HEADER MEMBRANE PROTEIN 03-FEB-24 8Y72 TITLE POSITIVE ALLOSTERIC MODULATOR(BMS986122)-BOUND MU-OPIOID RECEPTOR-GI TITLE 2 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; 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: E; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: MU-TYPE OPIOID RECEPTOR; COMPND 24 CHAIN: R; COMPND 25 SYNONYM: M-OR-1,MOR-1,MU OPIATE RECEPTOR,MU OPIOID RECEPTOR,MOP,HMOP; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 6; COMPND 28 MOLECULE: TYR-DAL-GLY-MEA-ETA; COMPND 29 CHAIN: D; 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: GNAI1; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 10 ORGANISM_COMMON: NORWAY RAT; SOURCE 11 ORGANISM_TAXID: 10116; 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: BOS TAURUS; SOURCE 17 ORGANISM_COMMON: DOMESTIC CATTLE; SOURCE 18 ORGANISM_TAXID: 9913; SOURCE 19 GENE: GNG2; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 24 ORGANISM_TAXID: 32630; SOURCE 25 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: OPRM1, MOR1; SOURCE 32 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 34 MOL_ID: 6; SOURCE 35 SYNTHETIC: YES; SOURCE 36 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 37 ORGANISM_TAXID: 32630 KEYWDS POSITIVE ALLOSTERIC MODULATOR, BMS986122, MU-OPIOID RECEPTOR, KEYWDS 2 ALLOSTERIC AGONISM, ALLOSTERIC OPIOID ANALGESICS, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.LUO,Y.XU,Y.WANG,Y.ZHUANG,H.E.XU REVDAT 1 06-AUG-25 8Y72 0 JRNL AUTH P.LUO,Y.XU,Y.WANG,Y.ZHUANG,H.E.XU JRNL TITL STRUCTURE BASED DESIGN OF A POSITIVE ALLOSTERIC MODULATOR OF JRNL TITL 2 MU-OPIOID RECEPTOR FOR SYNERGISTIC ANALGESIA JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.65 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) : 2.650 REMARK 3 NUMBER OF PARTICLES : 380272 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 8Y72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1300045066. 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 : POSITIVE ALLOSTERIC REMARK 245 MODULATOR(BMS986122)-BOUND MU- REMARK 245 OPIOID RECEPTOR-GI 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 : 7.20 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) : 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) : 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, C, E, R, D 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 400 REMARK 400 COMPOUND REMARK 400 REMARK 400 THE DAMGO IS PEPTIDE-LIKE, A MEMBER OF SYNTHETIC OPIOID CLASS. REMARK 400 REMARK 400 GROUP: 1 REMARK 400 NAME: DAMGO REMARK 400 CHAIN: D REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER REMARK 400 DESCRIPTION: NULL 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 GLY A 2 REMARK 465 CYS A 3 REMARK 465 ILE A 56 REMARK 465 HIS A 57 REMARK 465 GLU A 58 REMARK 465 ALA A 59 REMARK 465 GLY A 60 REMARK 465 TYR A 61 REMARK 465 SER A 62 REMARK 465 GLU A 63 REMARK 465 GLU A 64 REMARK 465 GLU A 65 REMARK 465 CYS A 66 REMARK 465 LYS A 67 REMARK 465 GLN A 68 REMARK 465 TYR A 69 REMARK 465 LYS A 70 REMARK 465 ALA A 71 REMARK 465 VAL A 72 REMARK 465 VAL A 73 REMARK 465 TYR A 74 REMARK 465 SER A 75 REMARK 465 ASN A 76 REMARK 465 THR A 77 REMARK 465 ILE A 78 REMARK 465 GLN A 79 REMARK 465 SER A 80 REMARK 465 ILE A 81 REMARK 465 ILE A 82 REMARK 465 ALA A 83 REMARK 465 ILE A 84 REMARK 465 ILE A 85 REMARK 465 ARG A 86 REMARK 465 ALA A 87 REMARK 465 MET A 88 REMARK 465 GLY A 89 REMARK 465 ARG A 90 REMARK 465 LEU A 91 REMARK 465 LYS A 92 REMARK 465 ILE A 93 REMARK 465 ASP A 94 REMARK 465 PHE A 95 REMARK 465 GLY A 96 REMARK 465 ASP A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 ARG A 100 REMARK 465 ALA A 101 REMARK 465 ASP A 102 REMARK 465 ASP A 103 REMARK 465 ALA A 104 REMARK 465 ARG A 105 REMARK 465 GLN A 106 REMARK 465 LEU A 107 REMARK 465 PHE A 108 REMARK 465 VAL A 109 REMARK 465 LEU A 110 REMARK 465 ALA A 111 REMARK 465 GLY A 112 REMARK 465 ALA A 113 REMARK 465 ALA A 114 REMARK 465 GLU A 115 REMARK 465 GLU A 116 REMARK 465 GLY A 117 REMARK 465 PHE A 118 REMARK 465 MET A 119 REMARK 465 THR A 120 REMARK 465 ALA A 121 REMARK 465 GLU A 122 REMARK 465 LEU A 123 REMARK 465 ALA A 124 REMARK 465 GLY A 125 REMARK 465 VAL A 126 REMARK 465 ILE A 127 REMARK 465 LYS A 128 REMARK 465 ARG A 129 REMARK 465 LEU A 130 REMARK 465 TRP A 131 REMARK 465 LYS A 132 REMARK 465 ASP A 133 REMARK 465 SER A 134 REMARK 465 GLY A 135 REMARK 465 VAL A 136 REMARK 465 GLN A 137 REMARK 465 ALA A 138 REMARK 465 CYS A 139 REMARK 465 PHE A 140 REMARK 465 ASN A 141 REMARK 465 ARG A 142 REMARK 465 SER A 143 REMARK 465 ARG A 144 REMARK 465 GLU A 145 REMARK 465 TYR A 146 REMARK 465 GLN A 147 REMARK 465 LEU A 148 REMARK 465 ASN A 149 REMARK 465 ASP A 150 REMARK 465 SER A 151 REMARK 465 ALA A 152 REMARK 465 ALA A 153 REMARK 465 TYR A 154 REMARK 465 TYR A 155 REMARK 465 LEU A 156 REMARK 465 ASN A 157 REMARK 465 ASP A 158 REMARK 465 LEU A 159 REMARK 465 ASP A 160 REMARK 465 ARG A 161 REMARK 465 ILE A 162 REMARK 465 ALA A 163 REMARK 465 GLN A 164 REMARK 465 PRO A 165 REMARK 465 ASN A 166 REMARK 465 TYR A 167 REMARK 465 ILE A 168 REMARK 465 PRO A 169 REMARK 465 THR A 170 REMARK 465 GLN A 171 REMARK 465 GLN A 172 REMARK 465 ASP A 173 REMARK 465 VAL A 174 REMARK 465 LEU A 175 REMARK 465 ARG A 176 REMARK 465 THR A 177 REMARK 465 ARG A 178 REMARK 465 VAL A 179 REMARK 465 LYS A 180 REMARK 465 THR A 181 REMARK 465 MET B -12 REMARK 465 HIS B -11 REMARK 465 HIS B -10 REMARK 465 HIS 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 GLY B -3 REMARK 465 SER B -2 REMARK 465 LEU B -1 REMARK 465 LEU B 0 REMARK 465 GLN B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LEU B 4 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 LYS C 65 REMARK 465 PHE C 66 REMARK 465 PHE C 67 REMARK 465 CYS C 68 REMARK 465 MET E 1 REMARK 465 GLY E 122 REMARK 465 GLY E 123 REMARK 465 GLY E 124 REMARK 465 GLY E 125 REMARK 465 SER E 126 REMARK 465 GLY E 127 REMARK 465 GLY E 128 REMARK 465 GLY E 129 REMARK 465 GLY E 130 REMARK 465 SER E 131 REMARK 465 GLY E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 GLY E 135 REMARK 465 SER E 136 REMARK 465 ALA E 137 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 VAL R 1 REMARK 465 ASP R 2 REMARK 465 SER R 3 REMARK 465 SER R 4 REMARK 465 ALA R 5 REMARK 465 ALA R 6 REMARK 465 PRO R 7 REMARK 465 THR R 8 REMARK 465 ASN R 9 REMARK 465 ALA R 10 REMARK 465 SER R 11 REMARK 465 ASN R 12 REMARK 465 CYS R 13 REMARK 465 THR R 14 REMARK 465 ASP R 15 REMARK 465 ALA R 16 REMARK 465 LEU R 17 REMARK 465 ALA R 18 REMARK 465 TYR R 19 REMARK 465 SER R 20 REMARK 465 SER R 21 REMARK 465 CYS R 22 REMARK 465 SER R 23 REMARK 465 PRO R 24 REMARK 465 ALA R 25 REMARK 465 PRO R 26 REMARK 465 SER R 27 REMARK 465 PRO R 28 REMARK 465 GLY R 29 REMARK 465 SER R 30 REMARK 465 TRP R 31 REMARK 465 VAL R 32 REMARK 465 ASN R 33 REMARK 465 LEU R 34 REMARK 465 SER R 35 REMARK 465 HIS R 36 REMARK 465 LEU R 37 REMARK 465 ASP R 38 REMARK 465 GLY R 39 REMARK 465 ASN R 40 REMARK 465 LEU R 41 REMARK 465 SER R 42 REMARK 465 ASP R 43 REMARK 465 PRO R 44 REMARK 465 CYS R 45 REMARK 465 GLY R 46 REMARK 465 PRO R 47 REMARK 465 ASN R 48 REMARK 465 ARG R 49 REMARK 465 THR R 50 REMARK 465 ASP R 51 REMARK 465 LEU R 52 REMARK 465 GLY R 53 REMARK 465 GLY R 54 REMARK 465 ARG R 55 REMARK 465 ASP R 56 REMARK 465 SER R 57 REMARK 465 LEU R 58 REMARK 465 CYS R 59 REMARK 465 PRO R 60 REMARK 465 PRO R 61 REMARK 465 THR R 62 REMARK 465 GLY R 63 REMARK 465 SER R 64 REMARK 465 PRO R 65 REMARK 465 CYS R 353 REMARK 465 ILE R 354 REMARK 465 PRO R 355 REMARK 465 THR R 356 REMARK 465 SER R 357 REMARK 465 SER R 358 REMARK 465 ASN R 359 REMARK 465 ILE R 360 REMARK 465 GLU R 361 REMARK 465 GLN R 362 REMARK 465 GLN R 363 REMARK 465 ASN R 364 REMARK 465 SER R 365 REMARK 465 THR R 366 REMARK 465 ARG R 367 REMARK 465 ILE R 368 REMARK 465 ARG R 369 REMARK 465 GLN R 370 REMARK 465 ASN R 371 REMARK 465 THR R 372 REMARK 465 ARG R 373 REMARK 465 ASP R 374 REMARK 465 HIS R 375 REMARK 465 PRO R 376 REMARK 465 SER R 377 REMARK 465 THR R 378 REMARK 465 ALA R 379 REMARK 465 ASN R 380 REMARK 465 THR R 381 REMARK 465 VAL R 382 REMARK 465 ASP R 383 REMARK 465 ARG R 384 REMARK 465 THR R 385 REMARK 465 ASN R 386 REMARK 465 HIS R 387 REMARK 465 GLN R 388 REMARK 465 HIS R 389 REMARK 465 HIS R 390 REMARK 465 HIS R 391 REMARK 465 HIS R 392 REMARK 465 HIS R 393 REMARK 465 HIS R 394 REMARK 465 HIS R 395 REMARK 465 HIS R 396 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 OG SER A 293 OE1 GLU A 298 1.94 REMARK 500 OG SER E 147 OE1 GLU E 247 2.08 REMARK 500 O CYS A 254 NZ LYS A 317 2.09 REMARK 500 CG1 VAL R 145 CZ MEA D 4 2.13 REMARK 500 O ASP B 228 OG SER B 245 2.13 REMARK 500 OG1 THR B 274 O VAL B 315 2.18 REMARK 500 OE2 GLU A 8 OH TYR E 176 2.18 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 TYR D 1 C DAL D 2 N 0.184 REMARK 500 DAL D 2 C GLY D 3 N 0.168 REMARK 500 GLY D 3 C MEA D 4 N 0.207 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 TYR D 1 CB - CG - CD2 ANGL. DEV. = -9.1 DEGREES REMARK 500 TYR D 1 CB - CG - CD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 DAL D 2 N - CA - CB ANGL. DEV. = 11.1 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 ASP B 153 -168.80 -161.83 REMARK 500 MET E 193 -4.93 64.51 REMARK 500 THR E 211 -3.54 75.85 REMARK 500 LEU E 238 89.87 42.70 REMARK 500 ARG R 97 -59.00 -134.89 REMARK 500 THR R 99 -57.02 -134.84 REMARK 500 LYS R 100 123.32 74.67 REMARK 500 MET R 101 89.94 -69.67 REMARK 500 VAL R 145 -60.80 -91.41 REMARK 500 CYS R 219 38.36 -99.65 REMARK 500 HIS R 225 -87.62 24.48 REMARK 500 THR R 227 -57.22 75.48 REMARK 500 DAL D 2 39.44 -116.13 REMARK 500 MEA D 4 -72.20 -77.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39010 RELATED DB: EMDB REMARK 900 POSITIVE ALLOSTERIC MODULATOR(BMS986122)-BOUND MU-OPIOID RECEPTOR- REMARK 900 GI COMPLEX DBREF 8Y72 A 1 354 UNP P63096 GNAI1_HUMAN 1 354 DBREF 8Y72 B 2 340 UNP P54311 GBB1_RAT 2 340 DBREF 8Y72 C 1 68 UNP P63212 GBG2_BOVIN 1 68 DBREF 8Y72 E 1 248 PDB 8Y72 8Y72 1 248 DBREF 8Y72 R 2 388 UNP P35372 OPRM_HUMAN 2 388 DBREF 8Y72 D 1 5 PDB 8Y72 8Y72 1 5 SEQADV 8Y72 ALA A 203 UNP P63096 GLY 203 ENGINEERED MUTATION SEQADV 8Y72 SER A 326 UNP P63096 ALA 326 ENGINEERED MUTATION SEQADV 8Y72 MET B -12 UNP P54311 INITIATING METHIONINE SEQADV 8Y72 HIS B -11 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -10 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -9 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -8 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -7 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -6 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -5 UNP P54311 EXPRESSION TAG SEQADV 8Y72 HIS B -4 UNP P54311 EXPRESSION TAG SEQADV 8Y72 GLY B -3 UNP P54311 EXPRESSION TAG SEQADV 8Y72 SER B -2 UNP P54311 EXPRESSION TAG SEQADV 8Y72 LEU B -1 UNP P54311 EXPRESSION TAG SEQADV 8Y72 LEU B 0 UNP P54311 EXPRESSION TAG SEQADV 8Y72 GLN B 1 UNP P54311 EXPRESSION TAG SEQADV 8Y72 ASP R -6 UNP P35372 EXPRESSION TAG SEQADV 8Y72 TYR R -5 UNP P35372 EXPRESSION TAG SEQADV 8Y72 LYS R -4 UNP P35372 EXPRESSION TAG SEQADV 8Y72 ASP R -3 UNP P35372 EXPRESSION TAG SEQADV 8Y72 ASP R -2 UNP P35372 EXPRESSION TAG SEQADV 8Y72 ASP R -1 UNP P35372 EXPRESSION TAG SEQADV 8Y72 ASP R 0 UNP P35372 EXPRESSION TAG SEQADV 8Y72 VAL R 1 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 389 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 390 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 391 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 392 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 393 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 394 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 395 UNP P35372 EXPRESSION TAG SEQADV 8Y72 HIS R 396 UNP P35372 EXPRESSION TAG SEQRES 1 A 354 MET GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL SEQRES 2 A 354 GLU ARG SER LYS MET ILE ASP ARG ASN LEU ARG GLU ASP SEQRES 3 A 354 GLY GLU LYS ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU SEQRES 4 A 354 GLY ALA GLY GLU SER GLY LYS SER THR ILE VAL LYS GLN SEQRES 5 A 354 MET LYS ILE ILE HIS GLU ALA GLY TYR SER GLU GLU GLU SEQRES 6 A 354 CYS LYS GLN TYR LYS ALA VAL VAL TYR SER ASN THR ILE SEQRES 7 A 354 GLN SER ILE ILE ALA ILE ILE ARG ALA MET GLY ARG LEU SEQRES 8 A 354 LYS ILE ASP PHE GLY ASP SER ALA ARG ALA ASP ASP ALA SEQRES 9 A 354 ARG GLN LEU PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY SEQRES 10 A 354 PHE MET THR ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU SEQRES 11 A 354 TRP LYS ASP SER GLY VAL GLN ALA CYS PHE ASN ARG SER SEQRES 12 A 354 ARG GLU TYR GLN LEU ASN ASP SER ALA ALA TYR TYR LEU SEQRES 13 A 354 ASN ASP LEU ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO SEQRES 14 A 354 THR GLN GLN ASP VAL LEU ARG THR ARG VAL LYS THR THR SEQRES 15 A 354 GLY ILE VAL GLU THR HIS PHE THR PHE LYS ASP LEU HIS SEQRES 16 A 354 PHE LYS MET PHE ASP VAL GLY ALA GLN ARG SER GLU ARG SEQRES 17 A 354 LYS LYS TRP ILE HIS CYS PHE GLU GLY VAL THR ALA ILE SEQRES 18 A 354 ILE PHE CYS VAL ALA LEU SER ASP TYR ASP LEU VAL LEU SEQRES 19 A 354 ALA GLU ASP GLU GLU MET ASN ARG MET HIS GLU SER MET SEQRES 20 A 354 LYS LEU PHE ASP SER ILE CYS ASN ASN LYS TRP PHE THR SEQRES 21 A 354 ASP THR SER ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU SEQRES 22 A 354 PHE GLU GLU LYS ILE LYS LYS SER PRO LEU THR ILE CYS SEQRES 23 A 354 TYR PRO GLU TYR ALA GLY SER ASN THR TYR GLU GLU ALA SEQRES 24 A 354 ALA ALA TYR ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS SEQRES 25 A 354 ARG LYS ASP THR LYS GLU ILE TYR THR HIS PHE THR CYS SEQRES 26 A 354 SER THR ASP THR LYS ASN VAL GLN PHE VAL PHE ASP ALA SEQRES 27 A 354 VAL THR ASP VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS SEQRES 28 A 354 GLY LEU PHE SEQRES 1 B 353 MET HIS HIS HIS HIS HIS HIS HIS HIS GLY SER LEU LEU SEQRES 2 B 353 GLN SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN SEQRES 3 B 353 LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA SEQRES 4 B 353 ASP ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO SEQRES 5 B 353 VAL GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG SEQRES 6 B 353 GLY HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR SEQRES 7 B 353 ASP SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS SEQRES 8 B 353 LEU ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS SEQRES 9 B 353 ALA ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA SEQRES 10 B 353 TYR ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU SEQRES 11 B 353 ASP ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU SEQRES 12 B 353 GLY ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR SEQRES 13 B 353 GLY TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN SEQRES 14 B 353 ILE VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP SEQRES 15 B 353 ASP ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY SEQRES 16 B 353 HIS THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP SEQRES 17 B 353 THR ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA SEQRES 18 B 353 LYS LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR SEQRES 19 B 353 PHE THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE SEQRES 20 B 353 PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP SEQRES 21 B 353 ALA THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU SEQRES 22 B 353 LEU MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE SEQRES 23 B 353 THR SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU SEQRES 24 B 353 ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA SEQRES 25 B 353 LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP SEQRES 26 B 353 ASN ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET SEQRES 27 B 353 ALA VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE SEQRES 28 B 353 TRP ASN SEQRES 1 C 68 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 C 68 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 C 68 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 C 68 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 C 68 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 C 68 PHE PHE CYS SEQRES 1 E 248 MET VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 248 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 E 248 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 E 248 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 E 248 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 E 248 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 E 248 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 E 248 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 E 248 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 E 248 THR VAL SER ALA GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 E 248 SER GLY GLY GLY GLY SER ALA ASP ILE VAL MET THR GLN SEQRES 12 E 248 ALA THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SEQRES 13 E 248 SER ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER SEQRES 14 E 248 ASN GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO SEQRES 15 E 248 GLY GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN SEQRES 16 E 248 LEU ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SEQRES 17 E 248 SER GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU SEQRES 18 E 248 ALA GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU SEQRES 19 E 248 GLU TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU SEQRES 20 E 248 LEU SEQRES 1 R 403 ASP TYR LYS ASP ASP ASP ASP VAL ASP SER SER ALA ALA SEQRES 2 R 403 PRO THR ASN ALA SER ASN CYS THR ASP ALA LEU ALA TYR SEQRES 3 R 403 SER SER CYS SER PRO ALA PRO SER PRO GLY SER TRP VAL SEQRES 4 R 403 ASN LEU SER HIS LEU ASP GLY ASN LEU SER ASP PRO CYS SEQRES 5 R 403 GLY PRO ASN ARG THR ASP LEU GLY GLY ARG ASP SER LEU SEQRES 6 R 403 CYS PRO PRO THR GLY SER PRO SER MET ILE THR ALA ILE SEQRES 7 R 403 THR ILE MET ALA LEU TYR SER ILE VAL CYS VAL VAL GLY SEQRES 8 R 403 LEU PHE GLY ASN PHE LEU VAL MET TYR VAL ILE VAL ARG SEQRES 9 R 403 TYR THR LYS MET LYS THR ALA THR ASN ILE TYR ILE PHE SEQRES 10 R 403 ASN LEU ALA LEU ALA ASP ALA LEU ALA THR SER THR LEU SEQRES 11 R 403 PRO PHE GLN SER VAL ASN TYR LEU MET GLY THR TRP PRO SEQRES 12 R 403 PHE GLY THR ILE LEU CYS LYS ILE VAL ILE SER ILE ASP SEQRES 13 R 403 TYR TYR ASN MET PHE THR SER ILE PHE THR LEU CYS THR SEQRES 14 R 403 MET SER VAL ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL SEQRES 15 R 403 LYS ALA LEU ASP PHE ARG THR PRO ARG ASN ALA LYS ILE SEQRES 16 R 403 ILE ASN VAL CYS ASN TRP ILE LEU SER SER ALA ILE GLY SEQRES 17 R 403 LEU PRO VAL MET PHE MET ALA THR THR LYS TYR ARG GLN SEQRES 18 R 403 GLY SER ILE ASP CYS THR LEU THR PHE SER HIS PRO THR SEQRES 19 R 403 TRP TYR TRP GLU ASN LEU LEU LYS ILE CYS VAL PHE ILE SEQRES 20 R 403 PHE ALA PHE ILE MET PRO VAL LEU ILE ILE THR VAL CYS SEQRES 21 R 403 TYR GLY LEU MET ILE LEU ARG LEU LYS SER VAL ARG MET SEQRES 22 R 403 LEU SER GLY SER LYS GLU LYS ASP ARG ASN LEU ARG ARG SEQRES 23 R 403 ILE THR ARG MET VAL LEU VAL VAL VAL ALA VAL PHE ILE SEQRES 24 R 403 VAL CYS TRP THR PRO ILE HIS ILE TYR VAL ILE ILE LYS SEQRES 25 R 403 ALA LEU VAL THR ILE PRO GLU THR THR PHE GLN THR VAL SEQRES 26 R 403 SER TRP HIS PHE CYS ILE ALA LEU GLY TYR THR ASN SER SEQRES 27 R 403 CYS LEU ASN PRO VAL LEU TYR ALA PHE LEU ASP GLU ASN SEQRES 28 R 403 PHE LYS ARG CYS PHE ARG GLU PHE CYS ILE PRO THR SER SEQRES 29 R 403 SER ASN ILE GLU GLN GLN ASN SER THR ARG ILE ARG GLN SEQRES 30 R 403 ASN THR ARG ASP HIS PRO SER THR ALA ASN THR VAL ASP SEQRES 31 R 403 ARG THR ASN HIS GLN HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 D 5 TYR DAL GLY MEA ETA HET DAL D 2 5 HET MEA D 4 12 HET ETA D 5 4 HET CLR R 401 28 HET CLR R 402 28 HET VV9 R 403 39 HETNAM DAL D-ALANINE HETNAM MEA N-METHYLPHENYLALANINE HETNAM ETA ETHANOLAMINE HETNAM CLR CHOLESTEROL HETNAM VV9 (2~{S})-2-(3-BROMANYL-4-METHOXY-PHENYL)-3-(4- HETNAM 2 VV9 CHLOROPHENYL)SULFONYL-1,3-THIAZOLIDINE HETSYN VV9 BMS-986122 FORMUL 6 DAL C3 H7 N O2 FORMUL 6 MEA C10 H13 N O2 FORMUL 6 ETA C2 H7 N O FORMUL 7 CLR 2(C27 H46 O) FORMUL 9 VV9 C16 H15 BR CL N O3 S2 HELIX 1 AA1 SER A 6 ARG A 32 1 27 HELIX 2 AA2 GLY A 42 SER A 44 5 3 HELIX 3 AA3 GLY A 45 ILE A 55 1 11 HELIX 4 AA4 GLU A 207 GLU A 216 5 10 HELIX 5 AA5 SER A 228 TYR A 230 5 3 HELIX 6 AA6 ASN A 241 ASN A 255 1 15 HELIX 7 AA7 LYS A 270 SER A 281 1 12 HELIX 8 AA8 THR A 295 ASP A 309 1 15 HELIX 9 AA9 THR A 327 GLY A 352 1 26 HELIX 10 AB1 GLN B 6 ALA B 26 1 21 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 ALA C 10 ASN C 24 1 15 HELIX 13 AB4 LYS C 29 HIS C 44 1 16 HELIX 14 AB5 ALA E 28 PHE E 32 5 5 HELIX 15 AB6 ARG E 87 THR E 91 5 5 HELIX 16 AB7 GLU E 221 VAL E 225 5 5 HELIX 17 AB8 MET R 67 VAL R 96 1 30 HELIX 18 AB9 THR R 103 SER R 121 1 19 HELIX 19 AC1 THR R 122 MET R 132 1 11 HELIX 20 AC2 PHE R 137 HIS R 173 1 37 HELIX 21 AC3 HIS R 173 ARG R 181 1 9 HELIX 22 AC4 THR R 182 SER R 197 1 16 HELIX 23 AC5 SER R 197 PHE R 206 1 10 HELIX 24 AC6 THR R 227 PHE R 243 1 17 HELIX 25 AC7 PHE R 243 VAL R 264 1 22 HELIX 26 AC8 ARG R 265 SER R 268 5 4 HELIX 27 AC9 SER R 270 VAL R 308 1 39 HELIX 28 AD1 THR R 313 ALA R 339 1 27 HELIX 29 AD2 ASP R 342 ARG R 350 1 9 SHEET 1 AA1 6 VAL A 185 THR A 190 0 SHEET 2 AA1 6 HIS A 195 ASP A 200 -1 O ASP A 200 N VAL A 185 SHEET 3 AA1 6 VAL A 34 GLY A 40 1 N LEU A 36 O LYS A 197 SHEET 4 AA1 6 ALA A 220 ALA A 226 1 O ILE A 222 N LEU A 39 SHEET 5 AA1 6 SER A 263 ASN A 269 1 O PHE A 267 N PHE A 223 SHEET 6 AA1 6 ILE A 319 PHE A 323 1 O TYR A 320 N LEU A 266 SHEET 1 AA2 4 ARG B 46 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 ASN B 340 -1 O LEU B 336 N LEU B 51 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 ALA B 60 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 SHEET 4 AA3 4 LYS B 89 PRO B 94 -1 O ILE B 93 N LEU B 79 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O ALA B 113 N ALA B 104 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 SER B 136 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 THR B 178 N LEU B 168 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 ALA B 208 ASP B 212 -1 O LYS B 209 N SER B 201 SHEET 4 AA6 4 CYS B 218 PHE B 222 -1 O ARG B 219 N LEU B 210 SHEET 1 AA7 4 ALA B 231 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 GLY B 244 -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 GLY B 288 N SER B 275 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 E 3 SER E 7 0 SHEET 2 AA9 4 SER E 17 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AA9 4 THR E 78 THR E 84 -1 O LEU E 79 N CYS E 22 SHEET 4 AA9 4 PHE E 68 ASP E 73 -1 N SER E 71 O PHE E 80 SHEET 1 AB1 6 GLY E 10 VAL E 12 0 SHEET 2 AB1 6 THR E 115 VAL E 119 1 O THR E 116 N GLY E 10 SHEET 3 AB1 6 ALA E 92 SER E 99 -1 N TYR E 94 O THR E 115 SHEET 4 AB1 6 GLY E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 SHEET 5 AB1 6 LEU E 45 ILE E 51 -1 O VAL E 48 N TRP E 36 SHEET 6 AB1 6 ILE E 58 TYR E 60 -1 O TYR E 59 N TYR E 50 SHEET 1 AB2 4 GLY E 10 VAL E 12 0 SHEET 2 AB2 4 THR E 115 VAL E 119 1 O THR E 116 N GLY E 10 SHEET 3 AB2 4 ALA E 92 SER E 99 -1 N TYR E 94 O THR E 115 SHEET 4 AB2 4 PHE E 110 TRP E 111 -1 O PHE E 110 N ARG E 98 SHEET 1 AB3 4 MET E 141 THR E 142 0 SHEET 2 AB3 4 VAL E 156 SER E 162 -1 O ARG E 161 N THR E 142 SHEET 3 AB3 4 ALA E 212 ILE E 217 -1 O PHE E 213 N CYS E 160 SHEET 4 AB3 4 PHE E 204 SER E 209 -1 N SER E 207 O THR E 214 SHEET 1 AB4 6 SER E 147 PRO E 149 0 SHEET 2 AB4 6 THR E 244 GLU E 247 1 O LYS E 245 N VAL E 148 SHEET 3 AB4 6 VAL E 227 GLN E 232 -1 N TYR E 228 O THR E 244 SHEET 4 AB4 6 LEU E 175 GLN E 180 -1 N GLN E 180 O VAL E 227 SHEET 5 AB4 6 GLN E 187 TYR E 191 -1 O LEU E 189 N TRP E 177 SHEET 6 AB4 6 ASN E 195 LEU E 196 -1 O ASN E 195 N TYR E 191 SHEET 1 AB5 2 LYS R 211 ARG R 213 0 SHEET 2 AB5 2 SER R 216 ASP R 218 -1 O SER R 216 N ARG R 213 SSBOND 1 CYS E 160 CYS E 230 1555 1555 2.04 SSBOND 2 CYS R 142 CYS R 219 1555 1555 2.05 LINK C TYR D 1 N DAL D 2 1555 1555 1.52 LINK C DAL D 2 N GLY D 3 1555 1555 1.50 LINK C GLY D 3 N MEA D 4 1555 1555 1.54 LINK C MEA D 4 N ETA D 5 1555 1555 1.47 CISPEP 1 TYR D 1 DAL D 2 0 -4.94 CISPEP 2 MEA D 4 ETA D 5 0 -1.83 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