HEADER REGULATOR 27-NOV-96 1NBD
TITLE CFTR NBD1, THEORETICAL MODEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CFTR;
COMPND 3 CHAIN: NULL;
COMPND 4 FRAGMENT: NBD1, FIRST (OR N-TERMINAL) NUCLEOTIDE-BINDING
COMPND 5 DOMAIN;
COMPND 6 SYNONYM: CFTR NBD1, CYSTIC FIBROSIS TRANSMEMBRANE
COMPND 7 CONDUCTANCE REGULATOR NUCLEOTIDE-BINDING DOMAIN 1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN
KEYWDS REGULATOR, ATP-BINDING, TRANSMEMBRANE, TRANSPORT,
KEYWDS 2 GLYCOPROTEIN, DUPLICATION, IONIC CHANNEL, PHOSPHORYLATION,
KEYWDS 3 POLYMORPHISM, DISEASE MUTATION
EXPDTA THEORETICAL MODEL
AUTHOR P.J.HOEDEMAEKER,A.R.DAVIDSON,D.R.ROSE
REVDAT 1 15-MAY-97 1NBD 0
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE MODEL WAS REFINED USING A
REMARK 3 COMBINATION OF ENERGY MINIMIZATION IN X-PLOR WITH
REMARK 3 STANDARD CHARMM PARAMETERS AND AUTOMATED ROTAMER
REMARK 3 SEARCHES IN INSIGHT II.
REMARK 4
REMARK 4 1NBD COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220 EXPERIMENT TYPE : THEORETICAL MODELLING
REMARK 220 MODELLING PROGRAM : THREADER, INSIGHT II V 9.5.0
REMARK 220 PROGRAM AUTHORS : D.T.JONES, BIOSYM
REMARK 220
REMARK 220 REMARK:
REMARK 220 THIS MODEL WAS BUILT USING THE STRUCTURE OF THE SECOND
REMARK 220 DOMAIN OF THE A CHAIN OF ASPARTATE AMINOTRANSFERASE
REMARK 220 (PDB ENTRY 7AAT).
REMARK 220
REMARK 220 THE QUALITY OF THE MODEL WAS ASSESSED USING TWO STRUCTURE
REMARK 220 VERIFICATION PROGRAMS: ERRAT AND VERIFY_3D
REMARK 220 (URL WWW.MBI.UCLA.EDU/MBIHOME.HTML).
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
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 ASP 425 CG OD1 OD2
REMARK 470 ASP 426 CG OD1 OD2
REMARK 470 SER 427 OG
REMARK 470 LEU 428 CG CD1 CD2
REMARK 470 PHE 429 CG CD1 CE1 CZ CE2 CD2
REMARK 470 PHE 430 CG CD1 CE1 CZ CE2 CD2
REMARK 470 SER 431 OG
REMARK 470 ASN 432 CG OD1 ND2
REMARK 470 PHE 433 CG CD1 CE1 CZ CE2 CD2
REMARK 470 SER 434 OG
REMARK 470 LEU 435 CG CD1 CD2
REMARK 470 LEU 436 CG CD1 CD2
REMARK 470 THR 438 OG1 CG2
REMARK 470 PRO 439 CG CD
REMARK 470 VAL 440 CG1 CG2
REMARK 470 LEU 441 CG CD1 CD2
REMARK 470 LYS 442 CG CD CE NZ
REMARK 470 ASP 443 CG OD1 OD2
REMARK 470 ILE 444 CG1 CD1 CG2
REMARK 470 ASN 445 CG OD1 ND2
REMARK 470 PHE 446 CG CD1 CE1 CZ CE2 CD2
REMARK 470 LYS 447 CG CD CE NZ
REMARK 470 ILE 448 CG1 CD1 CG2
REMARK 470 GLU 449 CG CD OE1 OE2
REMARK 470 ARG 450 CG CD NE CZ NH1 NH2
REMARK 470 GLN 452 CG CD OE1 NE2
REMARK 470 LEU 453 CG CD1 CD2
REMARK 470 LEU 454 CG CD1 CD2
REMARK 470 VAL 456 CG1 CG2
REMARK 470 SER 459 OG
REMARK 470 THR 460 OG1 CG2
REMARK 470 LYS 464 CG CD CE NZ
REMARK 470 THR 465 OG1 CG2
REMARK 470 SER 466 OG
REMARK 470 LEU 467 CG CD1 CD2
REMARK 470 LEU 468 CG CD1 CD2
REMARK 470 MET 469 CG SD CE
REMARK 470 MET 470 CG SD CE
REMARK 470 ILE 471 CG1 CD1 CG2
REMARK 470 MET 472 CG SD CE
REMARK 470 GLU 474 CG CD OE1 OE2
REMARK 470 LEU 475 CG CD1 CD2
REMARK 470 GLU 476 CG CD OE1 OE2
REMARK 470 PRO 477 CG CD
REMARK 470 SER 478 OG
REMARK 470 GLU 479 CG CD OE1 OE2
REMARK 470 LYS 481 CG CD CE NZ
REMARK 470 ILE 482 CG1 CD1 CG2
REMARK 470 LYS 483 CG CD CE NZ
REMARK 470 HIS 484 CG ND1 CE1 NE2 CD2
REMARK 470 SER 485 OG
REMARK 470 ARG 487 CG CD NE CZ NH1 NH2
REMARK 470 ILE 488 CG1 CD1 CG2
REMARK 470 SER 489 OG
REMARK 470 PHE 490 CG CD1 CE1 CZ CE2 CD2
REMARK 470 CYS 491 SG
REMARK 470 SER 492 OG
REMARK 470 GLN 493 CG CD OE1 NE2
REMARK 470 PHE 494 CG CD1 CE1 CZ CE2 CD2
REMARK 470 SER 495 OG
REMARK 470 TRP 496 CG CD1 NE1 CE2 CD2 CZ2 CH2 CZ3
REMARK 470 TRP 496 CE3
REMARK 470 ILE 497 CG1 CD1 CG2
REMARK 470 MET 498 CG SD CE
REMARK 470 PRO 499 CG CD
REMARK 470 THR 501 OG1 CG2
REMARK 470 ILE 502 CG1 CD1 CG2
REMARK 470 LYS 503 CG CD CE NZ
REMARK 470 GLU 504 CG CD OE1 OE2
REMARK 470 ASN 505 CG OD1 ND2
REMARK 470 ILE 506 CG1 CD1 CG2
REMARK 470 ILE 507 CG1 CD1 CG2
REMARK 470 PHE 508 CG CD1 CE1 CZ CE2 CD2
REMARK 470 VAL 510 CG1 CG2
REMARK 470 SER 511 OG
REMARK 470 TYR 512 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 ASP 513 CG OD1 OD2
REMARK 470 GLU 514 CG CD OE1 OE2
REMARK 470 TYR 515 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 ARG 516 CG CD NE CZ NH1 NH2
REMARK 470 TYR 517 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 ARG 518 CG CD NE CZ NH1 NH2
REMARK 470 SER 519 OG
REMARK 470 VAL 520 CG1 CG2
REMARK 470 ILE 521 CG1 CD1 CG2
REMARK 470 LYS 522 CG CD CE NZ
REMARK 470 CYS 524 SG
REMARK 470 GLN 525 CG CD OE1 NE2
REMARK 470 LEU 526 CG CD1 CD2
REMARK 470 GLU 527 CG CD OE1 OE2
REMARK 470 GLU 528 CG CD OE1 OE2
REMARK 470 ASP 529 CG OD1 OD2
REMARK 470 ILE 530 CG1 CD1 CG2
REMARK 470 SER 531 OG
REMARK 470 LYS 532 CG CD CE NZ
REMARK 470 PHE 533 CG CD1 CE1 CZ CE2 CD2
REMARK 470 GLU 535 CG CD OE1 OE2
REMARK 470 LYS 536 CG CD CE NZ
REMARK 470 ASP 537 CG OD1 OD2
REMARK 470 ASN 538 CG OD1 ND2
REMARK 470 ILE 539 CG1 CD1 CG2
REMARK 470 VAL 540 CG1 CG2
REMARK 470 LEU 541 CG CD1 CD2
REMARK 470 GLU 543 CG CD OE1 OE2
REMARK 470 ILE 546 CG1 CD1 CG2
REMARK 470 THR 547 OG1 CG2
REMARK 470 LEU 548 CG CD1 CD2
REMARK 470 SER 549 OG
REMARK 470 GLN 552 CG CD OE1 NE2
REMARK 470 ARG 553 CG CD NE CZ NH1 NH2
REMARK 470 ARG 555 CG CD NE CZ NH1 NH2
REMARK 470 ILE 556 CG1 CD1 CG2
REMARK 470 SER 557 OG
REMARK 470 LEU 558 CG CD1 CD2
REMARK 470 ARG 560 CG CD NE CZ NH1 NH2
REMARK 470 VAL 562 CG1 CG2
REMARK 470 TYR 563 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 LYS 564 CG CD CE NZ
REMARK 470 ASP 565 CG OD1 OD2
REMARK 470 ASP 567 CG OD1 OD2
REMARK 470 LEU 568 CG CD1 CD2
REMARK 470 TYR 569 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 LEU 570 CG CD1 CD2
REMARK 470 LEU 571 CG CD1 CD2
REMARK 470 ASP 572 CG OD1 OD2
REMARK 470 SER 573 OG
REMARK 470 PRO 574 CG CD
REMARK 470 PHE 575 CG CD1 CE1 CZ CE2 CD2
REMARK 470 TYR 577 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 LEU 578 CG CD1 CD2
REMARK 470 ASP 579 CG OD1 OD2
REMARK 470 VAL 580 CG1 CG2
REMARK 470 LEU 581 CG CD1 CD2
REMARK 470 THR 582 OG1 CG2
REMARK 470 GLU 583 CG CD OE1 OE2
REMARK 470 LYS 584 CG CD CE NZ
REMARK 470 GLU 585 CG CD OE1 OE2
REMARK 470 ILE 586 CG1 CD1 CG2
REMARK 470 PHE 587 CG CD1 CE1 CZ CE2 CD2
REMARK 470 GLU 588 CG CD OE1 OE2
REMARK 470 SER 589 OG
REMARK 470 CYS 590 SG
REMARK 470 VAL 591 CG1 CG2
REMARK 470 CYS 592 SG
REMARK 470 LYS 593 CG CD CE NZ
REMARK 470 LEU 594 CG CD1 CD2
REMARK 470 MET 595 CG SD CE
REMARK 470 ASN 597 CG OD1 ND2
REMARK 470 LYS 598 CG CD CE NZ
REMARK 470 THR 599 OG1 CG2
REMARK 470 ARG 600 CG CD NE CZ NH1 NH2
REMARK 470 ILE 601 CG1 CD1 CG2
REMARK 470 LEU 602 CG CD1 CD2
REMARK 470 VAL 603 CG1 CG2
REMARK 470 THR 604 OG1 CG2
REMARK 470 SER 605 OG
REMARK 470 LYS 606 CG CD CE NZ
REMARK 470 MET 607 CG SD CE
REMARK 470 GLU 608 CG CD OE1 OE2
REMARK 470 HIS 609 CG ND1 CE1 NE2 CD2
REMARK 470 LEU 610 CG CD1 CD2
REMARK 470 LYS 611 CG CD CE NZ
REMARK 470 LYS 612 CG CD CE NZ
REMARK 470 ASP 614 CG OD1 OD2
REMARK 470 LYS 615 CG CD CE NZ
REMARK 470 ILE 616 CG1 CD1 CG2
REMARK 470 LEU 617 CG CD1 CD2
REMARK 470 ILE 618 CG1 CD1 CG2
REMARK 470 LEU 619 CG CD1 CD2
REMARK 470 HIS 620 CG ND1 CE1 NE2 CD2
REMARK 470 GLU 621 CG CD OE1 OE2
REMARK 470 SER 623 OG
REMARK 470 SER 624 OG
REMARK 470 TYR 625 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 PHE 626 CG CD1 CE1 CZ CE2 CD2
REMARK 470 TYR 627 CG CD1 CE1 CZ CE2 CD2 OH
REMARK 470 THR 629 OG1 CG2
REMARK 470 PHE 630 CG CD1 CE1 CZ CE2 CD2
REMARK 470 SER 631 OG
REMARK 470 GLU 632 CG CD OE1 OE2
REMARK 470 LEU 633 CG CD1 CD2
REMARK 470 GLN 634 CG CD OE1 NE2
REMARK 470 ASN 635 CG OD1 ND2
REMARK 470 LEU 636 CG CD1 CD2
REMARK 470 GLN 637 CG CD OE1 NE2
REMARK 470 PRO 638 CG CD
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ATP
REMARK 800 SITE_DESCRIPTION: PUTATIVE ATP BINDING SITE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1NBD SWS P13569 1 - 424 NOT IN ATOMS LIST
REMARK 999 1NBD SWS P13569 639 - 1480 NOT IN ATOMS LIST
REMARK 999
REMARK 999 REFERENCE: THE SEQUENCE IS DESCRIBED IN RIORDAN ET AL.
REMARK 999 (1989)SCIENCE 245: P 1066-1073.
DBREF 1NBD 425 638 SWS P13569 CFTR_HUMAN 425 638
SEQRES 1 214 ASP ASP SER LEU PHE PHE SER ASN PHE SER LEU LEU GLY
SEQRES 2 214 THR PRO VAL LEU LYS ASP ILE ASN PHE LYS ILE GLU ARG
SEQRES 3 214 GLY GLN LEU LEU ALA VAL ALA GLY SER THR GLY ALA GLY
SEQRES 4 214 LYS THR SER LEU LEU MET MET ILE MET GLY GLU LEU GLU
SEQRES 5 214 PRO SER GLU GLY LYS ILE LYS HIS SER GLY ARG ILE SER
SEQRES 6 214 PHE CYS SER GLN PHE SER TRP ILE MET PRO GLY THR ILE
SEQRES 7 214 LYS GLU ASN ILE ILE PHE GLY VAL SER TYR ASP GLU TYR
SEQRES 8 214 ARG TYR ARG SER VAL ILE LYS ALA CYS GLN LEU GLU GLU
SEQRES 9 214 ASP ILE SER LYS PHE ALA GLU LYS ASP ASN ILE VAL LEU
SEQRES 10 214 GLY GLU GLY GLY ILE THR LEU SER GLY GLY GLN ARG ALA
SEQRES 11 214 ARG ILE SER LEU ALA ARG ALA VAL TYR LYS ASP ALA ASP
SEQRES 12 214 LEU TYR LEU LEU ASP SER PRO PHE GLY TYR LEU ASP VAL
SEQRES 13 214 LEU THR GLU LYS GLU ILE PHE GLU SER CYS VAL CYS LYS
SEQRES 14 214 LEU MET ALA ASN LYS THR ARG ILE LEU VAL THR SER LYS
SEQRES 15 214 MET GLU HIS LEU LYS LYS ALA ASP LYS ILE LEU ILE LEU
SEQRES 16 214 HIS GLU GLY SER SER TYR PHE TYR GLY THR PHE SER GLU
SEQRES 17 214 LEU GLN ASN LEU GLN PRO
HELIX 1 1 ASP 426 PHE 433 1 8
HELIX 2 2 GLY 463 LEU 475 1 13
HELIX 3 3 MET 498 ASN 505 5 8
HELIX 4 4 ALA 523 ASP 529 1 7
HELIX 5 5 ARG 555 ASP 565 1 11
HELIX 6 6 VAL 580 VAL 591 5 12
HELIX 7 7 MET 607 HIS 609 5 3
HELIX 8 8 GLY 622 LEU 636 5 15
SHEET 1 A 7 SER 511 TYR 515 0
SHEET 2 A 7 ARG 487 SER 492 1
SHEET 3 A 7 ASN 538 GLY 542 1
SHEET 4 A 7 LEU 568 SER 573 1
SHEET 5 A 7 LEU 602 LYS 606 1
SHEET 6 A 7 ASP 614 LEU 617 -1
SHEET 7 A 7 LEU 454 ALA 457 -1
SITE 1 ATP 2 LYS 464 ASP 572
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
Let's take a look at its 3D structure!
Please Take a Care Look for its 2' structure ( 8 helix, 4 sheet)
Now we can see more clear of the 8 different helix by color ( the 7
sheets are white)