HEADER MEMBRANE PROTEIN 27-DEC-24 9L80 TITLE STRUCTURE OF GPR119-GS COMPLEX BOUND TO AN ALLOSTERIC MODULATOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: ADENYLATE CYCLASE-STIMULATING G ALPHA PROTEIN; COMPND 6 EC: 3.6.5.-; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 11 BETA-1; COMPND 12 CHAIN: B; COMPND 13 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 3; COMPND 16 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 17 GAMMA-2; COMPND 18 CHAIN: G; COMPND 19 SYNONYM: G GAMMA-I; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 4; COMPND 22 MOLECULE: NB35; COMPND 23 CHAIN: N; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 5; COMPND 26 MOLECULE: GLUCOSE-DEPENDENT INSULINOTROPIC RECEPTOR; COMPND 27 CHAIN: R; COMPND 28 SYNONYM: G-PROTEIN COUPLED RECEPTOR 119; COMPND 29 ENGINEERED: YES; COMPND 30 MOL_ID: 6; COMPND 31 MOLECULE: SCFV16; COMPND 32 CHAIN: S; COMPND 33 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: GNAS, GNAS1, GSP; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; 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: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; 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: TRICHOPLUSIA NI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 24 ORGANISM_TAXID: 9844; SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 GENE: GPR119; SOURCE 32 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 36 ORGANISM_TAXID: 10090; SOURCE 37 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 38 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS GPCR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Q.SUN,G.HE,X.XU,X.LIU REVDAT 1 31-DEC-25 9L80 0 JRNL AUTH Q.SUN,G.HE,X.XU,X.LIU JRNL TITL STRUCTURE OF GPR119-GS COMPLEX BOUND TO AN ALLOSTERIC JRNL TITL 2 MODULATOR JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.33 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) : 3.330 REMARK 3 NUMBER OF PARTICLES : 106271 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9L80 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1300055132. 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 : STRUCTURE OF GPR119-GS COMPLEX REMARK 245 BOUND TO AN ALLOSTERIC 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 : 7.50 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 : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1300.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1600.00 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, G, N, R, S 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 A 9 REMARK 465 CYS A 10 REMARK 465 THR A 11 REMARK 465 LEU A 12 REMARK 465 LYS A 189 REMARK 465 GLN A 190 REMARK 465 MET A 191 REMARK 465 ARG A 192 REMARK 465 ILE A 193 REMARK 465 LEU A 194 REMARK 465 HIS A 195 REMARK 465 GLY A 196 REMARK 465 GLY A 197 REMARK 465 SER A 198 REMARK 465 GLY A 199 REMARK 465 GLY A 200 REMARK 465 SER A 201 REMARK 465 GLY A 202 REMARK 465 GLY A 203 REMARK 465 THR A 204 REMARK 465 SER A 205 REMARK 465 MET 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 G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 GLU G 63 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 HIS N 129 REMARK 465 HIS N 130 REMARK 465 HIS N 131 REMARK 465 HIS N 132 REMARK 465 HIS N 133 REMARK 465 HIS N 134 REMARK 465 GLU N 135 REMARK 465 PRO N 136 REMARK 465 GLU N 137 REMARK 465 ALA N 138 REMARK 465 MET R -23 REMARK 465 LYS R -22 REMARK 465 THR R -21 REMARK 465 ILE R -20 REMARK 465 ILE R -19 REMARK 465 ALA R -18 REMARK 465 LEU R -17 REMARK 465 SER R -16 REMARK 465 TYR R -15 REMARK 465 ILE R -14 REMARK 465 PHE R -13 REMARK 465 CYS R -12 REMARK 465 LEU R -11 REMARK 465 VAL R -10 REMARK 465 PHE R -9 REMARK 465 ALA R -8 REMARK 465 ASP R -7 REMARK 465 TYR R -6 REMARK 465 LYS R -5 REMARK 465 ASP R -4 REMARK 465 ASP R -3 REMARK 465 ASP R -2 REMARK 465 ASP R -1 REMARK 465 ALA R 0 REMARK 465 MET R 1 REMARK 465 GLU R 2 REMARK 465 SER R 3 REMARK 465 SER R 4 REMARK 465 PHE R 5 REMARK 465 SER R 6 REMARK 465 PHE R 7 REMARK 465 SER R 68 REMARK 465 PRO R 69 REMARK 465 SER R 70 REMARK 465 ARG R 71 REMARK 465 PRO R 72 REMARK 465 THR R 73 REMARK 465 GLN R 74 REMARK 465 GLY R 210 REMARK 465 GLY R 211 REMARK 465 TYR R 212 REMARK 465 ARG R 213 REMARK 465 SER R 214 REMARK 465 PRO R 215 REMARK 465 ARG R 216 REMARK 465 THR R 217 REMARK 465 ALA R 250 REMARK 465 CYS R 251 REMARK 465 GLN R 252 REMARK 465 GLU R 253 REMARK 465 CYS R 254 REMARK 465 HIS R 255 REMARK 465 LEU R 256 REMARK 465 TYR R 257 REMARK 465 LEU R 258 REMARK 465 VAL R 259 REMARK 465 LEU R 260 REMARK 465 VAL R 297 REMARK 465 LYS R 298 REMARK 465 LYS R 299 REMARK 465 VAL R 300 REMARK 465 LEU R 301 REMARK 465 THR R 302 REMARK 465 SER R 303 REMARK 465 PHE R 304 REMARK 465 LEU R 305 REMARK 465 LEU R 306 REMARK 465 PHE R 307 REMARK 465 LEU R 308 REMARK 465 SER R 309 REMARK 465 ALA R 310 REMARK 465 ARG R 311 REMARK 465 ASN R 312 REMARK 465 CYS R 313 REMARK 465 GLY R 314 REMARK 465 PRO R 315 REMARK 465 GLU R 316 REMARK 465 ARG R 317 REMARK 465 PRO R 318 REMARK 465 ARG R 319 REMARK 465 GLU R 320 REMARK 465 SER R 321 REMARK 465 SER R 322 REMARK 465 CYS R 323 REMARK 465 HIS R 324 REMARK 465 ILE R 325 REMARK 465 VAL R 326 REMARK 465 THR R 327 REMARK 465 ILE R 328 REMARK 465 SER R 329 REMARK 465 SER R 330 REMARK 465 SER R 331 REMARK 465 GLU R 332 REMARK 465 PHE R 333 REMARK 465 ASP R 334 REMARK 465 GLY R 335 REMARK 465 ASP S 1 REMARK 465 SER S 120A REMARK 465 GLY S 120B REMARK 465 GLY S 120C REMARK 465 GLY S 120D REMARK 465 GLY S 120E REMARK 465 SER S 120F REMARK 465 GLY S 120G REMARK 465 GLY S 120H REMARK 465 GLY S 120I REMARK 465 GLY S 120J REMARK 465 SER S 120K REMARK 465 GLY S 120L REMARK 465 GLY S 120M REMARK 465 GLY S 120N REMARK 465 GLY S 120O REMARK 465 SER S 120P REMARK 465 LYS S 236 REMARK 465 ALA S 237 REMARK 465 ALA S 238 REMARK 465 ALA S 239 REMARK 465 HIS S 240 REMARK 465 HIS S 241 REMARK 465 HIS S 242 REMARK 465 HIS S 243 REMARK 465 HIS S 244 REMARK 465 HIS S 245 REMARK 465 HIS S 246 REMARK 465 HIS S 247 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 ASP A 49 CG OD1 OD2 REMARK 470 LYS A 216 CG CD CE NZ REMARK 470 GLU A 258 CG CD OE1 OE2 REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 289 CG CD OE1 OE2 REMARK 470 GLU A 317 CG CD OE1 OE2 REMARK 470 ASP A 344 CG OD1 OD2 REMARK 470 ASP B 5 CG OD1 OD2 REMARK 470 GLU B 12 CG CD OE1 OE2 REMARK 470 ASP B 20 CG OD1 OD2 REMARK 470 ASP B 118 CG OD1 OD2 REMARK 470 SER B 161 OG REMARK 470 GLU B 172 CG CD OE1 OE2 REMARK 470 ASP B 195 CG OD1 OD2 REMARK 470 ARG B 214 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 215 CG CD OE1 OE2 REMARK 470 MET B 217 CG SD CE REMARK 470 ARG B 219 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 226 CG CD OE1 OE2 REMARK 470 ASP B 228 CG OD1 OD2 REMARK 470 ASP B 254 CG OD1 OD2 REMARK 470 ASP B 312 CG OD1 OD2 REMARK 470 SER B 331 OG REMARK 470 LYS G 32 CG CD CE NZ REMARK 470 GLN N 1 CG CD OE1 NE2 REMARK 470 THR N 113 OG1 CG2 REMARK 470 THR N 114 OG1 CG2 REMARK 470 GLN N 120 CG CD OE1 NE2 REMARK 470 SER N 128 OG REMARK 470 LEU R 31 CG CD1 CD2 REMARK 470 ASP R 37 CG OD1 OD2 REMARK 470 THR R 63 OG1 CG2 REMARK 470 GLN R 65 CG CD OE1 NE2 REMARK 470 LYS R 75 CG CD CE NZ REMARK 470 TYR R 134 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE R 143 CG1 CG2 CD1 REMARK 470 MET R 145 CG SD CE REMARK 470 GLN R 147 CG CD OE1 NE2 REMARK 470 GLN R 148 CG CD OE1 NE2 REMARK 470 THR R 149 OG1 CG2 REMARK 470 TYR R 151 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS R 152 CG CD CE NZ REMARK 470 GLN R 154 CG CD OE1 NE2 REMARK 470 SER R 156 OG REMARK 470 VAL R 160 CG1 CG2 REMARK 470 MET R 194 CG SD CE REMARK 470 LYS R 222 CG CD CE NZ REMARK 470 LEU R 236 CG CD1 CD2 REMARK 470 ILE R 246 CG1 CG2 CD1 REMARK 470 VAL R 247 CG1 CG2 REMARK 470 GLN R 248 CG CD OE1 NE2 REMARK 470 TYR R 263 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS R 284 CG CD CE NZ REMARK 470 HIS R 292 CG ND1 CD2 CE1 NE2 REMARK 470 LEU R 295 CG CD1 CD2 REMARK 470 GLN S 13 CG CD OE1 NE2 REMARK 470 ARG S 38 CG CD NE CZ NH1 NH2 REMARK 470 GLU S 42 CG CD OE1 OE2 REMARK 470 LYS S 43 CG CD CE NZ REMARK 470 ASP S 62 CG OD1 OD2 REMARK 470 LEU S 86 CG CD1 CD2 REMARK 470 GLN S 113 CG CD OE1 NE2 REMARK 470 THR S 138 OG1 CG2 REMARK 470 GLU S 141 CG CD OE1 OE2 REMARK 470 ASP S 189 CG OD1 OD2 REMARK 470 ARG S 206 CG CD NE CZ NH1 NH2 REMARK 470 LEU S 207 CG CD1 CD2 REMARK 470 GLU S 210 CG CD OE1 OE2 REMARK 470 GLU S 234 CG CD OE1 OE2 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 SER A 250 52.80 -93.21 REMARK 500 ARG B 68 -31.23 -130.16 REMARK 500 ASN B 268 41.85 35.31 REMARK 500 VAL N 48 -57.42 -125.63 REMARK 500 SER N 57 32.14 -145.91 REMARK 500 THR N 113 14.00 57.55 REMARK 500 LYS R 35 50.04 -92.77 REMARK 500 VAL S 48 -62.08 -123.55 REMARK 500 ASP S 62 75.33 -118.17 REMARK 500 THR S 63 -6.38 -144.46 REMARK 500 THR S 132 -5.86 74.49 REMARK 500 SER S 133 -144.00 52.42 REMARK 500 HIS S 155 50.67 -92.57 REMARK 500 SER S 156 11.65 57.12 REMARK 500 MET S 180 9.83 54.52 REMARK 500 LEU S 221 -38.60 -130.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9L79 RELATED DB: PDB REMARK 900 RELATED ID: EMD-62880 RELATED DB: EMDB REMARK 900 STRUCTURE OF GPR119-GS COMPLEX BOUND TO AN ALLOSTERIC MODULATOR DBREF 9L80 A 204 384 UNP P63092 GNAS2_HUMAN 204 394 DBREF 9L80 B 2 340 UNP P54311 GBB1_RAT 2 340 DBREF 9L80 G 1 68 UNP P63212 GBG2_BOVIN 1 68 DBREF 9L80 N 1 138 PDB 9L80 9L80 1 138 DBREF 9L80 R 1 335 UNP Q8TDV5 GP119_HUMAN 1 335 DBREF 9L80 S 1 247 PDB 9L80 9L80 1 247 SEQADV 9L80 GLY A 9 UNP P63092 EXPRESSION TAG SEQADV 9L80 CYS A 10 UNP P63092 EXPRESSION TAG SEQADV 9L80 THR A 11 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 12 UNP P63092 EXPRESSION TAG SEQADV 9L80 SER A 13 UNP P63092 EXPRESSION TAG SEQADV 9L80 ALA A 14 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLU A 15 UNP P63092 EXPRESSION TAG SEQADV 9L80 ASP A 16 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 17 UNP P63092 EXPRESSION TAG SEQADV 9L80 ALA A 18 UNP P63092 EXPRESSION TAG SEQADV 9L80 ALA A 19 UNP P63092 EXPRESSION TAG SEQADV 9L80 VAL A 20 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLU A 21 UNP P63092 EXPRESSION TAG SEQADV 9L80 ARG A 22 UNP P63092 EXPRESSION TAG SEQADV 9L80 SER A 23 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 24 UNP P63092 EXPRESSION TAG SEQADV 9L80 MET A 25 UNP P63092 EXPRESSION TAG SEQADV 9L80 ILE A 26 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLU A 27 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 28 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLN A 29 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 30 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLN A 31 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 32 UNP P63092 EXPRESSION TAG SEQADV 9L80 ASP A 33 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 34 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLN A 35 UNP P63092 EXPRESSION TAG SEQADV 9L80 VAL A 36 UNP P63092 EXPRESSION TAG SEQADV 9L80 TYR A 37 UNP P63092 EXPRESSION TAG SEQADV 9L80 ARG A 38 UNP P63092 EXPRESSION TAG SEQADV 9L80 ALA A 39 UNP P63092 EXPRESSION TAG SEQADV 9L80 THR A 40 UNP P63092 EXPRESSION TAG SEQADV 9L80 HIS A 41 UNP P63092 EXPRESSION TAG SEQADV 9L80 ARG A 42 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 43 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 44 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 45 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 46 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 47 UNP P63092 EXPRESSION TAG SEQADV 9L80 ALA A 48 UNP P63092 EXPRESSION TAG SEQADV 9L80 ASP A 49 UNP P63092 EXPRESSION TAG SEQADV 9L80 ASN A 50 UNP P63092 EXPRESSION TAG SEQADV 9L80 SER A 51 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 52 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 53 UNP P63092 EXPRESSION TAG SEQADV 9L80 SER A 54 UNP P63092 EXPRESSION TAG SEQADV 9L80 THR A 55 UNP P63092 EXPRESSION TAG SEQADV 9L80 ILE A 56 UNP P63092 EXPRESSION TAG SEQADV 9L80 VAL A 57 UNP P63092 EXPRESSION TAG SEQADV 9L80 LYS A 189 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLN A 190 UNP P63092 EXPRESSION TAG SEQADV 9L80 MET A 191 UNP P63092 EXPRESSION TAG SEQADV 9L80 ARG A 192 UNP P63092 EXPRESSION TAG SEQADV 9L80 ILE A 193 UNP P63092 EXPRESSION TAG SEQADV 9L80 LEU A 194 UNP P63092 EXPRESSION TAG SEQADV 9L80 HIS A 195 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 196 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 197 UNP P63092 EXPRESSION TAG SEQADV 9L80 SER A 198 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 199 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 200 UNP P63092 EXPRESSION TAG SEQADV 9L80 SER A 201 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 202 UNP P63092 EXPRESSION TAG SEQADV 9L80 GLY A 203 UNP P63092 EXPRESSION TAG SEQADV 9L80 ASP A 249 UNP P63092 ALA 249 ENGINEERED MUTATION SEQADV 9L80 ASP A 252 UNP P63092 SER 252 ENGINEERED MUTATION SEQADV 9L80 A UNP P63092 MET 255 DELETION SEQADV 9L80 A UNP P63092 VAL 256 DELETION SEQADV 9L80 A UNP P63092 ILE 257 DELETION SEQADV 9L80 A UNP P63092 ARG 258 DELETION SEQADV 9L80 A UNP P63092 GLU 259 DELETION SEQADV 9L80 A UNP P63092 ASP 260 DELETION SEQADV 9L80 A UNP P63092 ASN 261 DELETION SEQADV 9L80 A UNP P63092 GLN 262 DELETION SEQADV 9L80 A UNP P63092 THR 263 DELETION SEQADV 9L80 A UNP P63092 ASN 264 DELETION SEQADV 9L80 ASP A 262 UNP P63092 LEU 272 ENGINEERED MUTATION SEQADV 9L80 ALA A 362 UNP P63092 ILE 372 ENGINEERED MUTATION SEQADV 9L80 ILE A 365 UNP P63092 VAL 375 ENGINEERED MUTATION SEQADV 9L80 MET B -10 UNP P54311 INITIATING METHIONINE SEQADV 9L80 HIS B -9 UNP P54311 EXPRESSION TAG SEQADV 9L80 HIS B -8 UNP P54311 EXPRESSION TAG SEQADV 9L80 HIS B -7 UNP P54311 EXPRESSION TAG SEQADV 9L80 HIS B -6 UNP P54311 EXPRESSION TAG SEQADV 9L80 HIS B -5 UNP P54311 EXPRESSION TAG SEQADV 9L80 HIS B -4 UNP P54311 EXPRESSION TAG SEQADV 9L80 GLY B -3 UNP P54311 EXPRESSION TAG SEQADV 9L80 SER B -2 UNP P54311 EXPRESSION TAG SEQADV 9L80 LEU B -1 UNP P54311 EXPRESSION TAG SEQADV 9L80 LEU B 0 UNP P54311 EXPRESSION TAG SEQADV 9L80 GLN B 1 UNP P54311 EXPRESSION TAG SEQADV 9L80 MET R -23 UNP Q8TDV5 INITIATING METHIONINE SEQADV 9L80 LYS R -22 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 THR R -21 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ILE R -20 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ILE R -19 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ALA R -18 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 LEU R -17 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 SER R -16 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 TYR R -15 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ILE R -14 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 PHE R -13 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 CYS R -12 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 LEU R -11 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 VAL R -10 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 PHE R -9 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ALA R -8 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ASP R -7 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 TYR R -6 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 LYS R -5 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ASP R -4 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ASP R -3 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ASP R -2 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ASP R -1 UNP Q8TDV5 EXPRESSION TAG SEQADV 9L80 ALA R 0 UNP Q8TDV5 EXPRESSION TAG SEQRES 1 A 245 GLY CYS THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU SEQRES 2 A 245 ARG SER LYS MET ILE GLU LYS GLN LEU GLN LYS ASP LYS SEQRES 3 A 245 GLN VAL TYR ARG ALA THR HIS ARG LEU LEU LEU LEU GLY SEQRES 4 A 245 ALA ASP ASN SER GLY LYS SER THR ILE VAL LYS GLN MET SEQRES 5 A 245 ARG ILE LEU HIS GLY GLY SER GLY GLY SER GLY GLY THR SEQRES 6 A 245 SER GLY ILE PHE GLU THR LYS PHE GLN VAL ASP LYS VAL SEQRES 7 A 245 ASN PHE HIS MET PHE ASP VAL GLY GLY GLN ARG ASP GLU SEQRES 8 A 245 ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP VAL THR ALA SEQRES 9 A 245 ILE ILE PHE VAL VAL ASP SER SER ASP TYR ASN ARG LEU SEQRES 10 A 245 GLN GLU ALA LEU ASN ASP PHE LYS SER ILE TRP ASN ASN SEQRES 11 A 245 ARG TRP LEU ARG THR ILE SER VAL ILE LEU PHE LEU ASN SEQRES 12 A 245 LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SEQRES 13 A 245 SER LYS ILE GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR SEQRES 14 A 245 THR THR PRO GLU ASP ALA THR PRO GLU PRO GLY GLU ASP SEQRES 15 A 245 PRO ARG VAL THR ARG ALA LYS TYR PHE ILE ARG ASP GLU SEQRES 16 A 245 PHE LEU ARG ILE SER THR ALA SER GLY ASP GLY ARG HIS SEQRES 17 A 245 TYR CYS TYR PRO HIS PHE THR CYS ALA VAL ASP THR GLU SEQRES 18 A 245 ASN ALA ARG ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE SEQRES 19 A 245 GLN ARG MET HIS LEU ARG GLN TYR GLU LEU LEU SEQRES 1 B 351 MET HIS HIS HIS HIS HIS HIS GLY SER LEU LEU GLN SER SEQRES 2 B 351 GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN LEU LYS SEQRES 3 B 351 ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA ASP ALA SEQRES 4 B 351 THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO VAL GLY SEQRES 5 B 351 ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG GLY HIS SEQRES 6 B 351 LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR ASP SER SEQRES 7 B 351 ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS LEU ILE SEQRES 8 B 351 ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS ALA ILE SEQRES 9 B 351 PRO LEU ARG SER SER TRP VAL MET THR CYS ALA TYR ALA SEQRES 10 B 351 PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU ASP ASN SEQRES 11 B 351 ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU GLY ASN SEQRES 12 B 351 VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR GLY TYR SEQRES 13 B 351 LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN ILE VAL SEQRES 14 B 351 THR SER SER GLY ASP THR THR CYS ALA LEU TRP ASP ILE SEQRES 15 B 351 GLU THR GLY GLN GLN THR THR THR PHE THR GLY HIS THR SEQRES 16 B 351 GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP THR ARG SEQRES 17 B 351 LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA LYS LEU SEQRES 18 B 351 TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR PHE THR SEQRES 19 B 351 GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE PHE PRO SEQRES 20 B 351 ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP ALA THR SEQRES 21 B 351 CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU LEU MET SEQRES 22 B 351 THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE THR SER SEQRES 23 B 351 VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU ALA GLY SEQRES 24 B 351 TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA LEU LYS SEQRES 25 B 351 ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP ASN ARG SEQRES 26 B 351 VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET ALA VAL SEQRES 27 B 351 ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE TRP ASN SEQRES 1 G 68 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 68 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 68 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 68 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 68 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 68 PHE PHE CYS SEQRES 1 N 138 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 138 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 138 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 138 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 138 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 138 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 138 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 138 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 138 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 138 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER HIS HIS SEQRES 11 N 138 HIS HIS HIS HIS GLU PRO GLU ALA SEQRES 1 R 359 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 359 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLU SEQRES 3 R 359 SER SER PHE SER PHE GLY VAL ILE LEU ALA VAL LEU ALA SEQRES 4 R 359 SER LEU ILE ILE ALA THR ASN THR LEU VAL ALA VAL ALA SEQRES 5 R 359 VAL LEU LEU LEU ILE HIS LYS ASN ASP GLY VAL SER LEU SEQRES 6 R 359 CYS PHE THR LEU ASN LEU ALA VAL ALA ASP THR LEU ILE SEQRES 7 R 359 GLY VAL ALA ILE SER GLY LEU LEU THR ASP GLN LEU SER SEQRES 8 R 359 SER PRO SER ARG PRO THR GLN LYS THR LEU CYS SER LEU SEQRES 9 R 359 ARG MET ALA PHE VAL THR SER SER ALA ALA ALA SER VAL SEQRES 10 R 359 LEU THR VAL MET LEU ILE THR PHE ASP ARG TYR LEU ALA SEQRES 11 R 359 ILE LYS GLN PRO PHE ARG TYR LEU LYS ILE MET SER GLY SEQRES 12 R 359 PHE VAL ALA GLY ALA CYS ILE ALA GLY LEU TRP LEU VAL SEQRES 13 R 359 SER TYR LEU ILE GLY PHE LEU PRO LEU GLY ILE PRO MET SEQRES 14 R 359 PHE GLN GLN THR ALA TYR LYS GLY GLN CYS SER PHE PHE SEQRES 15 R 359 ALA VAL PHE HIS PRO HIS PHE VAL LEU THR LEU SER CYS SEQRES 16 R 359 VAL GLY PHE PHE PRO ALA MET LEU LEU PHE VAL PHE PHE SEQRES 17 R 359 TYR CYS ASP MET LEU LYS ILE ALA SER MET HIS SER GLN SEQRES 18 R 359 GLN ILE ARG LYS MET GLU HIS ALA GLY ALA MET ALA GLY SEQRES 19 R 359 GLY TYR ARG SER PRO ARG THR PRO SER ASP PHE LYS ALA SEQRES 20 R 359 LEU ARG THR VAL SER VAL LEU ILE GLY SER PHE ALA LEU SEQRES 21 R 359 SER TRP THR PRO PHE LEU ILE THR GLY ILE VAL GLN VAL SEQRES 22 R 359 ALA CYS GLN GLU CYS HIS LEU TYR LEU VAL LEU GLU ARG SEQRES 23 R 359 TYR LEU TRP LEU LEU GLY VAL GLY ASN SER LEU LEU ASN SEQRES 24 R 359 PRO LEU ILE TYR ALA TYR TRP GLN LYS GLU VAL ARG LEU SEQRES 25 R 359 GLN LEU TYR HIS MET ALA LEU GLY VAL LYS LYS VAL LEU SEQRES 26 R 359 THR SER PHE LEU LEU PHE LEU SER ALA ARG ASN CYS GLY SEQRES 27 R 359 PRO GLU ARG PRO ARG GLU SER SER CYS HIS ILE VAL THR SEQRES 28 R 359 ILE SER SER SER GLU PHE ASP GLY SEQRES 1 S 259 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 259 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 259 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 259 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 259 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 259 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 259 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 259 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 259 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 259 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 259 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 259 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 259 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 259 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 259 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 259 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 259 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 259 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 259 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 20 S 259 LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS HET DR7 R 401 102 HETNAM DR7 (3S,8S,9S,12S)-3,12-BIS(1,1-DIMETHYLETHYL)-8-HYDROXY-4, HETNAM 2 DR7 11-DIOXO-9-(PHENYLMETHYL)-6-[[4-(2-PYRIDINYL) HETNAM 3 DR7 PHENYL]METHYL]-2,5, 6,10,13-PENTAAZATETRADECANEDIOIC HETNAM 4 DR7 ACID DIMETHYL ESTER HETSYN DR7 ATAZANAVIR; METHYL [(1S,4S,5S,10S)-4-BENZYL-1,10-DI- HETSYN 2 DR7 TERT-BUTYL-5-HYDROXY-2,9,12-TRIOXO-7-(4-PYRIDIN-2- HETSYN 3 DR7 YLBENZYL)-13-OXA-3,7,8,11-TETRAAZATET RADEC-1- HETSYN 4 DR7 YL]CARBAMATE FORMUL 7 DR7 C38 H52 N6 O7 HELIX 1 AA1 SER A 13 ALA A 39 1 27 HELIX 2 AA2 GLY A 52 VAL A 57 1 6 HELIX 3 AA3 LYS A 233 CYS A 237 5 5 HELIX 4 AA4 ASP A 252 ASN A 254 5 3 HELIX 5 AA5 ARG A 255 ASN A 268 1 14 HELIX 6 AA6 LYS A 283 GLY A 294 1 12 HELIX 7 AA7 PHE A 302 TYR A 308 5 7 HELIX 8 AA8 ASP A 321 THR A 340 1 20 HELIX 9 AA9 ASN A 361 GLN A 380 1 20 HELIX 10 AB1 GLN B 6 ALA B 24 1 19 HELIX 11 AB2 THR B 29 ILE B 33 5 5 HELIX 12 AB3 ILE G 9 MET G 21 1 13 HELIX 13 AB4 GLU G 22 ILE G 25 5 4 HELIX 14 AB5 LYS G 29 ALA G 43 1 15 HELIX 15 AB6 HIS G 44 ASP G 48 5 5 HELIX 16 AB7 THR N 28 TYR N 32 5 5 HELIX 17 AB8 GLY N 62 LYS N 65 5 4 HELIX 18 AB9 VAL R 9 LYS R 35 1 27 HELIX 19 AC1 LEU R 41 THR R 63 1 23 HELIX 20 AC2 THR R 76 GLN R 109 1 34 HELIX 21 AC3 GLN R 109 LYS R 115 1 7 HELIX 22 AC4 SER R 118 LEU R 139 1 22 HELIX 23 AC5 PRO R 140 ILE R 143 5 4 HELIX 24 AC6 HIS R 162 HIS R 204 1 43 HELIX 25 AC7 SER R 219 ILE R 231 1 13 HELIX 26 AC8 PHE R 234 VAL R 249 1 16 HELIX 27 AC9 ARG R 262 TRP R 282 1 21 HELIX 28 AD1 GLN R 283 MET R 293 1 11 HELIX 29 AD2 ALA S 28 PHE S 32 5 5 SHEET 1 AA1 6 THR A 210 GLN A 213 0 SHEET 2 AA1 6 ASN A 218 PHE A 222 -1 O PHE A 219 N PHE A 212 SHEET 3 AA1 6 HIS A 41 LEU A 45 1 N HIS A 41 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ASP A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 276 ASN A 282 1 O ILE A 278 N ILE A 244 SHEET 6 AA1 6 CYS A 349 TYR A 350 1 O TYR A 350 N LEU A 279 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O ILE B 338 N ARG B 48 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 SER B 316 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 VAL B 71 N HIS B 62 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O TRP B 82 N LEU B 70 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 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O SER B 136 N ILE B 123 SHEET 1 AA5 4 LEU B 146 PHE B 151 0 SHEET 2 AA5 4 ILE B 157 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 MET B 188 SHEET 3 AA6 4 ALA B 208 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 GLN B 220 PHE B 222 -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 CYS B 250 ASP B 254 -1 O PHE B 253 N PHE B 241 SHEET 4 AA7 4 GLU B 260 THR B 263 -1 O LEU B 261 N LEU B 252 SHEET 1 AA8 4 ILE B 273 SER B 277 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 LEU B 308 N CYS B 294 SHEET 1 AA9 4 GLN N 3 LEU N 4 0 SHEET 2 AA9 4 SER N 17 SER N 25 -1 O SER N 25 N GLN N 3 SHEET 3 AA9 4 THR N 78 ASN N 84 -1 O MET N 83 N LEU N 18 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AB1 6 GLY N 10 LEU N 11 0 SHEET 2 AB1 6 THR N 122 THR N 125 1 O THR N 125 N GLY N 10 SHEET 3 AB1 6 VAL N 93 ARG N 98 -1 N TYR N 94 O THR N 122 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB1 6 SER N 59 TYR N 60 -1 O SER N 59 N ASP N 50 SHEET 1 AB2 4 GLN S 3 SER S 7 0 SHEET 2 AB2 4 LYS S 19 SER S 25 -1 O SER S 23 N VAL S 5 SHEET 3 AB2 4 THR S 78 MET S 83 -1 O LEU S 79 N CYS S 22 SHEET 4 AB2 4 PHE S 68 ASP S 73 -1 N THR S 69 O GLN S 82 SHEET 1 AB3 4 ILE S 58 TYR S 60 0 SHEET 2 AB3 4 LEU S 45 ILE S 51 -1 N TYR S 50 O TYR S 59 SHEET 3 AB3 4 GLY S 33 GLN S 39 -1 N ARG S 38 O GLU S 46 SHEET 4 AB3 4 MET S 93 SER S 99 -1 O SER S 99 N GLY S 33 SHEET 1 AB4 3 VAL S 143 ARG S 148 0 SHEET 2 AB4 3 ALA S 199 ILE S 204 -1 O LEU S 202 N ILE S 145 SHEET 3 AB4 3 PHE S 191 GLY S 195 -1 N SER S 192 O THR S 203 SHEET 1 AB5 5 ASN S 182 LEU S 183 0 SHEET 2 AB5 5 PRO S 173 TYR S 178 -1 N TYR S 178 O ASN S 182 SHEET 3 AB5 5 TYR S 163 GLN S 167 -1 N LEU S 166 O GLN S 174 SHEET 4 AB5 5 VAL S 214 MET S 218 -1 O MET S 218 N TYR S 163 SHEET 5 AB5 5 THR S 231 LYS S 232 -1 O THR S 231 N TYR S 215 SSBOND 1 CYS B 121 CYS B 149 1555 1555 2.04 SSBOND 2 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 3 CYS N 99 CYS N 107 1555 1555 2.04 SSBOND 4 CYS R 78 CYS R 155 1555 1555 2.03 SSBOND 5 CYS S 22 CYS S 96 1555 1555 2.04 SSBOND 6 CYS S 147 CYS S 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