HEADER SIGNALING PROTEIN 04-SEP-24 9JFK TITLE CRYO-EM STRUCTURE OF [PEN5]-UROTENSIN (4-11)-BOUNDED HUMAN UROTENSIN TITLE 2 RECEPTOR (UTS2R)-GQ COMPLEX 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: A; COMPND 5 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: G SUBUNIT Q (GI2-MINI-GQ CHIMERIC); COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 13 GAMMA-2; COMPND 14 CHAIN: D; COMPND 15 SYNONYM: G GAMMA-I; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 4; COMPND 18 MOLECULE: NANO BODY 35; COMPND 19 CHAIN: N; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: UROTENSIN-2 RECEPTOR; COMPND 23 CHAIN: R; COMPND 24 SYNONYM: UR-2-R,G-PROTEIN COUPLED RECEPTOR 14,UROTENSIN II RECEPTOR, COMPND 25 UR-II-R; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: ASP-LE1-PHE-TRP-LYS-TYR-CYS-VAL; COMPND 29 CHAIN: C; 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: 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 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: GNG2; SOURCE 19 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 23 ORGANISM_TAXID: 9844; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 MOL_ID: 5; SOURCE 27 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 28 ORGANISM_COMMON: HUMAN; SOURCE 29 ORGANISM_TAXID: 9606; SOURCE 30 GENE: UTS2R, GPR14; SOURCE 31 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 33 MOL_ID: 6; SOURCE 34 SYNTHETIC: YES; SOURCE 35 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 36 ORGANISM_TAXID: 32630 KEYWDS CRYO-EM, GPCR, UROTENSIN RECEPTOR, UTS2R, GQ, AGONIST, [PEN5]- KEYWDS 2 UROTENSIN (4-11), COMPLEX, SIGNALING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR H.E.XU,C.YOU,T.GAO,J.DUAN REVDAT 1 03-DEC-25 9JFK 0 JRNL AUTH T.GAO,C.YOU,Y.CAO,X.XU,Q.YUAN,S.SHEN,H.E.XU,J.DUAN JRNL TITL STRUCTURAL INSIGHTS INTO HORMONE RECOGNITION AND G-PROTEIN JRNL TITL 2 COUPLING OF THE UROTENSIN-II RECEPTOR. JRNL REF J.BIOL.CHEM. V. 301 10794 2025 JRNL REFN ESSN 1083-351X JRNL PMID 41062066 JRNL DOI 10.1016/J.JBC.2025.110794 REMARK 2 REMARK 2 RESOLUTION. 3.23 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, 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) : 3.230 REMARK 3 NUMBER OF PARTICLES : 168270 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 9JFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 10-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1300051068. 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 [PEN5] REMARK 245 -UROTENSIN (4-11)-BOUNDED HUMAN REMARK 245 UROTENSIN RECEPTOR (UTS2R)-GQ REMARK 245 COMPLEX 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 : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 5000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 30000.00 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) : 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 APPLY THE FOLLOWING TO CHAINS: A, B, D, N, R, C 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 -4 REMARK 465 GLY A -3 REMARK 465 SER A -2 REMARK 465 LEU A -1 REMARK 465 LEU A 0 REMARK 465 GLN A 1 REMARK 465 SER A 2 REMARK 465 GLU A 3 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 SER B 3 REMARK 465 THR B 4 REMARK 465 GLN B 52 REMARK 465 MET B 53 REMARK 465 ARG B 54 REMARK 465 ILE B 55 REMARK 465 LEU B 56 REMARK 465 HIS B 57 REMARK 465 GLY B 58 REMARK 465 GLY B 59 REMARK 465 SER B 60 REMARK 465 GLY B 61 REMARK 465 GLY B 62 REMARK 465 SER B 63 REMARK 465 GLY B 64 REMARK 465 GLY B 65 REMARK 465 THR B 66 REMARK 465 ALA D 2 REMARK 465 SER D 3 REMARK 465 ASN D 4 REMARK 465 ASN D 5 REMARK 465 THR D 6 REMARK 465 ALA D 7 REMARK 465 SER D 8 REMARK 465 ILE D 9 REMARK 465 ALA D 10 REMARK 465 ARG D 62 REMARK 465 GLU D 63 REMARK 465 LYS D 64 REMARK 465 LYS D 65 REMARK 465 PHE D 66 REMARK 465 PHE D 67 REMARK 465 CYS D 68 REMARK 465 ALA D 69 REMARK 465 ILE D 70 REMARK 465 LEU D 71 REMARK 465 SER N 127 REMARK 465 SER N 128 REMARK 465 MET R 1 REMARK 465 ALA R 2 REMARK 465 LEU R 3 REMARK 465 THR R 4 REMARK 465 PRO R 5 REMARK 465 GLU R 6 REMARK 465 SER R 7 REMARK 465 PRO R 8 REMARK 465 SER R 9 REMARK 465 SER R 10 REMARK 465 PHE R 11 REMARK 465 PRO R 12 REMARK 465 GLY R 13 REMARK 465 LEU R 14 REMARK 465 ALA R 15 REMARK 465 ALA R 16 REMARK 465 THR R 17 REMARK 465 GLY R 18 REMARK 465 SER R 19 REMARK 465 SER R 20 REMARK 465 VAL R 21 REMARK 465 PRO R 22 REMARK 465 GLU R 23 REMARK 465 PRO R 24 REMARK 465 PRO R 25 REMARK 465 GLY R 26 REMARK 465 GLY R 27 REMARK 465 PRO R 28 REMARK 465 ASN R 29 REMARK 465 ALA R 30 REMARK 465 THR R 31 REMARK 465 LEU R 32 REMARK 465 ASN R 33 REMARK 465 SER R 34 REMARK 465 SER R 35 REMARK 465 TRP R 36 REMARK 465 ALA R 37 REMARK 465 SER R 38 REMARK 465 PRO R 39 REMARK 465 THR R 40 REMARK 465 GLU R 41 REMARK 465 PRO R 42 REMARK 465 SER R 43 REMARK 465 SER R 44 REMARK 465 SER R 245 REMARK 465 PHE R 246 REMARK 465 LYS R 247 REMARK 465 ARG R 248 REMARK 465 ALA R 249 REMARK 465 ARG R 250 REMARK 465 ARG R 251 REMARK 465 PRO R 252 REMARK 465 GLY R 253 REMARK 465 ALA R 254 REMARK 465 ARG R 255 REMARK 465 ALA R 256 REMARK 465 ARG R 327 REMARK 465 GLY R 328 REMARK 465 ARG R 329 REMARK 465 VAL R 330 REMARK 465 ARG R 331 REMARK 465 GLY R 332 REMARK 465 PRO R 333 REMARK 465 GLY R 334 REMARK 465 SER R 335 REMARK 465 GLY R 336 REMARK 465 GLY R 337 REMARK 465 GLY R 338 REMARK 465 ARG R 339 REMARK 465 GLY R 340 REMARK 465 PRO R 341 REMARK 465 VAL R 342 REMARK 465 PRO R 343 REMARK 465 SER R 344 REMARK 465 LEU R 345 REMARK 465 GLN R 346 REMARK 465 PRO R 347 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 LEU A 4 CG CD1 CD2 REMARK 470 ASP A 5 CG OD1 OD2 REMARK 470 GLN A 6 CG CD OE1 NE2 REMARK 470 LEU A 7 CG CD1 CD2 REMARK 470 ARG A 8 CG CD NE CZ NH1 NH2 REMARK 470 GLN A 9 CG CD OE1 NE2 REMARK 470 GLU A 10 CG CD OE1 OE2 REMARK 470 GLU A 12 CG CD OE1 OE2 REMARK 470 GLN A 13 CG CD OE1 NE2 REMARK 470 LYS A 15 CG CD CE NZ REMARK 470 ASN A 16 CG OD1 ND2 REMARK 470 ARG A 19 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 20 CG OD1 OD2 REMARK 470 ARG A 42 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 96 CG CD NE CZ NH1 NH2 REMARK 470 SER A 97 OG REMARK 470 ASP A 170 CG OD1 OD2 REMARK 470 GLU A 172 CG CD OE1 OE2 REMARK 470 THR A 173 OG1 CG2 REMARK 470 MET A 217 CG SD CE REMARK 470 THR A 221 OG1 CG2 REMARK 470 SER A 245 OG REMARK 470 SER A 265 OG REMARK 470 ASP A 267 CG OD1 OD2 REMARK 470 ASP A 303 CG OD1 OD2 REMARK 470 SER A 331 OG REMARK 470 GLU B 28 CG CD OE1 OE2 REMARK 470 LYS B 29 CG CD CE NZ REMARK 470 ARG B 32 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 42 CG OD1 OD2 REMARK 470 LYS B 78 CG CD CE NZ REMARK 470 ASP B 102 CG OD1 OD2 REMARK 470 ARG B 135 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 152 CG CD CE NZ REMARK 470 ARG B 169 CG CD NE CZ NH1 NH2 REMARK 470 ASP B 206 CG OD1 OD2 REMARK 470 ARG B 241 CG CD NE CZ NH1 NH2 REMARK 470 VAL B 246 CG1 CG2 REMARK 470 GLN D 11 CG CD OE1 NE2 REMARK 470 ARG D 13 CG CD NE CZ NH1 NH2 REMARK 470 LEU D 15 CG CD1 CD2 REMARK 470 GLU D 17 CG CD OE1 OE2 REMARK 470 LYS D 20 CG CD CE NZ REMARK 470 ASN D 24 CG OD1 ND2 REMARK 470 VAL D 54 CG1 CG2 REMARK 470 GLU D 58 CG CD OE1 OE2 REMARK 470 TYR R 87 CG CD1 CD2 CE1 CE2 CZ OH 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 CD2 LEU R 272 OT1 CHO R 401 1.37 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ASP C 1 C LE1 C 2 N 0.151 REMARK 500 LE1 C 2 C PHE C 3 N 0.182 REMARK 500 PHE C 3 C TRP C 4 N 0.179 REMARK 500 TRP C 4 C LYS C 5 N 0.153 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 ARG A 52 -138.88 39.39 REMARK 500 GLU A 130 -5.48 74.85 REMARK 500 LEU A 190 119.34 -160.89 REMARK 500 ASP A 291 48.21 -90.42 REMARK 500 ALA A 309 -163.50 58.49 REMARK 500 PHE B 100 35.47 -98.86 REMARK 500 ARG B 117 -1.11 69.40 REMARK 500 VAL N 2 45.48 35.11 REMARK 500 ASP N 109 40.41 -108.09 REMARK 500 VAL R 112 70.07 49.27 REMARK 500 THR R 113 53.81 37.76 REMARK 500 GLU R 115 -103.40 52.24 REMARK 500 GLN R 160 32.70 -95.60 REMARK 500 LEU R 190 170.13 67.36 REMARK 500 ARG R 193 -167.94 -172.56 REMARK 500 LEU R 200 74.65 -116.01 REMARK 500 THR R 316 -50.29 -121.38 REMARK 500 TRP C 4 -152.31 58.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61433 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF PEN5]-UROTENSIN (4-11)-BOUNDED HUMAN UROTENSIN REMARK 900 RECEPTOR (UTS2R)-GQ COMPLEX DBREF 9JFK A 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9JFK B 1 246 PDB 9JFK 9JFK 1 246 DBREF 9JFK D 2 71 UNP P59768 GBG2_HUMAN 2 71 DBREF 9JFK N 1 128 PDB 9JFK 9JFK 1 128 DBREF 9JFK R 1 347 UNP Q9UKP6 UR2R_HUMAN 1 347 DBREF 9JFK C 1 8 PDB 9JFK 9JFK 1 8 SEQADV 9JFK MET A -4 UNP P62873 INITIATING METHIONINE SEQADV 9JFK GLY A -3 UNP P62873 EXPRESSION TAG SEQADV 9JFK SER A -2 UNP P62873 EXPRESSION TAG SEQADV 9JFK LEU A -1 UNP P62873 EXPRESSION TAG SEQADV 9JFK LEU A 0 UNP P62873 EXPRESSION TAG SEQADV 9JFK GLN A 1 UNP P62873 EXPRESSION TAG SEQRES 1 A 345 MET GLY SER LEU LEU GLN SER GLU LEU ASP GLN LEU ARG SEQRES 2 A 345 GLN GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA SEQRES 3 A 345 ARG LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR SEQRES 4 A 345 ASN ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR SEQRES 5 A 345 ARG ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA SEQRES 6 A 345 MET HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SEQRES 7 A 345 SER GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR SEQRES 8 A 345 THR ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP SEQRES 9 A 345 VAL MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL SEQRES 10 A 345 ALA CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN SEQRES 11 A 345 LEU LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU SEQRES 12 A 345 LEU ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE SEQRES 13 A 345 LEU ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR SEQRES 14 A 345 THR CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR SEQRES 15 A 345 THR THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SEQRES 16 A 345 SER LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA SEQRES 17 A 345 CYS ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY SEQRES 18 A 345 MET CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE SEQRES 19 A 345 ASN ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA SEQRES 20 A 345 THR GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU SEQRES 21 A 345 ARG ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN SEQRES 22 A 345 ILE ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER SEQRES 23 A 345 GLY ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS SEQRES 24 A 345 ASN VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL SEQRES 25 A 345 LEU ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL SEQRES 26 A 345 THR ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SEQRES 27 A 345 SER PHE LEU LYS ILE TRP ASN SEQRES 1 B 246 MET GLY SER THR VAL SER ALA GLU ASP LYS ALA ALA ALA SEQRES 2 B 246 GLU ARG SER LYS MET ILE ASP LYS ASN LEU ARG GLU ASP SEQRES 3 B 246 GLY GLU LYS ALA ARG ARG THR LEU ARG LEU LEU LEU LEU SEQRES 4 B 246 GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 B 246 MET ARG ILE LEU HIS GLY GLY SER GLY GLY SER GLY GLY SEQRES 6 B 246 THR SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS SEQRES 7 B 246 VAL ASN PHE HIS MET PHE ASP VAL GLY GLY GLN ARG ASP SEQRES 8 B 246 GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR SEQRES 9 B 246 ALA ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG SEQRES 10 B 246 LEU GLN GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN SEQRES 11 B 246 ASN ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU SEQRES 12 B 246 ASN LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY SEQRES 13 B 246 LYS SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG SEQRES 14 B 246 TYR THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU SEQRES 15 B 246 ASP PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG LYS SEQRES 16 B 246 GLU PHE VAL ASP ILE SER THR ALA SER GLY ASP GLY ARG SEQRES 17 B 246 HIS ILE CYS TYR PRO HIS PHE THR CYS ALA VAL ASP THR SEQRES 18 B 246 GLU ASN ALA ARG ARG ILE PHE ASN ASP CYS LYS ASP ILE SEQRES 19 B 246 ILE LEU GLN MET ASN LEU ARG GLU TYR ASN LEU VAL SEQRES 1 D 70 ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG LYS SEQRES 2 D 70 LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP ARG SEQRES 3 D 70 ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA TYR SEQRES 4 D 70 CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR PRO SEQRES 5 D 70 VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS PHE SEQRES 6 D 70 PHE CYS ALA ILE LEU SEQRES 1 N 128 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 128 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 128 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 128 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 128 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 128 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 128 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 128 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 128 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 R 347 MET ALA LEU THR PRO GLU SER PRO SER SER PHE PRO GLY SEQRES 2 R 347 LEU ALA ALA THR GLY SER SER VAL PRO GLU PRO PRO GLY SEQRES 3 R 347 GLY PRO ASN ALA THR LEU ASN SER SER TRP ALA SER PRO SEQRES 4 R 347 THR GLU PRO SER SER LEU GLU ASP LEU VAL ALA THR GLY SEQRES 5 R 347 THR ILE GLY THR LEU LEU SER ALA MET GLY VAL VAL GLY SEQRES 6 R 347 VAL VAL GLY ASN ALA TYR THR LEU VAL VAL THR CYS ARG SEQRES 7 R 347 SER LEU ARG ALA VAL ALA SER MET TYR VAL TYR VAL VAL SEQRES 8 R 347 ASN LEU ALA LEU ALA ASP LEU LEU TYR LEU LEU SER ILE SEQRES 9 R 347 PRO PHE ILE VAL ALA THR TYR VAL THR LYS GLU TRP HIS SEQRES 10 R 347 PHE GLY ASP VAL GLY CYS ARG VAL LEU PHE GLY LEU ASP SEQRES 11 R 347 PHE LEU THR MET HIS ALA SER ILE PHE THR LEU THR VAL SEQRES 12 R 347 MET SER SER GLU ARG TYR ALA ALA VAL LEU ARG PRO LEU SEQRES 13 R 347 ASP THR VAL GLN ARG PRO LYS GLY TYR ARG LYS LEU LEU SEQRES 14 R 347 ALA LEU GLY THR TRP LEU LEU ALA LEU LEU LEU THR LEU SEQRES 15 R 347 PRO VAL MET LEU ALA MET ARG LEU VAL ARG ARG GLY PRO SEQRES 16 R 347 LYS SER LEU CYS LEU PRO ALA TRP GLY PRO ARG ALA HIS SEQRES 17 R 347 ARG ALA TYR LEU THR LEU LEU PHE ALA THR SER ILE ALA SEQRES 18 R 347 GLY PRO GLY LEU LEU ILE GLY LEU LEU TYR ALA ARG LEU SEQRES 19 R 347 ALA ARG ALA TYR ARG ARG SER GLN ARG ALA SER PHE LYS SEQRES 20 R 347 ARG ALA ARG ARG PRO GLY ALA ARG ALA LEU ARG LEU VAL SEQRES 21 R 347 LEU GLY ILE VAL LEU LEU PHE TRP ALA CYS PHE LEU PRO SEQRES 22 R 347 PHE TRP LEU TRP GLN LEU LEU ALA GLN TYR HIS GLN ALA SEQRES 23 R 347 PRO LEU ALA PRO ARG THR ALA ARG ILE VAL ASN TYR LEU SEQRES 24 R 347 THR THR CYS LEU THR TYR GLY ASN SER CYS ALA ASN PRO SEQRES 25 R 347 PHE LEU TYR THR LEU LEU THR ARG ASN TYR ARG ASP HIS SEQRES 26 R 347 LEU ARG GLY ARG VAL ARG GLY PRO GLY SER GLY GLY GLY SEQRES 27 R 347 ARG GLY PRO VAL PRO SER LEU GLN PRO SEQRES 1 C 8 ASP LE1 PHE TRP LYS TYR CYS VAL HET LE1 C 2 8 HET CHO R 401 32 HET CHO R 402 32 HETNAM LE1 3-SULFANYL-L-VALINE HETNAM CHO GLYCOCHENODEOXYCHOLIC ACID HETSYN LE1 L-LE1ICILLAMINE; L-PENICILLAMINE FORMUL 6 LE1 C5 H11 N O2 S FORMUL 7 CHO 2(C26 H43 N O5) HELIX 1 AA1 LEU A 4 CYS A 25 1 22 HELIX 2 AA2 THR A 29 THR A 34 1 6 HELIX 3 AA3 THR A 128 ASN A 132 5 5 HELIX 4 AA4 SER B 6 ARG B 31 1 26 HELIX 5 AA5 LYS B 95 ASN B 101 5 7 HELIX 6 AA6 ARG B 117 ASN B 130 1 14 HELIX 7 AA7 LYS B 145 GLY B 156 1 12 HELIX 8 AA8 LYS B 159 PHE B 164 1 6 HELIX 9 AA9 PRO B 165 ALA B 168 5 4 HELIX 10 AB1 ASP B 183 GLY B 205 1 23 HELIX 11 AB2 GLU B 222 TYR B 243 1 22 HELIX 12 AB3 ALA D 12 ASN D 24 1 13 HELIX 13 AB4 LYS D 29 HIS D 44 1 16 HELIX 14 AB5 GLU R 46 SER R 79 1 34 HELIX 15 AB6 MET R 86 LEU R 102 1 17 HELIX 16 AB7 LEU R 102 ALA R 109 1 8 HELIX 17 AB8 GLY R 119 ARG R 154 1 36 HELIX 18 AB9 ARG R 154 GLN R 160 1 7 HELIX 19 AC1 GLY R 164 MET R 188 1 25 HELIX 20 AC2 ALA R 207 ILE R 220 1 14 HELIX 21 AC3 ILE R 220 GLN R 242 1 23 HELIX 22 AC4 ARG R 258 PHE R 271 1 14 HELIX 23 AC5 LEU R 272 TRP R 275 5 4 HELIX 24 AC6 LEU R 276 ALA R 281 1 6 HELIX 25 AC7 GLN R 282 HIS R 284 5 3 HELIX 26 AC8 ALA R 289 THR R 316 1 28 HELIX 27 AC9 THR R 319 LEU R 326 1 8 SHEET 1 AA1 4 ARG A 46 THR A 50 0 SHEET 2 AA1 4 LEU A 336 ASN A 340 -1 O ASN A 340 N ARG A 46 SHEET 3 AA1 4 VAL A 327 SER A 331 -1 N THR A 329 O LYS A 337 SHEET 4 AA1 4 VAL A 315 VAL A 320 -1 N SER A 316 O GLY A 330 SHEET 1 AA2 4 ILE A 58 TRP A 63 0 SHEET 2 AA2 4 LEU A 69 SER A 74 -1 O ALA A 73 N TYR A 59 SHEET 3 AA2 4 LYS A 78 ASP A 83 -1 O ILE A 80 N SER A 72 SHEET 4 AA2 4 ASN A 88 PRO A 94 -1 O ILE A 93 N LEU A 79 SHEET 1 AA3 4 VAL A 100 TYR A 105 0 SHEET 2 AA3 4 TYR A 111 GLY A 116 -1 O GLY A 115 N THR A 102 SHEET 3 AA3 4 CYS A 121 ASN A 125 -1 O TYR A 124 N VAL A 112 SHEET 4 AA3 4 ARG A 134 LEU A 139 -1 O LEU A 139 N CYS A 121 SHEET 1 AA4 4 LEU A 146 PHE A 151 0 SHEET 2 AA4 4 GLN A 156 SER A 161 -1 O SER A 160 N SER A 147 SHEET 3 AA4 4 THR A 165 ASP A 170 -1 O THR A 165 N SER A 161 SHEET 4 AA4 4 GLN A 176 THR A 181 -1 O THR A 177 N LEU A 168 SHEET 1 AA5 4 SER A 189 LEU A 192 0 SHEET 2 AA5 4 LEU A 198 ALA A 203 -1 O VAL A 200 N SER A 191 SHEET 3 AA5 4 SER A 207 ASP A 212 -1 O TRP A 211 N PHE A 199 SHEET 4 AA5 4 CYS A 218 PHE A 222 -1 O PHE A 222 N ALA A 208 SHEET 1 AA6 4 ILE A 229 PHE A 234 0 SHEET 2 AA6 4 ALA A 240 SER A 245 -1 O GLY A 244 N ALA A 231 SHEET 3 AA6 4 CYS A 250 ASP A 254 -1 O PHE A 253 N PHE A 241 SHEET 4 AA6 4 GLN A 259 TYR A 264 -1 O LEU A 261 N LEU A 252 SHEET 1 AA7 4 ILE A 273 PHE A 278 0 SHEET 2 AA7 4 LEU A 284 TYR A 289 -1 O LEU A 286 N SER A 277 SHEET 3 AA7 4 ASN A 293 ASP A 298 -1 O ASN A 293 N TYR A 289 SHEET 4 AA7 4 ARG A 304 VAL A 307 -1 O GLY A 306 N VAL A 296 SHEET 1 AA8 5 ILE B 69 VAL B 76 0 SHEET 2 AA8 5 VAL B 79 VAL B 86 -1 O PHE B 81 N PHE B 74 SHEET 3 AA8 5 LEU B 34 GLY B 40 1 N LEU B 34 O HIS B 82 SHEET 4 AA8 5 ALA B 105 ASP B 111 1 O ILE B 107 N LEU B 39 SHEET 5 AA8 5 SER B 138 ASN B 144 1 O PHE B 142 N VAL B 110 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 LEU N 18 SER N 25 -1 O ALA N 23 N GLN N 5 SHEET 3 AA9 4 THR N 78 MET N 83 -1 O LEU N 79 N CYS N 22 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N ASP N 73 O THR N 78 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 ALA N 97 N ASN N 35 SHEET 5 AB1 5 THR N 122 VAL N 124 -1 O THR N 122 N TYR N 94 SSBOND 1 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 2 CYS N 99 CYS N 107 1555 1555 2.03 SSBOND 3 CYS R 123 CYS R 199 1555 1555 2.04 SSBOND 4 LE1 C 2 CYS C 7 1555 1555 2.09 LINK C ASP C 1 N LE1 C 2 1555 1555 1.49 LINK C LE1 C 2 N PHE C 3 1555 1555 1.52 CISPEP 1 ASP C 1 LE1 C 2 0 0.01 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