HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 15-JUL-24 9IRB TITLE CRYOEM STRUCTURE OF HSLC15A4+FAB107 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUTE CARRIER FAMILY 15 MEMBER 4; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PEPTIDE TRANSPORTER 4,PEPTIDE/HISTIDINE TRANSPORTER 1,HPHT1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB107 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FAB107 LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 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: SLC15A4, PHT1, PTR4, FP12591; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_TAXID: 10090; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HSLC15A4+FAB107 COMPLEX, MEMBRANE PROTEIN, ANTIBODY, MEMBRANE KEYWDS 2 PROTEIN/IMMUNE SYSTEM, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Y.L.ZHU,Q.X.ZHANG,P.GAO REVDAT 1 20-AUG-25 9IRB 0 JRNL AUTH Y.ZHU,X.ZHANG,Q.ZHANG,P.SUN,K.LIU,X.NIE,J.MA,L.ZHANG,Y.GAO, JRNL AUTH 2 Y.WANG,S.LIU,A.GAO,L.ZHANG,P.GAO JRNL TITL DEVELOPMENT OF CONFORMATION-SELECTIVE ANTIBODIES TARGETING JRNL TITL 2 HUMAN SLC15A4. JRNL REF NAT COMMUN V. 16 7324 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40781080 JRNL DOI 10.1038/S41467-025-62759-X REMARK 2 REMARK 2 RESOLUTION. 3.15 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) : 3.150 REMARK 3 NUMBER OF PARTICLES : 552924 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 9IRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 16-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1300049096. 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 : HSLC15A4+FAB107 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 TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 QUANTUM (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1500.00 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) : 6000.00 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) : 200 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, 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 1 REMARK 465 GLU A 2 REMARK 465 GLY A 3 REMARK 465 SER A 4 REMARK 465 GLY A 5 REMARK 465 GLY A 6 REMARK 465 GLY A 7 REMARK 465 ALA A 8 REMARK 465 GLY A 9 REMARK 465 GLU A 10 REMARK 465 ARG A 11 REMARK 465 ALA A 12 REMARK 465 PRO A 13 REMARK 465 LEU A 14 REMARK 465 LEU A 15 REMARK 465 GLY A 16 REMARK 465 ALA A 17 REMARK 465 ARG A 18 REMARK 465 ARG A 19 REMARK 465 ALA A 20 REMARK 465 ALA A 21 REMARK 465 ALA A 22 REMARK 465 ALA A 23 REMARK 465 ALA A 24 REMARK 465 ALA A 25 REMARK 465 ALA A 26 REMARK 465 ALA A 27 REMARK 465 GLY A 28 REMARK 465 ALA A 29 REMARK 465 PHE A 30 REMARK 465 ALA A 31 REMARK 465 GLY A 32 REMARK 465 GLY A 134 REMARK 465 SER A 135 REMARK 465 ALA A 136 REMARK 465 ARG A 137 REMARK 465 LEU A 138 REMARK 465 LEU A 139 REMARK 465 ASN A 140 REMARK 465 CYS A 141 REMARK 465 THR A 142 REMARK 465 ALA A 143 REMARK 465 PRO A 144 REMARK 465 GLY A 145 REMARK 465 PRO A 146 REMARK 465 ASP A 147 REMARK 465 ALA A 148 REMARK 465 ALA A 149 REMARK 465 LEU A 264 REMARK 465 THR A 265 REMARK 465 TYR A 266 REMARK 465 SER A 267 REMARK 465 CYS A 268 REMARK 465 CYS A 269 REMARK 465 SER A 270 REMARK 465 GLN A 271 REMARK 465 LYS A 272 REMARK 465 ARG A 273 REMARK 465 SER A 274 REMARK 465 GLY A 275 REMARK 465 GLU A 276 REMARK 465 ARG A 277 REMARK 465 GLN A 278 REMARK 465 SER A 279 REMARK 465 ASN A 280 REMARK 465 GLY A 281 REMARK 465 GLU A 282 REMARK 465 GLY A 283 REMARK 465 ILE A 284 REMARK 465 GLY A 285 REMARK 465 VAL A 286 REMARK 465 PHE A 287 REMARK 465 GLN A 288 REMARK 465 GLN A 289 REMARK 465 SER A 290 REMARK 465 SER A 291 REMARK 465 LYS A 292 REMARK 465 GLN A 293 REMARK 465 SER A 294 REMARK 465 LEU A 295 REMARK 465 PHE A 296 REMARK 465 ASP A 297 REMARK 465 SER A 298 REMARK 465 CYS A 299 REMARK 465 LYS A 300 REMARK 465 MET A 301 REMARK 465 SER A 302 REMARK 465 HIS A 303 REMARK 465 HIS A 560 REMARK 465 ARG A 561 REMARK 465 ASP A 562 REMARK 465 HIS A 563 REMARK 465 GLN A 564 REMARK 465 ARG A 565 REMARK 465 SER A 566 REMARK 465 ARG A 567 REMARK 465 ALA A 568 REMARK 465 ASN A 569 REMARK 465 GLY A 570 REMARK 465 VAL A 571 REMARK 465 PRO A 572 REMARK 465 THR A 573 REMARK 465 SER A 574 REMARK 465 ARG A 575 REMARK 465 ARG A 576 REMARK 465 ALA A 577 REMARK 465 LYS A 578 REMARK 465 LEU A 579 REMARK 465 GLY A 580 REMARK 465 SER A 581 REMARK 465 GLU A 582 REMARK 465 ASN A 583 REMARK 465 LEU A 584 REMARK 465 TYR A 585 REMARK 465 PHE A 586 REMARK 465 GLN A 587 REMARK 465 GLY A 588 REMARK 465 GLY A 589 REMARK 465 SER A 590 REMARK 465 GLY A 591 REMARK 465 GLY A 592 REMARK 465 SER A 593 REMARK 465 GLY A 594 REMARK 465 HIS A 595 REMARK 465 HIS A 596 REMARK 465 HIS A 597 REMARK 465 HIS A 598 REMARK 465 HIS A 599 REMARK 465 HIS A 600 REMARK 465 HIS A 601 REMARK 465 HIS A 602 REMARK 465 SER H 122 REMARK 465 SER H 123 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 CYS A 153 31.02 -97.56 REMARK 500 VAL A 220 -64.12 -120.12 REMARK 500 ARG A 350 98.01 -69.14 REMARK 500 THR A 358 30.51 -94.68 REMARK 500 THR A 359 -167.08 -78.89 REMARK 500 PRO H 53 43.53 -78.12 REMARK 500 ASP H 66 -12.69 70.60 REMARK 500 SER H 85 71.70 53.00 REMARK 500 LYS H 104 -9.06 76.23 REMARK 500 ASP H 106 53.75 -92.05 REMARK 500 ASP H 111 -102.15 58.76 REMARK 500 SER L 50 16.14 58.73 REMARK 500 ALA L 51 -7.80 70.90 REMARK 500 ASP L 60 -8.34 73.42 REMARK 500 SER L 67 148.11 -172.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60808 RELATED DB: EMDB REMARK 900 HSLC15A4+FAB107 DBREF 9IRB A 1 577 UNP Q8N697 S15A4_HUMAN 1 577 DBREF 9IRB H 1 123 PDB 9IRB 9IRB 1 123 DBREF 9IRB L 1 107 PDB 9IRB 9IRB 1 107 SEQADV 9IRB LYS A 578 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB LEU A 579 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLY A 580 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB SER A 581 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLU A 582 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB ASN A 583 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB LEU A 584 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB TYR A 585 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB PHE A 586 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLN A 587 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLY A 588 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLY A 589 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB SER A 590 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLY A 591 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLY A 592 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB SER A 593 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB GLY A 594 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 595 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 596 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 597 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 598 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 599 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 600 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 601 UNP Q8N697 EXPRESSION TAG SEQADV 9IRB HIS A 602 UNP Q8N697 EXPRESSION TAG SEQRES 1 A 602 MET GLU GLY SER GLY GLY GLY ALA GLY GLU ARG ALA PRO SEQRES 2 A 602 LEU LEU GLY ALA ARG ARG ALA ALA ALA ALA ALA ALA ALA SEQRES 3 A 602 ALA GLY ALA PHE ALA GLY ARG ARG ALA ALA CYS GLY ALA SEQRES 4 A 602 VAL LEU LEU THR GLU LEU LEU GLU ARG ALA ALA PHE TYR SEQRES 5 A 602 GLY ILE THR SER ASN LEU VAL LEU PHE LEU ASN GLY ALA SEQRES 6 A 602 PRO PHE CYS TRP GLU GLY ALA GLN ALA SER GLU ALA LEU SEQRES 7 A 602 LEU LEU PHE MET GLY LEU THR TYR LEU GLY SER PRO PHE SEQRES 8 A 602 GLY GLY TRP LEU ALA ASP ALA ARG LEU GLY ARG ALA ARG SEQRES 9 A 602 ALA ILE LEU LEU SER LEU ALA LEU TYR LEU LEU GLY MET SEQRES 10 A 602 LEU ALA PHE PRO LEU LEU ALA ALA PRO ALA THR ARG ALA SEQRES 11 A 602 ALA LEU CYS GLY SER ALA ARG LEU LEU ASN CYS THR ALA SEQRES 12 A 602 PRO GLY PRO ASP ALA ALA ALA ARG CYS CYS SER PRO ALA SEQRES 13 A 602 THR PHE ALA GLY LEU VAL LEU VAL GLY LEU GLY VAL ALA SEQRES 14 A 602 THR VAL LYS ALA ASN ILE THR PRO PHE GLY ALA ASP GLN SEQRES 15 A 602 VAL LYS ASP ARG GLY PRO GLU ALA THR ARG ARG PHE PHE SEQRES 16 A 602 ASN TRP PHE TYR TRP SER ILE ASN LEU GLY ALA ILE LEU SEQRES 17 A 602 SER LEU GLY GLY ILE ALA TYR ILE GLN GLN ASN VAL SER SEQRES 18 A 602 PHE VAL THR GLY TYR ALA ILE PRO THR VAL CYS VAL GLY SEQRES 19 A 602 LEU ALA PHE VAL VAL PHE LEU CYS GLY GLN SER VAL PHE SEQRES 20 A 602 ILE THR LYS PRO PRO ASP GLY SER ALA PHE THR ASP MET SEQRES 21 A 602 PHE LYS ILE LEU THR TYR SER CYS CYS SER GLN LYS ARG SEQRES 22 A 602 SER GLY GLU ARG GLN SER ASN GLY GLU GLY ILE GLY VAL SEQRES 23 A 602 PHE GLN GLN SER SER LYS GLN SER LEU PHE ASP SER CYS SEQRES 24 A 602 LYS MET SER HIS GLY GLY PRO PHE THR GLU GLU LYS VAL SEQRES 25 A 602 GLU ASP VAL LYS ALA LEU VAL LYS ILE VAL PRO VAL PHE SEQRES 26 A 602 LEU ALA LEU ILE PRO TYR TRP THR VAL TYR PHE GLN MET SEQRES 27 A 602 GLN THR THR TYR VAL LEU GLN SER LEU HIS LEU ARG ILE SEQRES 28 A 602 PRO GLU ILE SER ASN ILE THR THR THR PRO HIS THR LEU SEQRES 29 A 602 PRO ALA ALA TRP LEU THR MET PHE ASP ALA VAL LEU ILE SEQRES 30 A 602 LEU LEU LEU ILE PRO LEU LYS ASP LYS LEU VAL ASP PRO SEQRES 31 A 602 ILE LEU ARG ARG HIS GLY LEU LEU PRO SER SER LEU LYS SEQRES 32 A 602 ARG ILE ALA VAL GLY MET PHE PHE VAL MET CYS SER ALA SEQRES 33 A 602 PHE ALA ALA GLY ILE LEU GLU SER LYS ARG LEU ASN LEU SEQRES 34 A 602 VAL LYS GLU LYS THR ILE ASN GLN THR ILE GLY ASN VAL SEQRES 35 A 602 VAL TYR HIS ALA ALA ASP LEU SER LEU TRP TRP GLN VAL SEQRES 36 A 602 PRO GLN TYR LEU LEU ILE GLY ILE SER GLU ILE PHE ALA SEQRES 37 A 602 SER ILE ALA GLY LEU GLU PHE ALA TYR SER ALA ALA PRO SEQRES 38 A 602 LYS SER MET GLN SER ALA ILE MET GLY LEU PHE PHE PHE SEQRES 39 A 602 PHE SER GLY VAL GLY SER PHE VAL GLY SER GLY LEU LEU SEQRES 40 A 602 ALA LEU VAL SER ILE LYS ALA ILE GLY TRP MET SER SER SEQRES 41 A 602 HIS THR ASP PHE GLY ASN ILE ASN GLY CYS TYR LEU ASN SEQRES 42 A 602 TYR TYR PHE PHE LEU LEU ALA ALA ILE GLN GLY ALA THR SEQRES 43 A 602 LEU LEU LEU PHE LEU ILE ILE SER VAL LYS TYR ASP HIS SEQRES 44 A 602 HIS ARG ASP HIS GLN ARG SER ARG ALA ASN GLY VAL PRO SEQRES 45 A 602 THR SER ARG ARG ALA LYS LEU GLY SER GLU ASN LEU TYR SEQRES 46 A 602 PHE GLN GLY GLY SER GLY GLY SER GLY HIS HIS HIS HIS SEQRES 47 A 602 HIS HIS HIS HIS SEQRES 1 H 123 GLN VAL GLN LEU GLN GLN PRO GLY THR GLU LEU VAL ARG SEQRES 2 H 123 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 123 TYR SER PHE THR ARG TYR TRP MET ASN TRP VAL LYS GLN SEQRES 4 H 123 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY MET VAL HIS SEQRES 5 H 123 PRO SER ASP SER GLU THR ARG LEU ASN GLN ASN PHE LYS SEQRES 6 H 123 ASP LYS ALA THR LEU THR VAL ASP LYS SER SER SER ILE SEQRES 7 H 123 ALA TYR MET GLN LEU SER SER PRO THR SER GLU ASP SER SEQRES 8 H 123 ALA VAL TYR TYR CYS ALA ARG TRP GLY ALA TYR TYR LYS SEQRES 9 H 123 TYR ASP TRP ASP TYR PHE ASP SER TRP GLY GLN GLY THR SEQRES 10 H 123 THR LEU THR VAL SER SER SEQRES 1 L 107 ASP ILE VAL MET THR GLN SER GLN LYS PHE MET SER THR SEQRES 2 L 107 SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS ALA SER SEQRES 3 L 107 GLN ASN VAL GLY THR ASN VAL VAL TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY GLN SER PRO LYS VAL LEU ILE TYR SER ALA SER SEQRES 5 L 107 TYR ARG TYR SER GLY VAL PRO ASP ARG ILE THR GLY SER SEQRES 6 L 107 GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN VAL SEQRES 7 L 107 GLN SER GLU ASP LEU ALA GLU TYR PHE CYS GLN GLN TYR SEQRES 8 L 107 ASN ASN PHE PRO TYR THR PHE GLY GLY GLY THR ASN LEU SEQRES 9 L 107 GLU ILE LYS HELIX 1 AA1 ARG A 33 SER A 56 1 24 HELIX 2 AA2 LEU A 58 GLY A 64 1 7 HELIX 3 AA3 ALA A 72 ARG A 99 1 28 HELIX 4 AA4 GLY A 101 LEU A 118 1 18 HELIX 5 AA5 LEU A 118 ALA A 125 1 8 HELIX 6 AA6 THR A 128 CYS A 133 1 6 HELIX 7 AA7 CYS A 153 ASP A 185 1 33 HELIX 8 AA8 GLY A 187 VAL A 220 1 34 HELIX 9 AA9 VAL A 223 GLN A 244 1 22 HELIX 10 AB1 GLY A 254 ILE A 263 1 10 HELIX 11 AB2 THR A 308 LEU A 328 1 21 HELIX 12 AB3 LEU A 328 HIS A 348 1 21 HELIX 13 AB4 ALA A 366 MET A 371 1 6 HELIX 14 AB5 MET A 371 LEU A 387 1 17 HELIX 15 AB6 LEU A 387 HIS A 395 1 9 HELIX 16 AB7 SER A 400 VAL A 430 1 31 HELIX 17 AB8 SER A 450 TRP A 453 5 4 HELIX 18 AB9 GLN A 454 ALA A 479 1 26 HELIX 19 AC1 MET A 484 SER A 511 1 28 HELIX 20 AC2 TYR A 531 HIS A 559 1 29 HELIX 21 AC3 SER H 28 TYR H 32 5 5 HELIX 22 AC4 THR H 87 SER H 91 5 5 SHEET 1 AA1 2 THR A 434 ILE A 439 0 SHEET 2 AA1 2 VAL A 442 ALA A 447 -1 O VAL A 442 N ILE A 439 SHEET 1 AA2 4 GLN H 3 GLN H 5 0 SHEET 2 AA2 4 SER H 17 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA2 4 ILE H 78 SER H 84 -1 O LEU H 83 N VAL H 18 SHEET 4 AA2 4 ALA H 68 ASP H 73 -1 N ASP H 73 O ILE H 78 SHEET 1 AA3 4 LEU H 45 VAL H 51 0 SHEET 2 AA3 4 MET H 34 GLN H 39 -1 N TRP H 36 O ILE H 48 SHEET 3 AA3 4 ALA H 92 ALA H 97 -1 O VAL H 93 N GLN H 39 SHEET 4 AA3 4 THR H 117 LEU H 119 -1 O THR H 117 N TYR H 94 SHEET 1 AA4 2 GLY H 100 TYR H 102 0 SHEET 2 AA4 2 TYR H 105 TYR H 109 -1 O TYR H 109 N GLY H 100 SHEET 1 AA5 5 PHE L 10 THR L 13 0 SHEET 2 AA5 5 THR L 102 ILE L 106 1 O GLU L 105 N MET L 11 SHEET 3 AA5 5 GLU L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA5 5 VAL L 33 GLN L 38 -1 N VAL L 34 O GLN L 89 SHEET 5 AA5 5 LYS L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 1 AA6 3 VAL L 19 LYS L 24 0 SHEET 2 AA6 3 ASP L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 3 AA6 3 ILE L 62 SER L 67 -1 N SER L 65 O THR L 72 SSBOND 1 CYS A 133 CYS A 153 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 CISPEP 1 ALA A 65 PRO A 66 0 -0.26 CISPEP 2 PHE L 94 PRO L 95 0 -0.30 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