HEADER LIPID TRANSPORT 17-OCT-23 8QV6 TITLE STRUCTURE OF HUMAN SPNS2 IN DDM COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPHINGOSINE-1-PHOSPHATE TRANSPORTER SPNS2; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY D12; COMPND 7 CHAIN: B; COMPND 8 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: SPNS2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL: EXPI293F; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACMAM; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHTBV1.1-CTGFP-SIII-10H; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 13 ORGANISM_TAXID: 30538; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PBXNPFLAGH KEYWDS SLC TRANSPORTER, MEMBRANE PROTEIN, S1P, EXPORTER, LIPID TRANSPORT EXPDTA ELECTRON MICROSCOPY AUTHOR H.Z.LI,A.C.W.PIKE,G.MCKINLEY,S.M.M.MUKHOPADHYAY,C.MOREAU,A.SCACIOC, AUTHOR 2 P.ABRUSCI,O.BORKOWSKA,R.CHALK,S.STEFANIC,N.BURGESS-BROWN,K.L.DUERR, AUTHOR 3 D.B.SAUER REVDAT 1 19-FEB-25 8QV6 0 JRNL AUTH H.Z.LI,A.C.W.PIKE,Y.N.CHANG,D.PRAKAASH,Z.GELOVA,J.STANKA, JRNL AUTH 2 C.MOREAU,H.C.SCOTT,F.WUNDER,G.WOLF,A.SCACIOC,G.MCKINLEY, JRNL AUTH 3 H.BATOULIS,S.MUKHOPADHYAY,A.GAROFOLI,A.PINTO-FERNANDEZ, JRNL AUTH 4 B.M.KESSLER,N.A.BURGESS-BROWN,S.STEFANIC,T.WIEDMER,K.L.DURR, JRNL AUTH 5 V.PUETTER,A.EHRMANN,S.KHALID,A.INGLES-PRIETO, JRNL AUTH 6 G.SUPERTI-FURGA,D.B.SAUER JRNL TITL TRANSPORT AND INHIBITION OF THE SPHINGOSINE-1-PHOSPHATE JRNL TITL 2 EXPORTER SPNS2. JRNL REF NAT COMMUN V. 16 721 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 39820269 JRNL DOI 10.1038/S41467-025-55942-7 REMARK 2 REMARK 2 RESOLUTION. 3.68 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, TOPAZ, EPU, CRYOSPARC, UCSF REMARK 3 CHIMERAX, COOT, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : OTHER 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) : 3.680 REMARK 3 NUMBER OF PARTICLES : 246225 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: MASKED LOCAL REFINEMENT IN CRYOSPARC WITH DETERGENT REMARK 3 MICELLE OMITTED REMARK 4 REMARK 4 8QV6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-23. REMARK 100 THE DEPOSITION ID IS D_1292134106. 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 SPNS2 WITH NANOBODY REMARK 245 D12 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 14.00 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 : 12014 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2400.00 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) : 2546.41 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 105000 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 1 REMARK 465 MET A 2 REMARK 465 CYS A 3 REMARK 465 LEU A 4 REMARK 465 GLU A 5 REMARK 465 CYS A 6 REMARK 465 ALA A 7 REMARK 465 SER A 8 REMARK 465 ALA A 9 REMARK 465 ALA A 10 REMARK 465 ALA A 11 REMARK 465 GLY A 12 REMARK 465 GLY A 13 REMARK 465 ALA A 14 REMARK 465 GLU A 15 REMARK 465 GLU A 16 REMARK 465 GLU A 17 REMARK 465 GLU A 18 REMARK 465 ALA A 19 REMARK 465 ASP A 20 REMARK 465 ALA A 21 REMARK 465 GLU A 22 REMARK 465 ARG A 23 REMARK 465 ARG A 24 REMARK 465 ARG A 25 REMARK 465 ARG A 26 REMARK 465 ARG A 27 REMARK 465 ARG A 28 REMARK 465 GLY A 29 REMARK 465 ALA A 30 REMARK 465 GLN A 31 REMARK 465 ARG A 32 REMARK 465 GLY A 33 REMARK 465 ALA A 34 REMARK 465 GLY A 35 REMARK 465 GLY A 36 REMARK 465 SER A 37 REMARK 465 GLY A 38 REMARK 465 CYS A 39 REMARK 465 CYS A 40 REMARK 465 GLY A 41 REMARK 465 ALA A 42 REMARK 465 ARG A 43 REMARK 465 GLY A 44 REMARK 465 ALA A 45 REMARK 465 GLY A 46 REMARK 465 GLY A 47 REMARK 465 ALA A 48 REMARK 465 GLY A 49 REMARK 465 VAL A 50 REMARK 465 SER A 51 REMARK 465 ALA A 52 REMARK 465 ALA A 53 REMARK 465 GLY A 54 REMARK 465 ASP A 55 REMARK 465 GLU A 56 REMARK 465 VAL A 57 REMARK 465 GLN A 58 REMARK 465 THR A 59 REMARK 465 LEU A 60 REMARK 465 SER A 61 REMARK 465 GLY A 62 REMARK 465 SER A 63 REMARK 465 VAL A 64 REMARK 465 ARG A 65 REMARK 465 ARG A 66 REMARK 465 ALA A 67 REMARK 465 PRO A 68 REMARK 465 THR A 69 REMARK 465 GLY A 70 REMARK 465 PRO A 71 REMARK 465 PRO A 72 REMARK 465 GLY A 73 REMARK 465 THR A 74 REMARK 465 PRO A 75 REMARK 465 GLY A 76 REMARK 465 THR A 77 REMARK 465 PRO A 78 REMARK 465 GLY A 79 REMARK 465 CYS A 80 REMARK 465 ALA A 81 REMARK 465 ALA A 82 REMARK 465 THR A 83 REMARK 465 ALA A 84 REMARK 465 LYS A 85 REMARK 465 GLY A 86 REMARK 465 PRO A 87 REMARK 465 GLY A 88 REMARK 465 ALA A 89 REMARK 465 GLN A 90 REMARK 465 GLN A 91 REMARK 465 PRO A 92 REMARK 465 LYS A 93 REMARK 465 PRO A 94 REMARK 465 ALA A 95 REMARK 465 SER A 96 REMARK 465 LEU A 97 REMARK 465 GLY A 98 REMARK 465 ARG A 99 REMARK 465 HIS A 288 REMARK 465 ALA A 289 REMARK 465 ASP A 290 REMARK 465 GLN A 291 REMARK 465 LEU A 292 REMARK 465 GLY A 293 REMARK 465 ASP A 294 REMARK 465 GLN A 295 REMARK 465 LEU A 296 REMARK 465 THR A 352 REMARK 465 CYS A 353 REMARK 465 ASN A 354 REMARK 465 SER A 355 REMARK 465 PRO A 356 REMARK 465 PRO A 357 REMARK 465 CYS A 358 REMARK 465 LEU A 540 REMARK 465 ALA A 541 REMARK 465 MET A 542 REMARK 465 PRO A 543 REMARK 465 PRO A 544 REMARK 465 ALA A 545 REMARK 465 SER A 546 REMARK 465 VAL A 547 REMARK 465 LYS A 548 REMARK 465 VAL A 549 REMARK 465 ALA A 550 REMARK 465 GLU A 551 REMARK 465 ASN A 552 REMARK 465 LEU A 553 REMARK 465 TYR A 554 REMARK 465 PHE A 555 REMARK 465 GLN A 556 REMARK 465 SER B 127 REMARK 465 SER B 128 REMARK 465 ALA B 129 REMARK 465 ASP B 130 REMARK 465 TYR B 131 REMARK 465 LYS B 132 REMARK 465 ASP B 133 REMARK 465 ASP B 134 REMARK 465 ASP B 135 REMARK 465 ASP B 136 REMARK 465 LYS B 137 REMARK 465 HIS 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 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 101 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 136 CG CD CE NZ REMARK 470 LYS A 168 CG CD CE NZ REMARK 470 CYS A 173 SG REMARK 470 LEU A 229 CG CD1 CD2 REMARK 470 LYS A 253 CG CD CE NZ REMARK 470 MET A 271 CG SD CE REMARK 470 LEU A 276 CG CD1 CD2 REMARK 470 LEU A 278 CG CD1 CD2 REMARK 470 THR A 284 OG1 CG2 REMARK 470 LYS A 285 CG CD CE NZ REMARK 470 ARG A 286 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 297 CG CD CE NZ REMARK 470 ARG A 299 CG CD NE CZ NH1 NH2 REMARK 470 THR A 300 OG1 CG2 REMARK 470 MET A 306 CG SD CE REMARK 470 GLN A 344 CG CD OE1 NE2 REMARK 470 LYS A 348 CG CD CE NZ REMARK 470 GLU A 351 CG CD OE1 OE2 REMARK 470 LEU A 376 CG CD1 CD2 REMARK 470 LYS A 491 CG CD CE NZ REMARK 470 LEU B 11 CG CD1 CD2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 GLU B 44 CG CD OE1 OE2 REMARK 470 GLU B 46 CG CD OE1 OE2 REMARK 470 ASP B 62 CG OD1 OD2 REMARK 470 MET B 83 CG SD CE REMARK 470 LYS B 87 CG CD CE NZ REMARK 470 GLU B 89 CG CD OE1 OE2 REMARK 470 LYS B 120 CG CD CE NZ 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 O PHE A 183 OG SER A 186 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 LYS A 224 -172.76 -173.27 REMARK 500 ILE A 279 -62.97 -108.95 REMARK 500 VAL B 48 -62.29 -120.10 REMARK 500 TYR B 60 -169.70 -126.11 REMARK 500 THR B 112 26.28 44.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 LMT A 601 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-18668 RELATED DB: EMDB REMARK 900 STRUCTURE OF HUMAN SPNS2 IN DDM DBREF 8QV6 A 1 549 UNP Q8IVW8 SPNS2_HUMAN 1 549 DBREF 8QV6 B 1 143 PDB 8QV6 8QV6 1 143 SEQADV 8QV6 ALA A 550 UNP Q8IVW8 EXPRESSION TAG SEQADV 8QV6 GLU A 551 UNP Q8IVW8 EXPRESSION TAG SEQADV 8QV6 ASN A 552 UNP Q8IVW8 EXPRESSION TAG SEQADV 8QV6 LEU A 553 UNP Q8IVW8 EXPRESSION TAG SEQADV 8QV6 TYR A 554 UNP Q8IVW8 EXPRESSION TAG SEQADV 8QV6 PHE A 555 UNP Q8IVW8 EXPRESSION TAG SEQADV 8QV6 GLN A 556 UNP Q8IVW8 EXPRESSION TAG SEQRES 1 A 556 MET MET CYS LEU GLU CYS ALA SER ALA ALA ALA GLY GLY SEQRES 2 A 556 ALA GLU GLU GLU GLU ALA ASP ALA GLU ARG ARG ARG ARG SEQRES 3 A 556 ARG ARG GLY ALA GLN ARG GLY ALA GLY GLY SER GLY CYS SEQRES 4 A 556 CYS GLY ALA ARG GLY ALA GLY GLY ALA GLY VAL SER ALA SEQRES 5 A 556 ALA GLY ASP GLU VAL GLN THR LEU SER GLY SER VAL ARG SEQRES 6 A 556 ARG ALA PRO THR GLY PRO PRO GLY THR PRO GLY THR PRO SEQRES 7 A 556 GLY CYS ALA ALA THR ALA LYS GLY PRO GLY ALA GLN GLN SEQRES 8 A 556 PRO LYS PRO ALA SER LEU GLY ARG GLY ARG GLY ALA ALA SEQRES 9 A 556 ALA ALA ILE LEU SER LEU GLY ASN VAL LEU ASN TYR LEU SEQRES 10 A 556 ASP ARG TYR THR VAL ALA GLY VAL LEU LEU ASP ILE GLN SEQRES 11 A 556 GLN HIS PHE GLY VAL LYS ASP ARG GLY ALA GLY LEU LEU SEQRES 12 A 556 GLN SER VAL PHE ILE CYS SER PHE MET VAL ALA ALA PRO SEQRES 13 A 556 ILE PHE GLY TYR LEU GLY ASP ARG PHE ASN ARG LYS VAL SEQRES 14 A 556 ILE LEU SER CYS GLY ILE PHE PHE TRP SER ALA VAL THR SEQRES 15 A 556 PHE SER SER SER PHE ILE PRO GLN GLN TYR PHE TRP LEU SEQRES 16 A 556 LEU VAL LEU SER ARG GLY LEU VAL GLY ILE GLY GLU ALA SEQRES 17 A 556 SER TYR SER THR ILE ALA PRO THR ILE ILE GLY ASP LEU SEQRES 18 A 556 PHE THR LYS ASN THR ARG THR LEU MET LEU SER VAL PHE SEQRES 19 A 556 TYR PHE ALA ILE PRO LEU GLY SER GLY LEU GLY TYR ILE SEQRES 20 A 556 THR GLY SER SER VAL LYS GLN ALA ALA GLY ASP TRP HIS SEQRES 21 A 556 TRP ALA LEU ARG VAL SER PRO VAL LEU GLY MET ILE THR SEQRES 22 A 556 GLY THR LEU ILE LEU ILE LEU VAL PRO ALA THR LYS ARG SEQRES 23 A 556 GLY HIS ALA ASP GLN LEU GLY ASP GLN LEU LYS ALA ARG SEQRES 24 A 556 THR SER TRP LEU ARG ASP MET LYS ALA LEU ILE ARG ASN SEQRES 25 A 556 ARG SER TYR VAL PHE SER SER LEU ALA THR SER ALA VAL SEQRES 26 A 556 SER PHE ALA THR GLY ALA LEU GLY MET TRP ILE PRO LEU SEQRES 27 A 556 TYR LEU HIS ARG ALA GLN VAL VAL GLN LYS THR ALA GLU SEQRES 28 A 556 THR CYS ASN SER PRO PRO CYS GLY ALA LYS ASP SER LEU SEQRES 29 A 556 ILE PHE GLY ALA ILE THR CYS PHE THR GLY PHE LEU GLY SEQRES 30 A 556 VAL VAL THR GLY ALA GLY ALA THR ARG TRP CYS ARG LEU SEQRES 31 A 556 LYS THR GLN ARG ALA ASP PRO LEU VAL CYS ALA VAL GLY SEQRES 32 A 556 MET LEU GLY SER ALA ILE PHE ILE CYS LEU ILE PHE VAL SEQRES 33 A 556 ALA ALA LYS SER SER ILE VAL GLY ALA TYR ILE CYS ILE SEQRES 34 A 556 PHE VAL GLY GLU THR LEU LEU PHE SER ASN TRP ALA ILE SEQRES 35 A 556 THR ALA ASP ILE LEU MET TYR VAL VAL ILE PRO THR ARG SEQRES 36 A 556 ARG ALA THR ALA VAL ALA LEU GLN SER PHE THR SER HIS SEQRES 37 A 556 LEU LEU GLY ASP ALA GLY SER PRO TYR LEU ILE GLY PHE SEQRES 38 A 556 ILE SER ASP LEU ILE ARG GLN SER THR LYS ASP SER PRO SEQRES 39 A 556 LEU TRP GLU PHE LEU SER LEU GLY TYR ALA LEU MET LEU SEQRES 40 A 556 CYS PRO PHE VAL VAL VAL LEU GLY GLY MET PHE PHE LEU SEQRES 41 A 556 ALA THR ALA LEU PHE PHE VAL SER ASP ARG ALA ARG ALA SEQRES 42 A 556 GLU GLN GLN VAL ASN GLN LEU ALA MET PRO PRO ALA SER SEQRES 43 A 556 VAL LYS VAL ALA GLU ASN LEU TYR PHE GLN SEQRES 1 B 143 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 143 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 143 ARG LEU LEU SER TRP TYR ASP MET ALA TRP PHE ARG GLN SEQRES 4 B 143 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA VAL THR SEQRES 5 B 143 SER THR GLY ALA GLY THR HIS TYR VAL ASP SER VAL LYS SEQRES 6 B 143 GLY ARG PHE THR ILE SER ARG VAL ASN ALA LYS ASN THR SEQRES 7 B 143 MET TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 B 143 ALA VAL TYR TYR CYS ALA ALA ALA ASN THR ARG LEU THR SEQRES 9 B 143 ALA LEU SER LEU ARG THR THR THR GLY SER TRP ALA TYR SEQRES 10 B 143 TRP GLY LYS GLY THR PRO VAL THR VAL SER SER ALA ASP SEQRES 11 B 143 TYR LYS ASP ASP ASP ASP LYS HIS HIS HIS HIS HIS HIS HET LMT A 601 24 HETNAM LMT DODECYL-BETA-D-MALTOSIDE FORMUL 3 LMT C24 H46 O11 HELIX 1 AA1 ARG A 101 TYR A 120 1 20 HELIX 2 AA2 TYR A 120 VAL A 125 1 6 HELIX 3 AA3 VAL A 125 GLY A 134 1 10 HELIX 4 AA4 LYS A 136 GLY A 162 1 27 HELIX 5 AA5 ASN A 166 SER A 186 1 21 HELIX 6 AA6 PHE A 193 PHE A 222 1 30 HELIX 7 AA7 LYS A 224 PHE A 236 1 13 HELIX 8 AA8 PHE A 236 GLY A 257 1 22 HELIX 9 AA9 TRP A 261 LEU A 280 1 20 HELIX 10 AB1 ALA A 298 ASN A 312 1 15 HELIX 11 AB2 ARG A 313 GLN A 347 1 35 HELIX 12 AB3 ALA A 360 ARG A 389 1 30 HELIX 13 AB4 ARG A 394 ALA A 418 1 25 HELIX 14 AB5 SER A 421 SER A 438 1 18 HELIX 15 AB6 SER A 438 VAL A 451 1 14 HELIX 16 AB7 ILE A 452 THR A 454 5 3 HELIX 17 AB8 ARG A 455 GLY A 471 1 17 HELIX 18 AB9 GLY A 474 SER A 489 1 16 HELIX 19 AC1 SER A 493 MET A 506 1 14 HELIX 20 AC2 MET A 506 GLN A 539 1 34 HELIX 21 AC3 LEU B 28 SER B 30 5 3 HELIX 22 AC4 LYS B 87 THR B 91 5 5 SHEET 1 AA1 4 LEU B 4 SER B 7 0 SHEET 2 AA1 4 LEU B 18 ALA B 24 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA1 4 PHE B 68 VAL B 73 -1 N VAL B 73 O THR B 78 SHEET 1 AA2 5 THR B 58 HIS B 59 0 SHEET 2 AA2 5 ARG B 45 VAL B 51 -1 N ALA B 50 O HIS B 59 SHEET 3 AA2 5 TYR B 32 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 4 AA2 5 ALA B 92 ASN B 100 -1 O VAL B 93 N GLN B 39 SHEET 5 AA2 5 TYR B 117 TRP B 118 -1 O TYR B 117 N ALA B 98 SHEET 1 AA3 5 THR B 58 HIS B 59 0 SHEET 2 AA3 5 ARG B 45 VAL B 51 -1 N ALA B 50 O HIS B 59 SHEET 3 AA3 5 TYR B 32 GLN B 39 -1 N ARG B 38 O GLU B 46 SHEET 4 AA3 5 ALA B 92 ASN B 100 -1 O VAL B 93 N GLN B 39 SHEET 5 AA3 5 THR B 122 VAL B 124 -1 O THR B 122 N TYR B 94 SSBOND 1 CYS B 22 CYS B 96 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