HEADER MEMBRANE PROTEIN 19-JUL-24 9G6X TITLE TTYH2 IN COMPLEX WITH SYBODY 1 IN GDN COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN TWEETY HOMOLOG 2; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: HTTY2,VOLUME-REGULATED ANION CHANNEL SUBUNIT TTYH2; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SYBODY 1; COMPND 8 CHAIN: C; COMPND 9 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: TTYH2, C17ORF29; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 11 ORGANISM_TAXID: 30538; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, SYBODY, NANOBODY, TTYH2, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.SUKALSKAIA,F.WEBER,B.PLOCHBERGER,R.DUTZLER REVDAT 1 21-MAY-25 9G6X 0 JRNL AUTH A.SUKALSKAIA,F.WEBER,B.PLOCHBERGER,R.DUTZLER JRNL TITL TTYH2 IN COMPLEX WITH SYBODY 1 IN GDN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.700 REMARK 3 NUMBER OF PARTICLES : 75814 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 9G6X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292140461. 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 : TTYH2 PURIFIED IN GDN IN REMARK 245 COMPLEX WITH SYBODY 1; REMARK 245 SYNTHETIC NANOBODY SELECTED FOR REMARK 245 BINDING TTYH2; TTYH2 PURIFIED REMARK 245 IN GDN 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 K3 BIOCONTINUUM (6K X REMARK 245 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) : 6848.00 REMARK 245 ILLUMINATION MODE : SPOT SCAN 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G 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 0 REMARK 465 SER A 1 REMARK 465 GLN A 2 REMARK 465 ALA A 3 REMARK 465 ALA A 4 REMARK 465 ARG A 5 REMARK 465 ARG A 74 REMARK 465 ARG A 75 REMARK 465 ASP A 76 REMARK 465 ASP A 77 REMARK 465 ALA A 78 REMARK 465 VAL A 79 REMARK 465 GLN A 80 REMARK 465 THR A 81 REMARK 465 LYS A 82 REMARK 465 GLN A 83 REMARK 465 HIS A 84 REMARK 465 HIS A 85 REMARK 465 SER A 86 REMARK 465 CYS A 87 REMARK 465 PHE A 417 REMARK 465 THR A 418 REMARK 465 THR A 419 REMARK 465 ARG A 420 REMARK 465 ASN A 421 REMARK 465 ARG A 422 REMARK 465 ASP A 423 REMARK 465 TYR A 424 REMARK 465 ASP A 425 REMARK 465 ASP A 426 REMARK 465 ILE A 427 REMARK 465 ASP A 428 REMARK 465 ASP A 429 REMARK 465 ASP A 430 REMARK 465 ASP A 431 REMARK 465 PRO A 432 REMARK 465 PHE A 433 REMARK 465 ASN A 434 REMARK 465 PRO A 435 REMARK 465 GLN A 436 REMARK 465 ALA A 437 REMARK 465 TRP A 438 REMARK 465 ARG A 439 REMARK 465 MET A 440 REMARK 465 ALA A 441 REMARK 465 ALA A 442 REMARK 465 HIS A 443 REMARK 465 SER A 444 REMARK 465 PRO A 445 REMARK 465 PRO A 446 REMARK 465 ARG A 447 REMARK 465 GLY A 448 REMARK 465 GLN A 449 REMARK 465 LEU A 450 REMARK 465 HIS A 451 REMARK 465 SER A 452 REMARK 465 PHE A 453 REMARK 465 CYS A 454 REMARK 465 SER A 455 REMARK 465 TYR A 456 REMARK 465 SER A 457 REMARK 465 SER A 458 REMARK 465 GLY A 459 REMARK 465 LEU A 460 REMARK 465 GLY A 461 REMARK 465 SER A 462 REMARK 465 GLN A 463 REMARK 465 THR A 464 REMARK 465 SER A 465 REMARK 465 LEU A 466 REMARK 465 GLN A 467 REMARK 465 PRO A 468 REMARK 465 PRO A 469 REMARK 465 ALA A 470 REMARK 465 GLN A 471 REMARK 465 THR A 472 REMARK 465 ILE A 473 REMARK 465 SER A 474 REMARK 465 ASN A 475 REMARK 465 ALA A 476 REMARK 465 PRO A 477 REMARK 465 VAL A 478 REMARK 465 SER A 479 REMARK 465 GLU A 480 REMARK 465 TYR A 481 REMARK 465 MET A 482 REMARK 465 ASN A 483 REMARK 465 GLN A 484 REMARK 465 ALA A 485 REMARK 465 MET A 486 REMARK 465 LEU A 487 REMARK 465 PHE A 488 REMARK 465 GLY A 489 REMARK 465 ARG A 490 REMARK 465 ASN A 491 REMARK 465 PRO A 492 REMARK 465 ARG A 493 REMARK 465 TYR A 494 REMARK 465 GLU A 495 REMARK 465 ASN A 496 REMARK 465 VAL A 497 REMARK 465 PRO A 498 REMARK 465 LEU A 499 REMARK 465 ILE A 500 REMARK 465 GLY A 501 REMARK 465 ARG A 502 REMARK 465 ALA A 503 REMARK 465 SER A 504 REMARK 465 PRO A 505 REMARK 465 PRO A 506 REMARK 465 PRO A 507 REMARK 465 THR A 508 REMARK 465 TYR A 509 REMARK 465 SER A 510 REMARK 465 PRO A 511 REMARK 465 SER A 512 REMARK 465 MET A 513 REMARK 465 ARG A 514 REMARK 465 ALA A 515 REMARK 465 THR A 516 REMARK 465 TYR A 517 REMARK 465 LEU A 518 REMARK 465 SER A 519 REMARK 465 VAL A 520 REMARK 465 ALA A 521 REMARK 465 ASP A 522 REMARK 465 GLU A 523 REMARK 465 HIS A 524 REMARK 465 LEU A 525 REMARK 465 ARG A 526 REMARK 465 HIS A 527 REMARK 465 TYR A 528 REMARK 465 GLY A 529 REMARK 465 ASN A 530 REMARK 465 GLN A 531 REMARK 465 PHE A 532 REMARK 465 PRO A 533 REMARK 465 ALA A 534 REMARK 465 ALA A 535 REMARK 465 LEU A 536 REMARK 465 GLU A 537 REMARK 465 VAL A 538 REMARK 465 LEU A 539 REMARK 465 PHE A 540 REMARK 465 GLN A 541 REMARK 465 GLY A 542 REMARK 465 PRO A 543 REMARK 465 GLN A 544 REMARK 465 GLY A 545 REMARK 465 THR A 546 REMARK 465 GLU A 547 REMARK 465 GLN A 548 REMARK 465 LYS A 549 REMARK 465 LEU A 550 REMARK 465 ILE A 551 REMARK 465 SER A 552 REMARK 465 GLU A 553 REMARK 465 GLU A 554 REMARK 465 ASP A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 GLY A 558 REMARK 465 ALA A 559 REMARK 465 SER A 560 REMARK 465 MET A 561 REMARK 465 ASP A 562 REMARK 465 GLU A 563 REMARK 465 LYS A 564 REMARK 465 THR A 565 REMARK 465 THR A 566 REMARK 465 GLY A 567 REMARK 465 TRP A 568 REMARK 465 ARG A 569 REMARK 465 GLY A 570 REMARK 465 GLY A 571 REMARK 465 HIS A 572 REMARK 465 VAL A 573 REMARK 465 VAL A 574 REMARK 465 GLU A 575 REMARK 465 GLY A 576 REMARK 465 LEU A 577 REMARK 465 ALA A 578 REMARK 465 GLY A 579 REMARK 465 GLU A 580 REMARK 465 LEU A 581 REMARK 465 GLU A 582 REMARK 465 GLN A 583 REMARK 465 LEU A 584 REMARK 465 ARG A 585 REMARK 465 ALA A 586 REMARK 465 ARG A 587 REMARK 465 LEU A 588 REMARK 465 GLU A 589 REMARK 465 HIS A 590 REMARK 465 HIS A 591 REMARK 465 PRO A 592 REMARK 465 GLN A 593 REMARK 465 GLY A 594 REMARK 465 GLN A 595 REMARK 465 ARG A 596 REMARK 465 GLU A 597 REMARK 465 PRO A 598 REMARK 465 MET B 0 REMARK 465 SER B 1 REMARK 465 GLN B 2 REMARK 465 ALA B 3 REMARK 465 ALA B 4 REMARK 465 ARG B 5 REMARK 465 ARG B 74 REMARK 465 ARG B 75 REMARK 465 ASP B 76 REMARK 465 ASP B 77 REMARK 465 ALA B 78 REMARK 465 VAL B 79 REMARK 465 GLN B 80 REMARK 465 THR B 81 REMARK 465 LYS B 82 REMARK 465 GLN B 83 REMARK 465 HIS B 84 REMARK 465 HIS B 85 REMARK 465 SER B 86 REMARK 465 CYS B 87 REMARK 465 PHE B 417 REMARK 465 THR B 418 REMARK 465 THR B 419 REMARK 465 ARG B 420 REMARK 465 ASN B 421 REMARK 465 ARG B 422 REMARK 465 ASP B 423 REMARK 465 TYR B 424 REMARK 465 ASP B 425 REMARK 465 ASP B 426 REMARK 465 ILE B 427 REMARK 465 ASP B 428 REMARK 465 ASP B 429 REMARK 465 ASP B 430 REMARK 465 ASP B 431 REMARK 465 PRO B 432 REMARK 465 PHE B 433 REMARK 465 ASN B 434 REMARK 465 PRO B 435 REMARK 465 GLN B 436 REMARK 465 ALA B 437 REMARK 465 TRP B 438 REMARK 465 ARG B 439 REMARK 465 MET B 440 REMARK 465 ALA B 441 REMARK 465 ALA B 442 REMARK 465 HIS B 443 REMARK 465 SER B 444 REMARK 465 PRO B 445 REMARK 465 PRO B 446 REMARK 465 ARG B 447 REMARK 465 GLY B 448 REMARK 465 GLN B 449 REMARK 465 LEU B 450 REMARK 465 HIS B 451 REMARK 465 SER B 452 REMARK 465 PHE B 453 REMARK 465 CYS B 454 REMARK 465 SER B 455 REMARK 465 TYR B 456 REMARK 465 SER B 457 REMARK 465 SER B 458 REMARK 465 GLY B 459 REMARK 465 LEU B 460 REMARK 465 GLY B 461 REMARK 465 SER B 462 REMARK 465 GLN B 463 REMARK 465 THR B 464 REMARK 465 SER B 465 REMARK 465 LEU B 466 REMARK 465 GLN B 467 REMARK 465 PRO B 468 REMARK 465 PRO B 469 REMARK 465 ALA B 470 REMARK 465 GLN B 471 REMARK 465 THR B 472 REMARK 465 ILE B 473 REMARK 465 SER B 474 REMARK 465 ASN B 475 REMARK 465 ALA B 476 REMARK 465 PRO B 477 REMARK 465 VAL B 478 REMARK 465 SER B 479 REMARK 465 GLU B 480 REMARK 465 TYR B 481 REMARK 465 MET B 482 REMARK 465 ASN B 483 REMARK 465 GLN B 484 REMARK 465 ALA B 485 REMARK 465 MET B 486 REMARK 465 LEU B 487 REMARK 465 PHE B 488 REMARK 465 GLY B 489 REMARK 465 ARG B 490 REMARK 465 ASN B 491 REMARK 465 PRO B 492 REMARK 465 ARG B 493 REMARK 465 TYR B 494 REMARK 465 GLU B 495 REMARK 465 ASN B 496 REMARK 465 VAL B 497 REMARK 465 PRO B 498 REMARK 465 LEU B 499 REMARK 465 ILE B 500 REMARK 465 GLY B 501 REMARK 465 ARG B 502 REMARK 465 ALA B 503 REMARK 465 SER B 504 REMARK 465 PRO B 505 REMARK 465 PRO B 506 REMARK 465 PRO B 507 REMARK 465 THR B 508 REMARK 465 TYR B 509 REMARK 465 SER B 510 REMARK 465 PRO B 511 REMARK 465 SER B 512 REMARK 465 MET B 513 REMARK 465 ARG B 514 REMARK 465 ALA B 515 REMARK 465 THR B 516 REMARK 465 TYR B 517 REMARK 465 LEU B 518 REMARK 465 SER B 519 REMARK 465 VAL B 520 REMARK 465 ALA B 521 REMARK 465 ASP B 522 REMARK 465 GLU B 523 REMARK 465 HIS B 524 REMARK 465 LEU B 525 REMARK 465 ARG B 526 REMARK 465 HIS B 527 REMARK 465 TYR B 528 REMARK 465 GLY B 529 REMARK 465 ASN B 530 REMARK 465 GLN B 531 REMARK 465 PHE B 532 REMARK 465 PRO B 533 REMARK 465 ALA B 534 REMARK 465 ALA B 535 REMARK 465 LEU B 536 REMARK 465 GLU B 537 REMARK 465 VAL B 538 REMARK 465 LEU B 539 REMARK 465 PHE B 540 REMARK 465 GLN B 541 REMARK 465 GLY B 542 REMARK 465 PRO B 543 REMARK 465 GLN B 544 REMARK 465 GLY B 545 REMARK 465 THR B 546 REMARK 465 GLU B 547 REMARK 465 GLN B 548 REMARK 465 LYS B 549 REMARK 465 LEU B 550 REMARK 465 ILE B 551 REMARK 465 SER B 552 REMARK 465 GLU B 553 REMARK 465 GLU B 554 REMARK 465 ASP B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 GLY B 558 REMARK 465 ALA B 559 REMARK 465 SER B 560 REMARK 465 MET B 561 REMARK 465 ASP B 562 REMARK 465 GLU B 563 REMARK 465 LYS B 564 REMARK 465 THR B 565 REMARK 465 THR B 566 REMARK 465 GLY B 567 REMARK 465 TRP B 568 REMARK 465 ARG B 569 REMARK 465 GLY B 570 REMARK 465 GLY B 571 REMARK 465 HIS B 572 REMARK 465 VAL B 573 REMARK 465 VAL B 574 REMARK 465 GLU B 575 REMARK 465 GLY B 576 REMARK 465 LEU B 577 REMARK 465 ALA B 578 REMARK 465 GLY B 579 REMARK 465 GLU B 580 REMARK 465 LEU B 581 REMARK 465 GLU B 582 REMARK 465 GLN B 583 REMARK 465 LEU B 584 REMARK 465 ARG B 585 REMARK 465 ALA B 586 REMARK 465 ARG B 587 REMARK 465 LEU B 588 REMARK 465 GLU B 589 REMARK 465 HIS B 590 REMARK 465 HIS B 591 REMARK 465 PRO B 592 REMARK 465 GLN B 593 REMARK 465 GLY B 594 REMARK 465 GLN B 595 REMARK 465 ARG B 596 REMARK 465 GLU B 597 REMARK 465 PRO B 598 REMARK 465 SER C 0 REMARK 465 ALA C 115 REMARK 465 GLY C 116 REMARK 465 ARG C 117 REMARK 465 ALA C 118 REMARK 465 GLY C 119 REMARK 465 GLU C 120 REMARK 465 GLN C 121 REMARK 465 LYS C 122 REMARK 465 LEU C 123 REMARK 465 ILE C 124 REMARK 465 SER C 125 REMARK 465 GLU C 126 REMARK 465 GLU C 127 REMARK 465 ASP C 128 REMARK 465 LEU C 129 REMARK 465 ASN C 130 REMARK 465 SER C 131 REMARK 465 ALA C 132 REMARK 465 VAL C 133 REMARK 465 ASP C 134 REMARK 465 HIS C 135 REMARK 465 HIS C 136 REMARK 465 HIS C 137 REMARK 465 HIS C 138 REMARK 465 HIS C 139 REMARK 465 HIS C 140 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 OH TYR B 41 OD2 ASP B 272 2.14 REMARK 500 OD1 ASN B 129 OG1 THR B 195 2.15 REMARK 500 O THR B 195 OG1 THR B 199 2.18 REMARK 500 NE2 GLN A 323 OD1 ASN A 352 2.19 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 LEU A 390 CA - CB - CG ANGL. DEV. = 18.1 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 SER A 35 81.14 -161.36 REMARK 500 LYS A 236 -168.66 -163.86 REMARK 500 ARG A 237 -132.40 60.71 REMARK 500 SER A 338 -2.60 67.58 REMARK 500 CYS A 382 -70.18 -57.72 REMARK 500 VAL B 30 -157.32 55.42 REMARK 500 VAL B 148 -64.82 -98.66 REMARK 500 ALA B 276 79.28 -158.21 REMARK 500 LYS B 415 -5.67 72.78 REMARK 500 GLN C 33 142.41 -172.83 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7P54 RELATED DB: PDB REMARK 900 7P54 CONTAINS TTYH2 WITHOUT THE SYBODY REMARK 900 RELATED ID: EMD-51106 RELATED DB: EMDB REMARK 900 TTYH2 IN COMPLEX WITH SYBODY 1 IN GDN DBREF 9G6X A 2 534 UNP Q9BSA4 TTYH2_HUMAN 2 534 DBREF 9G6X B 2 534 UNP Q9BSA4 TTYH2_HUMAN 2 534 DBREF 9G6X C 0 140 PDB 9G6X 9G6X 0 140 SEQADV 9G6X MET A 0 UNP Q9BSA4 INITIATING METHIONINE SEQADV 9G6X SER A 1 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA A 535 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 536 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 537 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X VAL A 538 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 539 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PHE A 540 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN A 541 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 542 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PRO A 543 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN A 544 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 545 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X THR A 546 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 547 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN A 548 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LYS A 549 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 550 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ILE A 551 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X SER A 552 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 553 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 554 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ASP A 555 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 556 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG A 557 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 558 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA A 559 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X SER A 560 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X MET A 561 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ASP A 562 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 563 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LYS A 564 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X THR A 565 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X THR A 566 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 567 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X TRP A 568 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG A 569 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 570 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 571 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X HIS A 572 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X VAL A 573 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X VAL A 574 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 575 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 576 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 577 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA A 578 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 579 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 580 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 581 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 582 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN A 583 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 584 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG A 585 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA A 586 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG A 587 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU A 588 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 589 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X HIS A 590 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X HIS A 591 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PRO A 592 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN A 593 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY A 594 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN A 595 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG A 596 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU A 597 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PRO A 598 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X MET B 0 UNP Q9BSA4 INITIATING METHIONINE SEQADV 9G6X SER B 1 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA B 535 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 536 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 537 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X VAL B 538 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 539 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PHE B 540 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN B 541 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 542 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PRO B 543 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN B 544 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 545 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X THR B 546 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 547 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN B 548 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LYS B 549 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 550 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ILE B 551 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X SER B 552 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 553 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 554 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ASP B 555 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 556 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG B 557 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 558 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA B 559 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X SER B 560 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X MET B 561 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ASP B 562 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 563 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LYS B 564 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X THR B 565 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X THR B 566 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 567 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X TRP B 568 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG B 569 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 570 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 571 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X HIS B 572 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X VAL B 573 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X VAL B 574 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 575 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 576 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 577 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA B 578 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 579 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 580 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 581 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 582 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN B 583 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 584 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG B 585 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ALA B 586 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG B 587 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X LEU B 588 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 589 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X HIS B 590 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X HIS B 591 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PRO B 592 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN B 593 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLY B 594 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLN B 595 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X ARG B 596 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X GLU B 597 UNP Q9BSA4 EXPRESSION TAG SEQADV 9G6X PRO B 598 UNP Q9BSA4 EXPRESSION TAG SEQRES 1 A 599 MET SER GLN ALA ALA ARG VAL ASP TYR ILE ALA PRO TRP SEQRES 2 A 599 TRP VAL VAL TRP LEU HIS SER VAL PRO HIS VAL GLY LEU SEQRES 3 A 599 ARG LEU GLN PRO VAL ASN SER THR PHE SER PRO GLY ASP SEQRES 4 A 599 GLU SER TYR GLN GLU SER LEU LEU PHE LEU GLY LEU VAL SEQRES 5 A 599 ALA ALA VAL CYS LEU GLY LEU ASN LEU ILE PHE LEU VAL SEQRES 6 A 599 ALA TYR LEU VAL CYS ALA CYS HIS CYS ARG ARG ASP ASP SEQRES 7 A 599 ALA VAL GLN THR LYS GLN HIS HIS SER CYS CYS ILE THR SEQRES 8 A 599 TRP THR ALA VAL VAL ALA GLY LEU ILE CYS CYS ALA ALA SEQRES 9 A 599 VAL GLY VAL GLY PHE TYR GLY ASN SER GLU THR ASN ASP SEQRES 10 A 599 GLY ALA TYR GLN LEU MET TYR SER LEU ASP ASP ALA ASN SEQRES 11 A 599 HIS THR PHE SER GLY ILE ASP ALA LEU VAL SER GLY THR SEQRES 12 A 599 THR GLN LYS MET LYS VAL ASP LEU GLU GLN HIS LEU ALA SEQRES 13 A 599 ARG LEU SER GLU ILE PHE ALA ALA ARG GLY ASP TYR LEU SEQRES 14 A 599 GLN THR LEU LYS PHE ILE GLN GLN MET ALA GLY SER VAL SEQRES 15 A 599 VAL VAL GLN LEU SER GLY LEU PRO VAL TRP ARG GLU VAL SEQRES 16 A 599 THR MET GLU LEU THR LYS LEU SER ASP GLN THR GLY TYR SEQRES 17 A 599 VAL GLU TYR TYR ARG TRP LEU SER TYR LEU LEU LEU PHE SEQRES 18 A 599 ILE LEU ASP LEU VAL ILE CYS LEU ILE ALA CYS LEU GLY SEQRES 19 A 599 LEU ALA LYS ARG SER LYS CYS LEU LEU ALA SER MET LEU SEQRES 20 A 599 CYS CYS GLY ALA LEU SER LEU LEU LEU SER TRP ALA SER SEQRES 21 A 599 LEU ALA ALA ASP GLY SER ALA ALA VAL ALA THR SER ASP SEQRES 22 A 599 PHE CYS VAL ALA PRO ASP THR PHE ILE LEU ASN VAL THR SEQRES 23 A 599 GLU GLY GLN ILE SER THR GLU VAL THR ARG TYR TYR LEU SEQRES 24 A 599 TYR CYS SER GLN SER GLY SER SER PRO PHE GLN GLN THR SEQRES 25 A 599 LEU THR THR PHE GLN ARG ALA LEU THR THR MET GLN ILE SEQRES 26 A 599 GLN VAL ALA GLY LEU LEU GLN PHE ALA VAL PRO LEU PHE SEQRES 27 A 599 SER THR ALA GLU GLU ASP LEU LEU ALA ILE GLN LEU LEU SEQRES 28 A 599 LEU ASN SER SER GLU SER SER LEU HIS GLN LEU THR ALA SEQRES 29 A 599 MET VAL ASP CYS ARG GLY LEU HIS LYS ASP TYR LEU ASP SEQRES 30 A 599 ALA LEU ALA GLY ILE CYS TYR ASP GLY LEU GLN GLY LEU SEQRES 31 A 599 LEU TYR LEU GLY LEU PHE SER PHE LEU ALA ALA LEU ALA SEQRES 32 A 599 PHE SER THR MET ILE CYS ALA GLY PRO ARG ALA TRP LYS SEQRES 33 A 599 HIS PHE THR THR ARG ASN ARG ASP TYR ASP ASP ILE ASP SEQRES 34 A 599 ASP ASP ASP PRO PHE ASN PRO GLN ALA TRP ARG MET ALA SEQRES 35 A 599 ALA HIS SER PRO PRO ARG GLY GLN LEU HIS SER PHE CYS SEQRES 36 A 599 SER TYR SER SER GLY LEU GLY SER GLN THR SER LEU GLN SEQRES 37 A 599 PRO PRO ALA GLN THR ILE SER ASN ALA PRO VAL SER GLU SEQRES 38 A 599 TYR MET ASN GLN ALA MET LEU PHE GLY ARG ASN PRO ARG SEQRES 39 A 599 TYR GLU ASN VAL PRO LEU ILE GLY ARG ALA SER PRO PRO SEQRES 40 A 599 PRO THR TYR SER PRO SER MET ARG ALA THR TYR LEU SER SEQRES 41 A 599 VAL ALA ASP GLU HIS LEU ARG HIS TYR GLY ASN GLN PHE SEQRES 42 A 599 PRO ALA ALA LEU GLU VAL LEU PHE GLN GLY PRO GLN GLY SEQRES 43 A 599 THR GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ARG GLY SEQRES 44 A 599 ALA SER MET ASP GLU LYS THR THR GLY TRP ARG GLY GLY SEQRES 45 A 599 HIS VAL VAL GLU GLY LEU ALA GLY GLU LEU GLU GLN LEU SEQRES 46 A 599 ARG ALA ARG LEU GLU HIS HIS PRO GLN GLY GLN ARG GLU SEQRES 47 A 599 PRO SEQRES 1 B 599 MET SER GLN ALA ALA ARG VAL ASP TYR ILE ALA PRO TRP SEQRES 2 B 599 TRP VAL VAL TRP LEU HIS SER VAL PRO HIS VAL GLY LEU SEQRES 3 B 599 ARG LEU GLN PRO VAL ASN SER THR PHE SER PRO GLY ASP SEQRES 4 B 599 GLU SER TYR GLN GLU SER LEU LEU PHE LEU GLY LEU VAL SEQRES 5 B 599 ALA ALA VAL CYS LEU GLY LEU ASN LEU ILE PHE LEU VAL SEQRES 6 B 599 ALA TYR LEU VAL CYS ALA CYS HIS CYS ARG ARG ASP ASP SEQRES 7 B 599 ALA VAL GLN THR LYS GLN HIS HIS SER CYS CYS ILE THR SEQRES 8 B 599 TRP THR ALA VAL VAL ALA GLY LEU ILE CYS CYS ALA ALA SEQRES 9 B 599 VAL GLY VAL GLY PHE TYR GLY ASN SER GLU THR ASN ASP SEQRES 10 B 599 GLY ALA TYR GLN LEU MET TYR SER LEU ASP ASP ALA ASN SEQRES 11 B 599 HIS THR PHE SER GLY ILE ASP ALA LEU VAL SER GLY THR SEQRES 12 B 599 THR GLN LYS MET LYS VAL ASP LEU GLU GLN HIS LEU ALA SEQRES 13 B 599 ARG LEU SER GLU ILE PHE ALA ALA ARG GLY ASP TYR LEU SEQRES 14 B 599 GLN THR LEU LYS PHE ILE GLN GLN MET ALA GLY SER VAL SEQRES 15 B 599 VAL VAL GLN LEU SER GLY LEU PRO VAL TRP ARG GLU VAL SEQRES 16 B 599 THR MET GLU LEU THR LYS LEU SER ASP GLN THR GLY TYR SEQRES 17 B 599 VAL GLU TYR TYR ARG TRP LEU SER TYR LEU LEU LEU PHE SEQRES 18 B 599 ILE LEU ASP LEU VAL ILE CYS LEU ILE ALA CYS LEU GLY SEQRES 19 B 599 LEU ALA LYS ARG SER LYS CYS LEU LEU ALA SER MET LEU SEQRES 20 B 599 CYS CYS GLY ALA LEU SER LEU LEU LEU SER TRP ALA SER SEQRES 21 B 599 LEU ALA ALA ASP GLY SER ALA ALA VAL ALA THR SER ASP SEQRES 22 B 599 PHE CYS VAL ALA PRO ASP THR PHE ILE LEU ASN VAL THR SEQRES 23 B 599 GLU GLY GLN ILE SER THR GLU VAL THR ARG TYR TYR LEU SEQRES 24 B 599 TYR CYS SER GLN SER GLY SER SER PRO PHE GLN GLN THR SEQRES 25 B 599 LEU THR THR PHE GLN ARG ALA LEU THR THR MET GLN ILE SEQRES 26 B 599 GLN VAL ALA GLY LEU LEU GLN PHE ALA VAL PRO LEU PHE SEQRES 27 B 599 SER THR ALA GLU GLU ASP LEU LEU ALA ILE GLN LEU LEU SEQRES 28 B 599 LEU ASN SER SER GLU SER SER LEU HIS GLN LEU THR ALA SEQRES 29 B 599 MET VAL ASP CYS ARG GLY LEU HIS LYS ASP TYR LEU ASP SEQRES 30 B 599 ALA LEU ALA GLY ILE CYS TYR ASP GLY LEU GLN GLY LEU SEQRES 31 B 599 LEU TYR LEU GLY LEU PHE SER PHE LEU ALA ALA LEU ALA SEQRES 32 B 599 PHE SER THR MET ILE CYS ALA GLY PRO ARG ALA TRP LYS SEQRES 33 B 599 HIS PHE THR THR ARG ASN ARG ASP TYR ASP ASP ILE ASP SEQRES 34 B 599 ASP ASP ASP PRO PHE ASN PRO GLN ALA TRP ARG MET ALA SEQRES 35 B 599 ALA HIS SER PRO PRO ARG GLY GLN LEU HIS SER PHE CYS SEQRES 36 B 599 SER TYR SER SER GLY LEU GLY SER GLN THR SER LEU GLN SEQRES 37 B 599 PRO PRO ALA GLN THR ILE SER ASN ALA PRO VAL SER GLU SEQRES 38 B 599 TYR MET ASN GLN ALA MET LEU PHE GLY ARG ASN PRO ARG SEQRES 39 B 599 TYR GLU ASN VAL PRO LEU ILE GLY ARG ALA SER PRO PRO SEQRES 40 B 599 PRO THR TYR SER PRO SER MET ARG ALA THR TYR LEU SER SEQRES 41 B 599 VAL ALA ASP GLU HIS LEU ARG HIS TYR GLY ASN GLN PHE SEQRES 42 B 599 PRO ALA ALA LEU GLU VAL LEU PHE GLN GLY PRO GLN GLY SEQRES 43 B 599 THR GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ARG GLY SEQRES 44 B 599 ALA SER MET ASP GLU LYS THR THR GLY TRP ARG GLY GLY SEQRES 45 B 599 HIS VAL VAL GLU GLY LEU ALA GLY GLU LEU GLU GLN LEU SEQRES 46 B 599 ARG ALA ARG LEU GLU HIS HIS PRO GLN GLY GLN ARG GLU SEQRES 47 B 599 PRO SEQRES 1 C 141 SER GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 C 141 GLN ALA GLY GLY SER LEU ARG LEU SER CYS THR ALA SER SEQRES 3 C 141 GLY PHE PRO VAL ALA PHE ALA GLN MET LYS TRP TYR ARG SEQRES 4 C 141 GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ALA ILE SEQRES 5 C 141 TRP SER MET GLY ASN GLU THR THR TYR ALA ASP SER VAL SEQRES 6 C 141 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 C 141 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 C 141 THR ALA VAL TYR TYR CYS ALA VAL GLU VAL GLY TYR GLY SEQRES 9 C 141 TYR HIS GLY GLN GLY THR GLN VAL THR VAL SER ALA GLY SEQRES 10 C 141 ARG ALA GLY GLU GLN LYS LEU ILE SER GLU GLU ASP LEU SEQRES 11 C 141 ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG B 601 14 HET NAG B 602 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 12(C8 H15 N O6) HELIX 1 AA1 PRO A 11 SER A 19 1 9 HELIX 2 AA2 ASP A 38 CYS A 73 1 36 HELIX 3 AA3 ILE A 89 PHE A 161 1 73 HELIX 4 AA4 ARG A 164 GLY A 187 1 24 HELIX 5 AA5 TRP A 191 LYS A 236 1 46 HELIX 6 AA6 LEU A 241 ALA A 276 1 36 HELIX 7 AA7 ALA A 276 THR A 285 1 10 HELIX 8 AA8 SER A 290 TYR A 299 1 10 HELIX 9 AA9 PHE A 308 PHE A 332 1 25 HELIX 10 AB1 ALA A 340 VAL A 365 1 26 HELIX 11 AB2 ASP A 366 CYS A 408 1 43 HELIX 12 AB3 PRO A 411 HIS A 416 5 6 HELIX 13 AB4 TRP B 12 SER B 19 1 8 HELIX 14 AB5 ASP B 38 CYS B 73 1 36 HELIX 15 AB6 ILE B 89 PHE B 161 1 73 HELIX 16 AB7 GLY B 165 LEU B 188 1 24 HELIX 17 AB8 TRP B 191 LYS B 236 1 46 HELIX 18 AB9 SER B 238 VAL B 275 1 38 HELIX 19 AC1 ALA B 276 THR B 285 1 10 HELIX 20 AC2 SER B 290 CYS B 300 1 11 HELIX 21 AC3 PHE B 308 VAL B 334 1 27 HELIX 22 AC4 ALA B 340 GLN B 360 1 21 HELIX 23 AC5 ASP B 366 TYR B 383 1 18 HELIX 24 AC6 TYR B 383 ALA B 409 1 27 HELIX 25 AC7 ALA B 409 TRP B 414 1 6 HELIX 26 AC8 ASP C 62 LYS C 65 5 4 HELIX 27 AC9 LYS C 87 THR C 91 5 5 SHEET 1 AA1 4 LEU C 4 SER C 7 0 SHEET 2 AA1 4 SER C 17 ALA C 24 -1 O THR C 23 N VAL C 5 SHEET 3 AA1 4 THR C 78 ASN C 84 -1 O MET C 83 N LEU C 18 SHEET 4 AA1 4 PHE C 68 ILE C 70 -1 N THR C 69 O GLN C 82 SHEET 1 AA2 6 LEU C 11 GLN C 13 0 SHEET 2 AA2 6 THR C 109 SER C 114 1 O THR C 112 N VAL C 12 SHEET 3 AA2 6 ALA C 92 ALA C 97 -1 N ALA C 92 O VAL C 111 SHEET 4 AA2 6 MET C 34 GLN C 39 -1 N TYR C 37 O TYR C 95 SHEET 5 AA2 6 GLU C 46 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AA2 6 THR C 58 TYR C 60 -1 O THR C 59 N ALA C 50 SSBOND 1 CYS A 274 CYS A 382 1555 1555 2.03 SSBOND 2 CYS A 300 CYS A 367 1555 1555 2.03 SSBOND 3 CYS B 274 CYS B 382 1555 1555 2.03 SSBOND 4 CYS B 300 CYS B 367 1555 1555 2.03 SSBOND 5 CYS C 22 CYS C 96 1555 1555 2.03 LINK ND2 ASN A 31 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 129 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 283 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 352 C1 NAG E 1 1555 1555 1.45 LINK ND2 ASN B 31 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 129 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN B 283 C1 NAG B 602 1555 1555 1.44 LINK ND2 ASN B 352 C1 NAG G 1 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 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