HEADER TRANSPORT PROTEIN 12-JAN-24 8XTX TITLE STRUCTURE OF A PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: GREEN FLUORESCENT PROTEIN,VESICULAR ACETYLCHOLINE COMPND 3 TRANSPORTER,ANTIBODY; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: VACHT,SOLUTE CARRIER FAMILY 18 MEMBER 3; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AEQUOREA VICTORIA, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 6100, 9606; SOURCE 5 GENE: GFP, SLC18A3, VACHT; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F KEYWDS TRANSPORTER, MEMBRANE PROTEIN, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR Y.ZHAO,Q.MA,Y.DONG,Y.MENG REVDAT 1 25-DEC-24 8XTX 0 JRNL AUTH Y.ZHAO,Q.MA,Y.DONG,Y.MENG JRNL TITL STRUCTURE OF A PROTEIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.40 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) : 3.400 REMARK 3 NUMBER OF PARTICLES : 115468 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8XTX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300044174. 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 : TRANSPORTER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 6000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 -202 REMARK 465 SER A -201 REMARK 465 LYS A -200 REMARK 465 GLY A -199 REMARK 465 GLU A -198 REMARK 465 GLU A -197 REMARK 465 LEU A -196 REMARK 465 PHE A -195 REMARK 465 THR A -194 REMARK 465 GLY A -193 REMARK 465 VAL A -192 REMARK 465 VAL A -191 REMARK 465 PRO A -190 REMARK 465 ILE A -189 REMARK 465 LEU A -188 REMARK 465 VAL A -187 REMARK 465 GLU A -186 REMARK 465 LEU A -185 REMARK 465 ASP A -184 REMARK 465 GLY A -183 REMARK 465 ASP A -182 REMARK 465 VAL A -181 REMARK 465 ASN A -180 REMARK 465 GLY A -179 REMARK 465 HIS A -178 REMARK 465 LYS A -177 REMARK 465 PHE A -176 REMARK 465 SER A -175 REMARK 465 VAL A -174 REMARK 465 ARG A -173 REMARK 465 GLY A -172 REMARK 465 GLU A -171 REMARK 465 GLY A -170 REMARK 465 GLU A -169 REMARK 465 GLY A -168 REMARK 465 ASP A -167 REMARK 465 ALA A -166 REMARK 465 THR A -165 REMARK 465 ASN A -164 REMARK 465 GLY A -163 REMARK 465 LYS A -162 REMARK 465 LEU A -161 REMARK 465 THR A -160 REMARK 465 LEU A -159 REMARK 465 LYS A -158 REMARK 465 PHE A -157 REMARK 465 ILE A -156 REMARK 465 CYS A -155 REMARK 465 THR A -154 REMARK 465 THR A -153 REMARK 465 GLY A -152 REMARK 465 LYS A -151 REMARK 465 LEU A -150 REMARK 465 PRO A -149 REMARK 465 VAL A -148 REMARK 465 PRO A -147 REMARK 465 TRP A -146 REMARK 465 PRO A -145 REMARK 465 THR A -144 REMARK 465 LEU A -143 REMARK 465 VAL A -142 REMARK 465 THR A -141 REMARK 465 THR A -140 REMARK 465 LEU A -139 REMARK 465 THR A -138 REMARK 465 TYR A -137 REMARK 465 GLY A -136 REMARK 465 VAL A -135 REMARK 465 GLN A -134 REMARK 465 CYS A -133 REMARK 465 PHE A -132 REMARK 465 SER A -131 REMARK 465 ARG A -130 REMARK 465 TYR A -129 REMARK 465 PRO A -128 REMARK 465 ASP A -127 REMARK 465 HIS A -126 REMARK 465 MET A -125 REMARK 465 LYS A -124 REMARK 465 ARG A -123 REMARK 465 HIS A -122 REMARK 465 ASP A -121 REMARK 465 PHE A -120 REMARK 465 PHE A -119 REMARK 465 LYS A -118 REMARK 465 SER A -117 REMARK 465 ALA A -116 REMARK 465 MET A -115 REMARK 465 PRO A -114 REMARK 465 GLU A -113 REMARK 465 GLY A -112 REMARK 465 TYR A -111 REMARK 465 VAL A -110 REMARK 465 GLN A -109 REMARK 465 GLU A -108 REMARK 465 ARG A -107 REMARK 465 THR A -106 REMARK 465 ILE A -105 REMARK 465 SER A -104 REMARK 465 PHE A -103 REMARK 465 LYS A -102 REMARK 465 ASP A -101 REMARK 465 ASP A -100 REMARK 465 GLY A -99 REMARK 465 THR A -98 REMARK 465 TYR A -97 REMARK 465 LYS A -96 REMARK 465 THR A -95 REMARK 465 ARG A -94 REMARK 465 ALA A -93 REMARK 465 GLU A -92 REMARK 465 VAL A -91 REMARK 465 LYS A -90 REMARK 465 PHE A -89 REMARK 465 GLU A -88 REMARK 465 GLY A -87 REMARK 465 ASP A -86 REMARK 465 THR A -85 REMARK 465 LEU A -84 REMARK 465 VAL A -83 REMARK 465 ASN A -82 REMARK 465 ARG A -81 REMARK 465 ILE A -80 REMARK 465 GLU A -79 REMARK 465 LEU A -78 REMARK 465 LYS A -77 REMARK 465 GLY A -76 REMARK 465 ILE A -75 REMARK 465 ASP A -74 REMARK 465 PHE A -73 REMARK 465 LYS A -72 REMARK 465 GLU A -71 REMARK 465 ASP A -70 REMARK 465 GLY A -69 REMARK 465 ASN A -68 REMARK 465 ILE A -67 REMARK 465 LEU A -66 REMARK 465 GLY A -65 REMARK 465 HIS A -64 REMARK 465 LYS A -63 REMARK 465 LEU A -62 REMARK 465 GLU A -61 REMARK 465 TYR A -60 REMARK 465 ASN A -59 REMARK 465 PHE A -58 REMARK 465 ASN A -57 REMARK 465 SER A -56 REMARK 465 HIS A -55 REMARK 465 ASN A -54 REMARK 465 VAL A -53 REMARK 465 TYR A -52 REMARK 465 ILE A -51 REMARK 465 THR A -50 REMARK 465 ALA A -49 REMARK 465 ASP A -48 REMARK 465 LYS A -47 REMARK 465 GLN A -46 REMARK 465 LYS A -45 REMARK 465 ASN A -44 REMARK 465 GLY A -43 REMARK 465 ILE A -42 REMARK 465 LYS A -41 REMARK 465 ALA A -40 REMARK 465 ASN A -39 REMARK 465 PHE A -38 REMARK 465 LYS A -37 REMARK 465 ILE A -36 REMARK 465 ARG A -35 REMARK 465 HIS A -34 REMARK 465 ASN A -33 REMARK 465 VAL A -32 REMARK 465 GLU A -31 REMARK 465 ASP A -30 REMARK 465 GLY A -29 REMARK 465 SER A -28 REMARK 465 VAL A -27 REMARK 465 GLN A -26 REMARK 465 LEU A -25 REMARK 465 ALA A -24 REMARK 465 ASP A -23 REMARK 465 HIS A -22 REMARK 465 TYR A -21 REMARK 465 GLN A -20 REMARK 465 GLN A -19 REMARK 465 ASN A -18 REMARK 465 THR A -17 REMARK 465 PRO A -16 REMARK 465 ILE A -15 REMARK 465 GLY A -14 REMARK 465 ASP A -13 REMARK 465 GLY A -12 REMARK 465 PRO A -11 REMARK 465 VAL A -10 REMARK 465 LEU A -9 REMARK 465 LEU A -8 REMARK 465 PRO A -7 REMARK 465 ASP A -6 REMARK 465 ASN A -5 REMARK 465 HIS A -4 REMARK 465 TYR A -3 REMARK 465 LEU A -2 REMARK 465 SER A -1 REMARK 465 THR A 0 REMARK 465 GLN A 1 REMARK 465 SER A 2 REMARK 465 VAL A 3 REMARK 465 LEU A 4 REMARK 465 SER A 5 REMARK 465 LYS A 6 REMARK 465 ASP A 7 REMARK 465 PRO A 8 REMARK 465 ASN A 9 REMARK 465 GLU A 10 REMARK 465 LYS A 11 REMARK 465 ARG A 12 REMARK 465 ASP A 13 REMARK 465 HIS A 14 REMARK 465 MET A 15 REMARK 465 VAL A 16 REMARK 465 LEU A 17 REMARK 465 LEU A 18 REMARK 465 GLU A 19 REMARK 465 PHE A 20 REMARK 465 VAL A 21 REMARK 465 THR A 22 REMARK 465 ALA A 23 REMARK 465 ALA A 24 REMARK 465 GLY A 25 REMARK 465 ILE A 26 REMARK 465 GLU A 27 REMARK 465 PRO A 28 REMARK 465 ARG A 29 REMARK 465 HIS A 63 REMARK 465 MET A 64 REMARK 465 ARG A 65 REMARK 465 GLY A 66 REMARK 465 GLY A 67 REMARK 465 GLY A 68 REMARK 465 GLU A 69 REMARK 465 GLY A 70 REMARK 465 PRO A 71 REMARK 465 THR A 72 REMARK 465 ARG A 73 REMARK 465 THR A 74 REMARK 465 PRO A 75 REMARK 465 GLU A 76 REMARK 465 VAL A 77 REMARK 465 TRP A 78 REMARK 465 GLU A 79 REMARK 465 PRO A 80 REMARK 465 THR A 81 REMARK 465 LEU A 82 REMARK 465 PRO A 83 REMARK 465 LEU A 84 REMARK 465 PRO A 85 REMARK 465 THR A 86 REMARK 465 PRO A 87 REMARK 465 ALA A 88 REMARK 465 ASN A 89 REMARK 465 ALA A 90 REMARK 465 SER A 91 REMARK 465 ALA A 92 REMARK 465 TYR A 93 REMARK 465 THR A 94 REMARK 465 ALA A 95 REMARK 465 ASN A 96 REMARK 465 THR A 97 REMARK 465 SER A 98 REMARK 465 ALA A 99 REMARK 465 SER A 100 REMARK 465 PRO A 101 REMARK 465 THR A 102 REMARK 465 ALA A 103 REMARK 465 ALA A 104 REMARK 465 TRP A 105 REMARK 465 PRO A 106 REMARK 465 ALA A 107 REMARK 465 GLY A 108 REMARK 465 SER A 109 REMARK 465 ALA A 110 REMARK 465 LEU A 111 REMARK 465 ARG A 112 REMARK 465 PRO A 113 REMARK 465 ARG A 114 REMARK 465 TYR A 115 REMARK 465 PRO A 116 REMARK 465 THR A 117 REMARK 465 GLU A 118 REMARK 465 SER A 119 REMARK 465 ALA A 269 REMARK 465 ALA A 270 REMARK 465 ARG A 271 REMARK 465 ALA A 272 REMARK 465 ARG A 273 REMARK 465 ALA A 274 REMARK 465 ASN A 275 REMARK 465 LEU A 276 REMARK 465 GLY A 477 REMARK 465 SER A 478 REMARK 465 GLY A 479 REMARK 465 GLN A 480 REMARK 465 VAL A 481 REMARK 465 GLN A 482 REMARK 465 LEU A 483 REMARK 465 VAL A 484 REMARK 465 GLU A 485 REMARK 465 SER A 486 REMARK 465 GLY A 487 REMARK 465 GLY A 488 REMARK 465 ALA A 489 REMARK 465 LEU A 490 REMARK 465 VAL A 491 REMARK 465 GLN A 492 REMARK 465 PRO A 493 REMARK 465 GLY A 494 REMARK 465 GLY A 495 REMARK 465 SER A 496 REMARK 465 LEU A 497 REMARK 465 ARG A 498 REMARK 465 LEU A 499 REMARK 465 SER A 500 REMARK 465 CYS A 501 REMARK 465 ALA A 502 REMARK 465 ALA A 503 REMARK 465 SER A 504 REMARK 465 GLY A 505 REMARK 465 PHE A 506 REMARK 465 PRO A 507 REMARK 465 VAL A 508 REMARK 465 ASN A 509 REMARK 465 ARG A 510 REMARK 465 TYR A 511 REMARK 465 SER A 512 REMARK 465 MET A 513 REMARK 465 ARG A 514 REMARK 465 TRP A 515 REMARK 465 TYR A 516 REMARK 465 ARG A 517 REMARK 465 GLN A 518 REMARK 465 ALA A 519 REMARK 465 PRO A 520 REMARK 465 GLY A 521 REMARK 465 LYS A 522 REMARK 465 GLU A 523 REMARK 465 ARG A 524 REMARK 465 GLU A 525 REMARK 465 TRP A 526 REMARK 465 VAL A 527 REMARK 465 ALA A 528 REMARK 465 GLY A 529 REMARK 465 MET A 530 REMARK 465 SER A 531 REMARK 465 SER A 532 REMARK 465 ALA A 533 REMARK 465 GLY A 534 REMARK 465 ASP A 535 REMARK 465 ARG A 536 REMARK 465 SER A 537 REMARK 465 SER A 538 REMARK 465 TYR A 539 REMARK 465 GLU A 540 REMARK 465 ASP A 541 REMARK 465 SER A 542 REMARK 465 VAL A 543 REMARK 465 LYS A 544 REMARK 465 GLY A 545 REMARK 465 ARG A 546 REMARK 465 PHE A 547 REMARK 465 THR A 548 REMARK 465 ILE A 549 REMARK 465 SER A 550 REMARK 465 ARG A 551 REMARK 465 ASP A 552 REMARK 465 ASP A 553 REMARK 465 ALA A 554 REMARK 465 ARG A 555 REMARK 465 ASN A 556 REMARK 465 THR A 557 REMARK 465 VAL A 558 REMARK 465 TYR A 559 REMARK 465 LEU A 560 REMARK 465 GLN A 561 REMARK 465 MET A 562 REMARK 465 ASN A 563 REMARK 465 SER A 564 REMARK 465 LEU A 565 REMARK 465 LYS A 566 REMARK 465 PRO A 567 REMARK 465 GLU A 568 REMARK 465 ASP A 569 REMARK 465 THR A 570 REMARK 465 ALA A 571 REMARK 465 VAL A 572 REMARK 465 TYR A 573 REMARK 465 TYR A 574 REMARK 465 CYS A 575 REMARK 465 ASN A 576 REMARK 465 VAL A 577 REMARK 465 ASN A 578 REMARK 465 VAL A 579 REMARK 465 GLY A 580 REMARK 465 PHE A 581 REMARK 465 GLU A 582 REMARK 465 TYR A 583 REMARK 465 TRP A 584 REMARK 465 GLY A 585 REMARK 465 GLN A 586 REMARK 465 GLY A 587 REMARK 465 THR A 588 REMARK 465 GLN A 589 REMARK 465 VAL A 590 REMARK 465 THR A 591 REMARK 465 VAL A 592 REMARK 465 SER A 593 REMARK 465 MET A 594 REMARK 465 GLY A 595 REMARK 465 TRP A 596 REMARK 465 SER A 597 REMARK 465 HIS A 598 REMARK 465 PRO A 599 REMARK 465 GLN A 600 REMARK 465 PHE A 601 REMARK 465 GLU A 602 REMARK 465 LYS A 603 REMARK 465 GLY A 604 REMARK 465 GLY A 605 REMARK 465 GLY A 606 REMARK 465 SER A 607 REMARK 465 GLY A 608 REMARK 465 GLY A 609 REMARK 465 GLY A 610 REMARK 465 SER A 611 REMARK 465 GLY A 612 REMARK 465 GLY A 613 REMARK 465 SER A 614 REMARK 465 ALA A 615 REMARK 465 TRP A 616 REMARK 465 SER A 617 REMARK 465 HIS A 618 REMARK 465 PRO A 619 REMARK 465 GLN A 620 REMARK 465 PHE A 621 REMARK 465 GLU A 622 REMARK 465 LYS A 623 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 PRO A 58 CA - N - CD ANGL. DEV. = -11.4 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 GLN A 31 -123.83 50.47 REMARK 500 ALA A 239 -61.03 -94.07 REMARK 500 PHE A 266 53.35 -90.57 REMARK 500 THR A 319 -4.17 77.46 REMARK 500 ALA A 321 43.21 36.66 REMARK 500 GLU A 326 47.89 -84.36 REMARK 500 MET A 327 -35.78 -130.54 REMARK 500 PRO A 333 49.37 -73.05 REMARK 500 ARG A 378 48.34 -86.36 REMARK 500 THR A 399 41.57 -85.12 REMARK 500 PRO A 436 1.69 -65.71 REMARK 500 PHE A 448 49.87 -82.90 REMARK 500 LEU A 460 46.90 -85.35 REMARK 500 LEU A 468 45.53 -86.44 REMARK 500 LEU A 469 36.15 -140.25 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38652 RELATED DB: EMDB REMARK 900 STRUCTURE OF A PROTEIN DBREF 8XTX A -202 26 UNP P42212 GFP_AEQVI 1 229 DBREF 8XTX A 27 476 UNP Q16572 VACHT_HUMAN 27 476 DBREF 8XTX A 477 623 PDB 8XTX 8XTX 477 623 SEQADV 8XTX ARG A -173 UNP P42212 SER 30 ENGINEERED MUTATION SEQADV 8XTX ASN A -164 UNP P42212 TYR 39 ENGINEERED MUTATION SEQADV 8XTX LEU A -139 UNP P42212 PHE 64 ENGINEERED MUTATION SEQADV 8XTX THR A -138 UNP P42212 SER 65 ENGINEERED MUTATION SEQADV 8XTX ARG A -123 UNP P42212 GLN 80 ENGINEERED MUTATION SEQADV 8XTX SER A -104 UNP P42212 PHE 99 ENGINEERED MUTATION SEQADV 8XTX THR A -98 UNP P42212 ASN 105 ENGINEERED MUTATION SEQADV 8XTX PHE A -58 UNP P42212 TYR 145 ENGINEERED MUTATION SEQADV 8XTX THR A -50 UNP P42212 MET 153 ENGINEERED MUTATION SEQADV 8XTX ALA A -40 UNP P42212 VAL 163 ENGINEERED MUTATION SEQADV 8XTX VAL A -32 UNP P42212 ILE 171 ENGINEERED MUTATION SEQADV 8XTX VAL A 3 UNP P42212 ALA 206 ENGINEERED MUTATION SEQRES 1 A 826 MET SER LYS GLY GLU GLU LEU PHE THR GLY VAL VAL PRO SEQRES 2 A 826 ILE LEU VAL GLU LEU ASP GLY ASP VAL ASN GLY HIS LYS SEQRES 3 A 826 PHE SER VAL ARG GLY GLU GLY GLU GLY ASP ALA THR ASN SEQRES 4 A 826 GLY LYS LEU THR LEU LYS PHE ILE CYS THR THR GLY LYS SEQRES 5 A 826 LEU PRO VAL PRO TRP PRO THR LEU VAL THR THR LEU THR SEQRES 6 A 826 TYR GLY VAL GLN CYS PHE SER ARG TYR PRO ASP HIS MET SEQRES 7 A 826 LYS ARG HIS ASP PHE PHE LYS SER ALA MET PRO GLU GLY SEQRES 8 A 826 TYR VAL GLN GLU ARG THR ILE SER PHE LYS ASP ASP GLY SEQRES 9 A 826 THR TYR LYS THR ARG ALA GLU VAL LYS PHE GLU GLY ASP SEQRES 10 A 826 THR LEU VAL ASN ARG ILE GLU LEU LYS GLY ILE ASP PHE SEQRES 11 A 826 LYS GLU ASP GLY ASN ILE LEU GLY HIS LYS LEU GLU TYR SEQRES 12 A 826 ASN PHE ASN SER HIS ASN VAL TYR ILE THR ALA ASP LYS SEQRES 13 A 826 GLN LYS ASN GLY ILE LYS ALA ASN PHE LYS ILE ARG HIS SEQRES 14 A 826 ASN VAL GLU ASP GLY SER VAL GLN LEU ALA ASP HIS TYR SEQRES 15 A 826 GLN GLN ASN THR PRO ILE GLY ASP GLY PRO VAL LEU LEU SEQRES 16 A 826 PRO ASP ASN HIS TYR LEU SER THR GLN SER VAL LEU SER SEQRES 17 A 826 LYS ASP PRO ASN GLU LYS ARG ASP HIS MET VAL LEU LEU SEQRES 18 A 826 GLU PHE VAL THR ALA ALA GLY ILE GLU PRO ARG ARG GLN SEQRES 19 A 826 ARG ARG LEU VAL LEU VAL ILE VAL CYS VAL ALA LEU LEU SEQRES 20 A 826 LEU ASP ASN MET LEU TYR MET VAL ILE VAL PRO ILE VAL SEQRES 21 A 826 PRO ASP TYR ILE ALA HIS MET ARG GLY GLY GLY GLU GLY SEQRES 22 A 826 PRO THR ARG THR PRO GLU VAL TRP GLU PRO THR LEU PRO SEQRES 23 A 826 LEU PRO THR PRO ALA ASN ALA SER ALA TYR THR ALA ASN SEQRES 24 A 826 THR SER ALA SER PRO THR ALA ALA TRP PRO ALA GLY SER SEQRES 25 A 826 ALA LEU ARG PRO ARG TYR PRO THR GLU SER GLU ASP VAL SEQRES 26 A 826 LYS ILE GLY VAL LEU PHE ALA SER LYS ALA ILE LEU GLN SEQRES 27 A 826 LEU LEU VAL ASN PRO LEU SER GLY PRO PHE ILE ASP ARG SEQRES 28 A 826 MET SER TYR ASP VAL PRO LEU LEU ILE GLY LEU GLY VAL SEQRES 29 A 826 MET PHE ALA SER THR VAL LEU PHE ALA PHE ALA GLU ASP SEQRES 30 A 826 TYR ALA THR LEU PHE ALA ALA ARG SER LEU GLN GLY LEU SEQRES 31 A 826 GLY SER ALA PHE ALA ASP THR SER GLY ILE ALA MET ILE SEQRES 32 A 826 ALA ASP LYS TYR PRO GLU GLU PRO GLU ARG SER ARG ALA SEQRES 33 A 826 LEU GLY VAL ALA LEU ALA PHE ILE SER PHE GLY SER LEU SEQRES 34 A 826 VAL ALA PRO PRO PHE GLY GLY ILE LEU TYR GLU PHE ALA SEQRES 35 A 826 GLY LYS ARG VAL PRO PHE LEU VAL LEU ALA ALA VAL SER SEQRES 36 A 826 LEU PHE ASP ALA LEU LEU LEU LEU ALA VAL ALA LYS PRO SEQRES 37 A 826 PHE SER ALA ALA ALA ARG ALA ARG ALA ASN LEU PRO VAL SEQRES 38 A 826 GLY THR PRO ILE HIS ARG LEU MET LEU ASP PRO TYR ILE SEQRES 39 A 826 ALA VAL VAL ALA GLY ALA LEU THR THR CYS ASN ILE PRO SEQRES 40 A 826 LEU ALA PHE LEU GLU PRO THR ILE ALA THR TRP MET LYS SEQRES 41 A 826 HIS THR MET ALA ALA SER GLU TRP GLU MET GLY MET ALA SEQRES 42 A 826 TRP LEU PRO ALA PHE VAL PRO HIS VAL LEU GLY VAL TYR SEQRES 43 A 826 LEU THR VAL ARG LEU ALA ALA ARG TYR PRO HIS LEU GLN SEQRES 44 A 826 TRP LEU TYR GLY ALA LEU GLY LEU ALA VAL ILE GLY ALA SEQRES 45 A 826 SER SER CYS ILE VAL PRO ALA CYS ARG SER PHE ALA PRO SEQRES 46 A 826 LEU VAL VAL SER LEU CYS GLY LEU CYS PHE GLY ILE ALA SEQRES 47 A 826 LEU VAL ASP THR ALA LEU LEU PRO THR LEU ALA PHE LEU SEQRES 48 A 826 VAL ASP VAL ARG HIS VAL SER VAL TYR GLY SER VAL TYR SEQRES 49 A 826 ALA ILE ALA ASP ILE SER TYR SER VAL ALA TYR ALA LEU SEQRES 50 A 826 GLY PRO ILE VAL ALA GLY HIS ILE VAL HIS SER LEU GLY SEQRES 51 A 826 PHE GLU GLN LEU SER LEU GLY MET GLY LEU ALA ASN LEU SEQRES 52 A 826 LEU TYR ALA PRO VAL LEU LEU LEU LEU ARG ASN VAL GLY SEQRES 53 A 826 LEU LEU THR GLY SER GLY GLN VAL GLN LEU VAL GLU SER SEQRES 54 A 826 GLY GLY ALA LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SEQRES 55 A 826 SER CYS ALA ALA SER GLY PHE PRO VAL ASN ARG TYR SER SEQRES 56 A 826 MET ARG TRP TYR ARG GLN ALA PRO GLY LYS GLU ARG GLU SEQRES 57 A 826 TRP VAL ALA GLY MET SER SER ALA GLY ASP ARG SER SER SEQRES 58 A 826 TYR GLU ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG SEQRES 59 A 826 ASP ASP ALA ARG ASN THR VAL TYR LEU GLN MET ASN SER SEQRES 60 A 826 LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN VAL SEQRES 61 A 826 ASN VAL GLY PHE GLU TYR TRP GLY GLN GLY THR GLN VAL SEQRES 62 A 826 THR VAL SER MET GLY TRP SER HIS PRO GLN PHE GLU LYS SEQRES 63 A 826 GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER ALA TRP SEQRES 64 A 826 SER HIS PRO GLN PHE GLU LYS HELIX 1 AA1 GLN A 31 LEU A 49 1 19 HELIX 2 AA2 ILE A 56 TYR A 60 5 5 HELIX 3 AA3 ASP A 121 ALA A 129 1 9 HELIX 4 AA4 ALA A 129 VAL A 138 1 10 HELIX 5 AA5 VAL A 138 ASP A 147 1 10 HELIX 6 AA6 ASP A 152 VAL A 167 1 16 HELIX 7 AA7 ASP A 174 TYR A 204 1 31 HELIX 8 AA8 GLU A 206 LEU A 226 1 21 HELIX 9 AA9 VAL A 227 ALA A 239 1 13 HELIX 10 AB1 ARG A 242 ALA A 263 1 22 HELIX 11 AB2 PRO A 281 MET A 286 1 6 HELIX 12 AB3 ASP A 288 ASN A 302 1 15 HELIX 13 AB4 ASN A 302 GLU A 309 1 8 HELIX 14 AB5 ILE A 312 LYS A 317 1 6 HELIX 15 AB6 GLU A 324 MET A 329 1 6 HELIX 16 AB7 TRP A 331 ALA A 334 5 4 HELIX 17 AB8 PHE A 335 TYR A 352 1 18 HELIX 18 AB9 TRP A 357 VAL A 374 1 18 HELIX 19 AC1 SER A 379 ARG A 412 1 34 HELIX 20 AC2 VAL A 420 SER A 429 1 10 HELIX 21 AC3 VAL A 430 GLY A 447 1 18 HELIX 22 AC4 GLN A 450 LEU A 460 1 11 HELIX 23 AC5 PRO A 464 LEU A 468 5 5 CISPEP 1 GLU A 309 PRO A 310 0 -1.14 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