HEADER SIGNALING PROTEIN 11-NOV-23 8UXV TITLE CONSENSUS OLFACTORY RECEPTOR CONSOR51 IN COMPLEX WITH MINI-GS TRIMERIC TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: NANOBODY 35; COMPND 3 CHAIN: N; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MINIGS399; COMPND 7 CHAIN: X; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 11 BETA-1; COMPND 12 CHAIN: Y; COMPND 13 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 17 GAMMA-2; COMPND 18 CHAIN: Z; COMPND 19 SYNONYM: G GAMMA-I; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 5; COMPND 22 MOLECULE: CONSOR51; COMPND 23 CHAIN: A; COMPND 24 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: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 GENE: GNAS; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: GNB1; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 GENE: GNG2; SOURCE 25 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 27 EXPRESSION_SYSTEM_STRAIN: HI5; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 30 ORGANISM_TAXID: 32630; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ODORANT, OLFACTION, GPCR, RECEPTOR, SIGNALING PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR C.B.BILLESBOELLE,C.L.DEL TORRENT,A.MANGLIK REVDAT 1 30-OCT-24 8UXV 0 JRNL AUTH C.A.DE MARCH,N.MA,C.B.BILLESBOELLE,J.TEWARI,C.L.DEL TORRENT, JRNL AUTH 2 W.J.C.VAN DER VELDEN,B.FAUST,N.VAIDEHI,A.MANGLIK,H.MATSUNAMI JRNL TITL ENGINEERED ODORANT RECEPTORS ILLUMINATE THE BASIS OF ODOUR JRNL TITL 2 DISCRIMINATION JRNL REF NATURE 2024 JRNL REFN ESSN 1476-4687 JRNL DOI 10.1038/S41586-024-08126-0 REMARK 2 REMARK 2 RESOLUTION. 3.20 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) : 3.200 REMARK 3 NUMBER OF PARTICLES : 204513 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 8UXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-23. REMARK 100 THE DEPOSITION ID IS D_1000279101. 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 : CONSOR51-MINIGS COMPLEX BOUND REMARK 245 TO NB35 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 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 : OTHER REMARK 245 NOMINAL MAGNIFICATION : 105000 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, X, Y, Z, A 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 SER N 127 REMARK 465 SER N 128 REMARK 465 LEU N 129 REMARK 465 GLU N 130 REMARK 465 VAL N 131 REMARK 465 LEU N 132 REMARK 465 PHE N 133 REMARK 465 GLN N 134 REMARK 465 GLY N 135 REMARK 465 PRO N 136 REMARK 465 GLY N 137 REMARK 465 HIS N 138 REMARK 465 HIS N 139 REMARK 465 HIS N 140 REMARK 465 HIS N 141 REMARK 465 HIS N 142 REMARK 465 HIS N 143 REMARK 465 HIS N 144 REMARK 465 HIS N 145 REMARK 465 GLY X -7 REMARK 465 GLY X -6 REMARK 465 SER X -5 REMARK 465 LEU X -4 REMARK 465 GLU X -3 REMARK 465 VAL X -2 REMARK 465 LEU X -1 REMARK 465 PHE X 0 REMARK 465 GLN X 1 REMARK 465 GLY X 2 REMARK 465 PRO X 3 REMARK 465 SER X 4 REMARK 465 GLY X 5 REMARK 465 ASN X 6 REMARK 465 SER X 7 REMARK 465 LYS X 8 REMARK 465 THR X 9 REMARK 465 GLU X 10 REMARK 465 ASP X 11 REMARK 465 GLN X 12 REMARK 465 ARG X 13 REMARK 465 ILE X 193 REMARK 465 LEU X 194 REMARK 465 HIS X 195 REMARK 465 GLY X 196 REMARK 465 GLY X 197 REMARK 465 SER X 198 REMARK 465 GLY X 199 REMARK 465 GLY X 200 REMARK 465 SER X 201 REMARK 465 GLY X 202 REMARK 465 GLY X 203 REMARK 465 THR X 204 REMARK 465 SER X 205 REMARK 465 GLU X 322 REMARK 465 ASP X 323 REMARK 465 ALA X 324 REMARK 465 THR X 325 REMARK 465 PRO X 326 REMARK 465 GLU X 327 REMARK 465 MET Y -29 REMARK 465 HIS Y -28 REMARK 465 HIS Y -27 REMARK 465 HIS Y -26 REMARK 465 HIS Y -25 REMARK 465 HIS Y -24 REMARK 465 HIS Y -23 REMARK 465 LEU Y -22 REMARK 465 GLU Y -21 REMARK 465 VAL Y -20 REMARK 465 LEU Y -19 REMARK 465 PHE Y -18 REMARK 465 GLN Y -17 REMARK 465 GLY Y -16 REMARK 465 PRO Y -15 REMARK 465 GLU Y -14 REMARK 465 ASP Y -13 REMARK 465 GLN Y -12 REMARK 465 VAL Y -11 REMARK 465 ASP Y -10 REMARK 465 PRO Y -9 REMARK 465 ARG Y -8 REMARK 465 LEU Y -7 REMARK 465 ILE Y -6 REMARK 465 ASP Y -5 REMARK 465 GLY Y -4 REMARK 465 LYS Y -3 REMARK 465 GLY Y -2 REMARK 465 SER Y -1 REMARK 465 SER Y 0 REMARK 465 GLY Y 1 REMARK 465 SER Y 2 REMARK 465 MET Z 1 REMARK 465 ALA Z 2 REMARK 465 SER Z 3 REMARK 465 ASN Z 4 REMARK 465 ASN Z 5 REMARK 465 THR Z 6 REMARK 465 GLU Z 63 REMARK 465 LYS Z 64 REMARK 465 LYS Z 65 REMARK 465 PHE Z 66 REMARK 465 PHE Z 67 REMARK 465 CYS Z 68 REMARK 465 ALA Z 69 REMARK 465 ILE Z 70 REMARK 465 LEU Z 71 REMARK 465 ASP A -9 REMARK 465 TYR A -8 REMARK 465 LYS A -7 REMARK 465 ASP A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ALA A -2 REMARK 465 SER A -1 REMARK 465 ILE A 0 REMARK 465 ASP A 1 REMARK 465 SER A 2 REMARK 465 ILE A 3 REMARK 465 ASN A 4 REMARK 465 ASN A 5 REMARK 465 SER A 6 REMARK 465 THR A 7 REMARK 465 SER A 8 REMARK 465 SER A 9 REMARK 465 ALA A 10 REMARK 465 LYS A 311 REMARK 465 LYS A 312 REMARK 465 ILE A 313 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 ASN X 14 CG OD1 ND2 REMARK 470 GLU X 15 CG CD OE1 OE2 REMARK 470 GLU X 16 CG CD OE1 OE2 REMARK 470 LYS X 17 CG CD CE NZ REMARK 470 GLU X 21 CG CD OE1 OE2 REMARK 470 LYS X 24 CG CD CE NZ REMARK 470 LYS X 25 CG CD CE NZ REMARK 470 LYS X 28 CG CD CE NZ REMARK 470 GLN X 31 CG CD OE1 NE2 REMARK 470 LYS X 32 CG CD CE NZ REMARK 470 GLN X 35 CG CD OE1 NE2 REMARK 470 ASP X 49 CG OD1 OD2 REMARK 470 ASN X 50 CG OD1 ND2 REMARK 470 SER X 54 OG REMARK 470 THR X 55 OG1 CG2 REMARK 470 LYS X 58 CG CD CE NZ REMARK 470 ARG X 61 CG CD NE CZ NH1 NH2 REMARK 470 ASP X 215 CG OD1 OD2 REMARK 470 LYS X 216 CG CD CE NZ REMARK 470 ASN X 218 CG OD1 ND2 REMARK 470 ASP X 229 CG OD1 OD2 REMARK 470 ASP X 240 CG OD1 OD2 REMARK 470 ASP X 249 CG OD1 OD2 REMARK 470 ASN X 264 CG OD1 ND2 REMARK 470 GLU X 268 CG CD OE1 OE2 REMARK 470 LYS X 274 CG CD CE NZ REMARK 470 ARG X 283 CG CD NE CZ NH1 NH2 REMARK 470 ASP X 295 CG OD1 OD2 REMARK 470 LEU X 296 CG CD1 CD2 REMARK 470 GLU X 299 CG CD OE1 OE2 REMARK 470 LYS X 305 CG CD CE NZ REMARK 470 LYS X 307 CG CD CE NZ REMARK 470 GLU X 314 CG CD OE1 OE2 REMARK 470 ARG X 317 CG CD NE CZ NH1 NH2 REMARK 470 GLU X 330 CG CD OE1 OE2 REMARK 470 ASP X 331 CG OD1 OD2 REMARK 470 ASP X 343 CG OD1 OD2 REMARK 470 ASP X 354 CG OD1 OD2 REMARK 470 ARG X 356 CG CD NE CZ NH1 NH2 REMARK 470 ASP X 368 CG OD1 OD2 REMARK 470 GLU X 370 CG CD OE1 OE2 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 OD2 ASP A 211 OH TYR A 253 2.09 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 VAL N 48 -56.16 -121.34 REMARK 500 ALA N 92 -179.63 -174.88 REMARK 500 TYR N 117 57.81 -95.04 REMARK 500 SER Y 334 36.73 71.56 REMARK 500 LEU A 56 32.23 -97.82 REMARK 500 SER A 172 -18.52 -140.13 REMARK 500 CYS A 190 -8.19 71.70 REMARK 500 ALA A 230 -165.23 64.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-42785 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-42786 RELATED DB: EMDB REMARK 900 CONSENSUS OLFACTORY RECEPTOR CONSOR51 IN COMPLEX WITH MINI-GS REMARK 900 TRIMERIC PROTEIN DBREF 8UXV N 1 145 PDB 8UXV 8UXV 1 145 DBREF1 8UXV X 204 394 UNP A0A804HIH4_HUMAN DBREF2 8UXV X A0A804HIH4 95 285 DBREF 8UXV Y 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8UXV Z 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8UXV A -9 313 PDB 8UXV 8UXV -9 313 SEQADV 8UXV GLY X -7 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X -6 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X -5 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X -4 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLU X -3 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV VAL X -2 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X -1 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV PHE X 0 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 1 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 2 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV PRO X 3 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X 4 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 5 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASN X 6 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X 7 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 8 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV THR X 9 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLU X 10 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASP X 11 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 12 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ARG X 13 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASN X 14 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLU X 15 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLU X 16 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 17 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ALA X 18 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 19 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ARG X 20 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLU X 21 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ALA X 22 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASN X 23 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 24 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 25 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ILE X 26 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLU X 27 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 28 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 29 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X 30 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 31 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 32 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASP X 33 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 34 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 35 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV VAL X 36 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV TYR X 37 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ARG X 38 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ALA X 39 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV THR X 40 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV HIS X 41 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ARG X 42 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X 43 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X 44 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X 45 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X 46 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 47 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ALA X 48 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASP X 49 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASN X 50 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X 51 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 52 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 53 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X 54 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV THR X 55 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ILE X 56 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV VAL X 57 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LYS X 58 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLN X 59 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV MET X 60 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ARG X 61 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ILE X 193 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV LEU X 194 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV HIS X 195 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 196 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 197 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X 198 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 199 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 200 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV SER X 201 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 202 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV GLY X 203 UNP A0A804HIH EXPRESSION TAG SEQADV 8UXV ASP X 249 UNP A0A804HIH ALA 140 CONFLICT SEQADV 8UXV ASP X 252 UNP A0A804HIH SER 143 CONFLICT SEQADV 8UXV X UNP A0A804HIH ASN 145 DELETION SEQADV 8UXV X UNP A0A804HIH MET 146 DELETION SEQADV 8UXV X UNP A0A804HIH VAL 147 DELETION SEQADV 8UXV X UNP A0A804HIH ILE 148 DELETION SEQADV 8UXV X UNP A0A804HIH ARG 149 DELETION SEQADV 8UXV X UNP A0A804HIH GLU 150 DELETION SEQADV 8UXV X UNP A0A804HIH ASP 151 DELETION SEQADV 8UXV X UNP A0A804HIH ASN 152 DELETION SEQADV 8UXV X UNP A0A804HIH GLN 153 DELETION SEQADV 8UXV X UNP A0A804HIH THR 154 DELETION SEQADV 8UXV ALA X 372 UNP A0A804HIH ILE 263 CONFLICT SEQADV 8UXV ILE X 375 UNP A0A804HIH VAL 266 CONFLICT SEQADV 8UXV MET Y -29 UNP P62873 INITIATING METHIONINE SEQADV 8UXV HIS Y -28 UNP P62873 EXPRESSION TAG SEQADV 8UXV HIS Y -27 UNP P62873 EXPRESSION TAG SEQADV 8UXV HIS Y -26 UNP P62873 EXPRESSION TAG SEQADV 8UXV HIS Y -25 UNP P62873 EXPRESSION TAG SEQADV 8UXV HIS Y -24 UNP P62873 EXPRESSION TAG SEQADV 8UXV HIS Y -23 UNP P62873 EXPRESSION TAG SEQADV 8UXV LEU Y -22 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLU Y -21 UNP P62873 EXPRESSION TAG SEQADV 8UXV VAL Y -20 UNP P62873 EXPRESSION TAG SEQADV 8UXV LEU Y -19 UNP P62873 EXPRESSION TAG SEQADV 8UXV PHE Y -18 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLN Y -17 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLY Y -16 UNP P62873 EXPRESSION TAG SEQADV 8UXV PRO Y -15 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLU Y -14 UNP P62873 EXPRESSION TAG SEQADV 8UXV ASP Y -13 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLN Y -12 UNP P62873 EXPRESSION TAG SEQADV 8UXV VAL Y -11 UNP P62873 EXPRESSION TAG SEQADV 8UXV ASP Y -10 UNP P62873 EXPRESSION TAG SEQADV 8UXV PRO Y -9 UNP P62873 EXPRESSION TAG SEQADV 8UXV ARG Y -8 UNP P62873 EXPRESSION TAG SEQADV 8UXV LEU Y -7 UNP P62873 EXPRESSION TAG SEQADV 8UXV ILE Y -6 UNP P62873 EXPRESSION TAG SEQADV 8UXV ASP Y -5 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLY Y -4 UNP P62873 EXPRESSION TAG SEQADV 8UXV LYS Y -3 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLY Y -2 UNP P62873 EXPRESSION TAG SEQADV 8UXV SER Y -1 UNP P62873 EXPRESSION TAG SEQADV 8UXV SER Y 0 UNP P62873 EXPRESSION TAG SEQADV 8UXV GLY Y 1 UNP P62873 EXPRESSION TAG SEQRES 1 N 145 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 145 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 145 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 145 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 145 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 145 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 145 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 145 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 145 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 145 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER LEU GLU SEQRES 11 N 145 VAL LEU PHE GLN GLY PRO GLY HIS HIS HIS HIS HIS HIS SEQRES 12 N 145 HIS HIS SEQRES 1 X 261 GLY GLY SER LEU GLU VAL LEU PHE GLN GLY PRO SER GLY SEQRES 2 X 261 ASN SER LYS THR GLU ASP GLN ARG ASN GLU GLU LYS ALA SEQRES 3 X 261 GLN ARG GLU ALA ASN LYS LYS ILE GLU LYS GLN LEU GLN SEQRES 4 X 261 LYS ASP LYS GLN VAL TYR ARG ALA THR HIS ARG LEU LEU SEQRES 5 X 261 LEU LEU GLY ALA ASP ASN SER GLY LYS SER THR ILE VAL SEQRES 6 X 261 LYS GLN MET ARG ILE LEU HIS GLY GLY SER GLY GLY SER SEQRES 7 X 261 GLY GLY THR SER GLY ILE PHE GLU THR LYS PHE GLN VAL SEQRES 8 X 261 ASP LYS VAL ASN PHE HIS MET PHE ASP VAL GLY GLY GLN SEQRES 9 X 261 ARG ASP GLU ARG ARG LYS TRP ILE GLN CYS PHE ASN ASP SEQRES 10 X 261 VAL THR ALA ILE ILE PHE VAL VAL ASP SER SER ASP TYR SEQRES 11 X 261 ASN ARG LEU GLN GLU ALA LEU ASN LEU PHE LYS SER ILE SEQRES 12 X 261 TRP ASN ASN ARG TRP LEU ARG THR ILE SER VAL ILE LEU SEQRES 13 X 261 PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU SEQRES 14 X 261 ALA GLY LYS SER LYS ILE GLU ASP TYR PHE PRO GLU PHE SEQRES 15 X 261 ALA ARG TYR THR THR PRO GLU ASP ALA THR PRO GLU PRO SEQRES 16 X 261 GLY GLU ASP PRO ARG VAL THR ARG ALA LYS TYR PHE ILE SEQRES 17 X 261 ARG ASP GLU PHE LEU ARG ILE SER THR ALA SER GLY ASP SEQRES 18 X 261 GLY ARG HIS TYR CYS TYR PRO HIS PHE THR CYS ALA VAL SEQRES 19 X 261 ASP THR GLU ASN ALA ARG ARG ILE PHE ASN ASP CYS ARG SEQRES 20 X 261 ASP ILE ILE GLN ARG MET HIS LEU ARG GLN TYR GLU LEU SEQRES 21 X 261 LEU SEQRES 1 Y 370 MET HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN SEQRES 2 Y 370 GLY PRO GLU ASP GLN VAL ASP PRO ARG LEU ILE ASP GLY SEQRES 3 Y 370 LYS GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG GLN SEQRES 4 Y 370 GLU ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG SEQRES 5 Y 370 LYS ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN SEQRES 6 Y 370 ASN ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG SEQRES 7 Y 370 ARG THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET SEQRES 8 Y 370 HIS TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER SEQRES 9 Y 370 GLN ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR SEQRES 10 Y 370 ASN LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL SEQRES 11 Y 370 MET THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA SEQRES 12 Y 370 CYS GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU SEQRES 13 Y 370 LYS THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU SEQRES 14 Y 370 ALA GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU SEQRES 15 Y 370 ASP ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR SEQRES 16 Y 370 CYS ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR SEQRES 17 Y 370 THR PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER SEQRES 18 Y 370 LEU ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS SEQRES 19 Y 370 ASP ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET SEQRES 20 Y 370 CYS ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN SEQRES 21 Y 370 ALA ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR SEQRES 22 Y 370 GLY SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG SEQRES 23 Y 370 ALA ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE SEQRES 24 Y 370 ILE CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY SEQRES 25 Y 370 ARG LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN SEQRES 26 Y 370 VAL TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU SEQRES 27 Y 370 ALA GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR SEQRES 28 Y 370 ASP ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER SEQRES 29 Y 370 PHE LEU LYS ILE TRP ASN SEQRES 1 Z 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 Z 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 Z 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 Z 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 Z 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 Z 71 PHE PHE CYS ALA ILE LEU SEQRES 1 A 323 ASP TYR LYS ASP ASP ASP ASP ALA SER ILE ASP SER ILE SEQRES 2 A 323 ASN ASN SER THR SER SER ALA ALA THR PHE LEU LEU THR SEQRES 3 A 323 GLY ILE PRO GLY LEU GLU ALA ALA HIS ILE TRP ILE SER SEQRES 4 A 323 ILE PRO PHE CYS PHE MET TYR LEU ILE ALA ILE LEU GLY SEQRES 5 A 323 ASN GLY THR ILE LEU PHE ILE ILE ARG THR GLU PRO SER SEQRES 6 A 323 LEU HIS GLU PRO MET TYR TYR PHE LEU SER MET LEU ALA SEQRES 7 A 323 ALA THR ASP LEU GLY LEU SER LEU SER THR LEU PRO THR SEQRES 8 A 323 VAL LEU GLY ILE PHE TRP PHE ASN ALA ARG GLU ILE SER SEQRES 9 A 323 PHE ASN ALA CYS PHE ALA GLN MET PHE PHE ILE HIS GLY SEQRES 10 A 323 PHE SER PHE MET GLU SER SER VAL LEU LEU ALA MET ALA SEQRES 11 A 323 PHE ASP ARG PHE VAL ALA ILE CYS ASN PRO LEU ARG TYR SEQRES 12 A 323 ALA SER ILE LEU THR ASN THR ARG VAL ALA LYS ILE GLY SEQRES 13 A 323 LEU ALA ILE LEU THR ARG SER PHE LEU LEU ILE LEU PRO SEQRES 14 A 323 LEU PRO PHE LEU LEU LYS ARG LEU PRO TYR CYS HIS SER SEQRES 15 A 323 ASN VAL LEU SER HIS SER TYR CYS LEU HIS GLN ASP VAL SEQRES 16 A 323 MET LYS LEU ALA CYS ALA ASP ILE ARG PHE ASN SER ILE SEQRES 17 A 323 TYR GLY LEU PHE VAL VAL LEU SER THR MET GLY LEU ASP SEQRES 18 A 323 SER LEU LEU ILE LEU PHE SER TYR ILE LEU ILE LEU LYS SEQRES 19 A 323 THR VAL LEU GLY ILE ALA SER ARG GLU GLU ARG LEU LYS SEQRES 20 A 323 ALA LEU ASN THR CYS VAL SER HIS ILE CYS ALA VAL LEU SEQRES 21 A 323 VAL PHE TYR VAL PRO MET ILE GLY LEU SER LEU VAL HIS SEQRES 22 A 323 ARG PHE GLY LYS HIS VAL PRO PRO VAL VAL HIS VAL LEU SEQRES 23 A 323 MET ALA ASN VAL TYR LEU LEU VAL PRO PRO VAL MET ASN SEQRES 24 A 323 PRO ILE ILE TYR SER VAL LYS THR LYS GLN ILE ARG LYS SEQRES 25 A 323 ARG ILE LEU ARG LEU PHE SER LEU LYS LYS ILE HELIX 1 AA1 THR N 28 TYR N 32 5 5 HELIX 2 AA2 GLY N 62 LYS N 65 5 4 HELIX 3 AA3 LYS N 87 THR N 91 5 5 HELIX 4 AA4 GLU X 15 THR X 40 1 26 HELIX 5 AA5 GLY X 52 MET X 60 1 9 HELIX 6 AA6 LYS X 233 ASN X 239 5 7 HELIX 7 AA7 ARG X 265 ASN X 278 1 14 HELIX 8 AA8 LYS X 293 GLY X 304 1 12 HELIX 9 AA9 PHE X 312 TYR X 318 5 7 HELIX 10 AB1 ASP X 331 SER X 352 1 22 HELIX 11 AB2 GLU X 370 TYR X 391 1 22 HELIX 12 AB3 LEU Y 4 CYS Y 25 1 22 HELIX 13 AB4 THR Y 29 THR Y 34 1 6 HELIX 14 AB5 ASN Y 35 ILE Y 37 5 3 HELIX 15 AB6 SER Z 8 ASN Z 24 1 17 HELIX 16 AB7 LYS Z 29 ALA Z 45 1 17 HELIX 17 AB8 LYS Z 46 ASP Z 48 5 3 HELIX 18 AB9 GLY A 20 ALA A 24 5 5 HELIX 19 AC1 ILE A 28 GLU A 53 1 26 HELIX 20 AC2 PRO A 54 HIS A 57 5 4 HELIX 21 AC3 GLU A 58 PHE A 88 1 31 HELIX 22 AC4 SER A 94 ASN A 129 1 36 HELIX 23 AC5 THR A 138 ILE A 157 1 20 HELIX 24 AC6 LEU A 158 LEU A 167 1 10 HELIX 25 AC7 LEU A 181 MET A 186 1 6 HELIX 26 AC8 LYS A 187 ALA A 189 5 3 HELIX 27 AC9 ILE A 193 GLY A 228 1 36 HELIX 28 AD1 SER A 231 GLY A 266 1 36 HELIX 29 AD2 PRO A 270 VAL A 284 1 15 HELIX 30 AD3 VAL A 284 SER A 294 1 11 HELIX 31 AD4 THR A 297 LEU A 310 1 14 SHEET 1 AA1 4 GLN N 3 SER N 7 0 SHEET 2 AA1 4 SER N 17 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AA1 4 THR N 78 ASN N 84 -1 O LEU N 81 N LEU N 20 SHEET 4 AA1 4 THR N 69 ASP N 73 -1 N THR N 69 O GLN N 82 SHEET 1 AA2 6 GLY N 10 LEU N 11 0 SHEET 2 AA2 6 THR N 122 THR N 125 1 O THR N 125 N GLY N 10 SHEET 3 AA2 6 ALA N 92 ARG N 98 -1 N TYR N 94 O THR N 122 SHEET 4 AA2 6 MET N 34 GLN N 39 -1 N VAL N 37 O TYR N 95 SHEET 5 AA2 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AA2 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SHEET 1 AA3 6 THR X 210 VAL X 214 0 SHEET 2 AA3 6 VAL X 217 PHE X 222 -1 O PHE X 219 N PHE X 212 SHEET 3 AA3 6 HIS X 41 LEU X 46 1 N LEU X 45 O PHE X 222 SHEET 4 AA3 6 ALA X 243 ASP X 249 1 O ILE X 245 N LEU X 44 SHEET 5 AA3 6 SER X 286 ASN X 292 1 O PHE X 290 N PHE X 246 SHEET 6 AA3 6 CYS X 359 PHE X 363 1 O HIS X 362 N LEU X 291 SHEET 1 AA4 4 ARG Y 46 LEU Y 51 0 SHEET 2 AA4 4 LEU Y 336 ASN Y 340 -1 O ILE Y 338 N ARG Y 48 SHEET 3 AA4 4 VAL Y 327 GLY Y 330 -1 N VAL Y 327 O TRP Y 339 SHEET 4 AA4 4 CYS Y 317 VAL Y 320 -1 N GLY Y 319 O ALA Y 328 SHEET 1 AA5 4 ILE Y 58 TRP Y 63 0 SHEET 2 AA5 4 LEU Y 70 SER Y 74 -1 O ALA Y 73 N ALA Y 60 SHEET 3 AA5 4 LYS Y 78 ILE Y 81 -1 O ILE Y 80 N SER Y 72 SHEET 4 AA5 4 HIS Y 91 PRO Y 94 -1 O ILE Y 93 N LEU Y 79 SHEET 1 AA6 4 VAL Y 100 TYR Y 105 0 SHEET 2 AA6 4 TYR Y 111 GLY Y 116 -1 O GLY Y 115 N MET Y 101 SHEET 3 AA6 4 ILE Y 120 ASN Y 125 -1 O TYR Y 124 N VAL Y 112 SHEET 4 AA6 4 ARG Y 134 ALA Y 140 -1 O SER Y 136 N ILE Y 123 SHEET 1 AA7 4 LEU Y 146 PHE Y 151 0 SHEET 2 AA7 4 GLN Y 156 SER Y 161 -1 O VAL Y 158 N ARG Y 150 SHEET 3 AA7 4 THR Y 165 ASP Y 170 -1 O TRP Y 169 N ILE Y 157 SHEET 4 AA7 4 GLN Y 176 THR Y 181 -1 O THR Y 178 N LEU Y 168 SHEET 1 AA8 4 VAL Y 187 LEU Y 192 0 SHEET 2 AA8 4 LEU Y 198 ALA Y 203 -1 O GLY Y 202 N MET Y 188 SHEET 3 AA8 4 ALA Y 208 ASP Y 212 -1 O TRP Y 211 N PHE Y 199 SHEET 4 AA8 4 CYS Y 218 PHE Y 222 -1 O ARG Y 219 N LEU Y 210 SHEET 1 AA9 4 ILE Y 229 PHE Y 234 0 SHEET 2 AA9 4 ALA Y 240 SER Y 245 -1 O GLY Y 244 N ASN Y 230 SHEET 3 AA9 4 CYS Y 250 ASP Y 254 -1 O PHE Y 253 N PHE Y 241 SHEET 4 AA9 4 GLN Y 259 TYR Y 264 -1 O LEU Y 261 N LEU Y 252 SHEET 1 AB1 4 ILE Y 273 PHE Y 278 0 SHEET 2 AB1 4 LEU Y 284 TYR Y 289 -1 O GLY Y 288 N SER Y 275 SHEET 3 AB1 4 CYS Y 294 ASP Y 298 -1 O TRP Y 297 N LEU Y 285 SHEET 4 AB1 4 ARG Y 304 LEU Y 308 -1 O ALA Y 305 N VAL Y 296 SHEET 1 AB2 2 PHE A 13 LEU A 14 0 SHEET 2 AB2 2 GLU A 92 ILE A 93 -1 O ILE A 93 N PHE A 13 SSBOND 1 CYS A 98 CYS A 180 1555 1555 2.03 SSBOND 2 CYS A 170 CYS A 190 1555 1555 2.04 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