 9 ARG A 31 1 23 HELIX 6 AA6 LYS A 46 VAL A 50 5 5 HELIX 7 AA7 ARG A 206 GLN A 211 1 6 HELIX 8 AA8 CYS A 212 ASN A 214 5 3 HELIX 9 AA9 ARG A 230 ASN A 243 1 14 HELIX 10 AB1 ASN A 244 ARG A 248 5 5 HELIX 11 AB2 LYS A 258 VAL A 266 1 9 HELIX 12 AB3 ASP A 296 ALA A 316 1 21 HELIX 13 AB4 GLU A 335 TYR A 356 1 22 HELIX 14 AB5 ALA S 27 PHE S 31 5 5 HELIX 15 AB6 SER S 52 GLY S 55 5 4 HELIX 16 AB7 ARG S 86 THR S 90 5 5 HELIX 17 AB8 GLU S 220 VAL S 224 5 5 HELIX 18 AB9 THR R 51 TYR R 82 1 32 HELIX 19 AC1 SER R 86 THR R 116 1 31 HELIX 20 AC2 GLY R 122 ASN R 157 1 36 HELIX 21 AC3 PRO R 158 GLY R 162 5 5 HELIX 22 AC4 ASP R 163 LEU R 182 1 20 HELIX 23 AC5 ILE R 184 PHE R 190 1 7 HELIX 24 AC6 ALA R 212 PHE R 228 1 17 HELIX 25 AC7 PHE R 228 HIS R 248 1 21 HELIX 26 AC8 ILE R 269 SER R 304 1 36 HELIX 27 AC9 PRO R 305 GLU R 310 1 6 HELIX 28 AD1 PRO R 314 PHE R 322 1 9 HELIX 29 AD2 PHE R 322 LEU R 338 1 17 SHEET 1 AA1 4 ARG B 51 LEU B 56 0 SHEET 2 AA1 4 LEU B 341 ASN B 345 -1 O LEU B 341 N LEU B 56 SHEET 3 AA1 4 VAL B 332 SER B 336 -1 N THR B 334 O LYS B 342 SHEET 4 AA1 4 VAL B 320 VAL B 325 -1 N CYS B 322 O GLY B 335 SHEET 1 AA2 4 ILE B 63 TRP B 68 0 SHEET 2 AA2 4 LEU B 74 SER B 79 -1 O ALA B 78 N TYR B 64 SHEET 3 AA2 4 LYS B 83 ASP B 88 -1 O TRP B 87 N LEU B 75 SHEET 4 AA2 4 LYS B 94 PRO B 99 -1 O ILE B 98 N LEU B 84 SHEET 1 AA3 4 VAL B 105 TYR B 110 0 SHEET 2 AA3 4 TYR B 116 GLY B 121 -1 O GLY B 120 N MET B 106 SHEET 3 AA3 4 CYS B 126 ASN B 130 -1 O TYR B 129 N VAL B 117 SHEET 4 AA3 4 ARG B 139 LEU B 144 -1 O ARG B 142 N ILE B 128 SHEET 1 AA4 4 LEU B 151 ASP B 158 0 SHEET 2 AA4 4 GLN B 161 SER B 166 -1 O VAL B 163 N ARG B 155 SHEET 3 AA4 4 CYS B 171 ASP B 175 -1 O TRP B 174 N ILE B 162 SHEET 4 AA4 4 GLN B 180 PHE B 185 -1 O PHE B 185 N CYS B 171 SHEET 1 AA5 4 VAL B 192 LEU B 197 0 SHEET 2 AA5 4 LEU B 203 ALA B 208 -1 O GLY B 207 N SER B 194 SHEET 3 AA5 4 ALA B 213 ASP B 217 -1 O TRP B 216 N PHE B 204 SHEET 4 AA5 4 CYS B 223 PHE B 227 -1 O ARG B 224 N LEU B 215 SHEET 1 AA6 4 ILE B 234 PHE B 239 0 SHEET 2 AA6 4 ALA B 245 SER B 250 -1 O GLY B 249 N ALA B 236 SHEET 3 AA6 4 THR B 254 ASP B 259 -1 O PHE B 258 N PHE B 246 SHEET 4 AA6 4 GLN B 264 TYR B 269 -1 O LEU B 266 N LEU B 257 SHEET 1 AA7 4 ILE B 278 PHE B 283 0 SHEET 2 AA7 4 LEU B 289 TYR B 294 -1 O LEU B 291 N SER B 282 SHEET 3 AA7 4 CYS B 299 ASP B 303 -1 O ASN B 300 N ALA B 292 SHEET 4 AA7 4 ARG B 309 LEU B 313 -1 O LEU B 313 N CYS B 299 SHEET 1 AA8 6 PHE A 183 VAL A 189 0 SHEET 2 AA8 6 VAL A 192 ASP A 198 -1 O PHE A 194 N PHE A 187 SHEET 3 AA8 6 LEU A 34 GLY A 40 1 N LEU A 34 O ASN A 193 SHEET 4 AA8 6 ALA A 218 ASP A 224 1 O ILE A 220 N LEU A 39 SHEET 5 AA8 6 SER A 251 ASN A 257 1 O PHE A 255 N PHE A 221 SHEET 6 AA8 6 CYS A 324 PHE A 328 1 O HIS A 327 N LEU A 256 SHEET 1 AA9 4 GLN S 2 SER S 6 0 SHEET 2 AA9 4 ARG S 17 SER S 24 -1 O SER S 22 N VAL S 4 SHEET 3 AA9 4 THR S 77 MET S 82 -1 O MET S 82 N ARG S 17 SHEET 4 AA9 4 PHE S 67 ASP S 72 -1 N ASP S 72 O THR S 77 SHEET 1 AB1 6 GLY S 9 VAL S 11 0 SHEET 2 AB1 6 THR S 114 VAL S 118 1 O THR S 117 N GLY S 9 SHEET 3 AB1 6 ALA S 91 SER S 98 -1 N TYR S 93 O THR S 114 SHEET 4 AB1 6 GLY S 32 GLN S 38 -1 N GLN S 38 O MET S 92 SHEET 5 AB1 6 LEU S 44 ILE S 50 -1 O ILE S 50 N MET S 33 SHEET 6 AB1 6 ILE S 57 TYR S 59 -1 O TYR S 58 N TYR S 49 SHEET 1 AB2 4 MET S 140 GLN S 142 0 SHEET 2 AB2 4 VAL S 155 SER S 161 -1 O ARG S 160 N THR S 141 SHEET 3 AB2 4 ALA S 211 ILE S 216 -1 O PHE S 212 N CYS S 159 SHEET 4 AB2 4 PHE S 203 GLY S 207 -1 N SER S 206 O THR S 213 SHEET 1 AB3 5 SER S 146 PRO S 148 0 SHEET 2 AB3 5 THR S 243 GLU S 246 1 O LYS S 244 N VAL S 147 SHEET 3 AB3 5 GLY S 225 GLN S 231 -1 N GLY S 225 O LEU S 245 SHEET 4 AB3 5 LEU S 174 GLN S 179 -1 N GLN S 179 O VAL S 226 SHEET 5 AB3 5 GLN S 186 ILE S 189 -1 O ILE S 189 N TRP S 176 SHEET 1 AB4 2 HIS R 191 THR R 192 0 SHEET 2 AB4 2 CYS R 204 ALA R 205 -1 O ALA R 205 N HIS R 191 SSBOND 1 CYS S 159 CYS S 229 1555 1555 2.72 SSBOND 2 CYS R 126 CYS R 204 1555 1555 2.03 LINK C PCA C 1 N HIS C 2 1555 1555 1.33 LINK C GLY C 10 N NH2 C 11 1555 1555 1.31 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