HEADER PEPTIDE BINDING PROTEIN 17-OCT-24 9K27 TITLE PRRP31 BOUND PROLACTIN-RELEASING PEPTIDE RECEPTOR COUPLED WITH GQ TITLE 2 PROTEIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROLACTIN-RELEASING PEPTIDE RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PRRP RECEPTOR,PRRPR,G-PROTEIN COUPLED RECEPTOR 10,HGR3; 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(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: C; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: SCFV16; COMPND 20 CHAIN: D; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(Q) SUBUNIT ALPHA; COMPND 24 CHAIN: E; COMPND 25 SYNONYM: GUANINE NUCLEOTIDE-BINDING PROTEIN ALPHA-Q; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: PROLACTIN-RELEASING PEPTIDE PRRP31; COMPND 29 CHAIN: F; 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: PRLHR, GPR10, GR3; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 1 BOLD-2017; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 2449148; 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 AFF. FRUGIPERDA 1 BOLD-2017; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 2449148; 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: SPODOPTERA AFF. FRUGIPERDA 1 BOLD-2017; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 2449148; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 1 BOLD-2017; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 2449148; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: GNAQ, GAQ; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 1 BOLD-2017; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 2449148; SOURCE 34 MOL_ID: 6; SOURCE 35 SYNTHETIC: YES; SOURCE 36 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 37 ORGANISM_COMMON: HUMAN; SOURCE 38 ORGANISM_TAXID: 9606 KEYWDS A PEPTIDE RELATED GPCR-GQ COMPLEX STRUCTRUAL PROTEIN, PEPTIDE BINDING KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Z.WU,Y.DU,G.CHEN REVDAT 1 29-JAN-25 9K27 0 JRNL AUTH Z.WU,Y.DU,X.JUN JRNL TITL A PEPTIDE RECEPTOR COMPLEX STRUCTURE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 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) : 2.680 REMARK 3 NUMBER OF PARTICLES : 129557 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 9K27 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300052692. 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 : PRRP31-PRRPR-GQ-SCFV16; PRRPR REMARK 245 -GQ-SCFV16; PRRP31 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.00 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 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) : 113.00 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, E, F REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 SER A 3 REMARK 465 SER A 4 REMARK 465 THR A 5 REMARK 465 THR A 6 REMARK 465 ARG A 7 REMARK 465 GLY A 8 REMARK 465 PRO A 9 REMARK 465 ARG A 10 REMARK 465 VAL A 11 REMARK 465 SER A 12 REMARK 465 ASP A 13 REMARK 465 LEU A 14 REMARK 465 PHE A 15 REMARK 465 SER A 16 REMARK 465 GLY A 17 REMARK 465 LEU A 18 REMARK 465 PRO A 19 REMARK 465 PRO A 20 REMARK 465 ALA A 21 REMARK 465 VAL A 22 REMARK 465 THR A 23 REMARK 465 THR A 24 REMARK 465 PRO A 25 REMARK 465 ALA A 26 REMARK 465 ASN A 27 REMARK 465 GLN A 28 REMARK 465 SER A 29 REMARK 465 ALA A 30 REMARK 465 GLU A 31 REMARK 465 ALA A 32 REMARK 465 SER A 33 REMARK 465 ALA A 34 REMARK 465 GLY A 35 REMARK 465 ASN A 36 REMARK 465 GLY A 37 REMARK 465 SER A 38 REMARK 465 VAL A 39 REMARK 465 ALA A 40 REMARK 465 GLY A 41 REMARK 465 ALA A 42 REMARK 465 ASP A 43 REMARK 465 ALA A 44 REMARK 465 PRO A 45 REMARK 465 ALA A 46 REMARK 465 VAL A 47 REMARK 465 THR A 48 REMARK 465 PRO A 49 REMARK 465 PHE A 50 REMARK 465 GLN A 51 REMARK 465 TRP A 353 REMARK 465 PRO A 354 REMARK 465 ARG A 355 REMARK 465 LYS A 356 REMARK 465 ILE A 357 REMARK 465 ALA A 358 REMARK 465 PRO A 359 REMARK 465 HIS A 360 REMARK 465 GLY A 361 REMARK 465 GLN A 362 REMARK 465 ASN A 363 REMARK 465 MET A 364 REMARK 465 THR A 365 REMARK 465 VAL A 366 REMARK 465 SER A 367 REMARK 465 VAL A 368 REMARK 465 VAL A 369 REMARK 465 ILE A 370 REMARK 465 HIS B -16 REMARK 465 HIS B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LEU B 4 REMARK 465 ASP B 5 REMARK 465 GLN B 6 REMARK 465 LEU B 7 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 SER C 3 REMARK 465 ASN C 4 REMARK 465 ASN C 5 REMARK 465 THR C 6 REMARK 465 ALA C 7 REMARK 465 SER C 8 REMARK 465 GLU C 63 REMARK 465 LYS C 64 REMARK 465 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 ALA C 69 REMARK 465 ILE C 70 REMARK 465 LEU C 71 REMARK 465 GLY D 139 REMARK 465 GLY D 140 REMARK 465 GLY D 141 REMARK 465 GLY D 142 REMARK 465 SER D 143 REMARK 465 GLY D 144 REMARK 465 GLY D 145 REMARK 465 GLY D 146 REMARK 465 GLY D 147 REMARK 465 SER D 148 REMARK 465 GLY D 149 REMARK 465 GLY D 150 REMARK 465 GLY D 151 REMARK 465 GLY D 152 REMARK 465 LYS D 265 REMARK 465 GLY D 266 REMARK 465 SER D 267 REMARK 465 LEU D 268 REMARK 465 GLU D 269 REMARK 465 VAL D 270 REMARK 465 LEU D 271 REMARK 465 PHE D 272 REMARK 465 GLN D 273 REMARK 465 GLY D 274 REMARK 465 PRO D 275 REMARK 465 ALA D 276 REMARK 465 ALA D 277 REMARK 465 ALA D 278 REMARK 465 MET E 1 REMARK 465 GLY E 2 REMARK 465 CYS E 3 REMARK 465 SER E 59 REMARK 465 GLY E 60 REMARK 465 TYR E 61 REMARK 465 SER E 62 REMARK 465 ASP E 63 REMARK 465 GLU E 64 REMARK 465 ASP E 65 REMARK 465 LYS E 66 REMARK 465 ARG E 67 REMARK 465 GLY E 68 REMARK 465 PHE E 69 REMARK 465 THR E 70 REMARK 465 LYS E 71 REMARK 465 LEU E 72 REMARK 465 VAL E 73 REMARK 465 TYR E 74 REMARK 465 GLN E 75 REMARK 465 ASN E 76 REMARK 465 ILE E 77 REMARK 465 PHE E 78 REMARK 465 THR E 79 REMARK 465 ALA E 80 REMARK 465 MET E 81 REMARK 465 GLN E 82 REMARK 465 ALA E 83 REMARK 465 MET E 84 REMARK 465 ILE E 85 REMARK 465 ARG E 86 REMARK 465 ALA E 87 REMARK 465 MET E 88 REMARK 465 ASP E 89 REMARK 465 THR E 90 REMARK 465 LEU E 91 REMARK 465 LYS E 92 REMARK 465 ILE E 93 REMARK 465 PRO E 94 REMARK 465 TYR E 95 REMARK 465 LYS E 96 REMARK 465 TYR E 97 REMARK 465 GLU E 98 REMARK 465 HIS E 99 REMARK 465 ASN E 100 REMARK 465 LYS E 101 REMARK 465 ALA E 102 REMARK 465 HIS E 103 REMARK 465 ALA E 104 REMARK 465 GLN E 105 REMARK 465 LEU E 106 REMARK 465 VAL E 107 REMARK 465 ARG E 108 REMARK 465 GLU E 109 REMARK 465 VAL E 110 REMARK 465 ASP E 111 REMARK 465 VAL E 112 REMARK 465 GLU E 113 REMARK 465 LYS E 114 REMARK 465 VAL E 115 REMARK 465 SER E 116 REMARK 465 ALA E 117 REMARK 465 PHE E 118 REMARK 465 GLU E 119 REMARK 465 ASN E 120 REMARK 465 PRO E 121 REMARK 465 TYR E 122 REMARK 465 VAL E 123 REMARK 465 ASP E 124 REMARK 465 ALA E 125 REMARK 465 ILE E 126 REMARK 465 LYS E 127 REMARK 465 SER E 128 REMARK 465 LEU E 129 REMARK 465 TRP E 130 REMARK 465 ASN E 131 REMARK 465 ASP E 132 REMARK 465 PRO E 133 REMARK 465 GLY E 134 REMARK 465 ILE E 135 REMARK 465 GLN E 136 REMARK 465 GLU E 137 REMARK 465 CYS E 138 REMARK 465 TYR E 139 REMARK 465 ASP E 140 REMARK 465 ARG E 141 REMARK 465 ARG E 142 REMARK 465 ARG E 143 REMARK 465 GLU E 144 REMARK 465 TYR E 145 REMARK 465 GLN E 146 REMARK 465 LEU E 147 REMARK 465 SER E 148 REMARK 465 ASP E 149 REMARK 465 SER E 150 REMARK 465 THR E 151 REMARK 465 LYS E 152 REMARK 465 TYR E 153 REMARK 465 TYR E 154 REMARK 465 LEU E 155 REMARK 465 ASN E 156 REMARK 465 ASP E 157 REMARK 465 LEU E 158 REMARK 465 ASP E 159 REMARK 465 ARG E 160 REMARK 465 VAL E 161 REMARK 465 ALA E 162 REMARK 465 ASP E 163 REMARK 465 PRO E 164 REMARK 465 ALA E 165 REMARK 465 TYR E 166 REMARK 465 LEU E 167 REMARK 465 PRO E 168 REMARK 465 THR E 169 REMARK 465 GLN E 170 REMARK 465 GLN E 171 REMARK 465 ASP E 172 REMARK 465 VAL E 173 REMARK 465 LEU E 174 REMARK 465 ARG E 175 REMARK 465 VAL E 176 REMARK 465 ARG E 177 REMARK 465 VAL E 178 REMARK 465 PRO E 179 REMARK 465 THR E 180 REMARK 465 SER F 1 REMARK 465 ARG F 2 REMARK 465 THR F 3 REMARK 465 HIS F 4 REMARK 465 ARG F 5 REMARK 465 HIS F 6 REMARK 465 SER F 7 REMARK 465 MET F 8 REMARK 465 GLU F 9 REMARK 465 ILE F 10 REMARK 465 ARG F 11 REMARK 465 THR F 12 REMARK 465 PRO F 13 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 NE2 HIS A 321 O PHE F 31 1.83 REMARK 500 OE1 GLN A 141 N NH2 F 33 2.12 REMARK 500 OG1 THR B 86 OD1 ASN B 88 2.15 REMARK 500 OH TYR E 229 OG SER E 280 2.17 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 PHE A 122 -2.13 71.02 REMARK 500 PRO A 124 53.96 -90.75 REMARK 500 PRO A 193 43.62 -78.09 REMARK 500 PRO A 205 -158.54 -80.94 REMARK 500 HIS A 206 -5.29 78.31 REMARK 500 ASP A 207 -10.99 73.67 REMARK 500 ASP A 309 136.72 -172.86 REMARK 500 ALA B 26 116.43 -161.60 REMARK 500 ASN B 35 48.74 -81.30 REMARK 500 ASP B 247 31.19 -96.64 REMARK 500 ARG B 251 151.26 -49.74 REMARK 500 PHE B 292 -5.85 79.78 REMARK 500 CYS B 294 49.07 -140.84 REMARK 500 ASN B 295 151.77 -48.60 REMARK 500 ALA B 302 60.04 60.34 REMARK 500 LEU B 308 57.66 -96.17 REMARK 500 SER D 69 -169.14 -76.80 REMARK 500 SER D 105 -167.14 -76.39 REMARK 500 GLU D 106 18.38 52.01 REMARK 500 ALA D 160 -1.53 67.77 REMARK 500 MET D 209 -14.07 72.68 REMARK 500 SER D 210 -38.62 -131.85 REMARK 500 SER D 223 -170.00 -163.22 REMARK 500 ARG E 32 40.77 -109.29 REMARK 500 GLU E 33 41.13 -102.04 REMARK 500 ASN E 216 76.07 -100.69 REMARK 500 LEU E 248 -7.51 71.47 REMARK 500 PHE E 258 58.56 -93.07 REMARK 500 ALA E 296 -1.96 64.79 REMARK 500 LEU E 310 36.22 -89.53 REMARK 500 ASN E 311 73.88 63.50 REMARK 500 ASP E 313 70.60 62.32 REMARK 500 SER E 314 73.19 63.40 REMARK 500 ASP E 315 0.00 83.58 REMARK 500 ARG F 26 70.25 38.19 REMARK 500 ARG F 30 -60.08 -94.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61992 RELATED DB: EMDB REMARK 900 PRRP31 BOUND PROLACTIN-RELEASING PEPTIDE RECEPTOR COUPLED WITH GQ REMARK 900 PROTEIN COMPLEX DBREF 9K27 A 1 370 UNP P49683 PRLHR_HUMAN 1 370 DBREF 9K27 B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 9K27 C 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 9K27 D 18 278 PDB 9K27 9K27 18 278 DBREF 9K27 E 19 353 UNP P50148 GNAQ_HUMAN 25 359 DBREF 9K27 F 1 31 UNP P81277 PRRP_HUMAN 23 53 SEQADV 9K27 HIS B -16 UNP P62873 EXPRESSION TAG SEQADV 9K27 HIS B -15 UNP P62873 EXPRESSION TAG SEQADV 9K27 HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 9K27 HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 9K27 HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 9K27 HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 9K27 LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 9K27 GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 9K27 VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 9K27 LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 9K27 PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 9K27 GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 9K27 GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 9K27 PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 9K27 GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 9K27 SER B -1 UNP P62873 EXPRESSION TAG SEQADV 9K27 SER B 0 UNP P62873 EXPRESSION TAG SEQADV 9K27 GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 9K27 PHE C 62 UNP P59768 ARG 62 CONFLICT SEQADV 9K27 MET E 1 UNP P50148 INITIATING METHIONINE SEQADV 9K27 GLY E 2 UNP P50148 EXPRESSION TAG SEQADV 9K27 CYS E 3 UNP P50148 EXPRESSION TAG SEQADV 9K27 THR E 4 UNP P50148 EXPRESSION TAG SEQADV 9K27 LEU E 5 UNP P50148 EXPRESSION TAG SEQADV 9K27 SER E 6 UNP P50148 EXPRESSION TAG SEQADV 9K27 ALA E 7 UNP P50148 EXPRESSION TAG SEQADV 9K27 GLU E 8 UNP P50148 EXPRESSION TAG SEQADV 9K27 ASP E 9 UNP P50148 EXPRESSION TAG SEQADV 9K27 LYS E 10 UNP P50148 EXPRESSION TAG SEQADV 9K27 ALA E 11 UNP P50148 EXPRESSION TAG SEQADV 9K27 ALA E 12 UNP P50148 EXPRESSION TAG SEQADV 9K27 VAL E 13 UNP P50148 EXPRESSION TAG SEQADV 9K27 GLU E 14 UNP P50148 EXPRESSION TAG SEQADV 9K27 ARG E 15 UNP P50148 EXPRESSION TAG SEQADV 9K27 SER E 16 UNP P50148 EXPRESSION TAG SEQADV 9K27 LYS E 17 UNP P50148 EXPRESSION TAG SEQADV 9K27 MET E 18 UNP P50148 EXPRESSION TAG SEQADV 9K27 NH2 F 33 UNP P81277 AMIDATION SEQRES 1 A 370 MET ALA SER SER THR THR ARG GLY PRO ARG VAL SER ASP SEQRES 2 A 370 LEU PHE SER GLY LEU PRO PRO ALA VAL THR THR PRO ALA SEQRES 3 A 370 ASN GLN SER ALA GLU ALA SER ALA GLY ASN GLY SER VAL SEQRES 4 A 370 ALA GLY ALA ASP ALA PRO ALA VAL THR PRO PHE GLN SER SEQRES 5 A 370 LEU GLN LEU VAL HIS GLN LEU LYS GLY LEU ILE VAL LEU SEQRES 6 A 370 LEU TYR SER VAL VAL VAL VAL VAL GLY LEU VAL GLY ASN SEQRES 7 A 370 CYS LEU LEU VAL LEU VAL ILE ALA ARG VAL ARG ARG LEU SEQRES 8 A 370 HIS ASN VAL THR ASN PHE LEU ILE GLY ASN LEU ALA LEU SEQRES 9 A 370 SER ASP VAL LEU MET CYS THR ALA CYS VAL PRO LEU THR SEQRES 10 A 370 LEU ALA TYR ALA PHE GLU PRO ARG GLY TRP VAL PHE GLY SEQRES 11 A 370 GLY GLY LEU CYS HIS LEU VAL PHE PHE LEU GLN PRO VAL SEQRES 12 A 370 THR VAL TYR VAL SER VAL PHE THR LEU THR THR ILE ALA SEQRES 13 A 370 VAL ASP ARG TYR VAL VAL LEU VAL HIS PRO LEU ARG ARG SEQRES 14 A 370 ARG ILE SER LEU ARG LEU SER ALA TYR ALA VAL LEU ALA SEQRES 15 A 370 ILE TRP ALA LEU SER ALA VAL LEU ALA LEU PRO ALA ALA SEQRES 16 A 370 VAL HIS THR TYR HIS VAL GLU LEU LYS PRO HIS ASP VAL SEQRES 17 A 370 ARG LEU CYS GLU GLU PHE TRP GLY SER GLN GLU ARG GLN SEQRES 18 A 370 ARG GLN LEU TYR ALA TRP GLY LEU LEU LEU VAL THR TYR SEQRES 19 A 370 LEU LEU PRO LEU LEU VAL ILE LEU LEU SER TYR VAL ARG SEQRES 20 A 370 VAL SER VAL LYS LEU ARG ASN ARG VAL VAL PRO GLY CYS SEQRES 21 A 370 VAL THR GLN SER GLN ALA ASP TRP ASP ARG ALA ARG ARG SEQRES 22 A 370 ARG ARG THR PHE CYS LEU LEU VAL VAL ILE VAL VAL VAL SEQRES 23 A 370 PHE ALA VAL CYS TRP LEU PRO LEU HIS VAL PHE ASN LEU SEQRES 24 A 370 LEU ARG ASP LEU ASP PRO HIS ALA ILE ASP PRO TYR ALA SEQRES 25 A 370 PHE GLY LEU VAL GLN LEU LEU CYS HIS TRP LEU ALA MET SEQRES 26 A 370 SER SER ALA CYS TYR ASN PRO PHE ILE TYR ALA TRP LEU SEQRES 27 A 370 HIS ASP SER PHE ARG GLU GLU LEU ARG LYS LEU LEU VAL SEQRES 28 A 370 ALA TRP PRO ARG LYS ILE ALA PRO HIS GLY GLN ASN MET SEQRES 29 A 370 THR VAL SER VAL VAL ILE SEQRES 1 B 357 HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN GLY SEQRES 2 B 357 PRO GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG GLN SEQRES 3 B 357 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 4 B 357 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 5 B 357 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 6 B 357 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 7 B 357 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 8 B 357 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 9 B 357 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 10 B 357 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 11 B 357 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 12 B 357 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 13 B 357 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 14 B 357 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 15 B 357 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 16 B 357 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 17 B 357 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 18 B 357 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 19 B 357 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 20 B 357 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 21 B 357 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 22 B 357 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 23 B 357 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 24 B 357 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 25 B 357 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 26 B 357 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 27 B 357 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 28 B 357 PHE LEU LYS ILE TRP ASN SEQRES 1 C 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 71 PRO VAL PRO ALA SER GLU ASN PRO PHE PHE GLU LYS LYS SEQRES 6 C 71 PHE PHE CYS ALA ILE LEU SEQRES 1 D 261 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 261 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 D 261 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 D 261 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 D 261 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 D 261 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 D 261 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 D 261 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 D 261 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 D 261 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 D 261 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 D 261 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 D 261 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 D 261 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 D 261 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 D 261 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 D 261 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 D 261 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 D 261 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 D 261 LYS GLY SER LEU GLU VAL LEU PHE GLN GLY PRO ALA ALA SEQRES 21 D 261 ALA SEQRES 1 E 353 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 E 353 GLU ARG SER LYS MET ILE GLU ARG GLN LEU ARG ARG ASP SEQRES 3 E 353 LYS ARG ASP ALA ARG ARG GLU LEU LYS LEU LEU LEU LEU SEQRES 4 E 353 GLY THR GLY GLU SER GLY LYS SER THR PHE ILE LYS GLN SEQRES 5 E 353 MET ARG ILE ILE HIS GLY SER GLY TYR SER ASP GLU ASP SEQRES 6 E 353 LYS ARG GLY PHE THR LYS LEU VAL TYR GLN ASN ILE PHE SEQRES 7 E 353 THR ALA MET GLN ALA MET ILE ARG ALA MET ASP THR LEU SEQRES 8 E 353 LYS ILE PRO TYR LYS TYR GLU HIS ASN LYS ALA HIS ALA SEQRES 9 E 353 GLN LEU VAL ARG GLU VAL ASP VAL GLU LYS VAL SER ALA SEQRES 10 E 353 PHE GLU ASN PRO TYR VAL ASP ALA ILE LYS SER LEU TRP SEQRES 11 E 353 ASN ASP PRO GLY ILE GLN GLU CYS TYR ASP ARG ARG ARG SEQRES 12 E 353 GLU TYR GLN LEU SER ASP SER THR LYS TYR TYR LEU ASN SEQRES 13 E 353 ASP LEU ASP ARG VAL ALA ASP PRO ALA TYR LEU PRO THR SEQRES 14 E 353 GLN GLN ASP VAL LEU ARG VAL ARG VAL PRO THR THR GLY SEQRES 15 E 353 ILE ILE GLU TYR PRO PHE ASP LEU GLN SER VAL ILE PHE SEQRES 16 E 353 ARG MET VAL ASP VAL GLY GLY GLN ARG SER GLU ARG ARG SEQRES 17 E 353 LYS TRP ILE HIS CYS PHE GLU ASN VAL THR SER ILE MET SEQRES 18 E 353 PHE LEU VAL ALA LEU SER GLU TYR ASP GLN VAL LEU VAL SEQRES 19 E 353 GLU SER ASP ASN GLU ASN ARG MET GLU GLU SER LYS ALA SEQRES 20 E 353 LEU PHE ARG THR ILE ILE THR TYR PRO TRP PHE GLN ASN SEQRES 21 E 353 SER SER VAL ILE LEU PHE LEU ASN LYS LYS ASP LEU LEU SEQRES 22 E 353 GLU GLU LYS ILE MET TYR SER HIS LEU VAL ASP TYR PHE SEQRES 23 E 353 PRO GLU TYR ASP GLY PRO GLN ARG ASP ALA GLN ALA ALA SEQRES 24 E 353 ARG GLU PHE ILE LEU LYS MET PHE VAL ASP LEU ASN PRO SEQRES 25 E 353 ASP SER ASP LYS ILE ILE TYR SER HIS PHE THR CYS ALA SEQRES 26 E 353 THR ASP THR GLU ASN ILE ARG PHE VAL PHE ALA ALA VAL SEQRES 27 E 353 LYS ASP THR ILE LEU GLN LEU ASN LEU LYS GLU TYR ASN SEQRES 28 E 353 LEU VAL SEQRES 1 F 32 SER ARG THR HIS ARG HIS SER MET GLU ILE ARG THR PRO SEQRES 2 F 32 ASP ILE ASN PRO ALA TRP TYR ALA SER ARG GLY ILE ARG SEQRES 3 F 32 PRO VAL GLY ARG PHE NH2 HET NH2 F 33 3 HETNAM NH2 AMINO GROUP FORMUL 6 NH2 H2 N HELIX 1 AA1 VAL A 56 GLN A 58 5 3 HELIX 2 AA2 LEU A 59 VAL A 88 1 30 HELIX 3 AA3 ASN A 93 ALA A 121 1 29 HELIX 4 AA4 GLY A 130 VAL A 164 1 35 HELIX 5 AA5 SER A 172 VAL A 196 1 25 HELIX 6 AA6 GLU A 219 TYR A 234 1 16 HELIX 7 AA7 TYR A 234 ASN A 254 1 21 HELIX 8 AA8 THR A 262 ASP A 304 1 43 HELIX 9 AA9 ALA A 312 ALA A 336 1 25 HELIX 10 AB1 HIS A 339 ALA A 352 1 14 HELIX 11 AB2 GLN B 9 CYS B 25 1 17 HELIX 12 AB3 THR B 29 ASN B 35 1 7 HELIX 13 AB4 ALA C 10 ALA C 23 1 14 HELIX 14 AB5 LYS C 29 HIS C 44 1 16 HELIX 15 AB6 ALA D 45 PHE D 49 5 5 HELIX 16 AB7 SER E 6 ALA E 30 1 25 HELIX 17 AB8 GLY E 45 HIS E 57 1 13 HELIX 18 AB9 GLU E 206 GLU E 215 5 10 HELIX 19 AC1 SER E 227 TYR E 229 5 3 HELIX 20 AC2 LEU E 233 ASN E 238 5 6 HELIX 21 AC3 ASN E 240 ALA E 247 1 8 HELIX 22 AC4 LYS E 269 ILE E 277 1 9 HELIX 23 AC5 HIS E 281 PHE E 286 1 6 HELIX 24 AC6 GLN E 297 ASP E 309 1 13 HELIX 25 AC7 GLU E 329 TYR E 350 1 22 HELIX 26 AC8 PRO F 17 ARG F 23 5 7 SHEET 1 AA1 2 THR A 198 TYR A 199 0 SHEET 2 AA1 2 GLU A 212 GLU A 213 -1 O GLU A 212 N TYR A 199 SHEET 1 AA2 4 ARG B 46 ARG B 52 0 SHEET 2 AA2 4 PHE B 335 ASN B 340 -1 O ASN B 340 N ARG B 46 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O ILE B 80 N SER B 72 SHEET 4 AA3 4 ASN B 88 PRO B 94 -1 O VAL B 90 N ILE B 81 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 SER B 122 N CYS B 114 SHEET 4 AA4 4 ARG B 134 ALA B 140 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O VAL B 158 N ARG B 150 SHEET 3 AA5 4 CYS B 166 LEU B 168 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 THR B 178 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 GLY B 202 N SER B 189 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 GLY B 244 N ASN B 230 SHEET 3 AA7 4 LEU B 252 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLN B 259 MET B 262 -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 VAL B 296 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 GLY B 306 -1 O ALA B 305 N VAL B 296 SHEET 1 AA9 4 GLN D 20 SER D 24 0 SHEET 2 AA9 4 GLY D 33 SER D 42 -1 O SER D 42 N GLN D 20 SHEET 3 AA9 4 THR D 95 LEU D 103 -1 O LEU D 98 N LEU D 37 SHEET 4 AA9 4 PHE D 85 ASP D 90 -1 N SER D 88 O PHE D 97 SHEET 1 AB1 5 GLY D 27 VAL D 29 0 SHEET 2 AB1 5 THR D 132 VAL D 136 1 O THR D 135 N VAL D 29 SHEET 3 AB1 5 ALA D 109 TYR D 111 -1 N TYR D 111 O THR D 132 SHEET 4 AB1 5 ARG D 55 GLN D 56 -1 N GLN D 56 O MET D 110 SHEET 5 AB1 5 LEU D 62 GLU D 63 -1 O GLU D 63 N ARG D 55 SHEET 1 AB2 3 TYR D 67 ILE D 68 0 SHEET 2 AB2 3 GLY D 50 HIS D 52 -1 N MET D 51 O ILE D 68 SHEET 3 AB2 3 VAL D 114 SER D 116 -1 O VAL D 114 N HIS D 52 SHEET 1 AB3 6 SER D 163 PRO D 165 0 SHEET 2 AB3 6 THR D 260 GLU D 263 1 O LYS D 261 N VAL D 164 SHEET 3 AB3 6 VAL D 243 GLN D 248 -1 N TYR D 244 O THR D 260 SHEET 4 AB3 6 LEU D 191 GLN D 196 -1 N PHE D 194 O TYR D 245 SHEET 5 AB3 6 GLN D 203 TYR D 207 -1 O LEU D 205 N TRP D 193 SHEET 6 AB3 6 ASN D 211 LEU D 212 -1 O ASN D 211 N TYR D 207 SHEET 1 AB4 3 SER D 173 ARG D 177 0 SHEET 2 AB4 3 ALA D 228 ILE D 233 -1 O PHE D 229 N CYS D 176 SHEET 3 AB4 3 PHE D 220 GLY D 224 -1 N SER D 223 O THR D 230 SHEET 1 AB5 6 ILE E 184 ASP E 189 0 SHEET 2 AB5 6 ILE E 194 ASP E 199 -1 O PHE E 195 N PHE E 188 SHEET 3 AB5 6 LYS E 35 GLY E 40 1 N LEU E 36 O VAL E 198 SHEET 4 AB5 6 SER E 219 ALA E 225 1 O MET E 221 N LEU E 39 SHEET 5 AB5 6 SER E 262 ASN E 268 1 O PHE E 266 N PHE E 222 SHEET 6 AB5 6 ILE E 318 PHE E 322 1 O TYR E 319 N LEU E 265 SSBOND 1 CYS A 134 CYS A 211 1555 1555 2.03 SSBOND 2 CYS D 39 CYS D 113 1555 1555 2.04 LINK C PHE F 31 N NH2 F 33 1555 1555 1.29 CISPEP 1 LYS A 204 PRO A 205 0 3.19 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