HEADER MEMBRANE PROTEIN 23-SEP-25 9YDP TITLE HUMAN DELTA OPIOID RECEPTOR COMPLEX WITH MINI-GI AND AGONIST DADLE COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS XLAS; COMPND 4 CHAIN: A; COMPND 5 EC: 3.6.5.-; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 9 BETA-1; COMPND 10 CHAIN: B; COMPND 11 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 15 GAMMA-2; COMPND 16 CHAIN: G; COMPND 17 SYNONYM: G GAMMA-I; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 4; COMPND 20 MOLECULE: NANOBODY 35; COMPND 21 CHAIN: N; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 5; COMPND 24 MOLECULE: DELTA-TYPE OPIOID RECEPTOR; COMPND 25 CHAIN: R; COMPND 26 SYNONYM: D-OR-1,DOR-1; COMPND 27 ENGINEERED: YES; COMPND 28 MOL_ID: 6; COMPND 29 MOLECULE: DADLE; COMPND 30 CHAIN: P; COMPND 31 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; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; 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: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; 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: TRICHOPLUSIA NI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7111; 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: OPRD1, OPRD; SOURCE 32 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 34 MOL_ID: 6; SOURCE 35 SYNTHETIC: YES; SOURCE 36 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 37 ORGANISM_TAXID: 9606 KEYWDS GPCR, OPIOID RECEPTOR, LIGAND BINDING, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.I.MOBBS,H.VENUGOPAL,D.M.THAL REVDAT 1 10-DEC-25 9YDP 0 JRNL AUTH J.I.MOBBS,M.D.NGUYEN,O.DEO,D.BARTUZI,H.VENUGOPAL,S.ALVI, JRNL AUTH 2 V.PHAM,N.BARNES,A.CHRISTOPOULOS,D.P.POOLE,S.E.CARBONE, JRNL AUTH 3 M.JORG,B.CAPUANO,J.CARLSSON,A.B.GONDIN,P.J.SCAMMELLS, JRNL AUTH 4 C.VALANT,D.M.THAL JRNL TITL STRUCTURE-GUIDED ALLOSTERIC MODULATION OF THE DELTA OPIOID JRNL TITL 2 RECEPTOR. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 41280124 JRNL DOI 10.1101/2025.10.16.682975 REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOLO, PHENIX, CRYOSPARC 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) : 1.950 REMARK 3 NUMBER OF PARTICLES : 124503 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 9YDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-25. REMARK 100 THE DEPOSITION ID IS D_1000300310. 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 : HUMAN DELTA OPIOID RECEPTOR REMARK 245 COMPLEX WITH MINI-GI AND REMARK 245 AGONIST DADLE 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 : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL 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 : 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, G, N, R, P 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 A -3 REMARK 465 CYS A -2 REMARK 465 THR A -1 REMARK 465 LEU A 0 REMARK 465 MET A 48 REMARK 465 ARG A 49 REMARK 465 ILE A 50 REMARK 465 LEU A 51 REMARK 465 HIS A 52 REMARK 465 GLY A 53 REMARK 465 GLY A 54 REMARK 465 SER A 55 REMARK 465 GLY A 56 REMARK 465 GLY A 57 REMARK 465 SER A 58 REMARK 465 GLY A 59 REMARK 465 GLY A 60 REMARK 465 THR A 61 REMARK 465 MET B -9 REMARK 465 HIS B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 HIS B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 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 MET N -21 REMARK 465 LYS N -20 REMARK 465 TYR N -19 REMARK 465 LEU N -18 REMARK 465 LEU N -17 REMARK 465 PRO N -16 REMARK 465 THR N -15 REMARK 465 ALA N -14 REMARK 465 ALA N -13 REMARK 465 ALA N -12 REMARK 465 GLY N -11 REMARK 465 LEU N -10 REMARK 465 LEU N -9 REMARK 465 LEU N -8 REMARK 465 LEU N -7 REMARK 465 ALA N -6 REMARK 465 ALA N -5 REMARK 465 GLN N -4 REMARK 465 PRO N -3 REMARK 465 ALA N -2 REMARK 465 MET N -1 REMARK 465 ALA N 0 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 ASP R -6 REMARK 465 TYR R -5 REMARK 465 LYS R -4 REMARK 465 ASP R -3 REMARK 465 ASP R -2 REMARK 465 ASP R -1 REMARK 465 ASP R 0 REMARK 465 ALA R 1 REMARK 465 GLU R 2 REMARK 465 PRO R 3 REMARK 465 ALA R 4 REMARK 465 PRO R 5 REMARK 465 SER R 6 REMARK 465 ALA R 7 REMARK 465 GLY R 8 REMARK 465 ALA R 9 REMARK 465 GLU R 10 REMARK 465 LEU R 11 REMARK 465 GLN R 12 REMARK 465 PRO R 13 REMARK 465 PRO R 14 REMARK 465 LEU R 15 REMARK 465 PHE R 16 REMARK 465 ALA R 17 REMARK 465 ASN R 18 REMARK 465 ALA R 19 REMARK 465 SER R 20 REMARK 465 ASP R 21 REMARK 465 ALA R 22 REMARK 465 TYR R 23 REMARK 465 PRO R 24 REMARK 465 SER R 25 REMARK 465 ALA R 26 REMARK 465 PHE R 27 REMARK 465 PRO R 28 REMARK 465 SER R 29 REMARK 465 ALA R 30 REMARK 465 GLY R 31 REMARK 465 ALA R 32 REMARK 465 ASN R 33 REMARK 465 ALA R 34 REMARK 465 SER R 35 REMARK 465 GLY R 36 REMARK 465 PRO R 37 REMARK 465 PRO R 38 REMARK 465 GLY R 39 REMARK 465 ALA R 40 REMARK 465 ARG R 41 REMARK 465 LYS R 335 REMARK 465 PRO R 336 REMARK 465 CYS R 337 REMARK 465 GLY R 338 REMARK 465 ARG R 339 REMARK 465 PRO R 340 REMARK 465 ASP R 341 REMARK 465 PRO R 342 REMARK 465 SER R 343 REMARK 465 SER R 344 REMARK 465 PHE R 345 REMARK 465 SER R 346 REMARK 465 ARG R 347 REMARK 465 ALA R 348 REMARK 465 ARG R 349 REMARK 465 GLU R 350 REMARK 465 ALA R 351 REMARK 465 THR R 352 REMARK 465 ALA R 353 REMARK 465 ARG R 354 REMARK 465 GLU R 355 REMARK 465 ARG R 356 REMARK 465 VAL R 357 REMARK 465 THR R 358 REMARK 465 ALA R 359 REMARK 465 CYS R 360 REMARK 465 THR R 361 REMARK 465 PRO R 362 REMARK 465 SER R 363 REMARK 465 ASP R 364 REMARK 465 GLY R 365 REMARK 465 PRO R 366 REMARK 465 GLY R 367 REMARK 465 GLY R 368 REMARK 465 GLY R 369 REMARK 465 ALA R 370 REMARK 465 ALA R 371 REMARK 465 ALA R 372 REMARK 465 HIS R 373 REMARK 465 HIS R 374 REMARK 465 HIS R 375 REMARK 465 HIS R 376 REMARK 465 HIS R 377 REMARK 465 HIS R 378 REMARK 465 HIS R 379 REMARK 465 HIS R 380 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 LYS A 5 CG CD CE NZ REMARK 470 LYS A 46 CG CD CE NZ REMARK 470 GLN A 47 CG CD OE1 NE2 REMARK 470 SER A 62 OG REMARK 470 LYS A 73 CG CD CE NZ REMARK 470 LYS A 152 CG CD CE NZ REMARK 470 LYS A 154 CG CD CE NZ REMARK 470 GLU A 156 CG CD OE1 OE2 REMARK 470 ASP A 157 CG OD1 OD2 REMARK 470 ARG A 164 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 169 CG CD OE1 OE2 REMARK 470 ASP A 170 CG OD1 OD2 REMARK 470 THR A 172 OG1 CG2 REMARK 470 GLU A 174 CG CD OE1 OE2 REMARK 470 SER B 2 OG REMARK 470 ARG B 129 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 130 CG CD OE1 OE2 REMARK 470 ARG B 134 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 215 CG CD OE1 OE2 REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 334 CG CD NE CZ NH1 NH2 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 73 -6.27 76.24 REMARK 500 CYS A 212 -169.20 -101.63 REMARK 500 ARG R 160 30.37 -97.64 REMARK 500 ARG R 291 -4.30 68.20 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-72825 RELATED DB: EMDB REMARK 900 HUMAN DELTA OPIOID RECEPTOR COMPLEX WITH MINI-GI AND AGONIST DADLE DBREF 9YDP A -3 241 PDB 9YDP 9YDP -3 241 DBREF 9YDP B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9YDP G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9YDP N -21 134 PDB 9YDP 9YDP -21 134 DBREF 9YDP R 2 372 UNP P41143 OPRD_HUMAN 2 372 DBREF 9YDP P 1 5 PDB 9YDP 9YDP 1 5 SEQADV 9YDP MET B -9 UNP P62873 EXPRESSION TAG SEQADV 9YDP HIS B -8 UNP P62873 EXPRESSION TAG SEQADV 9YDP HIS B -7 UNP P62873 EXPRESSION TAG SEQADV 9YDP HIS B -6 UNP P62873 EXPRESSION TAG SEQADV 9YDP HIS B -5 UNP P62873 EXPRESSION TAG SEQADV 9YDP HIS B -4 UNP P62873 EXPRESSION TAG SEQADV 9YDP HIS B -3 UNP P62873 EXPRESSION TAG SEQADV 9YDP GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9YDP SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9YDP SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9YDP GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 9YDP ASP R -6 UNP P41143 EXPRESSION TAG SEQADV 9YDP TYR R -5 UNP P41143 EXPRESSION TAG SEQADV 9YDP LYS R -4 UNP P41143 EXPRESSION TAG SEQADV 9YDP ASP R -3 UNP P41143 EXPRESSION TAG SEQADV 9YDP ASP R -2 UNP P41143 EXPRESSION TAG SEQADV 9YDP ASP R -1 UNP P41143 EXPRESSION TAG SEQADV 9YDP ASP R 0 UNP P41143 EXPRESSION TAG SEQADV 9YDP ALA R 1 UNP P41143 EXPRESSION TAG SEQADV 9YDP PHE R 27 UNP P41143 CYS 27 CONFLICT SEQADV 9YDP HIS R 373 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 374 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 375 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 376 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 377 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 378 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 379 UNP P41143 EXPRESSION TAG SEQADV 9YDP HIS R 380 UNP P41143 EXPRESSION TAG SEQRES 1 A 245 GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU SEQRES 2 A 245 ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP GLY SEQRES 3 A 245 GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU GLY SEQRES 4 A 245 ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN MET SEQRES 5 A 245 ARG ILE LEU HIS GLY GLY SER GLY GLY SER GLY GLY THR SEQRES 6 A 245 SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL SEQRES 7 A 245 ASN PHE HIS MET PHE ASP VAL GLY GLY GLN ARG ASP GLU SEQRES 8 A 245 ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA SEQRES 9 A 245 ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU SEQRES 10 A 245 GLN GLU ALA LEU ASN LEU PHE LYS SER ILE TRP ASN ASN SEQRES 11 A 245 ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN SEQRES 12 A 245 LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SEQRES 13 A 245 SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR SEQRES 14 A 245 THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP SEQRES 15 A 245 PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU SEQRES 16 A 245 PHE LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS SEQRES 17 A 245 TYR CYS TYR PRO HIS PHE THR CYS ALA VAL ASP THR GLU SEQRES 18 A 245 ASN ALA ARG ARG ILE PHE ASN ASP VAL THR ASP ILE ILE SEQRES 19 A 245 ILE LYS MET ASN LEU ARG ASP CYS GLY LEU PHE SEQRES 1 B 350 MET HIS HIS HIS HIS HIS HIS GLY SER SER GLY SER GLU SEQRES 2 B 350 LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS ASN SEQRES 3 B 350 GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA THR SEQRES 4 B 350 LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY ARG SEQRES 5 B 350 ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS LEU SEQRES 6 B 350 ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER ARG SEQRES 7 B 350 LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE ILE SEQRES 8 B 350 TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE PRO SEQRES 9 B 350 LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA PRO SEQRES 10 B 350 SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN ILE SEQRES 11 B 350 CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN VAL SEQRES 12 B 350 ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR LEU SEQRES 13 B 350 SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL THR SEQRES 14 B 350 SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE GLU SEQRES 15 B 350 THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR GLY SEQRES 16 B 350 ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG LEU SEQRES 17 B 350 PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU TRP SEQRES 18 B 350 ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR GLY SEQRES 19 B 350 HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO ASN SEQRES 20 B 350 GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR CYS SEQRES 21 B 350 ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET THR SEQRES 22 B 350 TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER VAL SEQRES 23 B 350 SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY TYR SEQRES 24 B 350 ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS ALA SEQRES 25 B 350 ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG VAL SEQRES 26 B 350 SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL ALA SEQRES 27 B 350 THR GLY SER TRP ASP SER 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 N 156 MET LYS TYR LEU LEU PRO THR ALA ALA ALA GLY LEU LEU SEQRES 2 N 156 LEU LEU ALA ALA GLN PRO ALA MET ALA GLN VAL GLN LEU SEQRES 3 N 156 GLN GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER SEQRES 4 N 156 LEU ARG LEU SER CYS ALA ALA SER GLY PHE THR PHE SER SEQRES 5 N 156 ASN TYR LYS MET ASN TRP VAL ARG GLN ALA PRO GLY LYS SEQRES 6 N 156 GLY LEU GLU TRP VAL SER ASP ILE SER GLN SER GLY ALA SEQRES 7 N 156 SER ILE SER TYR THR GLY SER VAL LYS GLY ARG PHE THR SEQRES 8 N 156 ILE SER ARG ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 9 N 156 MET ASN SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR SEQRES 10 N 156 CYS ALA ARG CYS PRO ALA PRO PHE THR ARG ASP CYS PHE SEQRES 11 N 156 ASP VAL THR SER THR THR TYR ALA TYR ARG GLY GLN GLY SEQRES 12 N 156 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 R 387 ASP TYR LYS ASP ASP ASP ASP ALA GLU PRO ALA PRO SER SEQRES 2 R 387 ALA GLY ALA GLU LEU GLN PRO PRO LEU PHE ALA ASN ALA SEQRES 3 R 387 SER ASP ALA TYR PRO SER ALA PHE PRO SER ALA GLY ALA SEQRES 4 R 387 ASN ALA SER GLY PRO PRO GLY ALA ARG SER ALA SER SER SEQRES 5 R 387 LEU ALA LEU ALA ILE ALA ILE THR ALA LEU TYR SER ALA SEQRES 6 R 387 VAL CYS ALA VAL GLY LEU LEU GLY ASN VAL LEU VAL MET SEQRES 7 R 387 PHE GLY ILE VAL ARG TYR THR LYS MET LYS THR ALA THR SEQRES 8 R 387 ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU SEQRES 9 R 387 ALA THR SER THR LEU PRO PHE GLN SER ALA LYS TYR LEU SEQRES 10 R 387 MET GLU THR TRP PRO PHE GLY GLU LEU LEU CYS LYS ALA SEQRES 11 R 387 VAL LEU SER ILE ASP TYR TYR ASN MET PHE THR SER ILE SEQRES 12 R 387 PHE THR LEU THR MET MET SER VAL ASP ARG TYR ILE ALA SEQRES 13 R 387 VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO SEQRES 14 R 387 ALA LYS ALA LYS LEU ILE ASN ILE CYS ILE TRP VAL LEU SEQRES 15 R 387 ALA SER GLY VAL GLY VAL PRO ILE MET VAL MET ALA VAL SEQRES 16 R 387 THR ARG PRO ARG ASP GLY ALA VAL VAL CYS MET LEU GLN SEQRES 17 R 387 PHE PRO SER PRO SER TRP TYR TRP ASP THR VAL THR LYS SEQRES 18 R 387 ILE CYS VAL PHE LEU PHE ALA PHE VAL VAL PRO ILE LEU SEQRES 19 R 387 ILE ILE THR VAL CYS TYR GLY LEU MET LEU LEU ARG LEU SEQRES 20 R 387 ARG SER VAL ARG LEU LEU SER GLY SER LYS GLU LYS ASP SEQRES 21 R 387 ARG SER LEU ARG ARG ILE THR ARG MET VAL LEU VAL VAL SEQRES 22 R 387 VAL GLY ALA PHE VAL VAL CYS TRP ALA PRO ILE HIS ILE SEQRES 23 R 387 PHE VAL ILE VAL TRP THR LEU VAL ASP ILE ASP ARG ARG SEQRES 24 R 387 ASP PRO LEU VAL VAL ALA ALA LEU HIS LEU CYS ILE ALA SEQRES 25 R 387 LEU GLY TYR ALA ASN SER SER LEU ASN PRO VAL LEU TYR SEQRES 26 R 387 ALA PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE ARG GLN SEQRES 27 R 387 LEU CYS ARG LYS PRO CYS GLY ARG PRO ASP PRO SER SER SEQRES 28 R 387 PHE SER ARG ALA ARG GLU ALA THR ALA ARG GLU ARG VAL SEQRES 29 R 387 THR ALA CYS THR PRO SER ASP GLY PRO GLY GLY GLY ALA SEQRES 30 R 387 ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 P 5 TYR DAL GLY PHE DLE HET DAL P 2 5 HET DLE P 5 9 HETNAM DAL D-ALANINE HETNAM DLE D-LEUCINE FORMUL 6 DAL C3 H7 N O2 FORMUL 6 DLE C6 H13 N O2 FORMUL 7 HOH *93(H2 O) HELIX 1 AA1 SER A 1 ARG A 27 1 27 HELIX 2 AA2 ASP A 37 ILE A 44 5 8 HELIX 3 AA3 LYS A 90 ASN A 96 5 7 HELIX 4 AA4 ASP A 109 ASN A 111 5 3 HELIX 5 AA5 ARG A 112 ASN A 125 1 14 HELIX 6 AA6 LYS A 140 GLY A 151 1 12 HELIX 7 AA7 LYS A 154 TYR A 158 5 5 HELIX 8 AA8 PHE A 159 TYR A 165 5 7 HELIX 9 AA9 ASP A 178 SER A 199 1 22 HELIX 10 AB1 GLU A 217 CYS A 238 1 22 HELIX 11 AB2 GLU B 3 ALA B 26 1 24 HELIX 12 AB3 THR B 29 THR B 34 1 6 HELIX 13 AB4 THR G 6 ASN G 24 1 19 HELIX 14 AB5 LYS G 29 HIS G 44 1 16 HELIX 15 AB6 THR N 28 TYR N 32 5 5 HELIX 16 AB7 GLY N 62 LYS N 65 5 4 HELIX 17 AB8 LYS N 87 THR N 91 5 5 HELIX 18 AB9 ALA R 43 TYR R 77 1 35 HELIX 19 AC1 THR R 82 SER R 100 1 19 HELIX 20 AC2 THR R 101 GLU R 112 1 12 HELIX 21 AC3 PHE R 116 HIS R 152 1 37 HELIX 22 AC4 HIS R 152 ARG R 160 1 9 HELIX 23 AC5 THR R 161 ALA R 176 1 16 HELIX 24 AC6 ALA R 176 MET R 186 1 11 HELIX 25 AC7 PRO R 205 PHE R 222 1 18 HELIX 26 AC8 PHE R 222 ARG R 241 1 20 HELIX 27 AC9 GLY R 248 VAL R 287 1 40 HELIX 28 AD1 ASP R 293 ALA R 319 1 27 HELIX 29 AD2 ASP R 322 ARG R 334 1 13 SHEET 1 AA1 6 ILE A 64 VAL A 71 0 SHEET 2 AA1 6 VAL A 74 VAL A 81 -1 O PHE A 76 N PHE A 69 SHEET 3 AA1 6 GLU A 28 GLY A 35 1 N VAL A 29 O HIS A 77 SHEET 4 AA1 6 ALA A 100 ASP A 106 1 O ILE A 102 N LEU A 34 SHEET 5 AA1 6 SER A 133 ASN A 139 1 O PHE A 137 N VAL A 105 SHEET 6 AA1 6 CYS A 206 PHE A 210 1 O HIS A 209 N LEU A 138 SHEET 1 AA2 4 THR B 47 ARG B 52 0 SHEET 2 AA2 4 PHE B 335 TRP B 339 -1 O LEU B 336 N LEU B 51 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N THR B 329 O LYS B 337 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 TRP B 63 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 ASN B 88 N ASP B 83 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 ILE B 120 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 ALA B 140 -1 O ARG B 137 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 CYS B 148 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 PHE B 180 N CYS B 166 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O VAL B 200 N SER B 191 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 ALA B 242 N CYS B 233 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLN B 259 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 LEU B 286 N SER B 277 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O GLY B 306 N VAL B 296 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 LEU N 18 SER N 25 -1 O SER N 25 N GLN N 3 SHEET 3 AA9 4 THR N 78 MET N 83 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N SER N 71 O TYR N 80 SHEET 1 AB1 6 LEU N 11 VAL N 12 0 SHEET 2 AB1 6 THR N 122 VAL N 126 1 O THR N 125 N VAL N 12 SHEET 3 AB1 6 ALA N 92 ARG N 98 -1 N ALA N 92 O VAL N 124 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB1 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SHEET 1 AB2 2 ALA R 187 ARG R 192 0 SHEET 2 AB2 2 ALA R 195 LEU R 200 -1 O ALA R 195 N ARG R 192 SSBOND 1 CYS N 99 CYS N 107 1555 1555 2.03 SSBOND 2 CYS R 121 CYS R 198 1555 1555 2.03 LINK C TYR P 1 N DAL P 2 1555 1555 1.33 LINK C DAL P 2 N GLY P 3 1555 1555 1.33 LINK C PHE P 4 N DLE P 5 1555 1555 1.33 CISPEP 1 SER R 204 PRO R 205 0 -10.20 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