HEADER SIGNALING PROTEIN/ANTAGONIST 15-JUN-15 5C1M TITLE CRYSTAL STRUCTURE OF ACTIVE MU-OPIOID RECEPTOR BOUND TO THE AGONIST TITLE 2 BU72 COMPND MOL_ID: 1; COMPND 2 MOLECULE: MU-TYPE OPIOID RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MOR-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY 39; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: OPRM1, MOR, OPRM; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LIGANDS, MICE, AGONISTS, MORPHINANS, ACTIVATION, RECEPTORS, OPIOID, KEYWDS 2 MU, NANOBODY, SIGNALING PROTEIN-ANTAGONIST COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR W.J.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS,E.N.FEINBERG, AUTHOR 2 A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON,T.S.THORSEN,R.KLING,S.GRANIER, AUTHOR 3 P.GMEINER,S.M.HUSBANDS,J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR, AUTHOR 4 B.K.KOBILKA REVDAT 4 02-SEP-15 5C1M 1 JRNL REVDAT 3 26-AUG-15 5C1M 1 REMARK REVDAT 2 19-AUG-15 5C1M 1 JRNL REVDAT 1 05-AUG-15 5C1M 0 JRNL AUTH W.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS, JRNL AUTH 2 E.N.FEINBERG,A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON, JRNL AUTH 3 T.S.THORSEN,R.C.KLING,S.GRANIER,P.GMEINER,S.M.HUSBANDS, JRNL AUTH 4 J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR,B.K.KOBILKA JRNL TITL STRUCTURAL INSIGHTS INTO MU-OPIOID RECEPTOR ACTIVATION. JRNL REF NATURE V. 524 315 2015 JRNL REFN ESSN 1476-4687 JRNL PMID 26245379 JRNL DOI 10.1038/NATURE14886 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.46 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 39948 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.187 REMARK 3 R VALUE (WORKING SET) : 0.185 REMARK 3 FREE R VALUE : 0.222 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 42.4638 - 5.0587 0.99 2882 152 0.1842 0.2098 REMARK 3 2 5.0587 - 4.0162 0.99 2731 144 0.1694 0.2056 REMARK 3 3 4.0162 - 3.5088 1.00 2759 145 0.1815 0.1963 REMARK 3 4 3.5088 - 3.1881 1.00 2700 143 0.1892 0.2338 REMARK 3 5 3.1881 - 2.9597 1.00 2706 142 0.1887 0.2527 REMARK 3 6 2.9597 - 2.7852 1.00 2719 143 0.1791 0.2279 REMARK 3 7 2.7852 - 2.6458 1.00 2686 142 0.1702 0.2116 REMARK 3 8 2.6458 - 2.5306 1.00 2706 142 0.1808 0.2172 REMARK 3 9 2.5306 - 2.4332 1.00 2687 141 0.1863 0.2492 REMARK 3 10 2.4332 - 2.3492 1.00 2654 140 0.2036 0.2630 REMARK 3 11 2.3492 - 2.2758 1.00 2709 143 0.2051 0.2420 REMARK 3 12 2.2758 - 2.2107 1.00 2650 139 0.2219 0.2872 REMARK 3 13 2.2107 - 2.1525 1.00 2676 141 0.2459 0.2583 REMARK 3 14 2.1525 - 2.1000 1.00 2685 141 0.2583 0.2871 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.760 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 43.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.62 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 3515 REMARK 3 ANGLE : 1.193 4790 REMARK 3 CHIRALITY : 0.089 560 REMARK 3 PLANARITY : 0.005 572 REMARK 3 DIHEDRAL : 14.848 1335 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -2.4100 13.6674 -38.6891 REMARK 3 T TENSOR REMARK 3 T11: 0.2443 T22: 0.2096 REMARK 3 T33: 0.3193 T12: 0.0044 REMARK 3 T13: -0.0101 T23: -0.0334 REMARK 3 L TENSOR REMARK 3 L11: 1.1470 L22: 0.9213 REMARK 3 L33: 3.1499 L12: 0.1458 REMARK 3 L13: -0.0856 L23: -0.0317 REMARK 3 S TENSOR REMARK 3 S11: -0.0820 S12: -0.1589 S13: 0.0916 REMARK 3 S21: -0.0369 S22: -0.0081 S23: 0.0099 REMARK 3 S31: -0.3262 S32: -0.0490 S33: 0.0703 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 5C1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-15. REMARK 100 THE DEPOSITION ID IS D_1000210873. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 7.0-7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63134 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 42.455 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.14200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.5100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 14.45100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.270 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: CUBIC REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: RECONSTITUTED IN 10:1 REMARK 280 MONOOLEIN:CHOLESTEROL MIX. PRECIPITANT SOLUTION:15-25% PEG300, REMARK 280 100 MM HEPES PH 7.0-7.5, 1% 1,2,3-HEPTANETRIOL, 0.5-1.0% REMARK 280 POLYPROPYLENE GLYCOL P 400, 100-300 MM (NH4)2HPO4, PH 7.5, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y,-Z REMARK 290 8555 X,-Y,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 104.95000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 104.95000 REMARK 290 REMARK 290 REMARK: NULL 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19530 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY B 103 REMARK 465 GLN B 104 REMARK 465 SER B 105 REMARK 465 SER B 106 REMARK 465 SER B 107 REMARK 465 PRO B 108 REMARK 465 TYR B 109 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 269 CG CD CE NZ REMARK 470 GLU A 270 CG CD OE1 OE2 REMARK 470 ARG A 273 CG CD NE CZ NH1 NH2 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 A 164 O HOH A 501 2.14 REMARK 500 N GLN B 3 O HOH B 201 2.17 REMARK 500 NH1 ARG B 99 O ASP B 110 2.19 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 HIS A 54 -94.65 -138.90 REMARK 500 THR A 132 147.65 -170.59 REMARK 500 ARG A 179 46.16 -95.48 REMARK 500 PHE A 241 -61.42 -129.52 REMARK 500 SER A 266 -76.71 -96.63 REMARK 500 SER A 268 -27.95 -146.12 REMARK 500 ARG B 29 18.68 55.32 REMARK 500 MET B 34 -9.87 -141.91 REMARK 500 ALA B 125 24.91 -78.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 402 REMARK 610 OLC A 403 REMARK 610 P6G A 407 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 4VO A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 407 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4DKL RELATED DB: PDB REMARK 900 4DKL CONTAINS THE SAME PROTEIN BOUND TO A MORPHINAN ANTAGONIST DBREF 5C1M A 52 347 UNP P42866 OPRM_MOUSE 52 347 DBREF 5C1M B 3 127 PDB 5C1M 5C1M 3 127 SEQRES 1 A 296 GLY SER HIS SER LEU YCM PRO GLN THR GLY SER PRO SER SEQRES 2 A 296 MET VAL THR ALA ILE THR ILE MET ALA LEU TYR SER ILE SEQRES 3 A 296 VAL CYS VAL VAL GLY LEU PHE GLY ASN PHE LEU VAL MET SEQRES 4 A 296 TYR VAL ILE VAL ARG TYR THR LYS MET LYS THR ALA THR SEQRES 5 A 296 ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU SEQRES 6 A 296 ALA THR SER THR LEU PRO PHE GLN SER VAL ASN TYR LEU SEQRES 7 A 296 MET GLY THR TRP PRO PHE GLY ASN ILE LEU CYS LYS ILE SEQRES 8 A 296 VAL ILE SER ILE ASP TYR TYR ASN MET PHE THR SER ILE SEQRES 9 A 296 PHE THR LEU CYS THR MET SER VAL ASP ARG TYR ILE ALA SEQRES 10 A 296 VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO SEQRES 11 A 296 ARG ASN ALA LYS ILE VAL ASN VAL CYS ASN TRP ILE LEU SEQRES 12 A 296 SER SER ALA ILE GLY LEU PRO VAL MET PHE MET ALA THR SEQRES 13 A 296 THR LYS TYR ARG GLN GLY SER ILE ASP CYS THR LEU THR SEQRES 14 A 296 PHE SER HIS PRO THR TRP TYR TRP GLU ASN LEU LEU LYS SEQRES 15 A 296 ILE CYS VAL PHE ILE PHE ALA PHE ILE MET PRO VAL LEU SEQRES 16 A 296 ILE ILE THR VAL CYS TYR GLY LEU MET ILE LEU ARG LEU SEQRES 17 A 296 LYS SER VAL ARG MET LEU SER GLY SER LYS GLU LYS ASP SEQRES 18 A 296 ARG ASN LEU ARG ARG ILE THR ARG MET VAL LEU VAL VAL SEQRES 19 A 296 VAL ALA VAL PHE ILE VAL CYS TRP THR PRO ILE HIS ILE SEQRES 20 A 296 TYR VAL ILE ILE LYS ALA LEU ILE THR ILE PRO GLU THR SEQRES 21 A 296 THR PHE GLN THR VAL SER TRP HIS PHE CYS ILE ALA LEU SEQRES 22 A 296 GLY TYR THR ASN SER CYS LEU ASN PRO VAL LEU TYR ALA SEQRES 23 A 296 PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE SEQRES 1 B 125 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL ARG SEQRES 2 B 125 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP SER GLU SEQRES 3 B 125 ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG ALA PRO SEQRES 4 B 125 GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR TRP SER SEQRES 5 B 125 GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA ASP ARG SEQRES 6 B 125 PHE THR THR SER ARG ASP VAL ALA ASN ASN THR LEU TYR SEQRES 7 B 125 LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR ALA VAL SEQRES 8 B 125 TYR TYR CYS ALA ALA ARG ALA PRO VAL GLY GLN SER SER SEQRES 9 B 125 SER PRO TYR ASP TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 B 125 VAL THR VAL SER SER ALA ALA ALA MODRES 5C1M YCM A 57 CYS MODIFIED RESIDUE HET YCM A 57 10 HET 4VO A 401 32 HET OLC A 402 16 HET OLC A 403 18 HET CLR A 404 28 HET PO4 A 405 5 HET P6G A 406 19 HET P6G A 407 13 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM 4VO (2S,3S,3AR,5AR,6R,11BR,11CS)-3A-METHOXY-3,14-DIMETHYL- HETNAM 2 4VO 2-PHENYL-2,3,3A,6,7,11C-HEXAHYDRO-1H-6,11B- HETNAM 3 4VO (EPIMINOETHANO)-3,5A-METHANONAPHTHO[2,1-G]INDOL-10-OL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CLR CHOLESTEROL HETNAM PO4 PHOSPHATE ION HETNAM P6G HEXAETHYLENE GLYCOL HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN 4VO BU72 HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN P6G POLYETHYLENE GLYCOL PEG400 FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 3 4VO C28 H32 N2 O2 FORMUL 4 OLC 2(C21 H40 O4) FORMUL 6 CLR C27 H46 O FORMUL 7 PO4 O4 P 3- FORMUL 8 P6G 2(C12 H26 O7) FORMUL 10 HOH *94(H2 O) HELIX 1 AA1 SER A 64 TYR A 96 1 33 HELIX 2 AA2 THR A 101 SER A 119 1 19 HELIX 3 AA3 THR A 120 GLY A 131 1 12 HELIX 4 AA4 PHE A 135 HIS A 171 1 37 HELIX 5 AA5 HIS A 171 ARG A 179 1 9 HELIX 6 AA6 THR A 180 MET A 205 1 26 HELIX 7 AA7 PRO A 224 PHE A 241 1 18 HELIX 8 AA8 PHE A 241 VAL A 262 1 22 HELIX 9 AA9 SER A 268 ILE A 306 1 39 HELIX 10 AB1 THR A 311 ALA A 337 1 27 HELIX 11 AB2 ASP A 340 ARG A 345 1 6 HELIX 12 AB3 LYS B 87 THR B 91 5 5 SHEET 1 AA1 2 ALA A 206 ARG A 211 0 SHEET 2 AA1 2 SER A 214 LEU A 219 -1 O SER A 214 N ARG A 211 SHEET 1 AA2 4 VAL B 7 SER B 9 0 SHEET 2 AA2 4 LEU B 20 VAL B 25 -1 O SER B 23 N SER B 9 SHEET 3 AA2 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 20 SHEET 4 AA2 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA3 6 GLY B 12 VAL B 14 0 SHEET 2 AA3 6 THR B 118 VAL B 122 1 O THR B 121 N GLY B 12 SHEET 3 AA3 6 ALA B 92 ARG B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AA3 6 TYR B 32 ARG B 39 -1 N TYR B 32 O ARG B 99 SHEET 5 AA3 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA3 6 PRO B 58 TYR B 60 -1 O THR B 59 N SER B 50 SHEET 1 AA4 4 GLY B 12 VAL B 14 0 SHEET 2 AA4 4 THR B 118 VAL B 122 1 O THR B 121 N GLY B 12 SHEET 3 AA4 4 ALA B 92 ARG B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AA4 4 TYR B 113 TRP B 114 -1 O TYR B 113 N ALA B 98 SSBOND 1 CYS A 140 CYS A 217 1555 1555 2.05 SSBOND 2 CYS B 24 CYS B 96 1555 1555 2.05 LINK C LEU A 56 N YCM A 57 1555 1555 1.33 LINK C YCM A 57 N PRO A 58 1555 1555 1.34 CISPEP 1 THR A 60 GLY A 61 0 1.07 CISPEP 2 HIS A 223 PRO A 224 0 -9.29 CISPEP 3 GLY A 267 SER A 268 0 -3.44 CISPEP 4 CYS A 346 PHE A 347 0 9.00 SITE 1 AC1 9 HIS A 54 SER A 55 GLN A 124 ASP A 147 SITE 2 AC1 9 VAL A 236 VAL A 300 TYR A 326 HOH A 526 SITE 3 AC1 9 HOH A 553 SITE 1 AC2 2 OLC A 403 CLR A 404 SITE 1 AC3 3 LEU A 254 ILE A 306 OLC A 402 SITE 1 AC4 5 PRO A 295 TYR A 299 ILE A 302 SER A 317 SITE 2 AC4 5 OLC A 402 SITE 1 AC5 3 HIS A 223 PRO A 224 THR A 225 SITE 1 AC6 5 THR A 160 PHE A 178 ASN A 191 TRP A 226 SITE 2 AC6 5 MET A 243 SITE 1 AC7 1 PHE A 84 CRYST1 44.430 144.000 209.900 90.00 90.00 90.00 I 21 21 21 8 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 0.022507 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006944 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004764 0.00000