HEADER PEPTIDE BINDING PROTEIN/IMMUNE SYSTEM 14-JUL-25 9PKV TITLE HU-38 FAB WITH PRAME PMHC COMPND MOL_ID: 1; COMPND 2 MOLECULE: MHC CLASS I ANTIGEN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VHH ANTIBODY; COMPND 7 CHAIN: K; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: PRAME PEPTIDE; COMPND 11 CHAIN: P; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: HU-38 HEAVY CHAIN; COMPND 15 CHAIN: H; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: BETA-2-MICROGLOBULIN; COMPND 19 CHAIN: B; COMPND 20 FRAGMENT: UNP RESIDUES 21-119; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 6; COMPND 23 MOLECULE: HU-38 LIGHT CHAIN; COMPND 24 CHAIN: L; COMPND 25 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: HLA-A; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_COMMON: LLAMA; SOURCE 11 ORGANISM_TAXID: 9844; SOURCE 12 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE; SOURCE 13 EXPRESSION_SYSTEM_COMMON: YEAST; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4932; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 22 ORGANISM_COMMON: MOUSE; SOURCE 23 ORGANISM_TAXID: 10090; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 28 MOL_ID: 5; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_COMMON: HUMAN; SOURCE 31 ORGANISM_TAXID: 9606; SOURCE 32 GENE: B2M, CDABP0092, HDCMA22P; SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 35 MOL_ID: 6; SOURCE 36 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 37 ORGANISM_COMMON: MOUSE; SOURCE 38 ORGANISM_TAXID: 10090; SOURCE 39 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 40 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 41 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 42 EXPRESSION_SYSTEM_CELL_LINE: EXPI293 KEYWDS PRAME, PMHC, PEPTIDE BINDING PROTEIN, PEPTIDE BINDING PROTEIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR D.E.MORTENSON,X.YU REVDAT 1 01-OCT-25 9PKV 0 JRNL AUTH S.KHAN,J.LUM,H.STEPHENSON,P.B.KOHLI,D.MORTENSON, JRNL AUTH 2 D.RAMAKRISHNAN,M.HUNG,S.DING,E.SETO,S.LU,R.YEN,D.JIN,B.LEE, JRNL AUTH 3 S.CLANCY,N.S.OAKDALE,N.NOVIKOV,D.KANG,R.LI,D.PAN,R.DAVE, JRNL AUTH 4 E.LANSDON,S.P.FLETCHER,A.V.GARG,N.THOMSEN,S.BALSITIS JRNL TITL A HIGHLY SELECTIVE TCR-MIMIC ANTIBODY REVEALS UNEXPECTED JRNL TITL 2 MECHANISMS OF HBV PEPTIDE-MHC RECOGNITION AND PREVIOUSLY JRNL TITL 3 UNKNOWN TARGET BIOLOGY. JRNL REF MABS V. 17 62998 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40990156 JRNL DOI 10.1080/19420862.2025.2562998 REMARK 2 REMARK 2 RESOLUTION. 2.72 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 2.720 REMARK 3 NUMBER OF PARTICLES : 553793 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 9PKV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000297921. 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 : COMPLEX OF HU38 FAB WITH PRAME REMARK 245 PMHC AND ANTI-KAPPA VHH 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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, K, P, H, B, L 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 A 0 REMARK 465 HIS A 192 REMARK 465 ALA A 193 REMARK 465 VAL A 194 REMARK 465 SER A 195 REMARK 465 ASP A 196 REMARK 465 HIS A 197 REMARK 465 GLU A 198 REMARK 465 ASP A 220 REMARK 465 GLY A 221 REMARK 465 GLU A 222 REMARK 465 ASP A 223 REMARK 465 GLN A 224 REMARK 465 THR A 225 REMARK 465 PRO A 250 REMARK 465 SER A 251 REMARK 465 GLY A 252 REMARK 465 GLN A 253 REMARK 465 GLU A 254 REMARK 465 GLN A 255 REMARK 465 ARG A 256 REMARK 465 TYR A 257 REMARK 465 ARG A 273 REMARK 465 TRP A 274 REMARK 465 GLU A 275 REMARK 465 PRO A 276 REMARK 465 GLY A 277 REMARK 465 SER A 278 REMARK 465 GLY A 279 REMARK 465 GLY A 280 REMARK 465 SER A 281 REMARK 465 GLY A 282 REMARK 465 GLY A 283 REMARK 465 SER A 284 REMARK 465 ALA A 285 REMARK 465 GLY A 286 REMARK 465 GLY A 287 REMARK 465 GLY A 288 REMARK 465 LEU A 289 REMARK 465 ASN A 290 REMARK 465 ASP A 291 REMARK 465 ILE A 292 REMARK 465 PHE A 293 REMARK 465 GLU A 294 REMARK 465 ALA A 295 REMARK 465 GLN A 296 REMARK 465 LYS A 297 REMARK 465 ILE A 298 REMARK 465 GLU A 299 REMARK 465 TRP A 300 REMARK 465 GLN K 2 REMARK 465 SER K 122 REMARK 465 GLN H 1 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 THR H 135 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 HIS H 217 REMARK 465 HIS H 218 REMARK 465 HIS H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 ASP H 225 REMARK 465 TYR H 226 REMARK 465 LYS H 227 REMARK 465 ASP H 228 REMARK 465 ASP H 229 REMARK 465 ASP H 230 REMARK 465 ASP H 231 REMARK 465 LYS H 232 REMARK 465 MET B 0 REMARK 465 PRO B 14 REMARK 465 ALA B 15 REMARK 465 GLU B 16 REMARK 465 ASN B 17 REMARK 465 GLY B 18 REMARK 465 LYS B 19 REMARK 465 PRO B 72 REMARK 465 THR B 73 REMARK 465 GLU B 74 REMARK 465 LYS B 75 REMARK 465 ASP B 76 REMARK 465 GLY L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 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 ARG A 108 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 137 CG OD1 OD2 REMARK 470 GLU A 177 CG CD OE1 OE2 REMARK 470 LYS A 268 CG CD CE NZ REMARK 470 GLN K 4 CG CD OE1 NE2 REMARK 470 GLN K 6 CG CD OE1 NE2 REMARK 470 SER K 8 OG REMARK 470 LEU K 12 CG CD1 CD2 REMARK 470 GLN K 14 CG CD OE1 NE2 REMARK 470 SER K 18 OG REMARK 470 SER K 26 OG REMARK 470 ARG K 28 CG CD NE CZ NH1 NH2 REMARK 470 THR K 29 OG1 CG2 REMARK 470 SER K 31 OG REMARK 470 ARG K 32 CG CD NE CZ NH1 NH2 REMARK 470 GLU K 45 CG CD OE1 OE2 REMARK 470 SER K 55 OG REMARK 470 ASP K 63 CG OD1 OD2 REMARK 470 ASP K 74 CG OD1 OD2 REMARK 470 LYS K 77 CG CD CE NZ REMARK 470 GLN K 83 CG CD OE1 NE2 REMARK 470 SER K 86 OG REMARK 470 GLU K 90 CG CD OE1 OE2 REMARK 470 GLN K 114 CG CD OE1 NE2 REMARK 470 SER K 121 OG REMARK 470 LYS H 75 CG CD CE NZ REMARK 470 ARG H 210 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 214 CG CD CE NZ REMARK 470 GLU B 36 CG CD OE1 OE2 REMARK 470 GLU B 44 CG CD OE1 OE2 REMARK 470 LYS B 58 CG CD CE NZ REMARK 470 LYS B 94 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 29 -119.69 61.15 REMARK 500 PRO A 57 -177.70 -66.79 REMARK 500 GLU A 58 8.59 53.76 REMARK 500 SER K 31 -30.39 -131.14 REMARK 500 VAL K 49 -60.68 -121.03 REMARK 500 ALA K 62 -162.95 -68.11 REMARK 500 SER H 30 -148.90 58.00 REMARK 500 SER H 113 57.38 -94.96 REMARK 500 ASP H 144 64.23 60.34 REMARK 500 SER H 156 -97.43 58.52 REMARK 500 SER L 30 -136.09 57.76 REMARK 500 ALA L 51 -6.78 72.87 REMARK 500 SER L 67 -61.42 -93.62 REMARK 500 ALA L 91 28.58 -141.00 REMARK 500 THR L 164 -167.94 -79.48 REMARK 500 ASP L 167 129.26 -37.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-71704 RELATED DB: EMDB REMARK 900 HU-38 FAB WITH PRAME PMHC DBREF 9PKV A 1 276 UNP Q8WLS4 Q8WLS4_HUMAN 25 300 DBREF 9PKV K 2 122 PDB 9PKV 9PKV 2 122 DBREF 9PKV P 1 9 PDB 9PKV 9PKV 1 9 DBREF 9PKV H 1 232 PDB 9PKV 9PKV 1 232 DBREF 9PKV B 1 99 UNP P61769 B2MG_HUMAN 21 119 DBREF 9PKV L 1 214 PDB 9PKV 9PKV 1 214 SEQADV 9PKV MET A 0 UNP Q8WLS4 INITIATING METHIONINE SEQADV 9PKV GLY A 277 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV SER A 278 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 279 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 280 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV SER A 281 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 282 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 283 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV SER A 284 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV ALA A 285 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 286 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 287 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLY A 288 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV LEU A 289 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV ASN A 290 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV ASP A 291 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV ILE A 292 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV PHE A 293 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLU A 294 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV ALA A 295 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLN A 296 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV LYS A 297 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV ILE A 298 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV GLU A 299 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV TRP A 300 UNP Q8WLS4 EXPRESSION TAG SEQADV 9PKV MET B 0 UNP P61769 INITIATING METHIONINE SEQRES 1 A 301 MET GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SEQRES 2 A 301 SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL SEQRES 3 A 301 GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER SEQRES 4 A 301 ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP SEQRES 5 A 301 ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR SEQRES 6 A 301 ARG LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP SEQRES 7 A 301 LEU GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA SEQRES 8 A 301 GLY SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL SEQRES 9 A 301 GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR SEQRES 10 A 301 ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP SEQRES 11 A 301 LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR SEQRES 12 A 301 THR LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN SEQRES 13 A 301 LEU ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU SEQRES 14 A 301 ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG SEQRES 15 A 301 THR ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SEQRES 16 A 301 SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER SEQRES 17 A 301 PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP SEQRES 18 A 301 GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR SEQRES 19 A 301 ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA SEQRES 20 A 301 VAL VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS SEQRES 21 A 301 HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU SEQRES 22 A 301 ARG TRP GLU PRO GLY SER GLY GLY SER GLY GLY SER ALA SEQRES 23 A 301 GLY GLY GLY LEU ASN ASP ILE PHE GLU ALA GLN LYS ILE SEQRES 24 A 301 GLU TRP SEQRES 1 K 121 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 K 121 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 K 121 ARG THR ILE SER ARG TYR ALA MET SER TRP PHE ARG GLN SEQRES 4 K 121 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA VAL ALA ARG SEQRES 5 K 121 ARG SER GLY ASP GLY ALA PHE TYR ALA ASP SER VAL GLN SEQRES 6 K 121 GLY ARG PHE THR VAL SER ARG ASP ASP ALA LYS ASN THR SEQRES 7 K 121 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 K 121 ALA VAL TYR TYR CYS ALA ILE ASP SER ASP THR PHE TYR SEQRES 9 K 121 SER GLY SER TYR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 K 121 THR VAL SER SER SEQRES 1 P 9 SER LEU LEU GLN HIS LEU ILE GLY LEU SEQRES 1 H 237 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 237 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 237 GLY SER ILE SER THR TYR TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 237 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 H 237 TYR SER GLY SER THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 237 ARG VAL THR ILE SER VAL ASP THR SER LYS ASN GLN PHE SEQRES 7 H 237 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP MET ALA SEQRES 8 H 237 VAL TYR TYR CYS ALA ARG ILE THR GLU ILE HIS ASP ALA SEQRES 9 H 237 PHE GLU ILE TRP GLY GLN GLY THR MET VAL THR VAL SER SEQRES 10 H 237 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 237 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 237 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 237 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 237 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 237 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 237 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 237 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 18 H 237 HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR LYS ASP ASP SEQRES 19 H 237 ASP ASP LYS SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET SEQRES 1 L 214 ASP ILE HIS MET THR GLN SER PRO SER SER VAL SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN GLY ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLU SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ALA SEQRES 8 L 214 ASN SER PHE PRO PHE THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 214 ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS FORMUL 7 HOH *191(H2 O) HELIX 1 AA1 TRP A 51 GLU A 55 5 5 HELIX 2 AA2 TYR A 59 TYR A 85 1 27 HELIX 3 AA3 ASP A 137 ALA A 150 1 14 HELIX 4 AA4 HIS A 151 GLY A 162 1 12 HELIX 5 AA5 GLY A 162 GLY A 175 1 14 HELIX 6 AA6 GLY A 175 GLN A 180 1 6 HELIX 7 AA7 PRO H 61 LYS H 64 5 4 HELIX 8 AA8 THR H 83 MET H 87 5 5 HELIX 9 AA9 PRO H 185 LEU H 189 5 5 HELIX 10 AB1 GLN L 79 PHE L 83 5 5 HELIX 11 AB2 SER L 121 LYS L 126 1 6 HELIX 12 AB3 LYS L 183 GLU L 187 1 5 SHEET 1 AA1 7 GLU A 46 PRO A 47 0 SHEET 2 AA1 7 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46 SHEET 3 AA1 7 ARG A 21 VAL A 28 -1 N ALA A 24 O PHE A 36 SHEET 4 AA1 7 MET A 5 VAL A 12 -1 N THR A 10 O ILE A 23 SHEET 5 AA1 7 THR A 94 VAL A 103 -1 O ARG A 97 N PHE A 9 SHEET 6 AA1 7 PHE A 109 TYR A 118 -1 O ARG A 111 N ASP A 102 SHEET 7 AA1 7 LYS A 121 ALA A 125 -1 O ILE A 124 N TYR A 116 SHEET 1 AA2 4 HIS A 188 THR A 190 0 SHEET 2 AA2 4 THR A 200 PHE A 208 -1 O TRP A 204 N HIS A 188 SHEET 3 AA2 4 PHE A 241 VAL A 248 -1 O LYS A 243 N ALA A 205 SHEET 4 AA2 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246 SHEET 1 AA3 4 HIS A 188 THR A 190 0 SHEET 2 AA3 4 THR A 200 PHE A 208 -1 O TRP A 204 N HIS A 188 SHEET 3 AA3 4 PHE A 241 VAL A 248 -1 O LYS A 243 N ALA A 205 SHEET 4 AA3 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242 SHEET 1 AA4 3 THR A 214 TRP A 217 0 SHEET 2 AA4 3 CYS A 259 GLN A 262 -1 O HIS A 260 N THR A 216 SHEET 3 AA4 3 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259 SHEET 1 AA5 4 GLN K 4 SER K 8 0 SHEET 2 AA5 4 SER K 18 SER K 26 -1 O SER K 26 N GLN K 4 SHEET 3 AA5 4 THR K 79 ASN K 85 -1 O MET K 84 N LEU K 19 SHEET 4 AA5 4 VAL K 71 ASP K 74 -1 N SER K 72 O TYR K 81 SHEET 1 AA6 3 GLY K 11 VAL K 13 0 SHEET 2 AA6 3 THR K 116 VAL K 120 1 O THR K 119 N VAL K 13 SHEET 3 AA6 3 ALA K 93 TYR K 95 -1 N TYR K 95 O THR K 116 SHEET 1 AA7 5 ALA K 59 TYR K 61 0 SHEET 2 AA7 5 ARG K 46 ALA K 52 -1 N VAL K 51 O PHE K 60 SHEET 3 AA7 5 ALA K 34 GLN K 40 -1 N MET K 35 O ALA K 52 SHEET 4 AA7 5 CYS K 97 ASP K 100 -1 O ASP K 100 N ALA K 34 SHEET 5 AA7 5 TYR K 109 TRP K 112 -1 O TYR K 111 N ILE K 99 SHEET 1 AA8 4 GLN H 3 GLU H 6 0 SHEET 2 AA8 4 GLU H 16 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA8 4 GLN H 77 VAL H 82C-1 O LEU H 80 N LEU H 20 SHEET 4 AA8 4 VAL H 67 ASP H 72 -1 N THR H 68 O LYS H 81 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA9 6 ALA H 88 ILE H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 6 TRP H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA9 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA9 6 THR H 57 TYR H 59 -1 O ASN H 58 N TYR H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB1 4 ALA H 88 ILE H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AB1 4 PHE H 100B TRP H 103 -1 O ILE H 102 N ARG H 94 SHEET 1 AB2 4 SER H 120 LEU H 124 0 SHEET 2 AB2 4 LEU H 138 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB2 4 TYR H 176 VAL H 182 -1 O VAL H 182 N LEU H 138 SHEET 4 AB2 4 HIS H 164 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB3 4 SER H 120 LEU H 124 0 SHEET 2 AB3 4 LEU H 138 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB3 4 TYR H 176 VAL H 182 -1 O VAL H 182 N LEU H 138 SHEET 4 AB3 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB4 3 THR H 151 TRP H 154 0 SHEET 2 AB4 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB4 3 THR H 205 VAL H 211 -1 O VAL H 211 N TYR H 194 SHEET 1 AB5 4 LYS B 6 SER B 11 0 SHEET 2 AB5 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AB5 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25 SHEET 4 AB5 4 VAL B 49 HIS B 51 -1 N GLU B 50 O TYR B 67 SHEET 1 AB6 4 LYS B 6 SER B 11 0 SHEET 2 AB6 4 ASN B 21 PHE B 30 -1 O SER B 28 N LYS B 6 SHEET 3 AB6 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25 SHEET 4 AB6 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63 SHEET 1 AB7 4 GLU B 44 ARG B 45 0 SHEET 2 AB7 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44 SHEET 3 AB7 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38 SHEET 4 AB7 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82 SHEET 1 AB8 4 MET L 4 SER L 7 0 SHEET 2 AB8 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AB8 4 PHE L 71 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB8 4 PHE L 62 GLU L 66 -1 N SER L 63 O THR L 74 SHEET 1 AB9 6 SER L 10 ALA L 13 0 SHEET 2 AB9 6 THR L 102 ILE L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AB9 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB9 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AB9 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AB9 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AC1 4 SER L 10 ALA L 13 0 SHEET 2 AC1 4 THR L 102 ILE L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AC1 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC1 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AC2 4 SER L 114 PHE L 118 0 SHEET 2 AC2 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AC2 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AC2 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AC3 3 ALA L 144 VAL L 150 0 SHEET 2 AC3 3 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 3 AC3 3 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.03 SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.03 SSBOND 3 CYS K 23 CYS K 97 1555 1555 2.03 SSBOND 4 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 5 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 6 CYS B 25 CYS B 80 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.03 CISPEP 1 TYR A 209 PRO A 210 0 1.77 CISPEP 2 PHE H 146 PRO H 147 0 -3.59 CISPEP 3 GLU H 148 PRO H 149 0 -6.12 CISPEP 4 HIS B 31 PRO B 32 0 2.16 CISPEP 5 SER L 7 PRO L 8 0 -5.15 CISPEP 6 PHE L 94 PRO L 95 0 2.65 CISPEP 7 TYR L 140 PRO L 141 0 1.93 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