HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 15-JUL-24 9IRC TITLE CYROEM STRUCTURE OF HSLC15A4+TASL+FAB235 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: TLR ADAPTER INTERACTING WITH SLC15A4 ON THE LYSOSOME; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FAB235 HEAVY CHAIN; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: FAB235 LIGHT CHAIN; COMPND 16 CHAIN: L; COMPND 17 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 GENE: TASL; SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 16 ORGANISM_TAXID: 10090; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 21 ORGANISM_TAXID: 10090; SOURCE 22 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HSLC15A4+TASL+FAB235 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 9IRC 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. 2.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 2.820 REMARK 3 NUMBER OF PARTICLES : 226165 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 9IRC 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_1300049107. 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+TASL+FAB235 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ALA A 150 REMARK 465 ARG A 151 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 HIS A 559 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 CYS B 20 REMARK 465 ALA B 21 REMARK 465 SER B 22 REMARK 465 TYR B 23 REMARK 465 ASN B 24 REMARK 465 GLU B 25 REMARK 465 PRO B 26 REMARK 465 VAL B 27 REMARK 465 ALA B 28 REMARK 465 GLY B 29 REMARK 465 ASP B 30 REMARK 465 GLN B 31 REMARK 465 GLY B 32 REMARK 465 LYS B 33 REMARK 465 GLU B 34 REMARK 465 PRO B 35 REMARK 465 ILE B 36 REMARK 465 SER B 37 REMARK 465 ASN B 38 REMARK 465 ALA B 39 REMARK 465 VAL B 40 REMARK 465 LEU B 41 REMARK 465 ASN B 42 REMARK 465 GLU B 43 REMARK 465 TYR B 44 REMARK 465 LEU B 45 REMARK 465 GLU B 46 REMARK 465 GLN B 47 REMARK 465 LYS B 48 REMARK 465 VAL B 49 REMARK 465 VAL B 50 REMARK 465 GLU B 51 REMARK 465 LEU B 52 REMARK 465 TYR B 53 REMARK 465 LYS B 54 REMARK 465 GLN B 55 REMARK 465 TYR B 56 REMARK 465 ILE B 57 REMARK 465 MET B 58 REMARK 465 ASP B 59 REMARK 465 THR B 60 REMARK 465 VAL B 61 REMARK 465 PHE B 62 REMARK 465 HIS B 63 REMARK 465 ASP B 64 REMARK 465 SER B 65 REMARK 465 SER B 66 REMARK 465 PRO B 67 REMARK 465 THR B 68 REMARK 465 GLN B 69 REMARK 465 ILE B 70 REMARK 465 LEU B 71 REMARK 465 ALA B 72 REMARK 465 SER B 73 REMARK 465 GLU B 74 REMARK 465 PHE B 75 REMARK 465 ILE B 76 REMARK 465 MET B 77 REMARK 465 THR B 78 REMARK 465 ASN B 79 REMARK 465 VAL B 80 REMARK 465 ASP B 81 REMARK 465 GLN B 82 REMARK 465 ILE B 83 REMARK 465 SER B 84 REMARK 465 LEU B 85 REMARK 465 GLN B 86 REMARK 465 VAL B 87 REMARK 465 SER B 88 REMARK 465 LYS B 89 REMARK 465 GLU B 90 REMARK 465 LYS B 91 REMARK 465 ASN B 92 REMARK 465 LEU B 93 REMARK 465 ASP B 94 REMARK 465 THR B 95 REMARK 465 SER B 96 REMARK 465 LYS B 97 REMARK 465 VAL B 98 REMARK 465 LYS B 99 REMARK 465 ASP B 100 REMARK 465 ILE B 101 REMARK 465 VAL B 102 REMARK 465 ILE B 103 REMARK 465 SER B 104 REMARK 465 HIS B 105 REMARK 465 LEU B 106 REMARK 465 LEU B 107 REMARK 465 GLN B 108 REMARK 465 LEU B 109 REMARK 465 VAL B 110 REMARK 465 SER B 111 REMARK 465 SER B 112 REMARK 465 GLU B 113 REMARK 465 ILE B 114 REMARK 465 SER B 115 REMARK 465 THR B 116 REMARK 465 PRO B 117 REMARK 465 SER B 118 REMARK 465 LEU B 119 REMARK 465 HIS B 120 REMARK 465 ILE B 121 REMARK 465 SER B 122 REMARK 465 GLN B 123 REMARK 465 TYR B 124 REMARK 465 SER B 125 REMARK 465 ASN B 126 REMARK 465 ILE B 127 REMARK 465 THR B 128 REMARK 465 PRO B 129 REMARK 465 LYS B 130 REMARK 465 LEU B 131 REMARK 465 GLY B 132 REMARK 465 SER B 133 REMARK 465 GLU B 134 REMARK 465 ASN B 135 REMARK 465 LEU B 136 REMARK 465 TYR B 137 REMARK 465 PHE B 138 REMARK 465 GLN B 139 REMARK 465 GLY B 140 REMARK 465 GLY B 141 REMARK 465 SER B 142 REMARK 465 GLY B 143 REMARK 465 GLY B 144 REMARK 465 SER B 145 REMARK 465 GLY B 146 REMARK 465 HIS B 147 REMARK 465 HIS B 148 REMARK 465 HIS B 149 REMARK 465 HIS B 150 REMARK 465 HIS B 151 REMARK 465 HIS B 152 REMARK 465 HIS B 153 REMARK 465 HIS B 154 REMARK 465 TRP B 155 REMARK 465 SER B 156 REMARK 465 HIS B 157 REMARK 465 PRO B 158 REMARK 465 GLN B 159 REMARK 465 PHE B 160 REMARK 465 GLU B 161 REMARK 465 LYS B 162 REMARK 465 TRP B 163 REMARK 465 SER B 164 REMARK 465 HIS B 165 REMARK 465 PRO B 166 REMARK 465 GLN B 167 REMARK 465 PHE B 168 REMARK 465 GLU B 169 REMARK 465 LYS B 170 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 OG SER A 346 OE1 GLN A 454 2.16 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 ASN A 63 57.20 -97.79 REMARK 500 CYS A 68 51.70 -91.68 REMARK 500 LEU A 100 -6.54 68.00 REMARK 500 CYS A 153 59.10 -91.88 REMARK 500 LYS A 300 -166.07 58.14 REMARK 500 SER A 302 -151.58 52.73 REMARK 500 HIS A 303 -128.26 33.84 REMARK 500 THR A 358 177.10 60.98 REMARK 500 THR A 360 71.18 37.60 REMARK 500 LEU A 397 29.88 47.24 REMARK 500 THR A 438 47.68 -82.53 REMARK 500 ALA A 468 -61.13 -106.31 REMARK 500 SER A 486 -4.61 70.06 REMARK 500 TRP B 18 -95.14 59.51 REMARK 500 GLU H 42 12.04 59.99 REMARK 500 THR H 101 42.79 -108.88 REMARK 500 THR L 52 13.54 50.05 REMARK 500 SER L 53 -36.11 -132.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG L 46 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60809 RELATED DB: EMDB REMARK 900 HSLC15A4+TASL+FAB235 DBREF 9IRC A 1 577 UNP Q8N697 S15A4_HUMAN 1 577 DBREF 9IRC B 35 129 UNP Q9D3J9 TASL_MOUSE 204 298 DBREF 9IRC H 1 120 PDB 9IRC 9IRC 1 120 DBREF 9IRC L 1 108 PDB 9IRC 9IRC 1 108 SEQADV 9IRC LYS A 578 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC LEU A 579 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLY A 580 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC SER A 581 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLU A 582 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC ASN A 583 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC LEU A 584 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC TYR A 585 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC PHE A 586 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLN A 587 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLY A 588 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLY A 589 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC SER A 590 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLY A 591 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLY A 592 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC SER A 593 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC GLY A 594 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 595 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 596 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 597 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 598 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 599 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 600 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 601 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC HIS A 602 UNP Q8N697 EXPRESSION TAG SEQADV 9IRC MET B 1 UNP Q9D3J9 INITIATING METHIONINE SEQADV 9IRC LEU B 2 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 3 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 4 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 5 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TYR B 6 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LEU B 7 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 8 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 9 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LEU B 10 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 11 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TYR B 12 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TRP B 13 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ASN B 14 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ASP B 15 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ILE B 16 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 17 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TRP B 18 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ASN B 19 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC CYS B 20 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ALA B 21 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 22 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TYR B 23 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ASN B 24 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 25 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC PRO B 26 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC VAL B 27 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ALA B 28 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 29 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ASP B 30 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLN B 31 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 32 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LYS B 33 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 34 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LYS B 130 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LEU B 131 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 132 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 133 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 134 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC ASN B 135 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LEU B 136 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TYR B 137 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC PHE B 138 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLN B 139 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 140 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 141 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 142 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 143 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 144 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 145 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLY B 146 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 147 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 148 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 149 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 150 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 151 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 152 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 153 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 154 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TRP B 155 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 156 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 157 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC PRO B 158 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLN B 159 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC PHE B 160 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 161 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LYS B 162 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC TRP B 163 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC SER B 164 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC HIS B 165 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC PRO B 166 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLN B 167 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC PHE B 168 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC GLU B 169 UNP Q9D3J9 EXPRESSION TAG SEQADV 9IRC LYS B 170 UNP Q9D3J9 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 B 170 MET LEU SER GLU GLY TYR LEU SER GLY LEU GLU TYR TRP SEQRES 2 B 170 ASN ASP ILE HIS TRP ASN CYS ALA SER TYR ASN GLU PRO SEQRES 3 B 170 VAL ALA GLY ASP GLN GLY LYS GLU PRO ILE SER ASN ALA SEQRES 4 B 170 VAL LEU ASN GLU TYR LEU GLU GLN LYS VAL VAL GLU LEU SEQRES 5 B 170 TYR LYS GLN TYR ILE MET ASP THR VAL PHE HIS ASP SER SEQRES 6 B 170 SER PRO THR GLN ILE LEU ALA SER GLU PHE ILE MET THR SEQRES 7 B 170 ASN VAL ASP GLN ILE SER LEU GLN VAL SER LYS GLU LYS SEQRES 8 B 170 ASN LEU ASP THR SER LYS VAL LYS ASP ILE VAL ILE SER SEQRES 9 B 170 HIS LEU LEU GLN LEU VAL SER SER GLU ILE SER THR PRO SEQRES 10 B 170 SER LEU HIS ILE SER GLN TYR SER ASN ILE THR PRO LYS SEQRES 11 B 170 LEU GLY SER GLU ASN LEU TYR PHE GLN GLY GLY SER GLY SEQRES 12 B 170 GLY SER GLY HIS HIS HIS HIS HIS HIS HIS HIS TRP SER SEQRES 13 B 170 HIS PRO GLN PHE GLU LYS TRP SER HIS PRO GLN PHE GLU SEQRES 14 B 170 LYS SEQRES 1 H 120 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 120 PRO GLY GLY SER ARG LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 120 PHE THR PHE SER ARG PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 120 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 H 120 SER GLY SER SER ASN ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 H 120 GLY ARG PHE THR ILE SER ARG ASP ASN PRO LYS ASN THR SEQRES 7 H 120 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 H 120 ALA MET TYR TYR CYS ALA ARG SER THR THR ILE ILE ARG SEQRES 9 H 120 ALA PHE PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR SEQRES 10 H 120 VAL SER SER SEQRES 1 L 108 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA SEQRES 2 L 108 SER LEU GLY GLU ARG VAL THR MET THR CYS THR ALA SER SEQRES 3 L 108 SER GLY VAL SER SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 108 LYS PRO GLY SER SER PRO ARG LEU TRP ILE TYR SER THR SEQRES 5 L 108 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 L 108 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 108 MET GLU ALA GLU ASP ALA ALA THR TYR TYR CYS HIS GLN SEQRES 8 L 108 TYR HIS ARG SER PRO TRP ALA PHE GLY GLY GLY THR LYS SEQRES 9 L 108 LEU GLU ILE LYS HELIX 1 AA1 ARG A 33 ASN A 63 1 31 HELIX 2 AA2 GLU A 70 ARG A 99 1 30 HELIX 3 AA3 ARG A 102 LEU A 118 1 17 HELIX 4 AA4 LEU A 118 ALA A 125 1 8 HELIX 5 AA5 ALA A 125 CYS A 133 1 9 HELIX 6 AA6 CYS A 153 LYS A 184 1 32 HELIX 7 AA7 GLY A 187 ASN A 219 1 33 HELIX 8 AA8 SER A 221 GLN A 244 1 24 HELIX 9 AA9 SER A 255 THR A 265 1 11 HELIX 10 AB1 THR A 308 HIS A 348 1 41 HELIX 11 AB2 ALA A 367 LEU A 387 1 21 HELIX 12 AB3 LEU A 387 GLY A 396 1 10 HELIX 13 AB4 SER A 400 LYS A 431 1 32 HELIX 14 AB5 SER A 450 TRP A 453 5 4 HELIX 15 AB6 GLN A 454 ALA A 468 1 15 HELIX 16 AB7 ALA A 468 ALA A 479 1 12 HELIX 17 AB8 PRO A 481 GLN A 485 5 5 HELIX 18 AB9 ALA A 487 SER A 511 1 25 HELIX 19 AC1 ASN A 526 CYS A 530 5 5 HELIX 20 AC2 TYR A 531 ASP A 558 1 28 HELIX 21 AC3 SER B 3 GLY B 9 1 7 HELIX 22 AC4 GLY B 9 ASN B 14 1 6 HELIX 23 AC5 ARG H 87 THR H 91 5 5 HELIX 24 AC6 SER L 30 SER L 32 5 3 HELIX 25 AC7 GLU L 80 ALA L 84 5 5 SHEET 1 AA1 2 ILE A 435 GLN A 437 0 SHEET 2 AA1 2 TYR A 444 ALA A 446 -1 O ALA A 446 N ILE A 435 SHEET 1 AA2 4 GLN H 3 SER H 7 0 SHEET 2 AA2 4 ARG H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA2 4 THR H 78 MET H 83 -1 O MET H 83 N ARG H 18 SHEET 4 AA2 4 PHE H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 AA3 6 LEU H 11 VAL H 12 0 SHEET 2 AA3 6 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AA3 6 ALA H 92 SER H 99 -1 N ALA H 92 O LEU H 116 SHEET 4 AA3 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA3 6 ILE H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AA4 4 LEU H 11 VAL H 12 0 SHEET 2 AA4 4 THR H 114 VAL H 118 1 O THR H 117 N VAL H 12 SHEET 3 AA4 4 ALA H 92 SER H 99 -1 N ALA H 92 O LEU H 116 SHEET 4 AA4 4 PHE H 107 TRP H 110 -1 O TYR H 109 N ARG H 98 SHEET 1 AA5 3 LEU L 4 SER L 7 0 SHEET 2 AA5 3 VAL L 19 VAL L 29 -1 O THR L 22 N SER L 7 SHEET 3 AA5 3 PHE L 63 ILE L 76 -1 O ILE L 76 N VAL L 19 SHEET 1 AA6 6 ILE L 10 ALA L 13 0 SHEET 2 AA6 6 THR L 103 ILE L 107 1 O GLU L 106 N ALA L 13 SHEET 3 AA6 6 THR L 86 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA6 6 LEU L 34 GLN L 39 -1 N HIS L 35 O HIS L 90 SHEET 5 AA6 6 ARG L 46 TYR L 50 -1 O TRP L 48 N TRP L 36 SHEET 6 AA6 6 ASN L 54 LEU L 55 -1 O ASN L 54 N TYR L 50 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 89 1555 1555 2.03 CISPEP 1 SER L 7 PRO L 8 0 -5.12 CISPEP 2 SER L 95 PRO L 96 0 -1.57 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