HEADER STRUCTURAL PROTEIN 19-FEB-25 9LYC TITLE CRYO-EM STRUCTURE OF GPR3-G PROTEIN-DIMER COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR 3; COMPND 3 CHAIN: A, D; COMPND 4 SYNONYM: ACCA ORPHAN RECEPTOR; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 14 ISOFORMS SHORT; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 20 GAMMA-2; COMPND 21 CHAIN: G; COMPND 22 SYNONYM: G GAMMA-I; COMPND 23 ENGINEERED: YES; COMPND 24 MOL_ID: 5; COMPND 25 MOLECULE: NANOBODY 35; COMPND 26 CHAIN: N; COMPND 27 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: GPR3, ACCA; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNAS, GNAS1, GSP; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: GNG2; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, G PROTEIN, CRYO-EM, MEMBRANE PROTEIN, STRUCTURAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR T.HUA,Z.J.LIU,X.T.LI,H.CHANG REVDAT 1 09-APR-25 9LYC 0 JRNL AUTH H.CHANG,X.T.LI,H.Q.TU,L.J.WU,Y.N.YU,J.L.LIU,N.CHEN,W.L.SHEN, JRNL AUTH 2 T.HUA JRNL TITL STRUCTURAL BASIS OF OLIGOMERIZATION-MODULATED ACTIVATION AND JRNL TITL 2 AUTOINHIBITION OF ORPHAN RECEPTOR GPR3. JRNL REF CELL REP V. 44 2025 JRNL REFN ESSN 2211-1247 JRNL DOI 10.1016/J.CELREP.2025.115478 REMARK 2 REMARK 2 RESOLUTION. 3.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 3.060 REMARK 3 NUMBER OF PARTICLES : 212083 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 9LYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056817. 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 : TERNARY COMPLEX OF GPR3 WITH REMARK 245 GUANINE NUCLEOTIDE-BINDING REMARK 245 PROTEIN AND NANOBODY 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 : 7.50 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 BIOQUANTUM (6K X REMARK 245 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 : 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, C, D, G, N 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 LEU A 233 REMARK 465 LEU A 234 REMARK 465 PRO A 235 REMARK 465 ALA A 236 REMARK 465 SER A 237 REMARK 465 HIS A 238 REMARK 465 TYR A 239 REMARK 465 VAL A 240 REMARK 465 CYS A 313 REMARK 465 CYS A 314 REMARK 465 MET C 1 REMARK 465 GLY C 2 REMARK 465 CYS C 3 REMARK 465 LEU C 4 REMARK 465 GLY C 5 REMARK 465 ASN C 6 REMARK 465 SER C 7 REMARK 465 LEU C 63 REMARK 465 HIS C 64 REMARK 465 VAL C 65 REMARK 465 ASN C 66 REMARK 465 GLY C 67 REMARK 465 PHE C 68 REMARK 465 ASN C 69 REMARK 465 GLY C 70 REMARK 465 GLU C 71 REMARK 465 GLY C 72 REMARK 465 GLY C 73 REMARK 465 GLU C 74 REMARK 465 GLU C 75 REMARK 465 ASP C 76 REMARK 465 PRO C 77 REMARK 465 GLN C 78 REMARK 465 ALA C 79 REMARK 465 ALA C 80 REMARK 465 ARG C 81 REMARK 465 SER C 82 REMARK 465 ASN C 83 REMARK 465 SER C 84 REMARK 465 ASP C 85 REMARK 465 GLY C 86 REMARK 465 GLU C 87 REMARK 465 LYS C 88 REMARK 465 ALA C 89 REMARK 465 THR C 90 REMARK 465 LYS C 91 REMARK 465 VAL C 92 REMARK 465 GLN C 93 REMARK 465 ASP C 94 REMARK 465 ILE C 95 REMARK 465 LYS C 96 REMARK 465 ASN C 97 REMARK 465 ASN C 98 REMARK 465 LEU C 99 REMARK 465 LYS C 100 REMARK 465 GLU C 101 REMARK 465 ALA C 102 REMARK 465 ILE C 103 REMARK 465 GLU C 104 REMARK 465 THR C 105 REMARK 465 ILE C 106 REMARK 465 VAL C 107 REMARK 465 ALA C 108 REMARK 465 ALA C 109 REMARK 465 MET C 110 REMARK 465 SER C 111 REMARK 465 ASN C 112 REMARK 465 LEU C 113 REMARK 465 VAL C 114 REMARK 465 PRO C 115 REMARK 465 PRO C 116 REMARK 465 VAL C 117 REMARK 465 GLU C 118 REMARK 465 LEU C 119 REMARK 465 ALA C 120 REMARK 465 ASN C 121 REMARK 465 PRO C 122 REMARK 465 GLU C 123 REMARK 465 ASN C 124 REMARK 465 GLN C 125 REMARK 465 PHE C 126 REMARK 465 ARG C 127 REMARK 465 VAL C 128 REMARK 465 ASP C 129 REMARK 465 TYR C 130 REMARK 465 ILE C 131 REMARK 465 LEU C 132 REMARK 465 SER C 133 REMARK 465 VAL C 134 REMARK 465 MET C 135 REMARK 465 ASN C 136 REMARK 465 VAL C 137 REMARK 465 PRO C 138 REMARK 465 ASP C 139 REMARK 465 PHE C 140 REMARK 465 ASP C 141 REMARK 465 PHE C 142 REMARK 465 PRO C 143 REMARK 465 PRO C 144 REMARK 465 GLU C 145 REMARK 465 PHE C 146 REMARK 465 TYR C 147 REMARK 465 GLU C 148 REMARK 465 HIS C 149 REMARK 465 ALA C 150 REMARK 465 LYS C 151 REMARK 465 ALA C 152 REMARK 465 LEU C 153 REMARK 465 TRP C 154 REMARK 465 GLU C 155 REMARK 465 ASP C 156 REMARK 465 GLU C 157 REMARK 465 GLY C 158 REMARK 465 VAL C 159 REMARK 465 ARG C 160 REMARK 465 ALA C 161 REMARK 465 CYS C 162 REMARK 465 TYR C 163 REMARK 465 GLU C 164 REMARK 465 ARG C 165 REMARK 465 SER C 166 REMARK 465 ASN C 167 REMARK 465 GLU C 168 REMARK 465 TYR C 169 REMARK 465 GLN C 170 REMARK 465 LEU C 171 REMARK 465 ILE C 172 REMARK 465 ASP C 173 REMARK 465 CYS C 174 REMARK 465 ALA C 175 REMARK 465 GLN C 176 REMARK 465 TYR C 177 REMARK 465 PHE C 178 REMARK 465 LEU C 179 REMARK 465 ASP C 180 REMARK 465 LYS C 181 REMARK 465 ILE C 182 REMARK 465 ASP C 183 REMARK 465 VAL C 184 REMARK 465 ILE C 185 REMARK 465 LYS C 186 REMARK 465 GLN C 187 REMARK 465 ALA C 188 REMARK 465 ASP C 189 REMARK 465 TYR C 190 REMARK 465 VAL C 191 REMARK 465 PRO C 192 REMARK 465 SER C 193 REMARK 465 ASP C 194 REMARK 465 GLN C 195 REMARK 465 ASP C 196 REMARK 465 LEU C 197 REMARK 465 LEU C 198 REMARK 465 ARG C 199 REMARK 465 CYS C 200 REMARK 465 ARG C 201 REMARK 465 VAL C 202 REMARK 465 LEU C 203 REMARK 465 ASN C 254 REMARK 465 MET C 255 REMARK 465 VAL C 256 REMARK 465 ILE C 257 REMARK 465 ARG C 258 REMARK 465 GLU C 259 REMARK 465 ASP C 260 REMARK 465 ASN C 261 REMARK 465 GLY D 32 REMARK 465 PRO D 33 REMARK 465 ALA D 34 REMARK 465 LEU D 234 REMARK 465 PRO D 235 REMARK 465 ALA D 236 REMARK 465 SER D 237 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 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 LYS C 8 CG CD CE NZ REMARK 470 THR C 9 OG1 CG2 REMARK 470 GLU C 10 CG CD OE1 OE2 REMARK 470 ASP C 11 CG OD1 OD2 REMARK 470 GLN C 12 CG CD OE1 NE2 REMARK 470 ARG C 13 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 262 CG CD OE1 NE2 REMARK 470 THR C 263 OG1 CG2 REMARK 470 ASP C 323 CG OD1 OD2 REMARK 470 THR C 325 OG1 CG2 REMARK 470 TYR D 144 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR D 239 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN G 5 CG OD1 ND2 REMARK 470 GLU G 58 CG CD OE1 OE2 REMARK 470 ARG G 62 CG CD NE CZ NH1 NH2 REMARK 470 SER N 127 OG REMARK 470 SER N 128 OG 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 OD1 ASP D 86 OG SER D 290 2.03 REMARK 500 OD1 ASP A 86 OG SER A 290 2.09 REMARK 500 OG SER N 52 OG SER N 57 2.18 REMARK 500 ND2 ASN B 88 OE1 GLN C 19 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES 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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) 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 ATM2 ATM3 REMARK 500 ASP B 258 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES 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 ALA A 34 -130.96 58.88 REMARK 500 ILE A 103 -56.69 -126.22 REMARK 500 ASN A 140 79.59 -101.82 REMARK 500 PRO B 107 44.98 -82.45 REMARK 500 SER B 108 -3.39 -142.87 REMARK 500 ASP B 298 -76.11 -63.40 REMARK 500 ALA B 299 -64.81 -131.52 REMARK 500 ALA C 226 17.61 57.76 REMARK 500 TYR C 391 51.75 -91.11 REMARK 500 GLU C 392 -112.43 48.93 REMARK 500 LEU C 393 -121.41 52.47 REMARK 500 TYR D 144 -164.96 62.56 REMARK 500 THR D 183 147.77 -174.22 REMARK 500 TYR N 117 56.75 -92.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63523 RELATED DB: EMDB DBREF 9LYC A 32 314 UNP P46089 GPR3_HUMAN 32 314 DBREF 9LYC B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9LYC C 1 394 UNP P63092 GNAS2_HUMAN 1 394 DBREF 9LYC D 32 314 UNP P46089 GPR3_HUMAN 32 314 DBREF 9LYC G 5 62 UNP P59768 GBG2_HUMAN 5 62 DBREF 9LYC N 1 128 PDB 9LYC 9LYC 1 128 SEQADV 9LYC ASN C 54 UNP P63092 SER 54 ENGINEERED MUTATION SEQADV 9LYC ALA C 226 UNP P63092 GLY 226 ENGINEERED MUTATION SEQADV 9LYC ALA C 268 UNP P63092 GLU 268 ENGINEERED MUTATION SEQADV 9LYC LYS C 271 UNP P63092 ASN 271 ENGINEERED MUTATION SEQADV 9LYC ASP C 274 UNP P63092 LYS 274 ENGINEERED MUTATION SEQADV 9LYC LYS C 280 UNP P63092 ARG 280 ENGINEERED MUTATION SEQADV 9LYC ASP C 284 UNP P63092 THR 284 ENGINEERED MUTATION SEQADV 9LYC THR C 285 UNP P63092 ILE 285 ENGINEERED MUTATION SEQRES 1 A 283 GLY PRO ALA ALA PRO LEU PRO SER PRO LYS ALA TRP ASP SEQRES 2 A 283 VAL VAL LEU CYS ILE SER GLY THR LEU VAL SER CYS GLU SEQRES 3 A 283 ASN ALA LEU VAL VAL ALA ILE ILE VAL GLY THR PRO ALA SEQRES 4 A 283 PHE ARG ALA PRO MET PHE LEU LEU VAL GLY SER LEU ALA SEQRES 5 A 283 VAL ALA ASP LEU LEU ALA GLY LEU GLY LEU VAL LEU HIS SEQRES 6 A 283 PHE ALA ALA VAL PHE CYS ILE GLY SER ALA GLU MET SER SEQRES 7 A 283 LEU VAL LEU VAL GLY VAL LEU ALA MET ALA PHE THR ALA SEQRES 8 A 283 SER ILE GLY SER LEU LEU ALA ILE THR VAL ASP ARG TYR SEQRES 9 A 283 LEU SER LEU TYR ASN ALA LEU THR TYR TYR SER GLU THR SEQRES 10 A 283 THR VAL THR ARG THR TYR VAL MET LEU ALA LEU VAL TRP SEQRES 11 A 283 GLY GLY ALA LEU GLY LEU GLY LEU LEU PRO VAL LEU ALA SEQRES 12 A 283 TRP ASN CYS LEU ASP GLY LEU THR THR CYS GLY VAL VAL SEQRES 13 A 283 TYR PRO LEU SER LYS ASN HIS LEU VAL VAL LEU ALA ILE SEQRES 14 A 283 ALA PHE PHE MET VAL PHE GLY ILE MET LEU GLN LEU TYR SEQRES 15 A 283 ALA GLN ILE CYS ARG ILE VAL CYS ARG HIS ALA GLN GLN SEQRES 16 A 283 ILE ALA LEU GLN ARG HIS LEU LEU PRO ALA SER HIS TYR SEQRES 17 A 283 VAL ALA THR ARG LYS GLY ILE ALA THR LEU ALA VAL VAL SEQRES 18 A 283 LEU GLY ALA PHE ALA ALA CYS TRP LEU PRO PHE THR VAL SEQRES 19 A 283 TYR CYS LEU LEU GLY ASP ALA HIS SER PRO PRO LEU TYR SEQRES 20 A 283 THR TYR LEU THR LEU LEU PRO ALA THR TYR ASN SER MET SEQRES 21 A 283 ILE ASN PRO ILE ILE TYR ALA PHE ARG ASN GLN ASP VAL SEQRES 22 A 283 GLN LYS VAL LEU TRP ALA VAL CYS CYS CYS SEQRES 1 B 339 SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU SEQRES 2 B 339 LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP SEQRES 3 B 339 ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL SEQRES 4 B 339 GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY SEQRES 5 B 339 HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SEQRES 6 B 339 SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU SEQRES 7 B 339 ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA SEQRES 8 B 339 ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR SEQRES 9 B 339 ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP SEQRES 10 B 339 ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY SEQRES 11 B 339 ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY SEQRES 12 B 339 TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE SEQRES 13 B 339 VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP SEQRES 14 B 339 ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS SEQRES 15 B 339 THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR SEQRES 16 B 339 ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS SEQRES 17 B 339 LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE SEQRES 18 B 339 THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE SEQRES 19 B 339 PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA SEQRES 20 B 339 THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU SEQRES 21 B 339 MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SEQRES 22 B 339 SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA SEQRES 23 B 339 GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU SEQRES 24 B 339 LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN SEQRES 25 B 339 ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA SEQRES 26 B 339 VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP SEQRES 27 B 339 ASN SEQRES 1 C 394 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2 C 394 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3 C 394 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4 C 394 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5 C 394 LYS ASN THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6 C 394 ASN GLY PHE ASN GLY GLU GLY GLY GLU GLU ASP PRO GLN SEQRES 7 C 394 ALA ALA ARG SER ASN SER ASP GLY GLU LYS ALA THR LYS SEQRES 8 C 394 VAL GLN ASP ILE LYS ASN ASN LEU LYS GLU ALA ILE GLU SEQRES 9 C 394 THR ILE VAL ALA ALA MET SER ASN LEU VAL PRO PRO VAL SEQRES 10 C 394 GLU LEU ALA ASN PRO GLU ASN GLN PHE ARG VAL ASP TYR SEQRES 11 C 394 ILE LEU SER VAL MET ASN VAL PRO ASP PHE ASP PHE PRO SEQRES 12 C 394 PRO GLU PHE TYR GLU HIS ALA LYS ALA LEU TRP GLU ASP SEQRES 13 C 394 GLU GLY VAL ARG ALA CYS TYR GLU ARG SER ASN GLU TYR SEQRES 14 C 394 GLN LEU ILE ASP CYS ALA GLN TYR PHE LEU ASP LYS ILE SEQRES 15 C 394 ASP VAL ILE LYS GLN ALA ASP TYR VAL PRO SER ASP GLN SEQRES 16 C 394 ASP LEU LEU ARG CYS ARG VAL LEU THR SER GLY ILE PHE SEQRES 17 C 394 GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS MET SEQRES 18 C 394 PHE ASP VAL GLY ALA GLN ARG ASP GLU ARG ARG LYS TRP SEQRES 19 C 394 ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE VAL SEQRES 20 C 394 VAL ALA SER SER SER TYR ASN MET VAL ILE ARG GLU ASP SEQRES 21 C 394 ASN GLN THR ASN ARG LEU GLN ALA ALA LEU LYS LEU PHE SEQRES 22 C 394 ASP SER ILE TRP ASN ASN LYS TRP LEU ARG ASP THR SER SEQRES 23 C 394 VAL ILE LEU PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU SEQRES 24 C 394 LYS VAL LEU ALA GLY LYS SER LYS ILE GLU ASP TYR PHE SEQRES 25 C 394 PRO GLU PHE ALA ARG TYR THR THR PRO GLU ASP ALA THR SEQRES 26 C 394 PRO GLU PRO GLY GLU ASP PRO ARG VAL THR ARG ALA LYS SEQRES 27 C 394 TYR PHE ILE ARG ASP GLU PHE LEU ARG ILE SER THR ALA SEQRES 28 C 394 SER GLY ASP GLY ARG HIS TYR CYS TYR PRO HIS PHE THR SEQRES 29 C 394 CYS ALA VAL ASP THR GLU ASN ILE ARG ARG VAL PHE ASN SEQRES 30 C 394 ASP CYS ARG ASP ILE ILE GLN ARG MET HIS LEU ARG GLN SEQRES 31 C 394 TYR GLU LEU LEU SEQRES 1 D 283 GLY PRO ALA ALA PRO LEU PRO SER PRO LYS ALA TRP ASP SEQRES 2 D 283 VAL VAL LEU CYS ILE SER GLY THR LEU VAL SER CYS GLU SEQRES 3 D 283 ASN ALA LEU VAL VAL ALA ILE ILE VAL GLY THR PRO ALA SEQRES 4 D 283 PHE ARG ALA PRO MET PHE LEU LEU VAL GLY SER LEU ALA SEQRES 5 D 283 VAL ALA ASP LEU LEU ALA GLY LEU GLY LEU VAL LEU HIS SEQRES 6 D 283 PHE ALA ALA VAL PHE CYS ILE GLY SER ALA GLU MET SER SEQRES 7 D 283 LEU VAL LEU VAL GLY VAL LEU ALA MET ALA PHE THR ALA SEQRES 8 D 283 SER ILE GLY SER LEU LEU ALA ILE THR VAL ASP ARG TYR SEQRES 9 D 283 LEU SER LEU TYR ASN ALA LEU THR TYR TYR SER GLU THR SEQRES 10 D 283 THR VAL THR ARG THR TYR VAL MET LEU ALA LEU VAL TRP SEQRES 11 D 283 GLY GLY ALA LEU GLY LEU GLY LEU LEU PRO VAL LEU ALA SEQRES 12 D 283 TRP ASN CYS LEU ASP GLY LEU THR THR CYS GLY VAL VAL SEQRES 13 D 283 TYR PRO LEU SER LYS ASN HIS LEU VAL VAL LEU ALA ILE SEQRES 14 D 283 ALA PHE PHE MET VAL PHE GLY ILE MET LEU GLN LEU TYR SEQRES 15 D 283 ALA GLN ILE CYS ARG ILE VAL CYS ARG HIS ALA GLN GLN SEQRES 16 D 283 ILE ALA LEU GLN ARG HIS LEU LEU PRO ALA SER HIS TYR SEQRES 17 D 283 VAL ALA THR ARG LYS GLY ILE ALA THR LEU ALA VAL VAL SEQRES 18 D 283 LEU GLY ALA PHE ALA ALA CYS TRP LEU PRO PHE THR VAL SEQRES 19 D 283 TYR CYS LEU LEU GLY ASP ALA HIS SER PRO PRO LEU TYR SEQRES 20 D 283 THR TYR LEU THR LEU LEU PRO ALA THR TYR ASN SER MET SEQRES 21 D 283 ILE ASN PRO ILE ILE TYR ALA PHE ARG ASN GLN ASP VAL SEQRES 22 D 283 GLN LYS VAL LEU TRP ALA VAL CYS CYS CYS SEQRES 1 G 58 ASN THR ALA SER ILE ALA GLN ALA ARG LYS LEU VAL GLU SEQRES 2 G 58 GLN LEU LYS MET GLU ALA ASN ILE ASP ARG ILE LYS VAL SEQRES 3 G 58 SER LYS ALA ALA ALA ASP LEU MET ALA TYR CYS GLU ALA SEQRES 4 G 58 HIS ALA LYS GLU ASP PRO LEU LEU THR PRO VAL PRO ALA SEQRES 5 G 58 SER GLU ASN PRO PHE ARG 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 HELIX 1 AA1 LYS A 41 THR A 68 1 28 HELIX 2 AA2 ALA A 73 PHE A 101 1 29 HELIX 3 AA3 SER A 105 ASN A 140 1 36 HELIX 4 AA4 SER A 146 GLY A 168 1 23 HELIX 5 AA5 LEU A 169 ALA A 174 1 6 HELIX 6 AA6 SER A 191 HIS A 232 1 42 HELIX 7 AA7 THR A 242 GLY A 270 1 29 HELIX 8 AA8 PRO A 276 THR A 282 1 7 HELIX 9 AA9 LEU A 283 ALA A 298 1 16 HELIX 10 AB1 ASN A 301 CYS A 312 1 12 HELIX 11 AB2 GLU B 3 CYS B 25 1 23 HELIX 12 AB3 THR B 29 ASN B 35 1 7 HELIX 13 AB4 ASP C 11 THR C 40 1 30 HELIX 14 AB5 GLY C 52 MET C 60 1 9 HELIX 15 AB6 GLN C 213 VAL C 217 5 5 HELIX 16 AB7 LYS C 233 ASN C 239 5 7 HELIX 17 AB8 ASN C 264 ASN C 279 1 16 HELIX 18 AB9 LEU C 296 GLY C 304 1 9 HELIX 19 AC1 LYS C 307 PHE C 312 1 6 HELIX 20 AC2 ASP C 331 SER C 352 1 22 HELIX 21 AC3 GLU C 370 TYR C 391 1 22 HELIX 22 AC4 LYS D 41 THR D 68 1 28 HELIX 23 AC5 ALA D 73 CYS D 102 1 30 HELIX 24 AC6 SER D 105 THR D 143 1 39 HELIX 25 AC7 THR D 148 ALA D 164 1 17 HELIX 26 AC8 ALA D 164 LEU D 170 1 7 HELIX 27 AC9 ASN D 176 LEU D 181 1 6 HELIX 28 AD1 SER D 191 HIS D 223 1 33 HELIX 29 AD2 HIS D 223 GLN D 230 1 8 HELIX 30 AD3 THR D 242 GLY D 270 1 29 HELIX 31 AD4 PRO D 275 ALA D 298 1 24 HELIX 32 AD5 ASN D 301 CYS D 314 1 14 HELIX 33 AD6 THR G 6 ASN G 24 1 19 HELIX 34 AD7 LYS G 29 HIS G 44 1 16 HELIX 35 AD8 ALA G 45 ASP G 48 5 4 HELIX 36 AD9 LYS N 87 THR N 91 5 5 SHEET 1 AA1 4 ARG B 46 LEU B 51 0 SHEET 2 AA1 4 LEU B 336 ASN B 340 -1 O LEU B 336 N LEU B 51 SHEET 3 AA1 4 VAL B 327 SER B 331 -1 N THR B 329 O LYS B 337 SHEET 4 AA1 4 VAL B 315 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA2 4 ILE B 58 TRP B 63 0 SHEET 2 AA2 4 LEU B 69 SER B 74 -1 O ALA B 73 N ALA B 60 SHEET 3 AA2 4 LYS B 78 ASP B 83 -1 O ILE B 80 N SER B 72 SHEET 4 AA2 4 ASN B 88 PRO B 94 -1 O VAL B 90 N ILE B 81 SHEET 1 AA3 4 THR B 102 TYR B 105 0 SHEET 2 AA3 4 TYR B 111 GLY B 115 -1 O ALA B 113 N ALA B 104 SHEET 3 AA3 4 CYS B 121 ASN B 125 -1 O SER B 122 N CYS B 114 SHEET 4 AA3 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA4 4 LEU B 146 PHE B 151 0 SHEET 2 AA4 4 GLN B 156 SER B 161 -1 O SER B 160 N CYS B 148 SHEET 3 AA4 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA4 4 GLN B 176 PHE B 180 -1 O THR B 178 N LEU B 168 SHEET 1 AA5 4 SER B 189 LEU B 192 0 SHEET 2 AA5 4 LEU B 198 GLY B 202 -1 O VAL B 200 N SER B 191 SHEET 3 AA5 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA5 4 CYS B 218 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA6 4 ILE B 229 PHE B 234 0 SHEET 2 AA6 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA6 4 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA6 4 GLN B 259 MET B 262 -1 O LEU B 261 N LEU B 252 SHEET 1 AA7 4 ILE B 273 PHE B 278 0 SHEET 2 AA7 4 LEU B 285 TYR B 289 -1 O GLY B 288 N SER B 275 SHEET 3 AA7 4 CYS B 294 TRP B 297 -1 O TRP B 297 N LEU B 285 SHEET 4 AA7 4 ARG B 304 LEU B 308 -1 O GLY B 306 N VAL B 296 SHEET 1 AA8 6 ILE C 207 LYS C 211 0 SHEET 2 AA8 6 PHE C 219 VAL C 224 -1 O MET C 221 N THR C 210 SHEET 3 AA8 6 HIS C 41 GLY C 47 1 N LEU C 43 O PHE C 222 SHEET 4 AA8 6 ALA C 243 ALA C 249 1 O ILE C 245 N LEU C 44 SHEET 5 AA8 6 SER C 286 ASN C 292 1 O ASN C 292 N VAL C 248 SHEET 6 AA8 6 CYS C 359 PHE C 363 1 O TYR C 360 N LEU C 289 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 81 N LEU N 20 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 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 ASN N 35 O ALA N 97 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O SER N 49 N TRP N 36 SHEET 6 AB1 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS A 177 CYS A 184 1555 1555 2.03 SSBOND 2 CYS D 177 CYS D 184 1555 1555 2.03 SSBOND 3 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 4 CYS N 99 CYS N 107 1555 1555 2.03 CISPEP 1 TYR A 188 PRO A 189 0 -6.68 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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