HEADER TRANSPORT PROTEIN 01-AUG-24 9CY1 TITLE OUTWARD-FACING OATP1B1 BOUND TO SYBODY SB5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 1B1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SLCO1B1,LIVER-SPECIFIC ORGANIC ANION TRANSPORTER 1,LST-1, COMPND 5 OATP-C,ORGANIC ANION TRANSPORTER SLC21A6,SODIUM-INDEPENDENT ORGANIC COMPND 6 ANION-TRANSPORTING POLYPEPTIDE 2,OATP-2,SOLUTE CARRIER FAMILY 21 COMPND 7 MEMBER 6; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: SYBODY 5; COMPND 11 CHAIN: B; COMPND 12 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: SLCO1B1, LST1, OATP1B1, OATP2, OATPC, SLC21A6; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 11 ORGANISM_TAXID: 32630; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS SOLUTE CARRIER, SYBODY, MEMBRANE PROTEIN, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR M.W.SUNG,J.A.LEES,S.HAN REVDAT 1 16-APR-25 9CY1 0 JRNL AUTH M.W.SUNG,K.HU,L.M.HURLIMANN,J.A.LEES,K.F.FENNELL,M.A.WEST, JRNL AUTH 2 C.COSTALES,A.D.RODRIGUES,I.ZIMMERMANN,R.J.P.DAWSON,S.LIU, JRNL AUTH 3 S.HAN JRNL TITL CYCLOSPORINE A STERICALLY INHIBITS STATIN TRANSPORT BY JRNL TITL 2 SOLUTE CARRIER OATP1B1 JRNL REF TO BE PUBLISHED JRNL REFN 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 : 58056 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 9CY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000286413. 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 : OUTWARD-FACING OATP1B1 BOUND TO REMARK 245 SYBODY 5 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 : TFS FALCON 4I (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 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) : 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) : 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 -25 REMARK 465 HIS A -24 REMARK 465 HIS A -23 REMARK 465 HIS A -22 REMARK 465 HIS A -21 REMARK 465 HIS A -20 REMARK 465 HIS A -19 REMARK 465 HIS A -18 REMARK 465 HIS A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 ASP A -14 REMARK 465 TYR A -13 REMARK 465 LYS A -12 REMARK 465 ASP A -11 REMARK 465 ASP A -10 REMARK 465 ASP A -9 REMARK 465 ASP A -8 REMARK 465 LYS A -7 REMARK 465 GLU A -6 REMARK 465 ASN A -5 REMARK 465 LEU A -4 REMARK 465 TYR A -3 REMARK 465 PHE A -2 REMARK 465 GLN A -1 REMARK 465 GLY A 0 REMARK 465 MET A 1 REMARK 465 ASP A 2 REMARK 465 GLN A 3 REMARK 465 ASN A 4 REMARK 465 GLN A 5 REMARK 465 HIS A 6 REMARK 465 LEU A 7 REMARK 465 ASN A 8 REMARK 465 LYS A 9 REMARK 465 THR A 10 REMARK 465 ALA A 11 REMARK 465 GLU A 12 REMARK 465 ALA A 13 REMARK 465 GLN A 14 REMARK 465 PRO A 15 REMARK 465 SER A 16 REMARK 465 GLU A 17 REMARK 465 ASN A 18 REMARK 465 LYS A 19 REMARK 465 LYS A 20 REMARK 465 THR A 21 REMARK 465 ARG A 22 REMARK 465 TYR A 23 REMARK 465 LYS A 125 REMARK 465 GLU A 126 REMARK 465 THR A 127 REMARK 465 ASN A 128 REMARK 465 ILE A 129 REMARK 465 ASN A 130 REMARK 465 SER A 131 REMARK 465 SER A 132 REMARK 465 GLU A 133 REMARK 465 ASN A 134 REMARK 465 SER A 135 REMARK 465 THR A 136 REMARK 465 SER A 137 REMARK 465 ASN A 145 REMARK 465 GLN A 146 REMARK 465 ILE A 147 REMARK 465 LEU A 148 REMARK 465 SER A 149 REMARK 465 LEU A 150 REMARK 465 ASN A 151 REMARK 465 ARG A 152 REMARK 465 ALA A 153 REMARK 465 SER A 154 REMARK 465 PRO A 155 REMARK 465 GLU A 156 REMARK 465 ILE A 157 REMARK 465 VAL A 158 REMARK 465 GLY A 159 REMARK 465 LYS A 160 REMARK 465 GLY A 161 REMARK 465 CYS A 162 REMARK 465 LEU A 163 REMARK 465 LYS A 164 REMARK 465 GLU A 165 REMARK 465 SER A 166 REMARK 465 GLY A 167 REMARK 465 LYS A 285 REMARK 465 PRO A 286 REMARK 465 GLN A 287 REMARK 465 LYS A 288 REMARK 465 GLU A 289 REMARK 465 ARG A 290 REMARK 465 LYS A 291 REMARK 465 ALA A 292 REMARK 465 SER A 293 REMARK 465 LEU A 294 REMARK 465 SER A 295 REMARK 465 LEU A 296 REMARK 465 HIS A 297 REMARK 465 VAL A 298 REMARK 465 LEU A 299 REMARK 465 GLU A 300 REMARK 465 THR A 301 REMARK 465 ASN A 302 REMARK 465 ASP A 303 REMARK 465 GLU A 304 REMARK 465 LYS A 305 REMARK 465 ASP A 306 REMARK 465 GLN A 307 REMARK 465 THR A 308 REMARK 465 ALA A 309 REMARK 465 ASN A 310 REMARK 465 LEU A 311 REMARK 465 THR A 312 REMARK 465 ASN A 313 REMARK 465 GLN A 314 REMARK 465 GLY A 315 REMARK 465 LYS A 316 REMARK 465 ASN A 317 REMARK 465 ILE A 318 REMARK 465 THR A 319 REMARK 465 LYS A 320 REMARK 465 ASN A 321 REMARK 465 VAL A 322 REMARK 465 THR A 323 REMARK 465 SER A 372 REMARK 465 LYS A 373 REMARK 465 ALA A 374 REMARK 465 ASN A 375 REMARK 465 ILE A 376 REMARK 465 LEU A 377 REMARK 465 LEU A 378 REMARK 465 SER A 493 REMARK 465 GLY A 494 REMARK 465 ASN A 495 REMARK 465 LYS A 496 REMARK 465 LYS A 497 REMARK 465 PRO A 498 REMARK 465 ILE A 499 REMARK 465 VAL A 500 REMARK 465 THR A 510 REMARK 465 GLY A 511 REMARK 465 LEU A 512 REMARK 465 GLN A 513 REMARK 465 ASN A 514 REMARK 465 ARG A 515 REMARK 465 ASN A 516 REMARK 465 TYR A 517 REMARK 465 SER A 518 REMARK 465 GLN A 652 REMARK 465 GLU A 653 REMARK 465 LYS A 654 REMARK 465 ASP A 655 REMARK 465 ILE A 656 REMARK 465 ASN A 657 REMARK 465 ALA A 658 REMARK 465 SER A 659 REMARK 465 GLU A 660 REMARK 465 ASN A 661 REMARK 465 GLY A 662 REMARK 465 SER A 663 REMARK 465 VAL A 664 REMARK 465 MET A 665 REMARK 465 ASP A 666 REMARK 465 GLU A 667 REMARK 465 ALA A 668 REMARK 465 ASN A 669 REMARK 465 LEU A 670 REMARK 465 GLU A 671 REMARK 465 SER A 672 REMARK 465 LEU A 673 REMARK 465 ASN A 674 REMARK 465 LYS A 675 REMARK 465 ASN A 676 REMARK 465 LYS A 677 REMARK 465 HIS A 678 REMARK 465 PHE A 679 REMARK 465 VAL A 680 REMARK 465 PRO A 681 REMARK 465 SER A 682 REMARK 465 ALA A 683 REMARK 465 GLY A 684 REMARK 465 ALA A 685 REMARK 465 ASP A 686 REMARK 465 SER A 687 REMARK 465 GLU A 688 REMARK 465 THR A 689 REMARK 465 HIS A 690 REMARK 465 CYS A 691 REMARK 465 ARG B 121 REMARK 465 ALA B 122 REMARK 465 GLY B 123 REMARK 465 GLU B 124 REMARK 465 GLN B 125 REMARK 465 LYS B 126 REMARK 465 LEU B 127 REMARK 465 ILE B 128 REMARK 465 SER B 129 REMARK 465 GLU B 130 REMARK 465 GLU B 131 REMARK 465 ASP B 132 REMARK 465 LEU B 133 REMARK 465 ASN B 134 REMARK 465 SER B 135 REMARK 465 ALA B 136 REMARK 465 VAL B 137 REMARK 465 ASP B 138 REMARK 465 HIS B 139 REMARK 465 HIS B 140 REMARK 465 HIS B 141 REMARK 465 HIS B 142 REMARK 465 HIS B 143 REMARK 465 HIS B 144 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 THR A 138 OG1 CG2 REMARK 470 LEU A 139 CG CD1 CD2 REMARK 470 SER A 140 OG REMARK 470 THR A 141 OG1 CG2 REMARK 470 LEU A 143 CG CD1 CD2 REMARK 470 ILE A 144 CG1 CG2 CD1 REMARK 470 VAL B 16 CG1 CG2 REMARK 470 GLN B 17 CG CD OE1 NE2 REMARK 470 GLU B 48 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 197 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES REMARK 500 LEU A 344 CA - CB - CG ANGL. DEV. = 15.8 DEGREES 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 ASP A 236 36.21 -97.22 REMARK 500 LEU A 438 -50.38 -120.44 REMARK 500 MET A 440 -169.16 -128.56 REMARK 500 CYS A 463 64.39 60.15 REMARK 500 ASN A 464 56.05 -92.16 REMARK 500 ALA B 18 -151.19 55.56 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-46004 RELATED DB: EMDB REMARK 900 OUTWARD-FACING OATP1B1 BOUND TO SYBODY SB5 DBREF 9CY1 A 1 691 UNP Q9Y6L6 SO1B1_HUMAN 1 691 DBREF 9CY1 B 1 144 PDB 9CY1 9CY1 1 144 SEQADV 9CY1 MET A -25 UNP Q9Y6L6 INITIATING METHIONINE SEQADV 9CY1 HIS A -24 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -23 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -22 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -21 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -20 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -19 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -18 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -17 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -16 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 HIS A -15 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 ASP A -14 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 TYR A -13 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 LYS A -12 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 ASP A -11 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 ASP A -10 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 ASP A -9 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 ASP A -8 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 LYS A -7 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 GLU A -6 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 ASN A -5 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 LEU A -4 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 TYR A -3 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 PHE A -2 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 GLN A -1 UNP Q9Y6L6 EXPRESSION TAG SEQADV 9CY1 GLY A 0 UNP Q9Y6L6 EXPRESSION TAG SEQRES 1 A 717 MET HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS ASP TYR SEQRES 2 A 717 LYS ASP ASP ASP ASP LYS GLU ASN LEU TYR PHE GLN GLY SEQRES 3 A 717 MET ASP GLN ASN GLN HIS LEU ASN LYS THR ALA GLU ALA SEQRES 4 A 717 GLN PRO SER GLU ASN LYS LYS THR ARG TYR CYS ASN GLY SEQRES 5 A 717 LEU LYS MET PHE LEU ALA ALA LEU SER LEU SER PHE ILE SEQRES 6 A 717 ALA LYS THR LEU GLY ALA ILE ILE MET LYS SER SER ILE SEQRES 7 A 717 ILE HIS ILE GLU ARG ARG PHE GLU ILE SER SER SER LEU SEQRES 8 A 717 VAL GLY PHE ILE ASP GLY SER PHE GLU ILE GLY ASN LEU SEQRES 9 A 717 LEU VAL ILE VAL PHE VAL SER TYR PHE GLY SER LYS LEU SEQRES 10 A 717 HIS ARG PRO LYS LEU ILE GLY ILE GLY CYS PHE ILE MET SEQRES 11 A 717 GLY ILE GLY GLY VAL LEU THR ALA LEU PRO HIS PHE PHE SEQRES 12 A 717 MET GLY TYR TYR ARG TYR SER LYS GLU THR ASN ILE ASN SEQRES 13 A 717 SER SER GLU ASN SER THR SER THR LEU SER THR CYS LEU SEQRES 14 A 717 ILE ASN GLN ILE LEU SER LEU ASN ARG ALA SER PRO GLU SEQRES 15 A 717 ILE VAL GLY LYS GLY CYS LEU LYS GLU SER GLY SER TYR SEQRES 16 A 717 MET TRP ILE TYR VAL PHE MET GLY ASN MET LEU ARG GLY SEQRES 17 A 717 ILE GLY GLU THR PRO ILE VAL PRO LEU GLY LEU SER TYR SEQRES 18 A 717 ILE ASP ASP PHE ALA LYS GLU GLY HIS SER SER LEU TYR SEQRES 19 A 717 LEU GLY ILE LEU ASN ALA ILE ALA MET ILE GLY PRO ILE SEQRES 20 A 717 ILE GLY PHE THR LEU GLY SER LEU PHE SER LYS MET TYR SEQRES 21 A 717 VAL ASP ILE GLY TYR VAL ASP LEU SER THR ILE ARG ILE SEQRES 22 A 717 THR PRO THR ASP SER ARG TRP VAL GLY ALA TRP TRP LEU SEQRES 23 A 717 ASN PHE LEU VAL SER GLY LEU PHE SER ILE ILE SER SER SEQRES 24 A 717 ILE PRO PHE PHE PHE LEU PRO GLN THR PRO ASN LYS PRO SEQRES 25 A 717 GLN LYS GLU ARG LYS ALA SER LEU SER LEU HIS VAL LEU SEQRES 26 A 717 GLU THR ASN ASP GLU LYS ASP GLN THR ALA ASN LEU THR SEQRES 27 A 717 ASN GLN GLY LYS ASN ILE THR LYS ASN VAL THR GLY PHE SEQRES 28 A 717 PHE GLN SER PHE LYS SER ILE LEU THR ASN PRO LEU TYR SEQRES 29 A 717 VAL MET PHE VAL LEU LEU THR LEU LEU GLN VAL SER SER SEQRES 30 A 717 TYR ILE GLY ALA PHE THR TYR VAL PHE LYS TYR VAL GLU SEQRES 31 A 717 GLN GLN TYR GLY GLN PRO SER SER LYS ALA ASN ILE LEU SEQRES 32 A 717 LEU GLY VAL ILE THR ILE PRO ILE PHE ALA SER GLY MET SEQRES 33 A 717 PHE LEU GLY GLY TYR ILE ILE LYS LYS PHE LYS LEU ASN SEQRES 34 A 717 THR VAL GLY ILE ALA LYS PHE SER CYS PHE THR ALA VAL SEQRES 35 A 717 MET SER LEU SER PHE TYR LEU LEU TYR PHE PHE ILE LEU SEQRES 36 A 717 CYS GLU ASN LYS SER VAL ALA GLY LEU THR MET THR TYR SEQRES 37 A 717 ASP GLY ASN ASN PRO VAL THR SER HIS ARG ASP VAL PRO SEQRES 38 A 717 LEU SER TYR CYS ASN SER ASP CYS ASN CYS ASP GLU SER SEQRES 39 A 717 GLN TRP GLU PRO VAL CYS GLY ASN ASN GLY ILE THR TYR SEQRES 40 A 717 ILE SER PRO CYS LEU ALA GLY CYS LYS SER SER SER GLY SEQRES 41 A 717 ASN LYS LYS PRO ILE VAL PHE TYR ASN CYS SER CYS LEU SEQRES 42 A 717 GLU VAL THR GLY LEU GLN ASN ARG ASN TYR SER ALA HIS SEQRES 43 A 717 LEU GLY GLU CYS PRO ARG ASP ASP ALA CYS THR ARG LYS SEQRES 44 A 717 PHE TYR PHE PHE VAL ALA ILE GLN VAL LEU ASN LEU PHE SEQRES 45 A 717 PHE SER ALA LEU GLY GLY THR SER HIS VAL MET LEU ILE SEQRES 46 A 717 VAL LYS ILE VAL GLN PRO GLU LEU LYS SER LEU ALA LEU SEQRES 47 A 717 GLY PHE HIS SER MET VAL ILE ARG ALA LEU GLY GLY ILE SEQRES 48 A 717 LEU ALA PRO ILE TYR PHE GLY ALA LEU ILE ASP THR THR SEQRES 49 A 717 CYS ILE LYS TRP SER THR ASN ASN CYS GLY THR ARG GLY SEQRES 50 A 717 SER CYS ARG THR TYR ASN SER THR SER PHE SER ARG VAL SEQRES 51 A 717 TYR LEU GLY LEU SER SER MET LEU ARG VAL SER SER LEU SEQRES 52 A 717 VAL LEU TYR ILE ILE LEU ILE TYR ALA MET LYS LYS LYS SEQRES 53 A 717 TYR GLN GLU LYS ASP ILE ASN ALA SER GLU ASN GLY SER SEQRES 54 A 717 VAL MET ASP GLU ALA ASN LEU GLU SER LEU ASN LYS ASN SEQRES 55 A 717 LYS HIS PHE VAL PRO SER ALA GLY ALA ASP SER GLU THR SEQRES 56 A 717 HIS CYS SEQRES 1 B 144 GLY SER SER SER GLN VAL GLN LEU VAL GLU SER GLY GLY SEQRES 2 B 144 GLY LEU VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS SEQRES 3 B 144 ALA ALA SER GLY PHE PRO VAL ASN LEU SER TYR MET HIS SEQRES 4 B 144 TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL SEQRES 5 B 144 ALA ALA ILE SER SER TRP GLY TRP HIS THR GLU TYR ALA SEQRES 6 B 144 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7 B 144 ALA LYS ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS SEQRES 8 B 144 PRO GLU ASP THR ALA VAL TYR TYR CYS HIS VAL ARG VAL SEQRES 9 B 144 GLY ARG SER TYR PHE GLY GLN GLY THR GLN VAL SER VAL SEQRES 10 B 144 SER ALA GLY ARG ALA GLY GLU GLN LYS LEU ILE SER GLU SEQRES 11 B 144 GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS SEQRES 12 B 144 HIS HELIX 1 AA1 GLY A 26 SER A 51 1 26 HELIX 2 AA2 SER A 51 GLU A 60 1 10 HELIX 3 AA3 SER A 62 GLY A 88 1 27 HELIX 4 AA4 HIS A 92 PHE A 117 1 26 HELIX 5 AA5 MET A 170 GLU A 185 1 16 HELIX 6 AA6 ILE A 188 ALA A 200 1 13 HELIX 7 AA7 HIS A 204 ALA A 216 1 13 HELIX 8 AA8 MET A 217 LYS A 232 1 16 HELIX 9 AA9 ALA A 257 ILE A 274 1 18 HELIX 10 AB1 PRO A 275 LEU A 279 5 5 HELIX 11 AB2 PHE A 325 THR A 334 1 10 HELIX 12 AB3 ASN A 335 TYR A 367 1 33 HELIX 13 AB4 ILE A 381 LYS A 401 1 21 HELIX 14 AB5 ASN A 403 LEU A 423 1 21 HELIX 15 AB6 LEU A 424 PHE A 427 5 4 HELIX 16 AB7 SER A 457 SER A 461 5 5 HELIX 17 AB8 ASP A 527 GLY A 551 1 25 HELIX 18 AB9 GLY A 551 VAL A 563 1 13 HELIX 19 AC1 GLN A 564 GLU A 566 5 3 HELIX 20 AC2 LEU A 567 GLY A 583 1 17 HELIX 21 AC3 ILE A 585 ASP A 596 1 12 HELIX 22 AC4 ASN A 617 TYR A 651 1 35 HELIX 23 AC5 LYS B 91 THR B 95 5 5 SHEET 1 AA1 4 VAL A 435 ALA A 436 0 SHEET 2 AA1 4 THR A 480 TYR A 481 1 O THR A 480 N ALA A 436 SHEET 3 AA1 4 VAL A 473 CYS A 474 -1 N VAL A 473 O TYR A 481 SHEET 4 AA1 4 HIS A 520 LEU A 521 -1 O HIS A 520 N CYS A 474 SHEET 1 AA2 2 CYS A 489 SER A 491 0 SHEET 2 AA2 2 TYR A 502 CYS A 504 -1 O TYR A 502 N SER A 491 SHEET 1 AA3 2 CYS A 599 TRP A 602 0 SHEET 2 AA3 2 CYS A 613 TYR A 616 -1 O THR A 615 N ILE A 600 SHEET 1 AA4 4 GLN B 7 SER B 11 0 SHEET 2 AA4 4 SER B 21 SER B 29 -1 O SER B 29 N GLN B 7 SHEET 3 AA4 4 THR B 82 ASN B 88 -1 O MET B 87 N LEU B 22 SHEET 4 AA4 4 PHE B 72 ASP B 77 -1 N THR B 73 O GLN B 86 SHEET 1 AA5 2 VAL B 16 GLN B 17 0 SHEET 2 AA5 2 VAL B 117 SER B 118 1 O SER B 118 N VAL B 16 SHEET 1 AA6 5 THR B 62 TYR B 64 0 SHEET 2 AA6 5 ARG B 49 ILE B 55 -1 N ALA B 54 O GLU B 63 SHEET 3 AA6 5 MET B 38 GLN B 43 -1 N ARG B 42 O GLU B 50 SHEET 4 AA6 5 VAL B 97 VAL B 102 -1 O TYR B 99 N TYR B 41 SHEET 5 AA6 5 TYR B 108 PHE B 109 -1 O TYR B 108 N VAL B 102 SHEET 1 AA7 5 THR B 62 TYR B 64 0 SHEET 2 AA7 5 ARG B 49 ILE B 55 -1 N ALA B 54 O GLU B 63 SHEET 3 AA7 5 MET B 38 GLN B 43 -1 N ARG B 42 O GLU B 50 SHEET 4 AA7 5 VAL B 97 VAL B 102 -1 O TYR B 99 N TYR B 41 SHEET 5 AA7 5 THR B 113 GLN B 114 -1 O THR B 113 N TYR B 98 SSBOND 1 CYS A 430 CYS A 530 1555 1555 2.04 SSBOND 2 CYS A 459 CYS A 506 1555 1555 2.03 SSBOND 3 CYS A 465 CYS A 485 1555 1555 2.03 SSBOND 4 CYS A 474 CYS A 524 1555 1555 2.03 SSBOND 5 CYS A 489 CYS A 504 1555 1555 2.03 SSBOND 6 CYS A 599 CYS A 613 1555 1555 2.03 SSBOND 7 CYS B 26 CYS B 100 1555 1555 2.03 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000