HEADER STRUCTURAL PROTEIN/IMMUNE SYSTEM 16-OCT-24 9K1B TITLE CRYO-EM STRUCTURE OF HUMAN TAURINE TRANSPORTER TAUT BOUND WITH TAURINE TITLE 2 IN AN OCCLUDED STATE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SODIUM- AND CHLORIDE-DEPENDENT TAURINE TRANSPORTER; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SODIUM- AND CHLORIDE- DEPENDENT TAURINE TRANSPORTER TAUT, COMPND 5 SOLUTE CARRIER FAMILY 6 MEMBER 6; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: FRAGMENT ANTIGEN BINDING HEAVY CHAIN; COMPND 10 CHAIN: H; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: FRAGMENT ANTIGEN BINDING LIGHT CHAIN; COMPND 14 CHAIN: L; COMPND 15 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: SLC6A6; 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_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SUBSTRATE PROTEIN TRANSPORTER, STRUCTURAL PROTEIN/IMMUNE SYSTEM, KEYWDS 2 STRUCTURAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR B.DU,K.YAN REVDAT 1 20-AUG-25 9K1B 0 JRNL AUTH B.DU,K.YAN JRNL TITL MOLECULAR BASIS OF HUAMN TAURINE TRANSPORTER REUPTAKE AND JRNL TITL 2 INHIBITION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.34 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) : 3.340 REMARK 3 NUMBER OF PARTICLES : 192228 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 9K1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 18-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1300052273. 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 : HUMAN TAURINE TRANSPORTER REMARK 245 COMPLEX WITH TAURINE IN REMARK 245 OCCLUDED STATE 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 POLARA 300 REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 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) : 5000.00 REMARK 245 ILLUMINATION MODE : OTHER 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 THR A 3 REMARK 465 LYS A 4 REMARK 465 GLU A 5 REMARK 465 LYS A 6 REMARK 465 LEU A 7 REMARK 465 GLN A 8 REMARK 465 CYS A 9 REMARK 465 LEU A 10 REMARK 465 LYS A 11 REMARK 465 ASP A 12 REMARK 465 PHE A 13 REMARK 465 HIS A 14 REMARK 465 LYS A 15 REMARK 465 ASP A 16 REMARK 465 ILE A 17 REMARK 465 LEU A 18 REMARK 465 LYS A 19 REMARK 465 PRO A 20 REMARK 465 SER A 21 REMARK 465 PRO A 22 REMARK 465 GLY A 23 REMARK 465 LYS A 24 REMARK 465 SER A 25 REMARK 465 PRO A 26 REMARK 465 GLY A 27 REMARK 465 THR A 28 REMARK 465 ARG A 29 REMARK 465 PRO A 30 REMARK 465 GLU A 31 REMARK 465 ASP A 32 REMARK 465 GLU A 33 REMARK 465 ALA A 34 REMARK 465 GLU A 35 REMARK 465 GLY A 36 REMARK 465 LYS A 37 REMARK 465 LYS A 180 REMARK 465 SER A 181 REMARK 465 VAL A 182 REMARK 465 TRP A 183 REMARK 465 ILE A 184 REMARK 465 THR A 185 REMARK 465 ILE A 186 REMARK 465 SER A 187 REMARK 465 SER A 188 REMARK 465 PRO A 585 REMARK 465 ASN A 586 REMARK 465 ARG A 587 REMARK 465 TRP A 588 REMARK 465 ALA A 589 REMARK 465 VAL A 590 REMARK 465 GLU A 591 REMARK 465 ARG A 592 REMARK 465 GLU A 593 REMARK 465 GLY A 594 REMARK 465 ALA A 595 REMARK 465 THR A 596 REMARK 465 PRO A 597 REMARK 465 TYR A 598 REMARK 465 ASN A 599 REMARK 465 SER A 600 REMARK 465 ARG A 601 REMARK 465 THR A 602 REMARK 465 VAL A 603 REMARK 465 MET A 604 REMARK 465 ASN A 605 REMARK 465 GLY A 606 REMARK 465 ALA A 607 REMARK 465 LEU A 608 REMARK 465 VAL A 609 REMARK 465 LYS A 610 REMARK 465 PRO A 611 REMARK 465 THR A 612 REMARK 465 HIS A 613 REMARK 465 ILE A 614 REMARK 465 ILE A 615 REMARK 465 VAL A 616 REMARK 465 GLU A 617 REMARK 465 THR A 618 REMARK 465 MET A 619 REMARK 465 MET A 620 REMARK 465 GLY A 621 REMARK 465 SER A 622 REMARK 465 ASP A 623 REMARK 465 GLU A 624 REMARK 465 VAL A 625 REMARK 465 ASP A 626 REMARK 465 ALA A 627 REMARK 465 GLY A 628 REMARK 465 SER A 629 REMARK 465 HIS A 630 REMARK 465 HIS A 631 REMARK 465 HIS A 632 REMARK 465 HIS A 633 REMARK 465 HIS A 634 REMARK 465 HIS A 635 REMARK 465 HIS A 636 REMARK 465 HIS A 637 REMARK 465 HIS A 638 REMARK 465 HIS A 639 REMARK 465 GLY A 640 REMARK 465 SER A 641 REMARK 465 VAL A 642 REMARK 465 GLU A 643 REMARK 465 ASP A 644 REMARK 465 TYR A 645 REMARK 465 LYS A 646 REMARK 465 ASP A 647 REMARK 465 ASP A 648 REMARK 465 ASP A 649 REMARK 465 ASP A 650 REMARK 465 LYS A 651 REMARK 465 GLY L 108 REMARK 465 SER L 109 REMARK 465 ASP L 110 REMARK 465 GLU L 111 REMARK 465 VAL L 112 REMARK 465 ASP L 113 REMARK 465 ALA L 114 REMARK 465 GLY L 115 REMARK 465 SER L 116 REMARK 465 HIS L 117 REMARK 465 HIS L 118 REMARK 465 HIS L 119 REMARK 465 HIS L 120 REMARK 465 HIS L 121 REMARK 465 HIS L 122 REMARK 465 HIS L 123 REMARK 465 HIS L 124 REMARK 465 HIS L 125 REMARK 465 HIS L 126 REMARK 465 GLY L 127 REMARK 465 SER L 128 REMARK 465 VAL L 129 REMARK 465 GLU L 130 REMARK 465 ASP L 131 REMARK 465 TYR L 132 REMARK 465 LYS L 133 REMARK 465 ASP L 134 REMARK 465 ASP L 135 REMARK 465 ASP L 136 REMARK 465 ASP L 137 REMARK 465 LYS L 138 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 GLN A 40 CG CD OE1 NE2 REMARK 470 GLU A 42 CG CD OE1 OE2 REMARK 470 PHE A 150 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE A 153 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 155 CG CD CE NZ REMARK 470 GLU A 156 CG CD OE1 OE2 REMARK 470 HIS A 161 CG ND1 CD2 CE1 NE2 REMARK 470 ASN A 163 CG OD1 ND2 REMARK 470 HIS A 170 CG ND1 CD2 CE1 NE2 REMARK 470 MET A 172 CG SD CE REMARK 470 GLU A 173 CG CD OE1 OE2 REMARK 470 ASP A 174 CG OD1 OD2 REMARK 470 THR A 175 OG1 CG2 REMARK 470 MET A 176 CG SD CE REMARK 470 LYS A 178 CG CD CE NZ REMARK 470 ASN A 179 CG OD1 ND2 REMARK 470 ASN A 190 CG OD1 ND2 REMARK 470 LEU A 216 CG CD1 CD2 REMARK 470 LYS A 217 CG CD CE NZ REMARK 470 ASP A 219 CG OD1 OD2 REMARK 470 LYS A 237 CG CD CE NZ REMARK 470 VAL A 239 CG1 CG2 REMARK 470 ARG A 240 CG CD NE CZ NH1 NH2 REMARK 470 THR A 242 OG1 CG2 REMARK 470 LYS A 244 CG CD CE NZ REMARK 470 TYR A 247 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 PHE A 248 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 260 CG CD1 CD2 REMARK 470 TYR A 279 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASP A 281 CG OD1 OD2 REMARK 470 ARG A 284 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 286 CG CD OE1 OE2 REMARK 470 ASP A 287 CG OD1 OD2 REMARK 470 GLN A 289 CG CD OE1 NE2 REMARK 470 LYS A 317 CG CD CE NZ REMARK 470 ARG A 324 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 325 CG OD1 OD2 REMARK 470 ASP A 358 CG OD1 OD2 REMARK 470 GLU A 364 CG CD OE1 OE2 REMARK 470 LEU A 383 CG CD1 CD2 REMARK 470 GLU A 408 CG CD OE1 OE2 REMARK 470 PHE A 421 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 423 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 424 CG CD CE NZ REMARK 470 TYR A 426 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 427 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 429 CG CD OE1 OE2 REMARK 470 PHE A 434 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER A 464 OG REMARK 470 PHE A 498 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 505 CG CD CE NZ REMARK 470 LYS A 526 CG CD CE NZ REMARK 470 LYS A 534 CG CD CE NZ REMARK 470 GLN A 567 CG CD OE1 NE2 REMARK 470 GLU A 569 CG CD OE1 OE2 REMARK 470 PHE A 572 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 575 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 577 CG CD CE NZ REMARK 470 ARG A 583 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 1 CG CD OE1 OE2 REMARK 470 SER H 7 OG REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 19 CG CD CE NZ REMARK 470 SER H 25 OG REMARK 470 GLU H 42 CG CD OE1 OE2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 ARG H 44 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 46 CG CD OE1 OE2 REMARK 470 ASP H 62 CG OD1 OD2 REMARK 470 ASP H 73 CG OD1 OD2 REMARK 470 ARG H 76 CG CD NE CZ NH1 NH2 REMARK 470 ASN H 77 CG OD1 ND2 REMARK 470 GLU H 82 CG CD OE1 OE2 REMARK 470 MET H 83 CG SD CE REMARK 470 ARG H 87 CG CD NE CZ NH1 NH2 REMARK 470 SER H 88 OG REMARK 470 GLU H 89 CG CD OE1 OE2 REMARK 470 ASP H 90 CG OD1 OD2 REMARK 470 GLN H 111 CG CD OE1 NE2 REMARK 470 GLU L 1 CG CD OE1 OE2 REMARK 470 THR L 5 OG1 CG2 REMARK 470 SER L 7 OG REMARK 470 ILE L 10 CG1 CG2 CD1 REMARK 470 SER L 12 OG REMARK 470 SER L 14 OG REMARK 470 GLU L 17 CG CD OE1 OE2 REMARK 470 LYS L 18 CG CD CE NZ REMARK 470 THR L 20 OG1 CG2 REMARK 470 THR L 22 OG1 CG2 REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 SER L 26 OG REMARK 470 SER L 27 OG REMARK 470 SER L 28 OG REMARK 470 LYS L 40 CG CD CE NZ REMARK 470 SER L 41 OG REMARK 470 LYS L 46 CG CD CE NZ REMARK 470 ARG L 62 CG CD NE CZ NH1 NH2 REMARK 470 SER L 68 OG REMARK 470 THR L 70 OG1 CG2 REMARK 470 SER L 77 OG REMARK 470 GLU L 80 CG CD OE1 OE2 REMARK 470 GLU L 82 CG CD OE1 OE2 REMARK 470 ASP L 83 CG OD1 OD2 REMARK 470 SER L 101 OG REMARK 470 LYS L 104 CG CD CE NZ REMARK 470 LEU L 105 CG CD1 CD2 REMARK 470 GLU L 106 CG CD OE1 OE2 REMARK 470 MET L 107 CG SD CE 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 58 O1 TAU A 701 2.02 REMARK 500 NH2 ARG H 98 OD2 ASP H 107 2.16 REMARK 500 REMARK 500 REMARK: NULL 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 VAL A 562 CG1 - CB - CG2 ANGL. DEV. = 10.9 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 ILE A 116 -60.26 -95.56 REMARK 500 PHE A 120 30.13 -95.80 REMARK 500 MET A 380 32.21 -98.99 REMARK 500 LEU A 383 70.02 50.21 REMARK 500 ALA A 463 14.80 59.59 REMARK 500 SER A 464 27.84 -140.14 REMARK 500 VAL A 510 -54.06 -124.52 REMARK 500 LYS A 534 14.07 56.62 REMARK 500 ARG H 98 58.08 -96.07 REMARK 500 PRO L 15 41.75 -78.39 REMARK 500 THR L 52 -16.87 71.26 REMARK 500 SER L 53 -7.02 -147.82 REMARK 500 ALA L 56 -179.47 -68.52 REMARK 500 ALA L 61 -2.24 71.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 702 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY A 56 O REMARK 620 2 VAL A 59 O 100.3 REMARK 620 3 LEU A 398 O 146.7 105.9 REMARK 620 4 SER A 402 OG 77.5 121.1 105.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 703 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN A 63 OD1 REMARK 620 2 SER A 301 O 153.1 REMARK 620 3 SER A 301 OG 84.1 88.1 REMARK 620 4 ASN A 333 OD1 84.5 122.0 96.0 REMARK 620 N 1 2 3 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-61970 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HUMAN TAURINE TRANSPORTER TAUT BOUND WITH REMARK 900 TAURINE IN AN OCCLUDED STATE DBREF 9K1B A 1 620 UNP P31641 SC6A6_HUMAN 1 620 DBREF 9K1B H 1 118 PDB 9K1B 9K1B 1 118 DBREF 9K1B L 1 138 PDB 9K1B 9K1B 1 138 SEQADV 9K1B HIS A 319 UNP P31641 LYS 319 ENGINEERED MUTATION SEQADV 9K1B ASN A 320 UNP P31641 TYR 320 ENGINEERED MUTATION SEQADV 9K1B VAL A 322 UNP P31641 SER 322 ENGINEERED MUTATION SEQADV 9K1B ASN A 486 UNP P31641 ASP 486 ENGINEERED MUTATION SEQADV 9K1B ARG A 487 UNP P31641 ASN 487 ENGINEERED MUTATION SEQADV 9K1B PHE A 488 UNP P31641 LEU 488 ENGINEERED MUTATION SEQADV 9K1B SER A 489 UNP P31641 TYR 489 ENGINEERED MUTATION SEQADV 9K1B GLU A 490 UNP P31641 ASP 490 ENGINEERED MUTATION SEQADV 9K1B ASP A 491 UNP P31641 GLY 491 ENGINEERED MUTATION SEQADV 9K1B ARG A 493 UNP P31641 GLU 493 ENGINEERED MUTATION SEQADV 9K1B PHE A 498 UNP P31641 TYR 498 ENGINEERED MUTATION SEQADV 9K1B PRO A 499 UNP P31641 ARG 499 ENGINEERED MUTATION SEQADV 9K1B GLY A 621 UNP P31641 EXPRESSION TAG SEQADV 9K1B SER A 622 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 623 UNP P31641 EXPRESSION TAG SEQADV 9K1B GLU A 624 UNP P31641 EXPRESSION TAG SEQADV 9K1B VAL A 625 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 626 UNP P31641 EXPRESSION TAG SEQADV 9K1B ALA A 627 UNP P31641 EXPRESSION TAG SEQADV 9K1B GLY A 628 UNP P31641 EXPRESSION TAG SEQADV 9K1B SER A 629 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 630 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 631 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 632 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 633 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 634 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 635 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 636 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 637 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 638 UNP P31641 EXPRESSION TAG SEQADV 9K1B HIS A 639 UNP P31641 EXPRESSION TAG SEQADV 9K1B GLY A 640 UNP P31641 EXPRESSION TAG SEQADV 9K1B SER A 641 UNP P31641 EXPRESSION TAG SEQADV 9K1B VAL A 642 UNP P31641 EXPRESSION TAG SEQADV 9K1B GLU A 643 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 644 UNP P31641 EXPRESSION TAG SEQADV 9K1B TYR A 645 UNP P31641 EXPRESSION TAG SEQADV 9K1B LYS A 646 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 647 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 648 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 649 UNP P31641 EXPRESSION TAG SEQADV 9K1B ASP A 650 UNP P31641 EXPRESSION TAG SEQADV 9K1B LYS A 651 UNP P31641 EXPRESSION TAG SEQRES 1 A 651 MET ALA THR LYS GLU LYS LEU GLN CYS LEU LYS ASP PHE SEQRES 2 A 651 HIS LYS ASP ILE LEU LYS PRO SER PRO GLY LYS SER PRO SEQRES 3 A 651 GLY THR ARG PRO GLU ASP GLU ALA GLU GLY LYS PRO PRO SEQRES 4 A 651 GLN ARG GLU LYS TRP SER SER LYS ILE ASP PHE VAL LEU SEQRES 5 A 651 SER VAL ALA GLY GLY PHE VAL GLY LEU GLY ASN VAL TRP SEQRES 6 A 651 ARG PHE PRO TYR LEU CYS TYR LYS ASN GLY GLY GLY ALA SEQRES 7 A 651 PHE LEU ILE PRO TYR PHE ILE PHE LEU PHE GLY SER GLY SEQRES 8 A 651 LEU PRO VAL PHE PHE LEU GLU ILE ILE ILE GLY GLN TYR SEQRES 9 A 651 THR SER GLU GLY GLY ILE THR CYS TRP GLU LYS ILE CYS SEQRES 10 A 651 PRO LEU PHE SER GLY ILE GLY TYR ALA SER VAL VAL ILE SEQRES 11 A 651 VAL SER LEU LEU ASN VAL TYR TYR ILE VAL ILE LEU ALA SEQRES 12 A 651 TRP ALA THR TYR TYR LEU PHE GLN SER PHE GLN LYS GLU SEQRES 13 A 651 LEU PRO TRP ALA HIS CYS ASN HIS SER TRP ASN THR PRO SEQRES 14 A 651 HIS CYS MET GLU ASP THR MET ARG LYS ASN LYS SER VAL SEQRES 15 A 651 TRP ILE THR ILE SER SER THR ASN PHE THR SER PRO VAL SEQRES 16 A 651 ILE GLU PHE TRP GLU ARG ASN VAL LEU SER LEU SER PRO SEQRES 17 A 651 GLY ILE ASP HIS PRO GLY SER LEU LYS TRP ASP LEU ALA SEQRES 18 A 651 LEU CYS LEU LEU LEU VAL TRP LEU VAL CYS PHE PHE CYS SEQRES 19 A 651 ILE TRP LYS GLY VAL ARG SER THR GLY LYS VAL VAL TYR SEQRES 20 A 651 PHE THR ALA THR PHE PRO PHE ALA MET LEU LEU VAL LEU SEQRES 21 A 651 LEU VAL ARG GLY LEU THR LEU PRO GLY ALA GLY ALA GLY SEQRES 22 A 651 ILE LYS PHE TYR LEU TYR PRO ASP ILE THR ARG LEU GLU SEQRES 23 A 651 ASP PRO GLN VAL TRP ILE ASP ALA GLY THR GLN ILE PHE SEQRES 24 A 651 PHE SER TYR ALA ILE CYS LEU GLY ALA MET THR SER LEU SEQRES 25 A 651 GLY SER TYR ASN LYS TYR HIS ASN ASN VAL TYR ARG ASP SEQRES 26 A 651 CYS MET LEU LEU GLY CYS LEU ASN SER GLY THR SER PHE SEQRES 27 A 651 VAL SER GLY PHE ALA ILE PHE SER ILE LEU GLY PHE MET SEQRES 28 A 651 ALA GLN GLU GLN GLY VAL ASP ILE ALA ASP VAL ALA GLU SEQRES 29 A 651 SER GLY PRO GLY LEU ALA PHE ILE ALA TYR PRO LYS ALA SEQRES 30 A 651 VAL THR MET MET PRO LEU PRO THR PHE TRP SER ILE LEU SEQRES 31 A 651 PHE PHE ILE MET LEU LEU LEU LEU GLY LEU ASP SER GLN SEQRES 32 A 651 PHE VAL GLU VAL GLU GLY GLN ILE THR SER LEU VAL ASP SEQRES 33 A 651 LEU TYR PRO SER PHE LEU ARG LYS GLY TYR ARG ARG GLU SEQRES 34 A 651 ILE PHE ILE ALA PHE VAL CYS SER ILE SER TYR LEU LEU SEQRES 35 A 651 GLY LEU THR MET VAL THR GLU GLY GLY MET TYR VAL PHE SEQRES 36 A 651 GLN LEU PHE ASP TYR TYR ALA ALA SER GLY VAL CYS LEU SEQRES 37 A 651 LEU TRP VAL ALA PHE PHE GLU CYS PHE VAL ILE ALA TRP SEQRES 38 A 651 ILE TYR GLY GLY ASN ARG PHE SER GLU ASP ILE ARG ASP SEQRES 39 A 651 MET ILE GLY PHE PRO PRO GLY PRO TRP MET LYS TYR SER SEQRES 40 A 651 TRP ALA VAL ILE THR PRO VAL LEU CYS VAL GLY CYS PHE SEQRES 41 A 651 ILE PHE SER LEU VAL LYS TYR VAL PRO LEU THR TYR ASN SEQRES 42 A 651 LYS THR TYR VAL TYR PRO ASN TRP ALA ILE GLY LEU GLY SEQRES 43 A 651 TRP SER LEU ALA LEU SER SER MET LEU CYS VAL PRO LEU SEQRES 44 A 651 VAL ILE VAL ILE ARG LEU CYS GLN THR GLU GLY PRO PHE SEQRES 45 A 651 LEU VAL ARG VAL LYS TYR LEU LEU THR PRO ARG GLU PRO SEQRES 46 A 651 ASN ARG TRP ALA VAL GLU ARG GLU GLY ALA THR PRO TYR SEQRES 47 A 651 ASN SER ARG THR VAL MET ASN GLY ALA LEU VAL LYS PRO SEQRES 48 A 651 THR HIS ILE ILE VAL GLU THR MET MET GLY SER ASP GLU SEQRES 49 A 651 VAL ASP ALA GLY SER HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 50 A 651 HIS HIS GLY SER VAL GLU ASP TYR LYS ASP ASP ASP ASP SEQRES 51 A 651 LYS SEQRES 1 H 118 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 118 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 118 PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 118 SER PRO GLU LYS ARG LEU GLU TRP VAL ALA GLU ILE SER SEQRES 5 H 118 SER GLY GLY ARG TYR ILE TYR TYR SER ASP THR VAL THR SEQRES 6 H 118 GLY ARG PHE THR ILE SER ARG ASP ASN ALA ARG ASN ILE SEQRES 7 H 118 LEU HIS LEU GLU MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 118 ALA MET TYR TYR CYS ALA ARG GLY GLU VAL ARG GLN ARG SEQRES 9 H 118 GLY PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SEQRES 10 H 118 SER SEQRES 1 L 138 GLU ASN VAL LEU THR GLN SER PRO ALA ILE MET SER THR SEQRES 2 L 138 SER PRO GLY GLU LYS VAL THR MET THR CYS ARG ALA SER SEQRES 3 L 138 SER SER VAL GLY SER SER TYR LEU HIS TRP TYR GLN GLN SEQRES 4 L 138 LYS SER GLY ALA SER PRO LYS LEU TRP ILE TYR SER THR SEQRES 5 L 138 SER ASN LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SEQRES 6 L 138 SER GLY SER GLY THR SER TYR SER LEU THR ILE SER SER SEQRES 7 L 138 VAL GLU ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 138 PHE SER GLY TYR PRO LEU THR PHE GLY SER GLY THR LYS SEQRES 9 L 138 LEU GLU MET GLY SER ASP GLU VAL ASP ALA GLY SER HIS SEQRES 10 L 138 HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY SER VAL GLU SEQRES 11 L 138 ASP TYR LYS ASP ASP ASP ASP LYS HET TAU A 701 7 HET NA A 702 1 HET NA A 703 1 HET CL A 704 1 HETNAM TAU 2-AMINOETHANESULFONIC ACID HETNAM NA SODIUM ION HETNAM CL CHLORIDE ION FORMUL 4 TAU C2 H7 N O3 S FORMUL 5 NA 2(NA 1+) FORMUL 7 CL CL 1- HELIX 1 AA1 SER A 46 VAL A 59 1 14 HELIX 2 AA2 GLY A 60 TRP A 65 1 6 HELIX 3 AA3 TRP A 65 ASN A 74 1 10 HELIX 4 AA4 GLY A 75 ALA A 78 5 4 HELIX 5 AA5 PHE A 79 THR A 105 1 27 HELIX 6 AA6 CYS A 112 CYS A 117 1 6 HELIX 7 AA7 PRO A 118 PHE A 120 5 3 HELIX 8 AA8 SER A 121 PHE A 153 1 33 HELIX 9 AA9 LEU A 157 HIS A 161 5 5 HELIX 10 AB1 GLU A 173 LYS A 178 1 6 HELIX 11 AB2 SER A 193 VAL A 203 1 11 HELIX 12 AB3 LYS A 217 TRP A 236 1 20 HELIX 13 AB4 LYS A 244 ALA A 250 1 7 HELIX 14 AB5 THR A 251 THR A 266 1 16 HELIX 15 AB6 GLY A 269 TYR A 279 1 11 HELIX 16 AB7 ASP A 281 ASP A 287 5 7 HELIX 17 AB8 PRO A 288 ALA A 303 1 16 HELIX 18 AB9 GLY A 307 TYR A 315 1 9 HELIX 19 AC1 VAL A 322 GLY A 356 1 35 HELIX 20 AC2 ASP A 358 VAL A 362 5 5 HELIX 21 AC3 GLY A 368 THR A 379 1 12 HELIX 22 AC4 LEU A 383 ASP A 416 1 34 HELIX 23 AC5 GLY A 425 LEU A 444 1 20 HELIX 24 AC6 THR A 445 VAL A 447 5 3 HELIX 25 AC7 GLY A 450 ALA A 462 1 13 HELIX 26 AC8 GLY A 465 ILE A 482 1 18 HELIX 27 AC9 GLY A 484 GLY A 497 1 14 HELIX 28 AD1 GLY A 501 VAL A 510 1 10 HELIX 29 AD2 VAL A 510 LYS A 526 1 17 HELIX 30 AD3 PRO A 539 LEU A 555 1 17 HELIX 31 AD4 LEU A 555 GLN A 567 1 13 HELIX 32 AD5 PRO A 571 LEU A 580 1 10 HELIX 33 AD6 ASN H 74 ARG H 76 5 3 HELIX 34 AD7 ARG H 87 THR H 91 5 5 HELIX 35 AD8 GLY L 30 SER L 32 5 3 SHEET 1 AA1 2 THR A 531 TYR A 532 0 SHEET 2 AA1 2 TYR A 536 VAL A 537 -1 O TYR A 536 N TYR A 532 SHEET 1 AA2 4 GLN H 3 SER H 7 0 SHEET 2 AA2 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA2 4 ILE H 78 MET H 83 -1 O LEU H 79 N CYS H 22 SHEET 4 AA2 4 PHE H 68 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AA3 6 LEU H 11 VAL H 12 0 SHEET 2 AA3 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12 SHEET 3 AA3 6 ALA H 92 ALA H 97 -1 N TYR H 94 O THR H 113 SHEET 4 AA3 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA3 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AA3 6 ILE H 58 TYR H 60 -1 O TYR H 59 N GLU H 50 SHEET 1 AA4 4 LEU L 4 GLN L 6 0 SHEET 2 AA4 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA4 4 SER L 71 ILE L 76 -1 O LEU L 74 N MET L 21 SHEET 4 AA4 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA5 6 ILE L 10 SER L 12 0 SHEET 2 AA5 6 THR L 103 GLU L 106 1 O LYS L 104 N MET L 11 SHEET 3 AA5 6 ALA L 85 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA5 6 LEU L 34 GLN L 39 -1 N HIS L 35 O GLN L 90 SHEET 5 AA5 6 LYS L 46 TYR L 50 -1 O LYS L 46 N GLN L 38 SHEET 6 AA5 6 ASN L 54 LEU L 55 -1 O ASN L 54 N TYR L 50 SHEET 1 AA6 4 ILE L 10 SER L 12 0 SHEET 2 AA6 4 THR L 103 GLU L 106 1 O LYS L 104 N MET L 11 SHEET 3 AA6 4 ALA L 85 GLN L 91 -1 N TYR L 87 O THR L 103 SHEET 4 AA6 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SSBOND 1 CYS A 162 CYS A 171 1555 1555 2.03 SSBOND 2 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.03 LINK O GLY A 56 NA NA A 702 1555 1555 2.74 LINK O VAL A 59 NA NA A 702 1555 1555 2.06 LINK OD1 ASN A 63 NA NA A 703 1555 1555 2.45 LINK O SER A 301 NA NA A 703 1555 1555 2.54 LINK OG SER A 301 NA NA A 703 1555 1555 2.01 LINK OD1 ASN A 333 NA NA A 703 1555 1555 2.84 LINK O LEU A 398 NA NA A 702 1555 1555 2.81 LINK OG SER A 402 NA NA A 702 1555 1555 1.94 CISPEP 1 TYR L 95 PRO L 96 0 -2.41 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