HEADER TRANSPORT PROTEIN 08-JUN-17 5W3S TITLE CRYO-ELECTRON MICROSCOPY STRUCTURE OF A TRPML3 ION CHANNEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: MUCOLIPIN-3 ISOFORM 1; COMPND 3 CHAIN: A, B, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CALLITHRIX JACCHUS; SOURCE 3 ORGANISM_COMMON: WHITE-TUFTED-EAR MARMOSET; SOURCE 4 ORGANISM_TAXID: 9483; SOURCE 5 GENE: MCOLN3; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC KEYWDS TRANSIENT RECEPTOR POTENTIAL CHANNEL, MUCOLIPIN, ION CHANNEL, KEYWDS 2 MEMBRANE TRANSPORT, TRPML, TRP CHANNEL, CALCIUM CHANNEL, PIP2, PI(3, KEYWDS 3 5)P2, LIPID-GATED CHANNEL, MUCOLIPIDOSIS, LYSOSOMAL ION CHANNEL, KEYWDS 4 LYSOSOME, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR M.HIRSCHI,M.A.HERZIK,J.WIE,Y.SUO,W.F.BORSCHEL,D.REN,G.C.LANDER, AUTHOR 2 S.Y.LEE REVDAT 3 01-NOV-17 5W3S 1 JRNL REVDAT 2 25-OCT-17 5W3S 1 JRNL REVDAT 1 11-OCT-17 5W3S 0 JRNL AUTH M.HIRSCHI,M.A.HERZIK,J.WIE,Y.SUO,W.F.BORSCHEL,D.REN, JRNL AUTH 2 G.C.LANDER,S.Y.LEE JRNL TITL CRYO-ELECTRON MICROSCOPY STRUCTURE OF THE LYSOSOMAL JRNL TITL 2 CALCIUM-PERMEABLE CHANNEL TRPML3. JRNL REF NATURE V. 550 411 2017 JRNL REFN ESSN 1476-4687 JRNL PMID 29019979 JRNL DOI 10.1038/NATURE24055 REMARK 2 REMARK 2 RESOLUTION. 2.94 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) : 2.940 REMARK 3 NUMBER OF PARTICLES : 104084 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 5W3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1000227960. 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 : TRANSIENT RECEPTOR POTENTIAL REMARK 245 MUCOLIPIN 3 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 TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 63.00 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 33250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 87220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -356.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 MET A 1 REMARK 465 ALA A 2 REMARK 465 ASN A 3 REMARK 465 PRO A 4 REMARK 465 GLU A 5 REMARK 465 ILE A 6 REMARK 465 VAL A 7 REMARK 465 ILE A 8 REMARK 465 SER A 9 REMARK 465 SER A 10 REMARK 465 CYS A 11 REMARK 465 SER A 12 REMARK 465 SER A 13 REMARK 465 HIS A 14 REMARK 465 GLU A 15 REMARK 465 GLU A 16 REMARK 465 GLU A 17 REMARK 465 ASN A 18 REMARK 465 ARG A 19 REMARK 465 CYS A 20 REMARK 465 ASN A 21 REMARK 465 PHE A 22 REMARK 465 ASN A 23 REMARK 465 GLN A 24 REMARK 465 HIS A 25 REMARK 465 THR A 26 REMARK 465 SER A 27 REMARK 465 PRO A 28 REMARK 465 SER A 29 REMARK 465 GLU A 30 REMARK 465 GLU A 31 REMARK 465 LEU A 32 REMARK 465 LYS A 149 REMARK 465 GLY A 150 REMARK 465 THR A 151 REMARK 465 ASP A 152 REMARK 465 GLN A 153 REMARK 465 GLY A 197 REMARK 465 THR A 198 REMARK 465 PRO A 199 REMARK 465 ALA A 200 REMARK 465 GLU A 527 REMARK 465 CYS A 528 REMARK 465 LYS A 529 REMARK 465 ASP A 530 REMARK 465 LEU A 531 REMARK 465 PRO A 532 REMARK 465 ASN A 533 REMARK 465 SER A 534 REMARK 465 GLY A 535 REMARK 465 LYS A 536 REMARK 465 PHE A 537 REMARK 465 ARG A 538 REMARK 465 LEU A 539 REMARK 465 GLU A 540 REMARK 465 ASP A 541 REMARK 465 ASP A 542 REMARK 465 PRO A 543 REMARK 465 PRO A 544 REMARK 465 VAL A 545 REMARK 465 SER A 546 REMARK 465 LEU A 547 REMARK 465 PHE A 548 REMARK 465 CYS A 549 REMARK 465 CYS A 550 REMARK 465 CYS A 551 REMARK 465 LYS A 552 REMARK 465 LYS A 553 REMARK 465 SER A 554 REMARK 465 ASN A 555 REMARK 465 LEU A 556 REMARK 465 GLU A 557 REMARK 465 VAL A 558 REMARK 465 LEU A 559 REMARK 465 PHE A 560 REMARK 465 GLN A 561 REMARK 465 MET B 1 REMARK 465 ALA B 2 REMARK 465 ASN B 3 REMARK 465 PRO B 4 REMARK 465 GLU B 5 REMARK 465 ILE B 6 REMARK 465 VAL B 7 REMARK 465 ILE B 8 REMARK 465 SER B 9 REMARK 465 SER B 10 REMARK 465 CYS B 11 REMARK 465 SER B 12 REMARK 465 SER B 13 REMARK 465 HIS B 14 REMARK 465 GLU B 15 REMARK 465 GLU B 16 REMARK 465 GLU B 17 REMARK 465 ASN B 18 REMARK 465 ARG B 19 REMARK 465 CYS B 20 REMARK 465 ASN B 21 REMARK 465 PHE B 22 REMARK 465 ASN B 23 REMARK 465 GLN B 24 REMARK 465 HIS B 25 REMARK 465 THR B 26 REMARK 465 SER B 27 REMARK 465 PRO B 28 REMARK 465 SER B 29 REMARK 465 GLU B 30 REMARK 465 GLU B 31 REMARK 465 LEU B 32 REMARK 465 LYS B 149 REMARK 465 GLY B 150 REMARK 465 THR B 151 REMARK 465 ASP B 152 REMARK 465 GLN B 153 REMARK 465 GLY B 197 REMARK 465 THR B 198 REMARK 465 PRO B 199 REMARK 465 ALA B 200 REMARK 465 GLU B 527 REMARK 465 CYS B 528 REMARK 465 LYS B 529 REMARK 465 ASP B 530 REMARK 465 LEU B 531 REMARK 465 PRO B 532 REMARK 465 ASN B 533 REMARK 465 SER B 534 REMARK 465 GLY B 535 REMARK 465 LYS B 536 REMARK 465 PHE B 537 REMARK 465 ARG B 538 REMARK 465 LEU B 539 REMARK 465 GLU B 540 REMARK 465 ASP B 541 REMARK 465 ASP B 542 REMARK 465 PRO B 543 REMARK 465 PRO B 544 REMARK 465 VAL B 545 REMARK 465 SER B 546 REMARK 465 LEU B 547 REMARK 465 PHE B 548 REMARK 465 CYS B 549 REMARK 465 CYS B 550 REMARK 465 CYS B 551 REMARK 465 LYS B 552 REMARK 465 LYS B 553 REMARK 465 SER B 554 REMARK 465 ASN B 555 REMARK 465 LEU B 556 REMARK 465 GLU B 557 REMARK 465 VAL B 558 REMARK 465 LEU B 559 REMARK 465 PHE B 560 REMARK 465 GLN B 561 REMARK 465 MET C 1 REMARK 465 ALA C 2 REMARK 465 ASN C 3 REMARK 465 PRO C 4 REMARK 465 GLU C 5 REMARK 465 ILE C 6 REMARK 465 VAL C 7 REMARK 465 ILE C 8 REMARK 465 SER C 9 REMARK 465 SER C 10 REMARK 465 CYS C 11 REMARK 465 SER C 12 REMARK 465 SER C 13 REMARK 465 HIS C 14 REMARK 465 GLU C 15 REMARK 465 GLU C 16 REMARK 465 GLU C 17 REMARK 465 ASN C 18 REMARK 465 ARG C 19 REMARK 465 CYS C 20 REMARK 465 ASN C 21 REMARK 465 PHE C 22 REMARK 465 ASN C 23 REMARK 465 GLN C 24 REMARK 465 HIS C 25 REMARK 465 THR C 26 REMARK 465 SER C 27 REMARK 465 PRO C 28 REMARK 465 SER C 29 REMARK 465 GLU C 30 REMARK 465 GLU C 31 REMARK 465 LEU C 32 REMARK 465 LYS C 149 REMARK 465 GLY C 150 REMARK 465 THR C 151 REMARK 465 ASP C 152 REMARK 465 GLN C 153 REMARK 465 GLY C 197 REMARK 465 THR C 198 REMARK 465 PRO C 199 REMARK 465 ALA C 200 REMARK 465 GLU C 527 REMARK 465 CYS C 528 REMARK 465 LYS C 529 REMARK 465 ASP C 530 REMARK 465 LEU C 531 REMARK 465 PRO C 532 REMARK 465 ASN C 533 REMARK 465 SER C 534 REMARK 465 GLY C 535 REMARK 465 LYS C 536 REMARK 465 PHE C 537 REMARK 465 ARG C 538 REMARK 465 LEU C 539 REMARK 465 GLU C 540 REMARK 465 ASP C 541 REMARK 465 ASP C 542 REMARK 465 PRO C 543 REMARK 465 PRO C 544 REMARK 465 VAL C 545 REMARK 465 SER C 546 REMARK 465 LEU C 547 REMARK 465 PHE C 548 REMARK 465 CYS C 549 REMARK 465 CYS C 550 REMARK 465 CYS C 551 REMARK 465 LYS C 552 REMARK 465 LYS C 553 REMARK 465 SER C 554 REMARK 465 ASN C 555 REMARK 465 LEU C 556 REMARK 465 GLU C 557 REMARK 465 VAL C 558 REMARK 465 LEU C 559 REMARK 465 PHE C 560 REMARK 465 GLN C 561 REMARK 465 MET D 1 REMARK 465 ALA D 2 REMARK 465 ASN D 3 REMARK 465 PRO D 4 REMARK 465 GLU D 5 REMARK 465 ILE D 6 REMARK 465 VAL D 7 REMARK 465 ILE D 8 REMARK 465 SER D 9 REMARK 465 SER D 10 REMARK 465 CYS D 11 REMARK 465 SER D 12 REMARK 465 SER D 13 REMARK 465 HIS D 14 REMARK 465 GLU D 15 REMARK 465 GLU D 16 REMARK 465 GLU D 17 REMARK 465 ASN D 18 REMARK 465 ARG D 19 REMARK 465 CYS D 20 REMARK 465 ASN D 21 REMARK 465 PHE D 22 REMARK 465 ASN D 23 REMARK 465 GLN D 24 REMARK 465 HIS D 25 REMARK 465 THR D 26 REMARK 465 SER D 27 REMARK 465 PRO D 28 REMARK 465 SER D 29 REMARK 465 GLU D 30 REMARK 465 GLU D 31 REMARK 465 LEU D 32 REMARK 465 LYS D 149 REMARK 465 GLY D 150 REMARK 465 THR D 151 REMARK 465 ASP D 152 REMARK 465 GLN D 153 REMARK 465 GLY D 197 REMARK 465 THR D 198 REMARK 465 PRO D 199 REMARK 465 ALA D 200 REMARK 465 GLU D 527 REMARK 465 CYS D 528 REMARK 465 LYS D 529 REMARK 465 ASP D 530 REMARK 465 LEU D 531 REMARK 465 PRO D 532 REMARK 465 ASN D 533 REMARK 465 SER D 534 REMARK 465 GLY D 535 REMARK 465 LYS D 536 REMARK 465 PHE D 537 REMARK 465 ARG D 538 REMARK 465 LEU D 539 REMARK 465 GLU D 540 REMARK 465 ASP D 541 REMARK 465 ASP D 542 REMARK 465 PRO D 543 REMARK 465 PRO D 544 REMARK 465 VAL D 545 REMARK 465 SER D 546 REMARK 465 LEU D 547 REMARK 465 PHE D 548 REMARK 465 CYS D 549 REMARK 465 CYS D 550 REMARK 465 CYS D 551 REMARK 465 LYS D 552 REMARK 465 LYS D 553 REMARK 465 SER D 554 REMARK 465 ASN D 555 REMARK 465 LEU D 556 REMARK 465 GLU D 557 REMARK 465 VAL D 558 REMARK 465 LEU D 559 REMARK 465 PHE D 560 REMARK 465 GLN D 561 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 LEU A 33 CG CD1 CD2 REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2 REMARK 470 TRP A 54 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 54 CZ3 CH2 REMARK 470 MET A 110 CG SD CE REMARK 470 ASN A 148 CG OD1 ND2 REMARK 470 GLU A 192 CG CD OE1 OE2 REMARK 470 PHE A 194 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 201 CG CD OE1 OE2 REMARK 470 LYS A 250 CG CD CE NZ REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 ASP A 328 CG OD1 OD2 REMARK 470 VAL A 329 CG1 CG2 REMARK 470 HIS A 510 CG ND1 CD2 CE1 NE2 REMARK 470 LEU B 33 CG CD1 CD2 REMARK 470 ARG B 40 CG CD NE CZ NH1 NH2 REMARK 470 TRP B 54 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 54 CZ3 CH2 REMARK 470 MET B 110 CG SD CE REMARK 470 ASN B 148 CG OD1 ND2 REMARK 470 GLU B 192 CG CD OE1 OE2 REMARK 470 PHE B 194 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU B 201 CG CD OE1 OE2 REMARK 470 LYS B 250 CG CD CE NZ REMARK 470 LYS B 280 CG CD CE NZ REMARK 470 ASP B 328 CG OD1 OD2 REMARK 470 VAL B 329 CG1 CG2 REMARK 470 HIS B 510 CG ND1 CD2 CE1 NE2 REMARK 470 LEU C 33 CG CD1 CD2 REMARK 470 ARG C 40 CG CD NE CZ NH1 NH2 REMARK 470 TRP C 54 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 54 CZ3 CH2 REMARK 470 MET C 110 CG SD CE REMARK 470 ASN C 148 CG OD1 ND2 REMARK 470 GLU C 192 CG CD OE1 OE2 REMARK 470 PHE C 194 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU C 201 CG CD OE1 OE2 REMARK 470 LYS C 250 CG CD CE NZ REMARK 470 LYS C 280 CG CD CE NZ REMARK 470 ASP C 328 CG OD1 OD2 REMARK 470 VAL C 329 CG1 CG2 REMARK 470 HIS C 510 CG ND1 CD2 CE1 NE2 REMARK 470 LEU D 33 CG CD1 CD2 REMARK 470 ARG D 40 CG CD NE CZ NH1 NH2 REMARK 470 TRP D 54 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 54 CZ3 CH2 REMARK 470 MET D 110 CG SD CE REMARK 470 ASN D 148 CG OD1 ND2 REMARK 470 GLU D 192 CG CD OE1 OE2 REMARK 470 PHE D 194 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU D 201 CG CD OE1 OE2 REMARK 470 LYS D 250 CG CD CE NZ REMARK 470 LYS D 280 CG CD CE NZ REMARK 470 ASP D 328 CG OD1 OD2 REMARK 470 VAL D 329 CG1 CG2 REMARK 470 HIS D 510 CG ND1 CD2 CE1 NE2 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 ASN A 172 HZ2 LYS C 270 1.56 REMARK 500 O ASN C 172 HZ2 LYS D 270 1.59 REMARK 500 OG1 THR D 242 O ASP D 263 2.05 REMARK 500 OG1 THR A 242 O ASP A 263 2.05 REMARK 500 OG1 THR C 242 O ASP C 263 2.05 REMARK 500 OG1 THR B 242 O ASP B 263 2.05 REMARK 500 O TRP C 475 OG SER C 478 2.12 REMARK 500 O TRP A 475 OG SER A 478 2.12 REMARK 500 O TRP B 475 OG SER B 478 2.12 REMARK 500 O TRP D 475 OG SER D 478 2.12 REMARK 500 O TYR D 426 OH TYR D 481 2.12 REMARK 500 O TYR B 426 OH TYR B 481 2.12 REMARK 500 O TYR A 426 OH TYR A 481 2.12 REMARK 500 O TYR C 426 OH TYR C 481 2.12 REMARK 500 O TYR D 133 OH TYR D 146 2.16 REMARK 500 O TYR A 133 OH TYR A 146 2.16 REMARK 500 O TYR C 133 OH TYR C 146 2.16 REMARK 500 O TYR B 133 OH TYR B 146 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 ARG A 109 24.45 80.37 REMARK 500 ASP A 112 13.76 56.09 REMARK 500 GLU A 192 74.87 -116.07 REMARK 500 ASN A 205 30.32 -92.17 REMARK 500 PHE A 210 -5.33 75.11 REMARK 500 LEU A 213 140.07 -170.42 REMARK 500 SER A 253 20.66 -145.91 REMARK 500 ASP A 328 27.43 -160.24 REMARK 500 ASP A 371 -39.90 -133.82 REMARK 500 ASN A 456 33.34 -97.46 REMARK 500 GLU A 520 -4.22 75.77 REMARK 500 ARG B 109 24.39 80.43 REMARK 500 ASP B 112 13.79 56.10 REMARK 500 GLU B 192 74.88 -116.07 REMARK 500 ASN B 205 30.40 -92.21 REMARK 500 PHE B 210 -5.31 75.12 REMARK 500 LEU B 213 140.06 -170.45 REMARK 500 SER B 253 20.73 -145.99 REMARK 500 ASP B 328 27.39 -160.25 REMARK 500 ASP B 371 -39.94 -133.92 REMARK 500 ASN B 456 33.38 -97.45 REMARK 500 GLU B 520 -4.25 75.79 REMARK 500 ARG C 109 24.39 80.40 REMARK 500 ASP C 112 13.73 56.09 REMARK 500 GLU C 192 74.85 -116.09 REMARK 500 ASN C 205 30.33 -92.14 REMARK 500 PHE C 210 -5.43 75.22 REMARK 500 LEU C 213 140.12 -170.39 REMARK 500 SER C 253 20.68 -145.94 REMARK 500 ASP C 328 27.51 -160.25 REMARK 500 ASP C 371 -39.92 -133.85 REMARK 500 ASN C 456 33.32 -97.48 REMARK 500 GLU C 520 -4.26 75.80 REMARK 500 ARG D 109 24.45 80.42 REMARK 500 ASP D 112 13.75 56.10 REMARK 500 GLU D 192 74.90 -116.07 REMARK 500 ASN D 205 30.31 -92.17 REMARK 500 PHE D 210 -5.41 75.15 REMARK 500 LEU D 213 140.08 -170.42 REMARK 500 SER D 253 20.59 -145.90 REMARK 500 ASP D 328 27.39 -160.23 REMARK 500 ASP D 371 -39.91 -133.84 REMARK 500 ASN D 456 33.33 -97.41 REMARK 500 GLU D 520 -4.25 75.78 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 3PE A 604 REMARK 610 Y01 A 605 REMARK 610 3PE B 603 REMARK 610 Y01 B 604 REMARK 610 3PE C 601 REMARK 610 Y01 C 602 REMARK 610 3PE D 603 REMARK 610 Y01 D 604 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 3PE A 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 A 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 3PE B 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 B 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 3PE C 601 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 605 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 606 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 C 607 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 602 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 3PE D 603 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 604 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Y01 D 605 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5W3S RELATED DB: PDB REMARK 900 RELATED ID: EMD-8764 RELATED DB: EMDB REMARK 900 CRYO-ELECTRON MICROSCOPY STRUCTURE OF A TRPML3 ION CHANNEL DBREF 5W3S A 1 553 UNP F6RG56 F6RG56_CALJA 1 553 DBREF 5W3S B 1 553 UNP F6RG56 F6RG56_CALJA 1 553 DBREF 5W3S C 1 553 UNP F6RG56 F6RG56_CALJA 1 553 DBREF 5W3S D 1 553 UNP F6RG56 F6RG56_CALJA 1 553 SEQADV 5W3S GLN A 138 UNP F6RG56 ASN 138 ENGINEERED MUTATION SEQADV 5W3S SER A 554 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S ASN A 555 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU A 556 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLU A 557 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S VAL A 558 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU A 559 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S PHE A 560 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN A 561 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN B 138 UNP F6RG56 ASN 138 ENGINEERED MUTATION SEQADV 5W3S SER B 554 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S ASN B 555 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU B 556 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLU B 557 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S VAL B 558 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU B 559 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S PHE B 560 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN B 561 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN C 138 UNP F6RG56 ASN 138 ENGINEERED MUTATION SEQADV 5W3S SER C 554 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S ASN C 555 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU C 556 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLU C 557 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S VAL C 558 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU C 559 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S PHE C 560 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN C 561 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN D 138 UNP F6RG56 ASN 138 ENGINEERED MUTATION SEQADV 5W3S SER D 554 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S ASN D 555 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU D 556 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLU D 557 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S VAL D 558 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S LEU D 559 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S PHE D 560 UNP F6RG56 EXPRESSION TAG SEQADV 5W3S GLN D 561 UNP F6RG56 EXPRESSION TAG SEQRES 1 A 561 MET ALA ASN PRO GLU ILE VAL ILE SER SER CYS SER SER SEQRES 2 A 561 HIS GLU GLU GLU ASN ARG CYS ASN PHE ASN GLN HIS THR SEQRES 3 A 561 SER PRO SER GLU GLU LEU LEU LEU GLU ASP GLN MET ARG SEQRES 4 A 561 ARG LYS LEU LYS PHE PHE PHE MET ASN PRO CYS GLU LYS SEQRES 5 A 561 PHE TRP ALA ARG GLY ARG LYS PRO TRP LYS LEU ALA ILE SEQRES 6 A 561 GLN ILE LEU LYS ILE ALA MET VAL THR ILE GLN LEU VAL SEQRES 7 A 561 LEU PHE GLY LEU SER ASN GLN MET VAL VAL ALA PHE LYS SEQRES 8 A 561 GLU GLU ASN THR VAL ALA PHE LYS HIS LEU PHE LEU LYS SEQRES 9 A 561 GLY TYR ILE ASP ARG MET ASP ASP THR TYR ALA VAL TYR SEQRES 10 A 561 THR GLN SER ASP VAL TYR ASP GLN ILE ILE PHE ALA VAL SEQRES 11 A 561 ASN GLN TYR LEU GLN LEU TYR GLN VAL SER VAL GLY ASN SEQRES 12 A 561 HIS ALA TYR GLU ASN LYS GLY THR ASP GLN SER ALA MET SEQRES 13 A 561 ALA ILE CYS GLN HIS PHE TYR LYS ARG GLY ASN ILE TYR SEQRES 14 A 561 PRO GLY ASN ASP THR PHE ASP ILE ASP PRO GLU ILE GLU SEQRES 15 A 561 THR ASP CYS PHE PHE VAL GLU PRO ASP GLU PRO PHE HIS SEQRES 16 A 561 ILE GLY THR PRO ALA GLU ASN LYS LEU ASN LEU THR LEU SEQRES 17 A 561 ASP PHE HIS ARG LEU LEU THR VAL GLU LEU GLN PHE LYS SEQRES 18 A 561 LEU LYS ALA ILE ASN LEU GLN THR VAL ARG HIS GLN GLU SEQRES 19 A 561 LEU PRO ASP CYS TYR ASP PHE THR LEU THR ILE THR PHE SEQRES 20 A 561 ASP ASN LYS ALA HIS SER GLY ARG ILE LYS ILE SER LEU SEQRES 21 A 561 ASP ASN ASP ILE SER ILE ARG GLU CYS LYS ASP TRP HIS SEQRES 22 A 561 VAL SER GLY SER ILE GLN LYS ASN THR HIS ASN MET MET SEQRES 23 A 561 ILE PHE ASP ALA PHE VAL ILE LEU THR CYS LEU VAL SER SEQRES 24 A 561 LEU ILE LEU CYS ILE ARG SER VAL ILE SER GLY LEU GLN SEQRES 25 A 561 LEU GLN GLN GLU PHE VAL ASN PHE PHE LEU LEU HIS TYR SEQRES 26 A 561 LYS LYS ASP VAL SER VAL SER ASP GLN MET GLU PHE VAL SEQRES 27 A 561 ASN GLY TRP TYR ILE MET ILE ILE ILE SER ASP ILE LEU SEQRES 28 A 561 THR ILE ILE GLY SER ILE LEU LYS MET GLU ILE GLN ALA SEQRES 29 A 561 LYS SER LEU THR SER TYR ASP VAL CYS SER ILE LEU LEU SEQRES 30 A 561 GLY THR SER THR MET LEU VAL TRP LEU GLY VAL ILE ARG SEQRES 31 A 561 TYR LEU GLY PHE PHE ALA LYS TYR ASN LEU LEU ILE LEU SEQRES 32 A 561 THR LEU GLN ALA ALA LEU PRO ASN VAL ILE ARG PHE CYS SEQRES 33 A 561 CYS CYS ALA ALA MET ILE TYR LEU GLY TYR CYS PHE CYS SEQRES 34 A 561 GLY TRP ILE VAL LEU GLY PRO TYR HIS ASN LYS PHE ARG SEQRES 35 A 561 SER LEU ASN MET VAL SER GLU CYS LEU PHE SER LEU ILE SEQRES 36 A 561 ASN GLY ASP ASP MET PHE ALA THR PHE ALA LYS MET GLN SEQRES 37 A 561 GLN LYS SER TYR LEU VAL TRP LEU PHE SER ARG ILE TYR SEQRES 38 A 561 LEU TYR SER PHE ILE SER LEU PHE ILE TYR MET ILE LEU SEQRES 39 A 561 SER LEU PHE ILE ALA LEU ILE THR ASP THR TYR GLU THR SEQRES 40 A 561 ILE LYS HIS TYR GLN GLN ASP GLY PHE PRO GLU THR GLU SEQRES 41 A 561 LEU ARG THR PHE ILE SER GLU CYS LYS ASP LEU PRO ASN SEQRES 42 A 561 SER GLY LYS PHE ARG LEU GLU ASP ASP PRO PRO VAL SER SEQRES 43 A 561 LEU PHE CYS CYS CYS LYS LYS SER ASN LEU GLU VAL LEU SEQRES 44 A 561 PHE GLN SEQRES 1 B 561 MET ALA ASN PRO GLU ILE VAL ILE SER SER CYS SER SER SEQRES 2 B 561 HIS GLU GLU GLU ASN ARG CYS ASN PHE ASN GLN HIS THR SEQRES 3 B 561 SER PRO SER GLU GLU LEU LEU LEU GLU ASP GLN MET ARG SEQRES 4 B 561 ARG LYS LEU LYS PHE PHE PHE MET ASN PRO CYS GLU LYS SEQRES 5 B 561 PHE TRP ALA ARG GLY ARG LYS PRO TRP LYS LEU ALA ILE SEQRES 6 B 561 GLN ILE LEU LYS ILE ALA MET VAL THR ILE GLN LEU VAL SEQRES 7 B 561 LEU PHE GLY LEU SER ASN GLN MET VAL VAL ALA PHE LYS SEQRES 8 B 561 GLU GLU ASN THR VAL ALA PHE LYS HIS LEU PHE LEU LYS SEQRES 9 B 561 GLY TYR ILE ASP ARG MET ASP ASP THR TYR ALA VAL TYR SEQRES 10 B 561 THR GLN SER ASP VAL TYR ASP GLN ILE ILE PHE ALA VAL SEQRES 11 B 561 ASN GLN TYR LEU GLN LEU TYR GLN VAL SER VAL GLY ASN SEQRES 12 B 561 HIS ALA TYR GLU ASN LYS GLY THR ASP GLN SER ALA MET SEQRES 13 B 561 ALA ILE CYS GLN HIS PHE TYR LYS ARG GLY ASN ILE TYR SEQRES 14 B 561 PRO GLY ASN ASP THR PHE ASP ILE ASP PRO GLU ILE GLU SEQRES 15 B 561 THR ASP CYS PHE PHE VAL GLU PRO ASP GLU PRO PHE HIS SEQRES 16 B 561 ILE GLY THR PRO ALA GLU ASN LYS LEU ASN LEU THR LEU SEQRES 17 B 561 ASP PHE HIS ARG LEU LEU THR VAL GLU LEU GLN PHE LYS SEQRES 18 B 561 LEU LYS ALA ILE ASN LEU GLN THR VAL ARG HIS GLN GLU SEQRES 19 B 561 LEU PRO ASP CYS TYR ASP PHE THR LEU THR ILE THR PHE SEQRES 20 B 561 ASP ASN LYS ALA HIS SER GLY ARG ILE LYS ILE SER LEU SEQRES 21 B 561 ASP ASN ASP ILE SER ILE ARG GLU CYS LYS ASP TRP HIS SEQRES 22 B 561 VAL SER GLY SER ILE GLN LYS ASN THR HIS ASN MET MET SEQRES 23 B 561 ILE PHE ASP ALA PHE VAL ILE LEU THR CYS LEU VAL SER SEQRES 24 B 561 LEU ILE LEU CYS ILE ARG SER VAL ILE SER GLY LEU GLN SEQRES 25 B 561 LEU GLN GLN GLU PHE VAL ASN PHE PHE LEU LEU HIS TYR SEQRES 26 B 561 LYS LYS ASP VAL SER VAL SER ASP GLN MET GLU PHE VAL SEQRES 27 B 561 ASN GLY TRP TYR ILE MET ILE ILE ILE SER ASP ILE LEU SEQRES 28 B 561 THR ILE ILE GLY SER ILE LEU LYS MET GLU ILE GLN ALA SEQRES 29 B 561 LYS SER LEU THR SER TYR ASP VAL CYS SER ILE LEU LEU SEQRES 30 B 561 GLY THR SER THR MET LEU VAL TRP LEU GLY VAL ILE ARG SEQRES 31 B 561 TYR LEU GLY PHE PHE ALA LYS TYR ASN LEU LEU ILE LEU SEQRES 32 B 561 THR LEU GLN ALA ALA LEU PRO ASN VAL ILE ARG PHE CYS SEQRES 33 B 561 CYS CYS ALA ALA MET ILE TYR LEU GLY TYR CYS PHE CYS SEQRES 34 B 561 GLY TRP ILE VAL LEU GLY PRO TYR HIS ASN LYS PHE ARG SEQRES 35 B 561 SER LEU ASN MET VAL SER GLU CYS LEU PHE SER LEU ILE SEQRES 36 B 561 ASN GLY ASP ASP MET PHE ALA THR PHE ALA LYS MET GLN SEQRES 37 B 561 GLN LYS SER TYR LEU VAL TRP LEU PHE SER ARG ILE TYR SEQRES 38 B 561 LEU TYR SER PHE ILE SER LEU PHE ILE TYR MET ILE LEU SEQRES 39 B 561 SER LEU PHE ILE ALA LEU ILE THR ASP THR TYR GLU THR SEQRES 40 B 561 ILE LYS HIS TYR GLN GLN ASP GLY PHE PRO GLU THR GLU SEQRES 41 B 561 LEU ARG THR PHE ILE SER GLU CYS LYS ASP LEU PRO ASN SEQRES 42 B 561 SER GLY LYS PHE ARG LEU GLU ASP ASP PRO PRO VAL SER SEQRES 43 B 561 LEU PHE CYS CYS CYS LYS LYS SER ASN LEU GLU VAL LEU SEQRES 44 B 561 PHE GLN SEQRES 1 C 561 MET ALA ASN PRO GLU ILE VAL ILE SER SER CYS SER SER SEQRES 2 C 561 HIS GLU GLU GLU ASN ARG CYS ASN PHE ASN GLN HIS THR SEQRES 3 C 561 SER PRO SER GLU GLU LEU LEU LEU GLU ASP GLN MET ARG SEQRES 4 C 561 ARG LYS LEU LYS PHE PHE PHE MET ASN PRO CYS GLU LYS SEQRES 5 C 561 PHE TRP ALA ARG GLY ARG LYS PRO TRP LYS LEU ALA ILE SEQRES 6 C 561 GLN ILE LEU LYS ILE ALA MET VAL THR ILE GLN LEU VAL SEQRES 7 C 561 LEU PHE GLY LEU SER ASN GLN MET VAL VAL ALA PHE LYS SEQRES 8 C 561 GLU GLU ASN THR VAL ALA PHE LYS HIS LEU PHE LEU LYS SEQRES 9 C 561 GLY TYR ILE ASP ARG MET ASP ASP THR TYR ALA VAL TYR SEQRES 10 C 561 THR GLN SER ASP VAL TYR ASP GLN ILE ILE PHE ALA VAL SEQRES 11 C 561 ASN GLN TYR LEU GLN LEU TYR GLN VAL SER VAL GLY ASN SEQRES 12 C 561 HIS ALA TYR GLU ASN LYS GLY THR ASP GLN SER ALA MET SEQRES 13 C 561 ALA ILE CYS GLN HIS PHE TYR LYS ARG GLY ASN ILE TYR SEQRES 14 C 561 PRO GLY ASN ASP THR PHE ASP ILE ASP PRO GLU ILE GLU SEQRES 15 C 561 THR ASP CYS PHE PHE VAL GLU PRO ASP GLU PRO PHE HIS SEQRES 16 C 561 ILE GLY THR PRO ALA GLU ASN LYS LEU ASN LEU THR LEU SEQRES 17 C 561 ASP PHE HIS ARG LEU LEU THR VAL GLU LEU GLN PHE LYS SEQRES 18 C 561 LEU LYS ALA ILE ASN LEU GLN THR VAL ARG HIS GLN GLU SEQRES 19 C 561 LEU PRO ASP CYS TYR ASP PHE THR LEU THR ILE THR PHE SEQRES 20 C 561 ASP ASN LYS ALA HIS SER GLY ARG ILE LYS ILE SER LEU SEQRES 21 C 561 ASP ASN ASP ILE SER ILE ARG GLU CYS LYS ASP TRP HIS SEQRES 22 C 561 VAL SER GLY SER ILE GLN LYS ASN THR HIS ASN MET MET SEQRES 23 C 561 ILE PHE ASP ALA PHE VAL ILE LEU THR CYS LEU VAL SER SEQRES 24 C 561 LEU ILE LEU CYS ILE ARG SER VAL ILE SER GLY LEU GLN SEQRES 25 C 561 LEU GLN GLN GLU PHE VAL ASN PHE PHE LEU LEU HIS TYR SEQRES 26 C 561 LYS LYS ASP VAL SER VAL SER ASP GLN MET GLU PHE VAL SEQRES 27 C 561 ASN GLY TRP TYR ILE MET ILE ILE ILE SER ASP ILE LEU SEQRES 28 C 561 THR ILE ILE GLY SER ILE LEU LYS MET GLU ILE GLN ALA SEQRES 29 C 561 LYS SER LEU THR SER TYR ASP VAL CYS SER ILE LEU LEU SEQRES 30 C 561 GLY THR SER THR MET LEU VAL TRP LEU GLY VAL ILE ARG SEQRES 31 C 561 TYR LEU GLY PHE PHE ALA LYS TYR ASN LEU LEU ILE LEU SEQRES 32 C 561 THR LEU GLN ALA ALA LEU PRO ASN VAL ILE ARG PHE CYS SEQRES 33 C 561 CYS CYS ALA ALA MET ILE TYR LEU GLY TYR CYS PHE CYS SEQRES 34 C 561 GLY TRP ILE VAL LEU GLY PRO TYR HIS ASN LYS PHE ARG SEQRES 35 C 561 SER LEU ASN MET VAL SER GLU CYS LEU PHE SER LEU ILE SEQRES 36 C 561 ASN GLY ASP ASP MET PHE ALA THR PHE ALA LYS MET GLN SEQRES 37 C 561 GLN LYS SER TYR LEU VAL TRP LEU PHE SER ARG ILE TYR SEQRES 38 C 561 LEU TYR SER PHE ILE SER LEU PHE ILE TYR MET ILE LEU SEQRES 39 C 561 SER LEU PHE ILE ALA LEU ILE THR ASP THR TYR GLU THR SEQRES 40 C 561 ILE LYS HIS TYR GLN GLN ASP GLY PHE PRO GLU THR GLU SEQRES 41 C 561 LEU ARG THR PHE ILE SER GLU CYS LYS ASP LEU PRO ASN SEQRES 42 C 561 SER GLY LYS PHE ARG LEU GLU ASP ASP PRO PRO VAL SER SEQRES 43 C 561 LEU PHE CYS CYS CYS LYS LYS SER ASN LEU GLU VAL LEU SEQRES 44 C 561 PHE GLN SEQRES 1 D 561 MET ALA ASN PRO GLU ILE VAL ILE SER SER CYS SER SER SEQRES 2 D 561 HIS GLU GLU GLU ASN ARG CYS ASN PHE ASN GLN HIS THR SEQRES 3 D 561 SER PRO SER GLU GLU LEU LEU LEU GLU ASP GLN MET ARG SEQRES 4 D 561 ARG LYS LEU LYS PHE PHE PHE MET ASN PRO CYS GLU LYS SEQRES 5 D 561 PHE TRP ALA ARG GLY ARG LYS PRO TRP LYS LEU ALA ILE SEQRES 6 D 561 GLN ILE LEU LYS ILE ALA MET VAL THR ILE GLN LEU VAL SEQRES 7 D 561 LEU PHE GLY LEU SER ASN GLN MET VAL VAL ALA PHE LYS SEQRES 8 D 561 GLU GLU ASN THR VAL ALA PHE LYS HIS LEU PHE LEU LYS SEQRES 9 D 561 GLY TYR ILE ASP ARG MET ASP ASP THR TYR ALA VAL TYR SEQRES 10 D 561 THR GLN SER ASP VAL TYR ASP GLN ILE ILE PHE ALA VAL SEQRES 11 D 561 ASN GLN TYR LEU GLN LEU TYR GLN VAL SER VAL GLY ASN SEQRES 12 D 561 HIS ALA TYR GLU ASN LYS GLY THR ASP GLN SER ALA MET SEQRES 13 D 561 ALA ILE CYS GLN HIS PHE TYR LYS ARG GLY ASN ILE TYR SEQRES 14 D 561 PRO GLY ASN ASP THR PHE ASP ILE ASP PRO GLU ILE GLU SEQRES 15 D 561 THR ASP CYS PHE PHE VAL GLU PRO ASP GLU PRO PHE HIS SEQRES 16 D 561 ILE GLY THR PRO ALA GLU ASN LYS LEU ASN LEU THR LEU SEQRES 17 D 561 ASP PHE HIS ARG LEU LEU THR VAL GLU LEU GLN PHE LYS SEQRES 18 D 561 LEU LYS ALA ILE ASN LEU GLN THR VAL ARG HIS GLN GLU SEQRES 19 D 561 LEU PRO ASP CYS TYR ASP PHE THR LEU THR ILE THR PHE SEQRES 20 D 561 ASP ASN LYS ALA HIS SER GLY ARG ILE LYS ILE SER LEU SEQRES 21 D 561 ASP ASN ASP ILE SER ILE ARG GLU CYS LYS ASP TRP HIS SEQRES 22 D 561 VAL SER GLY SER ILE GLN LYS ASN THR HIS ASN MET MET SEQRES 23 D 561 ILE PHE ASP ALA PHE VAL ILE LEU THR CYS LEU VAL SER SEQRES 24 D 561 LEU ILE LEU CYS ILE ARG SER VAL ILE SER GLY LEU GLN SEQRES 25 D 561 LEU GLN GLN GLU PHE VAL ASN PHE PHE LEU LEU HIS TYR SEQRES 26 D 561 LYS LYS ASP VAL SER VAL SER ASP GLN MET GLU PHE VAL SEQRES 27 D 561 ASN GLY TRP TYR ILE MET ILE ILE ILE SER ASP ILE LEU SEQRES 28 D 561 THR ILE ILE GLY SER ILE LEU LYS MET GLU ILE GLN ALA SEQRES 29 D 561 LYS SER LEU THR SER TYR ASP VAL CYS SER ILE LEU LEU SEQRES 30 D 561 GLY THR SER THR MET LEU VAL TRP LEU GLY VAL ILE ARG SEQRES 31 D 561 TYR LEU GLY PHE PHE ALA LYS TYR ASN LEU LEU ILE LEU SEQRES 32 D 561 THR LEU GLN ALA ALA LEU PRO ASN VAL ILE ARG PHE CYS SEQRES 33 D 561 CYS CYS ALA ALA MET ILE TYR LEU GLY TYR CYS PHE CYS SEQRES 34 D 561 GLY TRP ILE VAL LEU GLY PRO TYR HIS ASN LYS PHE ARG SEQRES 35 D 561 SER LEU ASN MET VAL SER GLU CYS LEU PHE SER LEU ILE SEQRES 36 D 561 ASN GLY ASP ASP MET PHE ALA THR PHE ALA LYS MET GLN SEQRES 37 D 561 GLN LYS SER TYR LEU VAL TRP LEU PHE SER ARG ILE TYR SEQRES 38 D 561 LEU TYR SER PHE ILE SER LEU PHE ILE TYR MET ILE LEU SEQRES 39 D 561 SER LEU PHE ILE ALA LEU ILE THR ASP THR TYR GLU THR SEQRES 40 D 561 ILE LYS HIS TYR GLN GLN ASP GLY PHE PRO GLU THR GLU SEQRES 41 D 561 LEU ARG THR PHE ILE SER GLU CYS LYS ASP LEU PRO ASN SEQRES 42 D 561 SER GLY LYS PHE ARG LEU GLU ASP ASP PRO PRO VAL SER SEQRES 43 D 561 LEU PHE CYS CYS CYS LYS LYS SER ASN LEU GLU VAL LEU SEQRES 44 D 561 PHE GLN HET Y01 A 601 35 HET NA A 602 1 HET NA A 603 1 HET 3PE A 604 18 HET Y01 A 605 32 HET Y01 A 606 35 HET Y01 B 601 35 HET Y01 B 602 35 HET 3PE B 603 18 HET Y01 B 604 32 HET 3PE C 601 18 HET Y01 C 602 32 HET NA C 603 1 HET NA C 604 1 HET NA C 605 1 HET Y01 C 606 35 HET Y01 C 607 35 HET NA D 601 1 HET Y01 D 602 35 HET 3PE D 603 18 HET Y01 D 604 32 HET Y01 D 605 35 HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETNAM NA SODIUM ION HETNAM 3PE 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE HETSYN 3PE 3-SN-PHOSPHATIDYLETHANOLAMINE FORMUL 5 Y01 12(C31 H50 O4) FORMUL 6 NA 6(NA 1+) FORMUL 8 3PE 4(C41 H82 N O8 P) FORMUL 27 HOH *4(H2 O) HELIX 1 AA1 LEU A 33 MET A 47 1 15 HELIX 2 AA2 CYS A 50 ALA A 55 1 6 HELIX 3 AA3 PRO A 60 LEU A 103 1 44 HELIX 4 AA4 THR A 118 GLN A 135 1 18 HELIX 5 AA5 GLN A 135 SER A 140 1 6 HELIX 6 AA6 PRO A 170 ASP A 173 5 4 HELIX 7 AA7 ASN A 284 LYS A 326 1 43 HELIX 8 AA8 VAL A 331 VAL A 338 1 8 HELIX 9 AA9 ASN A 339 SER A 366 1 28 HELIX 10 AB1 ASP A 371 TYR A 391 1 21 HELIX 11 AB2 PHE A 395 GLY A 435 1 41 HELIX 12 AB3 SER A 443 ASN A 456 1 14 HELIX 13 AB4 MET A 460 LYS A 466 1 7 HELIX 14 AB5 SER A 471 MET A 492 1 22 HELIX 15 AB6 ILE A 493 GLY A 515 1 23 HELIX 16 AB7 LEU A 521 SER A 526 1 6 HELIX 17 AB8 LEU B 34 MET B 47 1 14 HELIX 18 AB9 CYS B 50 ALA B 55 1 6 HELIX 19 AC1 PRO B 60 LEU B 103 1 44 HELIX 20 AC2 THR B 118 GLN B 135 1 18 HELIX 21 AC3 GLN B 135 SER B 140 1 6 HELIX 22 AC4 PRO B 170 ASP B 173 5 4 HELIX 23 AC5 ASN B 284 LYS B 326 1 43 HELIX 24 AC6 VAL B 331 VAL B 338 1 8 HELIX 25 AC7 ASN B 339 SER B 366 1 28 HELIX 26 AC8 ASP B 371 TYR B 391 1 21 HELIX 27 AC9 PHE B 395 GLY B 435 1 41 HELIX 28 AD1 SER B 443 ASN B 456 1 14 HELIX 29 AD2 MET B 460 LYS B 466 1 7 HELIX 30 AD3 SER B 471 MET B 492 1 22 HELIX 31 AD4 ILE B 493 GLY B 515 1 23 HELIX 32 AD5 LEU B 521 SER B 526 1 6 HELIX 33 AD6 LEU C 34 MET C 47 1 14 HELIX 34 AD7 CYS C 50 ALA C 55 1 6 HELIX 35 AD8 PRO C 60 LEU C 103 1 44 HELIX 36 AD9 THR C 118 GLN C 135 1 18 HELIX 37 AE1 GLN C 135 SER C 140 1 6 HELIX 38 AE2 PRO C 170 ASP C 173 5 4 HELIX 39 AE3 ASN C 284 LYS C 326 1 43 HELIX 40 AE4 VAL C 331 VAL C 338 1 8 HELIX 41 AE5 ASN C 339 SER C 366 1 28 HELIX 42 AE6 ASP C 371 TYR C 391 1 21 HELIX 43 AE7 PHE C 395 GLY C 435 1 41 HELIX 44 AE8 SER C 443 ASN C 456 1 14 HELIX 45 AE9 MET C 460 LYS C 466 1 7 HELIX 46 AF1 SER C 471 MET C 492 1 22 HELIX 47 AF2 ILE C 493 GLY C 515 1 23 HELIX 48 AF3 LEU C 521 SER C 526 1 6 HELIX 49 AF4 LEU D 34 MET D 47 1 14 HELIX 50 AF5 CYS D 50 ALA D 55 1 6 HELIX 51 AF6 PRO D 60 LEU D 103 1 44 HELIX 52 AF7 THR D 118 GLN D 135 1 18 HELIX 53 AF8 GLN D 135 SER D 140 1 6 HELIX 54 AF9 PRO D 170 ASP D 173 5 4 HELIX 55 AG1 ASN D 284 LYS D 326 1 43 HELIX 56 AG2 VAL D 331 VAL D 338 1 8 HELIX 57 AG3 ASN D 339 SER D 366 1 28 HELIX 58 AG4 ASP D 371 TYR D 391 1 21 HELIX 59 AG5 PHE D 395 GLY D 435 1 41 HELIX 60 AG6 SER D 443 ASN D 456 1 14 HELIX 61 AG7 MET D 460 LYS D 466 1 7 HELIX 62 AG8 SER D 471 MET D 492 1 22 HELIX 63 AG9 ILE D 493 GLY D 515 1 23 HELIX 64 AH1 LEU D 521 SER D 526 1 6 SHEET 1 AA1 5 ALA A 115 VAL A 116 0 SHEET 2 AA1 5 ILE A 256 ARG A 267 -1 O ILE A 256 N VAL A 116 SHEET 3 AA1 5 CYS A 238 ASP A 248 -1 N THR A 246 O SER A 259 SHEET 4 AA1 5 THR A 215 ILE A 225 -1 N LEU A 222 O PHE A 241 SHEET 5 AA1 5 ALA A 145 TYR A 146 -1 N ALA A 145 O LYS A 223 SHEET 1 AA2 8 ALA A 115 VAL A 116 0 SHEET 2 AA2 8 ILE A 256 ARG A 267 -1 O ILE A 256 N VAL A 116 SHEET 3 AA2 8 CYS A 238 ASP A 248 -1 N THR A 246 O SER A 259 SHEET 4 AA2 8 THR A 215 ILE A 225 -1 N LEU A 222 O PHE A 241 SHEET 5 AA2 8 MET A 156 TYR A 169 -1 N ALA A 157 O GLN A 219 SHEET 6 AA2 8 THR A 174 VAL A 188 -1 O ASP A 176 N ASN A 167 SHEET 7 AA2 8 TRP C 272 VAL C 274 1 O HIS C 273 N PHE A 175 SHEET 8 AA2 8 SER C 277 GLN C 279 -1 O SER C 277 N VAL C 274 SHEET 1 AA3 8 SER A 277 GLN A 279 0 SHEET 2 AA3 8 TRP A 272 VAL A 274 -1 N VAL A 274 O SER A 277 SHEET 3 AA3 8 THR B 174 VAL B 188 1 O PHE B 175 N HIS A 273 SHEET 4 AA3 8 MET B 156 TYR B 169 -1 N ASN B 167 O ASP B 176 SHEET 5 AA3 8 THR B 215 ILE B 225 -1 O GLN B 219 N ALA B 157 SHEET 6 AA3 8 CYS B 238 ASP B 248 -1 O PHE B 241 N LEU B 222 SHEET 7 AA3 8 ILE B 256 ARG B 267 -1 O SER B 259 N THR B 246 SHEET 8 AA3 8 ALA B 115 VAL B 116 -1 N VAL B 116 O ILE B 256 SHEET 1 AA4 6 SER A 277 GLN A 279 0 SHEET 2 AA4 6 TRP A 272 VAL A 274 -1 N VAL A 274 O SER A 277 SHEET 3 AA4 6 THR B 174 VAL B 188 1 O PHE B 175 N HIS A 273 SHEET 4 AA4 6 MET B 156 TYR B 169 -1 N ASN B 167 O ASP B 176 SHEET 5 AA4 6 THR B 215 ILE B 225 -1 O GLN B 219 N ALA B 157 SHEET 6 AA4 6 ALA B 145 TYR B 146 -1 N ALA B 145 O LYS B 223 SHEET 1 AA5 8 SER B 277 GLN B 279 0 SHEET 2 AA5 8 TRP B 272 VAL B 274 -1 N VAL B 274 O SER B 277 SHEET 3 AA5 8 THR D 174 VAL D 188 1 O PHE D 175 N HIS B 273 SHEET 4 AA5 8 MET D 156 TYR D 169 -1 N ASN D 167 O ASP D 176 SHEET 5 AA5 8 THR D 215 ILE D 225 -1 O GLN D 219 N ALA D 157 SHEET 6 AA5 8 CYS D 238 ASP D 248 -1 O PHE D 241 N LEU D 222 SHEET 7 AA5 8 ILE D 256 ARG D 267 -1 O SER D 259 N THR D 246 SHEET 8 AA5 8 ALA D 115 VAL D 116 -1 N VAL D 116 O ILE D 256 SHEET 1 AA6 6 SER B 277 GLN B 279 0 SHEET 2 AA6 6 TRP B 272 VAL B 274 -1 N VAL B 274 O SER B 277 SHEET 3 AA6 6 THR D 174 VAL D 188 1 O PHE D 175 N HIS B 273 SHEET 4 AA6 6 MET D 156 TYR D 169 -1 N ASN D 167 O ASP D 176 SHEET 5 AA6 6 THR D 215 ILE D 225 -1 O GLN D 219 N ALA D 157 SHEET 6 AA6 6 ALA D 145 TYR D 146 -1 N ALA D 145 O LYS D 223 SHEET 1 AA7 5 ALA C 115 VAL C 116 0 SHEET 2 AA7 5 ILE C 256 ARG C 267 -1 O ILE C 256 N VAL C 116 SHEET 3 AA7 5 CYS C 238 ASP C 248 -1 N THR C 246 O SER C 259 SHEET 4 AA7 5 THR C 215 ILE C 225 -1 N LEU C 222 O PHE C 241 SHEET 5 AA7 5 ALA C 145 TYR C 146 -1 N ALA C 145 O LYS C 223 SHEET 1 AA8 8 ALA C 115 VAL C 116 0 SHEET 2 AA8 8 ILE C 256 ARG C 267 -1 O ILE C 256 N VAL C 116 SHEET 3 AA8 8 CYS C 238 ASP C 248 -1 N THR C 246 O SER C 259 SHEET 4 AA8 8 THR C 215 ILE C 225 -1 N LEU C 222 O PHE C 241 SHEET 5 AA8 8 MET C 156 TYR C 169 -1 N ALA C 157 O GLN C 219 SHEET 6 AA8 8 THR C 174 VAL C 188 -1 O ASP C 176 N ASN C 167 SHEET 7 AA8 8 TRP D 272 VAL D 274 1 O HIS D 273 N PHE C 175 SHEET 8 AA8 8 SER D 277 GLN D 279 -1 O SER D 277 N VAL D 274 SITE 1 AC1 6 ALA A 419 ALA A 420 TYR A 423 SER A 448 SITE 2 AC1 6 Y01 B 601 3PE C 601 SITE 1 AC2 2 NA C 603 NA C 604 SITE 1 AC3 1 Y01 B 602 SITE 1 AC4 6 CYS A 50 ILE A 67 ILE A 70 THR A 74 SITE 2 AC4 6 TRP A 385 TYR A 391 SITE 1 AC5 6 TYR A 472 TRP A 475 TYR A 483 SER A 487 SITE 2 AC5 6 ASN C 445 Y01 C 606 SITE 1 AC6 6 ASN A 445 Y01 A 601 TYR B 472 TRP B 475 SITE 2 AC6 6 ILE B 480 TYR B 483 SITE 1 AC7 6 3PE A 604 ALA B 419 ALA B 420 TYR B 423 SITE 2 AC7 6 SER B 448 Y01 D 602 SITE 1 AC8 1 Y01 D 605 SITE 1 AC9 7 CYS B 50 ILE B 67 ILE B 70 THR B 74 SITE 2 AC9 7 TRP B 385 VAL B 388 TYR B 391 SITE 1 AD1 1 Y01 A 601 SITE 1 AD2 7 CYS C 50 ILE C 67 ILE C 70 THR C 74 SITE 2 AD2 7 TRP C 385 VAL C 388 TYR C 391 SITE 1 AD3 1 NA A 602 SITE 1 AD4 2 NA A 602 NA C 605 SITE 1 AD5 1 NA C 604 SITE 1 AD6 6 Y01 A 606 ALA C 419 ALA C 420 TYR C 423 SITE 2 AD6 6 SER C 448 3PE D 603 SITE 1 AD7 6 TYR C 472 TRP C 475 ILE C 480 TYR C 483 SITE 2 AD7 6 ASN D 445 Y01 D 605 SITE 1 AD8 7 ASN B 445 Y01 B 602 TYR D 472 TRP D 475 SITE 2 AD8 7 ILE D 480 TYR D 483 SER D 487 SITE 1 AD9 1 Y01 C 606 SITE 1 AE1 7 CYS D 50 ILE D 67 ILE D 70 THR D 74 SITE 2 AE1 7 TRP D 385 VAL D 388 TYR D 391 SITE 1 AE2 7 3PE B 603 Y01 C 607 CYS D 416 ALA D 419 SITE 2 AE2 7 ALA D 420 TYR D 423 SER D 448 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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