HEADER MEMBRANE PROTEIN 25-APR-24 9BJK TITLE INACTIVE MU OPIOID RECEPTOR BOUND TO NB6, NALOXONE AND NAM COMPND MOL_ID: 1; COMPND 2 MOLECULE: KAPPA OPIOID RECEPTOR NANOBODY 6; COMPND 3 CHAIN: N; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MU-TYPE OPIOID RECEPTOR; COMPND 7 CHAIN: R; COMPND 8 SYNONYM: M-OR-1,MOR-1; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 3 ORGANISM_TAXID: 9844; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 GENE: OPRM1, MOR, OPRM; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS G-PROTEIN COUPLED RECEPTOR, INACTIVE, OPIOID, ALLOSTERIC MODULATOR, KEYWDS 2 MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR E.S.O'BRIEN,H.WANG,K.KAAVYA KRISHNA,C.ZHANG,B.K.KOBILKA JRNL AUTH E.S.O'BRIEN,V.A.RANGARI,A.EL DAIBANI,S.O.EANS,H.R.HAMMOND, JRNL AUTH 2 E.WHITE,H.WANG,Y.SHIIMURA,K.KRISHNA KUMAR,Q.JIANG, JRNL AUTH 3 K.APPOURCHAUX,W.HUANG,C.ZHANG,B.J.KENNEDY,J.M.MATHIESEN, JRNL AUTH 4 T.CHE,J.P.MCLAUGHLIN,S.MAJUMDAR,B.K.KOBILKA JRNL TITL A MU-OPIOID RECEPTOR MODULATOR THAT WORKS COOPERATIVELY WITH JRNL TITL 2 NALOXONE. JRNL REF NATURE 2024 JRNL REFN ESSN 1476-4687 JRNL PMID 38961287 JRNL DOI 10.1038/S41586-024-07587-7 REMARK 2 REMARK 2 RESOLUTION. 3.26 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) : 3.260 REMARK 3 NUMBER OF PARTICLES : 128613 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 9BJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000283479. 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 : MU-TYPE OPIOID RECEPTOR WITH REMARK 245 KAPPA-TYPE OPIOID RECEPTOR ICL3 REMARK 245 IN COMPLEX WITH NB6, NALOXONE REMARK 245 AND A NEGATIVE ALLOSTERIC REMARK 245 MODULATOR REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1400.00 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) : 60.00 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, R 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 N 1 REMARK 465 ALA N 2 REMARK 465 GLN N 3 REMARK 465 VAL N 4 REMARK 465 GLN N 5 REMARK 465 LEU N 6 REMARK 465 GLN N 7 REMARK 465 GLU N 8 REMARK 465 SER N 9 REMARK 465 GLY N 10 REMARK 465 GLY N 11 REMARK 465 GLY N 12 REMARK 465 LEU N 13 REMARK 465 VAL N 14 REMARK 465 GLN N 15 REMARK 465 ALA N 16 REMARK 465 GLY N 17 REMARK 465 GLU N 18 REMARK 465 SER N 19 REMARK 465 LEU N 20 REMARK 465 ARG N 21 REMARK 465 LEU N 22 REMARK 465 SER N 23 REMARK 465 CYS N 24 REMARK 465 ALA N 25 REMARK 465 ALA N 26 REMARK 465 SER N 27 REMARK 465 GLY N 28 REMARK 465 ARG N 41 REMARK 465 VAL N 42 REMARK 465 SER N 43 REMARK 465 GLY N 44 REMARK 465 ASN N 45 REMARK 465 GLN N 46 REMARK 465 ARG N 47 REMARK 465 GLU N 48 REMARK 465 TYR N 61 REMARK 465 GLY N 62 REMARK 465 ASP N 63 REMARK 465 SER N 64 REMARK 465 VAL N 65 REMARK 465 LYS N 66 REMARK 465 GLY N 67 REMARK 465 ARG N 68 REMARK 465 PHE N 69 REMARK 465 ALA N 76 REMARK 465 LYS N 77 REMARK 465 ASN N 78 REMARK 465 THR N 79 REMARK 465 VAL N 80 REMARK 465 TYR N 81 REMARK 465 LEU N 82 REMARK 465 GLN N 83 REMARK 465 MET N 84 REMARK 465 SER N 85 REMARK 465 SER N 86 REMARK 465 LEU N 87 REMARK 465 LYS N 88 REMARK 465 PRO N 89 REMARK 465 GLU N 90 REMARK 465 ASP N 91 REMARK 465 THR N 92 REMARK 465 GLN N 115 REMARK 465 GLY N 116 REMARK 465 THR N 117 REMARK 465 GLN N 118 REMARK 465 VAL N 119 REMARK 465 THR N 120 REMARK 465 VAL N 121 REMARK 465 SER N 122 REMARK 465 SER N 123 REMARK 465 HIS N 124 REMARK 465 HIS N 125 REMARK 465 HIS N 126 REMARK 465 HIS N 127 REMARK 465 HIS N 128 REMARK 465 HIS N 129 REMARK 465 GLU N 130 REMARK 465 PRO N 131 REMARK 465 GLU N 132 REMARK 465 ALA N 133 REMARK 465 MET R -19 REMARK 465 LYS R -18 REMARK 465 THR R -17 REMARK 465 ILE R -16 REMARK 465 ILE R -15 REMARK 465 ALA R -14 REMARK 465 LEU R -13 REMARK 465 SER R -12 REMARK 465 TYR R -11 REMARK 465 ILE R -10 REMARK 465 PHE R -9 REMARK 465 CYS R -8 REMARK 465 LEU R -7 REMARK 465 VAL R -6 REMARK 465 PHE R -5 REMARK 465 ALA R -4 REMARK 465 ASP R -3 REMARK 465 TYR R -2 REMARK 465 LYS R -1 REMARK 465 ASP R 0 REMARK 465 ASP R 1 REMARK 465 ASP R 2 REMARK 465 ASP R 3 REMARK 465 ALA R 4 REMARK 465 MET R 5 REMARK 465 GLY R 6 REMARK 465 PRO R 7 REMARK 465 GLY R 8 REMARK 465 ASN R 9 REMARK 465 ILE R 10 REMARK 465 SER R 11 REMARK 465 ASP R 12 REMARK 465 CYS R 13 REMARK 465 SER R 14 REMARK 465 ASP R 15 REMARK 465 PRO R 16 REMARK 465 LEU R 17 REMARK 465 ALA R 18 REMARK 465 PRO R 19 REMARK 465 ALA 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 GLY R 27 REMARK 465 SER R 28 REMARK 465 TRP R 29 REMARK 465 LEU R 30 REMARK 465 ASN R 31 REMARK 465 LEU R 32 REMARK 465 SER R 33 REMARK 465 HIS R 34 REMARK 465 VAL R 35 REMARK 465 ASP R 36 REMARK 465 GLY R 37 REMARK 465 ASN R 38 REMARK 465 GLN R 39 REMARK 465 SER R 40 REMARK 465 ASP R 41 REMARK 465 PRO R 42 REMARK 465 CYS R 43 REMARK 465 GLY R 44 REMARK 465 PRO R 45 REMARK 465 ASN R 46 REMARK 465 ARG R 47 REMARK 465 THR R 48 REMARK 465 GLY R 49 REMARK 465 LEU R 50 REMARK 465 GLY R 51 REMARK 465 GLY R 52 REMARK 465 SER R 53 REMARK 465 HIS R 54 REMARK 465 SER R 55 REMARK 465 LEU R 56 REMARK 465 CYS R 57 REMARK 465 PRO R 58 REMARK 465 GLN R 59 REMARK 465 THR R 60 REMARK 465 GLY R 61 REMARK 465 SER R 62 REMARK 465 PRO R 63 REMARK 465 SER R 64 REMARK 465 CYS R 351 REMARK 465 ILE R 352 REMARK 465 PRO R 353 REMARK 465 THR R 354 REMARK 465 SER R 355 REMARK 465 SER R 356 REMARK 465 THR R 357 REMARK 465 ILE R 358 REMARK 465 GLU R 359 REMARK 465 GLN R 360 REMARK 465 GLN R 361 REMARK 465 ASN R 362 REMARK 465 SER R 363 REMARK 465 ALA R 364 REMARK 465 ARG R 365 REMARK 465 ILE R 366 REMARK 465 ARG R 367 REMARK 465 GLN R 368 REMARK 465 ASN R 369 REMARK 465 THR R 370 REMARK 465 ARG R 371 REMARK 465 GLU R 372 REMARK 465 HIS R 373 REMARK 465 PRO R 374 REMARK 465 SER R 375 REMARK 465 THR R 376 REMARK 465 ALA R 377 REMARK 465 ASN R 378 REMARK 465 THR R 379 REMARK 465 VAL R 380 REMARK 465 ASP R 381 REMARK 465 ARG R 382 REMARK 465 THR R 383 REMARK 465 ASN R 384 REMARK 465 HIS R 385 REMARK 465 GLN R 386 REMARK 465 LEU R 387 REMARK 465 GLU R 388 REMARK 465 ASN R 389 REMARK 465 LEU R 390 REMARK 465 GLU R 391 REMARK 465 ALA R 392 REMARK 465 GLU R 393 REMARK 465 THR R 394 REMARK 465 ALA R 395 REMARK 465 PRO R 396 REMARK 465 LEU R 397 REMARK 465 PRO R 398 REMARK 465 ASP R 399 REMARK 465 ILE R 400 REMARK 465 HIS R 401 REMARK 465 HIS R 402 REMARK 465 HIS R 403 REMARK 465 HIS R 404 REMARK 465 HIS R 405 REMARK 465 HIS R 406 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 THR N 29 OG1 CG2 REMARK 470 ILE N 30 CG1 CG2 CD1 REMARK 470 ARG N 32 CG CD NE CZ NH1 NH2 REMARK 470 TYR N 39 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG N 40 CG CD NE CZ NH1 NH2 REMARK 470 LEU N 49 CG CD1 CD2 REMARK 470 VAL N 50 CG1 CG2 REMARK 470 SER N 52 OG REMARK 470 ILE N 53 CG1 CG2 CD1 REMARK 470 SER N 55 OG REMARK 470 SER N 58 OG REMARK 470 THR N 59 OG1 CG2 REMARK 470 LYS N 60 CG CD CE NZ REMARK 470 THR N 70 OG1 CG2 REMARK 470 ILE N 71 CG1 CG2 CD1 REMARK 470 SER N 72 OG REMARK 470 ARG N 73 CG CD NE CZ NH1 NH2 REMARK 470 ASP N 74 CG OD1 OD2 REMARK 470 ASN N 75 CG OD1 ND2 REMARK 470 VAL N 94 CG1 CG2 REMARK 470 TYR N 95 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR N 96 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 CYS N 97 SG REMARK 470 THR N 103 OG1 CG2 REMARK 470 GLU N 107 CG CD OE1 OE2 REMARK 470 GLU N 108 CG CD OE1 OE2 REMARK 470 ASP N 111 CG OD1 OD2 REMARK 470 MET R 65 CG SD CE REMARK 470 VAL R 66 CG1 CG2 REMARK 470 VAL R 80 CG1 CG2 REMARK 470 PHE R 87 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU R 88 CG CD1 CD2 REMARK 470 ARG R 95 CG CD NE CZ NH1 NH2 REMARK 470 TYR R 96 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR R 97 OG1 CG2 REMARK 470 LYS R 98 CG CD CE NZ REMARK 470 LYS R 100 CG CD CE NZ REMARK 470 VAL R 173 CG1 CG2 REMARK 470 LYS R 174 CG CD CE NZ REMARK 470 LEU R 176 CG CD1 CD2 REMARK 470 ASP R 177 CG OD1 OD2 REMARK 470 ARG R 182 CG CD NE CZ NH1 NH2 REMARK 470 LYS R 185 CG CD CE NZ REMARK 470 MET R 203 CG SD CE REMARK 470 LYS R 209 CG CD CE NZ REMARK 470 TYR R 210 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG R 211 CG CD NE CZ NH1 NH2 REMARK 470 GLN R 212 CG CD OE1 NE2 REMARK 470 SER R 214 OG REMARK 470 ASP R 216 CG OD1 OD2 REMARK 470 THR R 220 OG1 CG2 REMARK 470 SER R 222 OG REMARK 470 MET R 243 CG SD CE REMARK 470 LEU R 257 CG CD1 CD2 REMARK 470 ARG R 258 CG CD NE CZ NH1 NH2 REMARK 470 SER R 261 OG REMARK 470 VAL R 262 CG1 CG2 REMARK 470 SER R 266 OG REMARK 470 SER R 268 OG REMARK 470 GLU R 270 CG CD OE1 OE2 REMARK 470 ARG R 273 CG CD NE CZ NH1 NH2 REMARK 470 ASN R 274 CG OD1 ND2 REMARK 470 ARG R 277 CG CD NE CZ NH1 NH2 REMARK 470 ILE R 306 CG1 CG2 CD1 REMARK 470 THR R 307 OG1 CG2 REMARK 470 ILE R 308 CG1 CG2 CD1 REMARK 470 GLU R 310 CG CD OE1 OE2 REMARK 470 THR R 311 OG1 CG2 REMARK 470 THR R 312 OG1 CG2 REMARK 470 PHE R 313 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR R 315 OG1 CG2 REMARK 470 GLU R 341 CG CD OE1 OE2 REMARK 470 LYS R 344 CG CD CE NZ REMARK 470 ARG R 345 CG CD NE CZ NH1 NH2 REMARK 470 ARG R 348 CG CD NE CZ NH1 NH2 REMARK 470 GLU R 349 CG CD OE1 OE2 REMARK 470 PHE R 350 CG CD1 CD2 CE1 CE2 CZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ARG N 32 139.53 -172.71 REMARK 500 ALA N 51 130.52 -171.64 REMARK 500 THR N 54 -166.31 -75.89 REMARK 500 ARG R 179 23.31 -143.48 REMARK 500 SER R 222 -73.85 -66.05 REMARK 500 PHE R 241 -60.37 -108.36 REMARK 500 THR R 307 60.39 61.52 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ALA R 240 PHE R 241 144.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44635 RELATED DB: EMDB REMARK 900 INACTIVE MU OPIOID RECEPTOR BOUND TO NB6, NALOXONE AND NAM DBREF 9BJK N 1 133 PDB 9BJK 9BJK 1 133 DBREF 9BJK R 6 398 UNP P42866 OPRM_MOUSE 6 398 SEQADV 9BJK MET R -19 UNP P42866 INITIATING METHIONINE SEQADV 9BJK LYS R -18 UNP P42866 EXPRESSION TAG SEQADV 9BJK THR R -17 UNP P42866 EXPRESSION TAG SEQADV 9BJK ILE R -16 UNP P42866 EXPRESSION TAG SEQADV 9BJK ILE R -15 UNP P42866 EXPRESSION TAG SEQADV 9BJK ALA R -14 UNP P42866 EXPRESSION TAG SEQADV 9BJK LEU R -13 UNP P42866 EXPRESSION TAG SEQADV 9BJK SER R -12 UNP P42866 EXPRESSION TAG SEQADV 9BJK TYR R -11 UNP P42866 EXPRESSION TAG SEQADV 9BJK ILE R -10 UNP P42866 EXPRESSION TAG SEQADV 9BJK PHE R -9 UNP P42866 EXPRESSION TAG SEQADV 9BJK CYS R -8 UNP P42866 EXPRESSION TAG SEQADV 9BJK LEU R -7 UNP P42866 EXPRESSION TAG SEQADV 9BJK VAL R -6 UNP P42866 EXPRESSION TAG SEQADV 9BJK PHE R -5 UNP P42866 EXPRESSION TAG SEQADV 9BJK ALA R -4 UNP P42866 EXPRESSION TAG SEQADV 9BJK ASP R -3 UNP P42866 EXPRESSION TAG SEQADV 9BJK TYR R -2 UNP P42866 EXPRESSION TAG SEQADV 9BJK LYS R -1 UNP P42866 EXPRESSION TAG SEQADV 9BJK ASP R 0 UNP P42866 EXPRESSION TAG SEQADV 9BJK ASP R 1 UNP P42866 EXPRESSION TAG SEQADV 9BJK ASP R 2 UNP P42866 EXPRESSION TAG SEQADV 9BJK ASP R 3 UNP P42866 EXPRESSION TAG SEQADV 9BJK ALA R 4 UNP P42866 EXPRESSION TAG SEQADV 9BJK MET R 5 UNP P42866 EXPRESSION TAG SEQADV 9BJK LEU R 264 UNP P42866 MET 264 ENGINEERED MUTATION SEQADV 9BJK ARG R 269 UNP P42866 LYS 269 ENGINEERED MUTATION SEQADV 9BJK ASP R 399 UNP P42866 EXPRESSION TAG SEQADV 9BJK ILE R 400 UNP P42866 EXPRESSION TAG SEQADV 9BJK HIS R 401 UNP P42866 EXPRESSION TAG SEQADV 9BJK HIS R 402 UNP P42866 EXPRESSION TAG SEQADV 9BJK HIS R 403 UNP P42866 EXPRESSION TAG SEQADV 9BJK HIS R 404 UNP P42866 EXPRESSION TAG SEQADV 9BJK HIS R 405 UNP P42866 EXPRESSION TAG SEQADV 9BJK HIS R 406 UNP P42866 EXPRESSION TAG SEQRES 1 N 133 MET ALA GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 N 133 VAL GLN ALA GLY GLU SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 N 133 SER GLY THR ILE PHE ARG LEU TYR ASP MET GLY TRP TYR SEQRES 4 N 133 ARG ARG VAL SER GLY ASN GLN ARG GLU LEU VAL ALA SER SEQRES 5 N 133 ILE THR SER GLY GLY SER THR LYS TYR GLY ASP SER VAL SEQRES 6 N 133 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 N 133 THR VAL TYR LEU GLN MET SER SER LEU LYS PRO GLU ASP SEQRES 8 N 133 THR ALA VAL TYR TYR CYS ASN ALA GLU TYR ARG THR GLY SEQRES 9 N 133 ILE TRP GLU GLU LEU LEU ASP GLY TRP GLY GLN GLY THR SEQRES 10 N 133 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU SEQRES 11 N 133 PRO GLU ALA SEQRES 1 R 426 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 426 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLY SEQRES 3 R 426 PRO GLY ASN ILE SER ASP CYS SER ASP PRO LEU ALA PRO SEQRES 4 R 426 ALA SER CYS SER PRO ALA PRO GLY SER TRP LEU ASN LEU SEQRES 5 R 426 SER HIS VAL ASP GLY ASN GLN SER ASP PRO CYS GLY PRO SEQRES 6 R 426 ASN ARG THR GLY LEU GLY GLY SER HIS SER LEU CYS PRO SEQRES 7 R 426 GLN THR GLY SER PRO SER MET VAL THR ALA ILE THR ILE SEQRES 8 R 426 MET ALA LEU TYR SER ILE VAL CYS VAL VAL GLY LEU PHE SEQRES 9 R 426 GLY ASN PHE LEU VAL MET TYR VAL ILE VAL ARG TYR THR SEQRES 10 R 426 LYS MET LYS THR ALA THR ASN ILE TYR ILE PHE ASN LEU SEQRES 11 R 426 ALA LEU ALA ASP ALA LEU ALA THR SER THR LEU PRO PHE SEQRES 12 R 426 GLN SER VAL ASN TYR LEU MET GLY THR TRP PRO PHE GLY SEQRES 13 R 426 ASN ILE LEU CYS LYS ILE VAL ILE SER ILE ASP TYR TYR SEQRES 14 R 426 ASN MET PHE THR SER ILE PHE THR LEU CYS THR MET SER SEQRES 15 R 426 VAL ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA SEQRES 16 R 426 LEU ASP PHE ARG THR PRO ARG ASN ALA LYS ILE VAL ASN SEQRES 17 R 426 VAL CYS ASN TRP ILE LEU SER SER ALA ILE GLY LEU PRO SEQRES 18 R 426 VAL MET PHE MET ALA THR THR LYS TYR ARG GLN GLY SER SEQRES 19 R 426 ILE ASP CYS THR LEU THR PHE SER HIS PRO THR TRP TYR SEQRES 20 R 426 TRP GLU ASN LEU LEU LYS ILE CYS VAL PHE ILE PHE ALA SEQRES 21 R 426 PHE ILE MET PRO VAL LEU ILE ILE THR VAL CYS TYR GLY SEQRES 22 R 426 LEU MET ILE LEU ARG LEU LYS SER VAL ARG LEU LEU SER SEQRES 23 R 426 GLY SER ARG GLU LYS ASP ARG ASN LEU ARG ARG ILE THR SEQRES 24 R 426 ARG MET VAL LEU VAL VAL VAL ALA VAL PHE ILE VAL CYS SEQRES 25 R 426 TRP THR PRO ILE HIS ILE TYR VAL ILE ILE LYS ALA LEU SEQRES 26 R 426 ILE THR ILE PRO GLU THR THR PHE GLN THR VAL SER TRP SEQRES 27 R 426 HIS PHE CYS ILE ALA LEU GLY TYR THR ASN SER CYS LEU SEQRES 28 R 426 ASN PRO VAL LEU TYR ALA PHE LEU ASP GLU ASN PHE LYS SEQRES 29 R 426 ARG CYS PHE ARG GLU PHE CYS ILE PRO THR SER SER THR SEQRES 30 R 426 ILE GLU GLN GLN ASN SER ALA ARG ILE ARG GLN ASN THR SEQRES 31 R 426 ARG GLU HIS PRO SER THR ALA ASN THR VAL ASP ARG THR SEQRES 32 R 426 ASN HIS GLN LEU GLU ASN LEU GLU ALA GLU THR ALA PRO SEQRES 33 R 426 LEU PRO ASP ILE HIS HIS HIS HIS HIS HIS HET APV R 501 24 HET APU R 502 44 FORMUL 3 APV FORMUL 4 APU HELIX 1 AA1 VAL R 66 TYR R 96 1 31 HELIX 2 AA2 ASN R 104 SER R 119 1 16 HELIX 3 AA3 THR R 120 GLY R 131 1 12 HELIX 4 AA4 ASN R 137 HIS R 171 1 35 HELIX 5 AA5 HIS R 171 PHE R 178 1 8 HELIX 6 AA6 THR R 180 MET R 205 1 26 HELIX 7 AA7 TRP R 226 MET R 243 1 18 HELIX 8 AA8 MET R 243 VAL R 262 1 20 HELIX 9 AA9 SER R 268 ILE R 306 1 39 HELIX 10 AB1 THR R 311 ASP R 340 1 30 HELIX 11 AB2 ASP R 340 PHE R 350 1 11 SHEET 1 AA1 3 ARG N 32 GLY N 37 0 SHEET 2 AA1 3 ASN N 98 ARG N 102 -1 O ASN N 98 N GLY N 37 SHEET 3 AA1 3 LEU N 110 TRP N 113 -1 O LEU N 110 N TYR N 101 SHEET 1 AA2 2 ALA R 206 THR R 208 0 SHEET 2 AA2 2 CYS R 217 LEU R 219 -1 O THR R 218 N THR R 207 SSBOND 1 CYS R 140 CYS R 217 1555 1555 2.03 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