HEADER MEMBRANE PROTEIN 14-DEC-23 8XFS TITLE LGR4-RSPO2-ZNRF3 RING DOMAIN (1:2:2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN COUPLED RECEPTOR COMPND 3 4; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: G-PROTEIN COUPLED RECEPTOR 48; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE ZNRF3; COMPND 9 CHAIN: C, E; COMPND 10 SYNONYM: RING FINGER PROTEIN 203,RING-TYPE E3 UBIQUITIN TRANSFERASE COMPND 11 ZNRF3,ZINC/RING FINGER PROTEIN 3; COMPND 12 EC: 2.3.2.27; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: NANOBODY NB52; COMPND 16 CHAIN: F; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: R-SPONDIN-2; COMPND 20 CHAIN: B, D; COMPND 21 SYNONYM: CYSTEINE-RICH AND SINGLE THROMBOSPONDIN DOMAIN-CONTAINING COMPND 22 PROTEIN 2,CRISTIN-2,MCRISTIN-2,ROOF PLATE-SPECIFIC SPONDIN-2; COMPND 23 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: LGR4, GPR48; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: ZNRF3, KIAA1133, RNF203; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: CAMELUS BACTRIANUS; SOURCE 17 ORGANISM_TAXID: 9837; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 GENE: RSPO2; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS LGR4, ZNRF3 RING DOMAIN, 1:2:2, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR W.LU,G.YONG REVDAT 1 04-DEC-24 8XFS 0 JRNL AUTH W.LU JRNL TITL LGR4-RSPO2-ZNRF3 RING DOMAIN (1:2:2) JRNL REF TO BE PUBLISHED JRNL REFN 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 : 61066 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8XFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300043399. 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 : THE PENTAMER B COMPLEX OF LGR4 REMARK 245 -RSPO2-ZNRF3(RING) 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 : FEI TECNAI 20 REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 194.40 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, F, B, E, D 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 A 478 REMARK 465 TYR A 479 REMARK 465 ALA A 480 REMARK 465 ASN A 481 REMARK 465 LEU A 482 REMARK 465 ASN A 483 REMARK 465 THR A 484 REMARK 465 GLU A 485 REMARK 465 ASP A 486 REMARK 465 ASN A 487 REMARK 465 SER A 488 REMARK 465 LEU A 489 REMARK 465 GLN A 490 REMARK 465 ASP A 491 REMARK 465 HIS A 492 REMARK 465 SER A 493 REMARK 465 VAL A 494 REMARK 465 ALA A 495 REMARK 465 GLN A 496 REMARK 465 GLU A 497 REMARK 465 LYS A 498 REMARK 465 GLY A 499 REMARK 465 THR A 500 REMARK 465 ALA A 501 REMARK 465 ASP A 502 REMARK 465 ALA A 503 REMARK 465 ALA A 504 REMARK 465 ASN A 505 REMARK 465 VAL A 506 REMARK 465 THR A 507 REMARK 465 SER A 508 REMARK 465 THR A 509 REMARK 465 LEU A 510 REMARK 465 GLU A 511 REMARK 465 ASN A 512 REMARK 465 GLU A 513 REMARK 465 GLU A 514 REMARK 465 HIS A 515 REMARK 465 SER A 516 REMARK 465 GLN A 517 REMARK 465 ILE A 650 REMARK 465 MET A 651 REMARK 465 LYS A 652 REMARK 465 ASN A 653 REMARK 465 GLY A 654 REMARK 465 LYS A 655 REMARK 465 SER A 656 REMARK 465 GLU A 733 REMARK 465 LYS A 734 REMARK 465 GLU A 735 REMARK 465 ASP A 736 REMARK 465 LEU A 737 REMARK 465 SER A 738 REMARK 465 GLU A 739 REMARK 465 ASN A 740 REMARK 465 LYS C 241 REMARK 465 LEU C 242 REMARK 465 LYS C 243 REMARK 465 GLN C 244 REMARK 465 ARG C 245 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 ASP A 477 CG OD1 OD2 REMARK 470 LYS A 530 CG CD CE NZ REMARK 470 GLU A 533 CG CD OE1 OE2 REMARK 470 MET A 721 CG SD CE REMARK 470 LYS A 816 CG CD CE NZ REMARK 470 ASN C 110 CG OD1 ND2 REMARK 470 ARG C 211 CG CD NE CZ NH1 NH2 REMARK 470 GLN C 212 CG CD OE1 NE2 REMARK 470 THR C 214 OG1 CG2 REMARK 470 GLU C 215 CG CD OE1 OE2 REMARK 470 TYR C 216 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE C 217 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 54 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 57 CG CD OE1 NE2 REMARK 470 ASP B 130 CG OD1 OD2 REMARK 470 GLU B 137 CG CD OE1 OE2 REMARK 470 ARG E 208 CG CD NE CZ NH1 NH2 REMARK 470 ARG E 211 CG CD NE CZ NH1 NH2 REMARK 470 GLN E 212 CG CD OE1 NE2 REMARK 470 GLU E 215 CG CD OE1 OE2 REMARK 470 CYS D 43 SG REMARK 470 ARG D 54 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 57 CG CD OE1 NE2 REMARK 470 CYS D 124 SG REMARK 470 ASP D 130 CG OD1 OD2 REMARK 470 GLU D 137 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 OE1 GLN A 113 OG SER B 77 2.19 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 38 52.10 -92.36 REMARK 500 ARG A 39 41.42 39.56 REMARK 500 LYS A 99 51.36 -92.52 REMARK 500 LEU A 101 49.83 39.39 REMARK 500 SER A 164 56.14 -96.38 REMARK 500 LYS A 212 53.38 -91.87 REMARK 500 PHE A 221 51.94 -94.14 REMARK 500 LEU A 224 57.06 -92.04 REMARK 500 ASN A 226 -0.12 66.64 REMARK 500 THR A 329 -168.58 -163.34 REMARK 500 GLN A 340 -5.51 71.57 REMARK 500 LEU A 345 59.15 38.77 REMARK 500 ASN A 354 52.02 -93.43 REMARK 500 PHE A 361 59.09 -91.11 REMARK 500 CYS A 364 58.08 39.50 REMARK 500 LEU A 400 49.45 -91.23 REMARK 500 GLU A 424 51.61 -93.17 REMARK 500 ARG A 684 -7.75 71.71 REMARK 500 THR A 698 65.78 39.49 REMARK 500 GLU C 112 145.58 68.81 REMARK 500 ALA C 153 147.68 -170.65 REMARK 500 GLN C 212 -79.03 100.66 REMARK 500 GLU C 215 -123.33 58.03 REMARK 500 TYR C 216 -144.07 56.21 REMARK 500 PHE C 217 -96.40 55.16 REMARK 500 THR F 524 -31.48 -130.35 REMARK 500 PHE B 109 118.82 -160.11 REMARK 500 ARG B 121 -53.56 -120.36 REMARK 500 SER E 71 50.35 -92.15 REMARK 500 GLU E 215 -1.07 78.37 REMARK 500 PRO D 79 -177.10 -68.48 REMARK 500 PRO D 134 -179.95 -68.69 REMARK 500 MET D 139 -1.11 66.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38308 RELATED DB: EMDB REMARK 900 LGR4-RSPO2-ZNRF3 RING DOMAIN (1:2:2) DBREF 8XFS A 31 821 UNP Q9BXB1 LGR4_HUMAN 31 821 DBREF 8XFS C 56 245 UNP Q9ULT6 ZNRF3_HUMAN 56 245 DBREF 8XFS F 442 547 PDB 8XFS 8XFS 442 547 DBREF 8XFS B 41 141 UNP Q8BFU0 RSPO2_MOUSE 41 141 DBREF 8XFS E 56 245 UNP Q9ULT6 ZNRF3_HUMAN 56 245 DBREF 8XFS D 41 141 UNP Q8BFU0 RSPO2_MOUSE 41 141 SEQADV 8XFS ALA A 78 UNP Q9BXB1 LYS 78 CONFLICT SEQRES 1 A 791 ALA PRO CYS SER CYS ASP GLY ASP ARG ARG VAL ASP CYS SEQRES 2 A 791 SER GLY LYS GLY LEU THR ALA VAL PRO GLU GLY LEU SER SEQRES 3 A 791 ALA PHE THR GLN ALA LEU ASP ILE SER MET ASN ASN ILE SEQRES 4 A 791 THR GLN LEU PRO GLU ASP ALA PHE ALA ASN PHE PRO PHE SEQRES 5 A 791 LEU GLU GLU LEU GLN LEU ALA GLY ASN ASP LEU SER PHE SEQRES 6 A 791 ILE HIS PRO LYS ALA LEU SER GLY LEU LYS GLU LEU LYS SEQRES 7 A 791 VAL LEU THR LEU GLN ASN ASN GLN LEU LYS THR VAL PRO SEQRES 8 A 791 SER GLU ALA ILE ARG GLY LEU SER ALA LEU GLN SER LEU SEQRES 9 A 791 ARG LEU ASP ALA ASN HIS ILE THR SER VAL PRO GLU ASP SEQRES 10 A 791 SER PHE GLU GLY LEU VAL GLN LEU ARG HIS LEU TRP LEU SEQRES 11 A 791 ASP ASP ASN SER LEU THR GLU VAL PRO VAL HIS PRO LEU SEQRES 12 A 791 SER ASN LEU PRO THR LEU GLN ALA LEU THR LEU ALA LEU SEQRES 13 A 791 ASN LYS ILE SER SER ILE PRO ASP PHE ALA PHE THR ASN SEQRES 14 A 791 LEU SER SER LEU VAL VAL LEU HIS LEU HIS ASN ASN LYS SEQRES 15 A 791 ILE ARG SER LEU SER GLN HIS CYS PHE ASP GLY LEU ASP SEQRES 16 A 791 ASN LEU GLU THR LEU ASP LEU ASN TYR ASN ASN LEU GLY SEQRES 17 A 791 GLU PHE PRO GLN ALA ILE LYS ALA LEU PRO SER LEU LYS SEQRES 18 A 791 GLU LEU GLY PHE HIS SER ASN SER ILE SER VAL ILE PRO SEQRES 19 A 791 ASP GLY ALA PHE ASP GLY ASN PRO LEU LEU ARG THR ILE SEQRES 20 A 791 HIS LEU TYR ASP ASN PRO LEU SER PHE VAL GLY ASN SER SEQRES 21 A 791 ALA PHE HIS ASN LEU SER ASP LEU HIS SER LEU VAL ILE SEQRES 22 A 791 ARG GLY ALA SER MET VAL GLN GLN PHE PRO ASN LEU THR SEQRES 23 A 791 GLY THR VAL HIS LEU GLU SER LEU THR LEU THR GLY THR SEQRES 24 A 791 LYS ILE SER SER ILE PRO ASN ASN LEU CYS GLN GLU GLN SEQRES 25 A 791 LYS MET LEU ARG THR LEU ASP LEU SER TYR ASN ASN ILE SEQRES 26 A 791 ARG ASP LEU PRO SER PHE ASN GLY CYS HIS ALA LEU GLU SEQRES 27 A 791 GLU ILE SER LEU GLN ARG ASN GLN ILE TYR GLN ILE LYS SEQRES 28 A 791 GLU GLY THR PHE GLN GLY LEU ILE SER LEU ARG ILE LEU SEQRES 29 A 791 ASP LEU SER ARG ASN LEU ILE HIS GLU ILE HIS SER ARG SEQRES 30 A 791 ALA PHE ALA THR LEU GLY PRO ILE THR ASN LEU ASP VAL SEQRES 31 A 791 SER PHE ASN GLU LEU THR SER PHE PRO THR GLU GLY LEU SEQRES 32 A 791 ASN GLY LEU ASN GLN LEU LYS LEU VAL GLY ASN PHE LYS SEQRES 33 A 791 LEU LYS GLU ALA LEU ALA ALA LYS ASP PHE VAL ASN LEU SEQRES 34 A 791 ARG SER LEU SER VAL PRO TYR ALA TYR GLN CYS CYS ALA SEQRES 35 A 791 PHE TRP GLY CYS ASP SER TYR ALA ASN LEU ASN THR GLU SEQRES 36 A 791 ASP ASN SER LEU GLN ASP HIS SER VAL ALA GLN GLU LYS SEQRES 37 A 791 GLY THR ALA ASP ALA ALA ASN VAL THR SER THR LEU GLU SEQRES 38 A 791 ASN GLU GLU HIS SER GLN ILE ILE ILE HIS CYS THR PRO SEQRES 39 A 791 SER THR GLY ALA PHE LYS PRO CYS GLU TYR LEU LEU GLY SEQRES 40 A 791 SER TRP MET ILE ARG LEU THR VAL TRP PHE ILE PHE LEU SEQRES 41 A 791 VAL ALA LEU PHE PHE ASN LEU LEU VAL ILE LEU THR THR SEQRES 42 A 791 PHE ALA SER CYS THR SER LEU PRO SER SER LYS LEU PHE SEQRES 43 A 791 ILE GLY LEU ILE SER VAL SER ASN LEU PHE MET GLY ILE SEQRES 44 A 791 TYR THR GLY ILE LEU THR PHE LEU ASP ALA VAL SER TRP SEQRES 45 A 791 GLY ARG PHE ALA GLU PHE GLY ILE TRP TRP GLU THR GLY SEQRES 46 A 791 SER GLY CYS LYS VAL ALA GLY PHE LEU ALA VAL PHE SER SEQRES 47 A 791 SER GLU SER ALA ILE PHE LEU LEU MET LEU ALA THR VAL SEQRES 48 A 791 GLU ARG SER LEU SER ALA LYS ASP ILE MET LYS ASN GLY SEQRES 49 A 791 LYS SER ASN HIS LEU LYS GLN PHE ARG VAL ALA ALA LEU SEQRES 50 A 791 LEU ALA PHE LEU GLY ALA THR VAL ALA GLY CYS PHE PRO SEQRES 51 A 791 LEU PHE HIS ARG GLY GLU TYR SER ALA SER PRO LEU CYS SEQRES 52 A 791 LEU PRO PHE PRO THR GLY GLU THR PRO SER LEU GLY PHE SEQRES 53 A 791 THR VAL THR LEU VAL LEU LEU ASN SER LEU ALA PHE LEU SEQRES 54 A 791 LEU MET ALA VAL ILE TYR THR LYS LEU TYR CYS ASN LEU SEQRES 55 A 791 GLU LYS GLU ASP LEU SER GLU ASN SER GLN SER SER MET SEQRES 56 A 791 ILE LYS HIS VAL ALA TRP LEU ILE PHE THR ASN CYS ILE SEQRES 57 A 791 PHE PHE CYS PRO VAL ALA PHE PHE SER PHE ALA PRO LEU SEQRES 58 A 791 ILE THR ALA ILE SER ILE SER PRO GLU ILE MET LYS SER SEQRES 59 A 791 VAL THR LEU ILE PHE PHE PRO LEU PRO ALA CYS LEU ASN SEQRES 60 A 791 PRO VAL LEU TYR VAL PHE PHE ASN PRO LYS PHE LYS GLU SEQRES 61 A 791 ASP TRP LYS LEU LEU LYS ARG ARG VAL THR LYS SEQRES 1 C 190 LYS GLU THR ALA PHE VAL GLU VAL VAL LEU PHE GLU SER SEQRES 2 C 190 SER PRO SER GLY ASP TYR THR THR TYR THR THR GLY LEU SEQRES 3 C 190 THR GLY ARG PHE SER ARG ALA GLY ALA THR LEU SER ALA SEQRES 4 C 190 GLU GLY GLU ILE VAL GLN MET HIS PRO LEU GLY LEU CYS SEQRES 5 C 190 ASN ASN ASN ASP GLU GLU ASP LEU TYR GLU TYR GLY TRP SEQRES 6 C 190 VAL GLY VAL VAL LYS LEU GLU GLN PRO GLU LEU ASP PRO SEQRES 7 C 190 LYS PRO CYS LEU THR VAL LEU GLY LYS ALA LYS ARG ALA SEQRES 8 C 190 VAL GLN ARG GLY ALA THR ALA VAL ILE PHE ASP VAL SER SEQRES 9 C 190 GLU ASN PRO GLU ALA ILE ASP GLN LEU ASN GLN GLY SER SEQRES 10 C 190 GLU ASP PRO LEU LYS ARG PRO VAL VAL TYR VAL LYS GLY SEQRES 11 C 190 ALA ASP ALA ILE LYS LEU MET ASN ILE VAL ASN LYS GLN SEQRES 12 C 190 LYS VAL ALA ARG ALA ARG ILE GLN HIS ARG PRO PRO ARG SEQRES 13 C 190 GLN PRO THR GLU TYR PHE ASP MET GLY ILE PHE LEU ALA SEQRES 14 C 190 PHE PHE VAL VAL VAL SER LEU VAL CYS LEU ILE LEU LEU SEQRES 15 C 190 VAL LYS ILE LYS LEU LYS GLN ARG SEQRES 1 F 106 SER LEU ARG LEU SER CYS ALA ALA SER GLY TYR THR TYR SEQRES 2 F 106 SER PRO TYR CYS MET GLY TRP PHE ARG GLN ALA PRO GLY SEQRES 3 F 106 LYS ALA ARG GLU GLY VAL ALA THR VAL ASP LEU ASP GLY SEQRES 4 F 106 SER THR ILE TYR ALA ASP SER VAL LYS GLY ARG PHE THR SEQRES 5 F 106 ILE SER GLN ASP ASN ALA LYS ASN THR LEU TYR LEU GLN SEQRES 6 F 106 MET ASN SER LEU LYS PRO GLU ASP THR ALA MET TYR TYR SEQRES 7 F 106 CYS ALA SER ARG THR ARG ALA GLY VAL THR CYS GLY LEU SEQRES 8 F 106 ASN TRP ALA ILE PHE SER TYR TRP GLY GLN GLY THR GLN SEQRES 9 F 106 VAL THR SEQRES 1 B 101 LYS GLY CYS LEU SER CYS SER LYS ASP ASN GLY CYS SER SEQRES 2 B 101 ARG CYS GLN GLN LYS LEU PHE PHE PHE LEU ARG ARG GLU SEQRES 3 B 101 GLY MET ARG GLN TYR GLY GLU CYS LEU HIS SER CYS PRO SEQRES 4 B 101 SER GLY TYR TYR GLY HIS ARG ALA PRO ASP MET ASN ARG SEQRES 5 B 101 CYS ALA ARG CYS ARG ILE GLU ASN CYS ASP SER CYS PHE SEQRES 6 B 101 SER LYS ASP PHE CYS THR LYS CYS LYS VAL GLY PHE TYR SEQRES 7 B 101 LEU HIS ARG GLY ARG CYS PHE ASP GLU CYS PRO ASP GLY SEQRES 8 B 101 PHE ALA PRO LEU ASP GLU THR MET GLU CYS SEQRES 1 E 190 LYS GLU THR ALA PHE VAL GLU VAL VAL LEU PHE GLU SER SEQRES 2 E 190 SER PRO SER GLY ASP TYR THR THR TYR THR THR GLY LEU SEQRES 3 E 190 THR GLY ARG PHE SER ARG ALA GLY ALA THR LEU SER ALA SEQRES 4 E 190 GLU GLY GLU ILE VAL GLN MET HIS PRO LEU GLY LEU CYS SEQRES 5 E 190 ASN ASN ASN ASP GLU GLU ASP LEU TYR GLU TYR GLY TRP SEQRES 6 E 190 VAL GLY VAL VAL LYS LEU GLU GLN PRO GLU LEU ASP PRO SEQRES 7 E 190 LYS PRO CYS LEU THR VAL LEU GLY LYS ALA LYS ARG ALA SEQRES 8 E 190 VAL GLN ARG GLY ALA THR ALA VAL ILE PHE ASP VAL SER SEQRES 9 E 190 GLU ASN PRO GLU ALA ILE ASP GLN LEU ASN GLN GLY SER SEQRES 10 E 190 GLU ASP PRO LEU LYS ARG PRO VAL VAL TYR VAL LYS GLY SEQRES 11 E 190 ALA ASP ALA ILE LYS LEU MET ASN ILE VAL ASN LYS GLN SEQRES 12 E 190 LYS VAL ALA ARG ALA ARG ILE GLN HIS ARG PRO PRO ARG SEQRES 13 E 190 GLN PRO THR GLU TYR PHE ASP MET GLY ILE PHE LEU ALA SEQRES 14 E 190 PHE PHE VAL VAL VAL SER LEU VAL CYS LEU ILE LEU LEU SEQRES 15 E 190 VAL LYS ILE LYS LEU LYS GLN ARG SEQRES 1 D 101 LYS GLY CYS LEU SER CYS SER LYS ASP ASN GLY CYS SER SEQRES 2 D 101 ARG CYS GLN GLN LYS LEU PHE PHE PHE LEU ARG ARG GLU SEQRES 3 D 101 GLY MET ARG GLN TYR GLY GLU CYS LEU HIS SER CYS PRO SEQRES 4 D 101 SER GLY TYR TYR GLY HIS ARG ALA PRO ASP MET ASN ARG SEQRES 5 D 101 CYS ALA ARG CYS ARG ILE GLU ASN CYS ASP SER CYS PHE SEQRES 6 D 101 SER LYS ASP PHE CYS THR LYS CYS LYS VAL GLY PHE TYR SEQRES 7 D 101 LEU HIS ARG GLY ARG CYS PHE ASP GLU CYS PRO ASP GLY SEQRES 8 D 101 PHE ALA PRO LEU ASP GLU THR MET GLU CYS HELIX 1 AA1 PRO A 121 ARG A 126 1 6 HELIX 2 AA2 PRO A 169 SER A 174 1 6 HELIX 3 AA3 GLN A 242 LEU A 247 5 6 HELIX 4 AA4 LYS A 381 GLN A 386 5 6 HELIX 5 AA5 TYR A 466 ALA A 472 1 7 HELIX 6 AA6 SER A 538 ALA A 565 1 28 HELIX 7 AA7 PRO A 571 SER A 601 1 31 HELIX 8 AA8 ARG A 604 GLU A 613 1 10 HELIX 9 AA9 GLY A 615 ASP A 649 1 35 HELIX 10 AB1 HIS A 658 HIS A 683 1 26 HELIX 11 AB2 PHE A 706 LEU A 732 1 27 HELIX 12 AB3 GLN A 742 PHE A 768 1 27 HELIX 13 AB4 SER A 778 PHE A 790 1 13 HELIX 14 AB5 PRO A 791 ASN A 805 1 15 HELIX 15 AB6 ASN A 805 LYS A 821 1 17 HELIX 16 AB7 GLN C 128 ASP C 132 5 5 HELIX 17 AB8 THR C 138 GLY C 150 1 13 HELIX 18 AB9 ASN C 161 GLY C 171 1 11 HELIX 19 AC1 LYS C 184 GLN C 198 1 15 HELIX 20 AC2 PHE C 217 ILE C 240 1 24 HELIX 21 AC3 ASP F 486 LYS F 489 5 4 HELIX 22 AC4 LYS F 511 THR F 515 5 5 HELIX 23 AC5 ASN F 533 PHE F 537 5 5 HELIX 24 AC6 HIS E 102 LEU E 106 5 5 HELIX 25 AC7 GLN E 128 ASP E 132 5 5 HELIX 26 AC8 THR E 138 GLY E 150 1 13 HELIX 27 AC9 ASN E 161 GLY E 171 1 11 HELIX 28 AD1 GLY E 185 GLN E 198 1 14 HELIX 29 AD2 PHE E 217 ARG E 245 1 29 SHEET 1 AA111 VAL A 41 ASP A 42 0 SHEET 2 AA111 ALA A 61 ASP A 63 1 O ALA A 61 N VAL A 41 SHEET 3 AA111 GLU A 85 GLN A 87 1 O GLU A 85 N LEU A 62 SHEET 4 AA111 VAL A 109 THR A 111 1 O VAL A 109 N LEU A 86 SHEET 5 AA111 SER A 133 ARG A 135 1 O SER A 133 N LEU A 110 SHEET 6 AA111 LEU A 158 TRP A 159 1 O TRP A 159 N LEU A 134 SHEET 7 AA111 ALA A 181 THR A 183 1 O ALA A 181 N LEU A 158 SHEET 8 AA111 VAL A 205 HIS A 207 1 O VAL A 205 N LEU A 182 SHEET 9 AA111 THR A 229 ASP A 231 1 O THR A 229 N LEU A 206 SHEET 10 AA111 GLU A 252 PHE A 255 1 O GLU A 252 N LEU A 230 SHEET 11 AA111 THR A 276 LEU A 279 1 O HIS A 278 N LEU A 253 SHEET 1 AA2 2 GLN A 71 LEU A 72 0 SHEET 2 AA2 2 PHE A 95 ILE A 96 1 O PHE A 95 N LEU A 72 SHEET 1 AA3 2 SER A 191 ILE A 192 0 SHEET 2 AA3 2 SER A 215 LEU A 216 1 O SER A 215 N ILE A 192 SHEET 1 AA4 9 SER A 300 ILE A 303 0 SHEET 2 AA4 9 SER A 323 LEU A 326 1 O THR A 325 N ILE A 303 SHEET 3 AA4 9 THR A 347 LEU A 350 1 O ASP A 349 N LEU A 326 SHEET 4 AA4 9 GLU A 369 LEU A 372 1 O SER A 371 N LEU A 350 SHEET 5 AA4 9 ILE A 393 LEU A 396 1 O ASP A 395 N LEU A 372 SHEET 6 AA4 9 ASN A 417 VAL A 420 1 O ASP A 419 N LEU A 396 SHEET 7 AA4 9 GLN A 438 LYS A 440 1 O GLN A 438 N LEU A 418 SHEET 8 AA4 9 SER A 461 SER A 463 1 O SER A 461 N LEU A 439 SHEET 9 AA4 9 HIS A 521 CYS A 522 1 O HIS A 521 N LEU A 462 SHEET 1 AA5 8 TYR C 74 THR C 82 0 SHEET 2 AA5 8 PHE C 60 SER C 68 -1 N LEU C 65 O TYR C 77 SHEET 3 AA5 8 ARG C 202 GLN C 206 -1 O GLN C 206 N PHE C 60 SHEET 4 AA5 8 ALA C 94 MET C 101 -1 N GLY C 96 O ALA C 203 SHEET 5 AA5 8 TRP C 120 LYS C 125 1 O VAL C 121 N VAL C 99 SHEET 6 AA5 8 ALA C 151 ASP C 157 1 O ILE C 155 N GLY C 122 SHEET 7 AA5 8 VAL C 180 VAL C 183 1 O VAL C 181 N VAL C 154 SHEET 8 AA5 8 ARG C 84 PHE C 85 -1 N ARG C 84 O TYR C 182 SHEET 1 AA6 3 LEU F 443 ALA F 448 0 SHEET 2 AA6 3 THR F 502 MET F 507 -1 O MET F 507 N LEU F 443 SHEET 3 AA6 3 THR F 493 ASP F 497 -1 N THR F 493 O GLN F 506 SHEET 1 AA7 5 ILE F 483 TYR F 484 0 SHEET 2 AA7 5 ARG F 470 THR F 475 -1 N THR F 475 O ILE F 483 SHEET 3 AA7 5 TYR F 457 GLN F 464 -1 N TRP F 461 O VAL F 473 SHEET 4 AA7 5 ALA F 516 ARG F 523 -1 O MET F 517 N GLN F 464 SHEET 5 AA7 5 TYR F 539 TRP F 540 -1 O TYR F 539 N SER F 522 SHEET 1 AA8 5 ILE F 483 TYR F 484 0 SHEET 2 AA8 5 ARG F 470 THR F 475 -1 N THR F 475 O ILE F 483 SHEET 3 AA8 5 TYR F 457 GLN F 464 -1 N TRP F 461 O VAL F 473 SHEET 4 AA8 5 ALA F 516 ARG F 523 -1 O MET F 517 N GLN F 464 SHEET 5 AA8 5 THR F 544 VAL F 546 -1 O VAL F 546 N ALA F 516 SHEET 1 AA9 2 PHE B 60 GLU B 66 0 SHEET 2 AA9 2 ARG B 69 LEU B 75 -1 O GLU B 73 N PHE B 62 SHEET 1 AB1 2 TYR B 82 HIS B 85 0 SHEET 2 AB1 2 ARG B 92 ARG B 95 -1 O ALA B 94 N TYR B 83 SHEET 1 AB2 2 CYS B 101 SER B 106 0 SHEET 2 AB2 2 PHE B 109 CYS B 113 -1 O PHE B 109 N SER B 106 SHEET 1 AB3 2 TYR B 118 LEU B 119 0 SHEET 2 AB3 2 CYS B 124 PHE B 125 -1 O PHE B 125 N TYR B 118 SHEET 1 AB4 8 THR E 58 SER E 69 0 SHEET 2 AB4 8 ASP E 73 PHE E 85 -1 O TYR E 77 N LEU E 65 SHEET 3 AB4 8 VAL E 180 VAL E 183 -1 O TYR E 182 N ARG E 84 SHEET 4 AB4 8 ALA E 151 ASP E 157 1 N PHE E 156 O VAL E 183 SHEET 5 AB4 8 TRP E 120 LYS E 125 1 N GLY E 122 O ILE E 155 SHEET 6 AB4 8 ALA E 94 GLN E 100 1 N VAL E 99 O VAL E 121 SHEET 7 AB4 8 ALA E 203 GLN E 206 -1 O ILE E 205 N ALA E 94 SHEET 8 AB4 8 THR E 58 SER E 69 -1 N GLU E 62 O ARG E 204 SHEET 1 AB5 2 PHE D 60 GLU D 66 0 SHEET 2 AB5 2 ARG D 69 LEU D 75 -1 O GLU D 73 N PHE D 62 SHEET 1 AB6 2 TYR D 82 ARG D 86 0 SHEET 2 AB6 2 ASN D 91 ARG D 95 -1 O ARG D 92 N HIS D 85 SSBOND 1 CYS A 339 CYS A 364 1555 1555 2.04 SSBOND 2 CYS A 470 CYS A 522 1555 1555 2.03 SSBOND 3 CYS A 471 CYS A 532 1555 1555 2.03 SSBOND 4 CYS F 447 CYS F 520 1555 1555 2.03 SSBOND 5 CYS B 55 CYS B 74 1555 1555 2.02 SSBOND 6 CYS B 78 CYS B 93 1555 1555 2.03 SSBOND 7 CYS B 96 CYS B 104 1555 1555 2.03 SSBOND 8 CYS B 101 CYS B 110 1555 1555 2.03 SSBOND 9 CYS B 113 CYS B 124 1555 1555 2.03 SSBOND 10 CYS B 128 CYS B 141 1555 1555 2.03 SSBOND 11 CYS D 55 CYS D 74 1555 1555 2.03 SSBOND 12 CYS D 78 CYS D 93 1555 1555 2.03 SSBOND 13 CYS D 96 CYS D 104 1555 1555 2.03 SSBOND 14 CYS D 128 CYS D 141 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