HEADER TRANSCRIPTION/DNA 18-JUN-24 9CB5 TITLE CRYSTAL STRUCTURE OF NUCLEOLIN IN COMPLEX WITH MYC PROMOTER G- TITLE 2 QUADRUPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEOLIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: PROTEIN C23; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: MYC PROMOTER G-QUADRUPLEX; COMPND 8 CHAIN: C, F; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: FAB HEAVY CHAIN; COMPND 12 CHAIN: D, G; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: FAB LIGHT CHAIN; COMPND 16 CHAIN: H, I; COMPND 17 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: NCL; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 MOL_ID: 2; SOURCE 9 SYNTHETIC: YES; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 21 ORGANISM_COMMON: HUMAN; SOURCE 22 ORGANISM_TAXID: 9606; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MYC G-QUADRUPLEX, NUCLEOLIN, MODULAR PROTEIN, TRANSCRIPTION FACTOR, KEYWDS 2 G4-EPIGENETIC, TRANSCRIPTION, TRANSCRIPTION-DNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR L.CHEN,J.DICKERHOFF,N.NOINAJ,D.YANG REVDAT 1 30-APR-25 9CB5 0 JRNL AUTH L.CHEN,J.DICKERHOFF,K.W.ZHENG,S.ERRAMILLI,H.FENG,G.WU, JRNL AUTH 2 B.ONEL,Y.CHEN,K.B.WANG,M.CARVER,C.LIN,S.SAKAI,J.WAN, JRNL AUTH 3 C.VINSON,L.HURLEY,A.A.KOSSIAKOFF,N.DENG,Y.BAI,N.NOINAJ, JRNL AUTH 4 D.YANG JRNL TITL STRUCTURAL BASIS FOR NUCLEOLIN RECOGNITION OF MYC PROMOTER JRNL TITL 2 G-QUADRUPLEX. JRNL REF SCIENCE V. 388 R1752 2025 JRNL REFN ESSN 1095-9203 JRNL PMID 40245140 JRNL DOI 10.1126/SCIENCE.ADR1752 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.43 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 3 NUMBER OF REFLECTIONS : 56511 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.232 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.540 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 48.4300 - 6.2700 1.00 4276 156 0.2058 0.1988 REMARK 3 2 6.2700 - 4.9800 1.00 4082 150 0.2030 0.2292 REMARK 3 3 4.9800 - 4.3500 0.99 4035 149 0.1687 0.1799 REMARK 3 4 4.3500 - 3.9500 0.99 3968 145 0.1884 0.2137 REMARK 3 5 3.9500 - 3.6700 0.99 4000 147 0.2118 0.2257 REMARK 3 6 3.6700 - 3.4500 0.99 3970 146 0.2223 0.2646 REMARK 3 7 3.4500 - 3.2800 0.97 3874 141 0.2340 0.2671 REMARK 3 8 3.2800 - 3.1400 0.96 3835 140 0.2656 0.3248 REMARK 3 9 3.1400 - 3.0200 0.95 3803 140 0.3037 0.3402 REMARK 3 10 3.0200 - 2.9100 0.95 3803 139 0.3069 0.3136 REMARK 3 11 2.9100 - 2.8200 0.95 3810 140 0.3171 0.3480 REMARK 3 12 2.8200 - 2.7400 0.96 3787 139 0.3307 0.3349 REMARK 3 13 2.7400 - 2.6700 0.96 3820 141 0.3542 0.4320 REMARK 3 14 2.6700 - 2.6000 0.96 3449 126 0.3924 0.4131 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.260 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.88 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 10472 REMARK 3 ANGLE : 0.556 14464 REMARK 3 CHIRALITY : 0.040 1617 REMARK 3 PLANARITY : 0.004 1682 REMARK 3 DIHEDRAL : 18.522 3744 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 9.4735 -15.3436 7.8566 REMARK 3 T TENSOR REMARK 3 T11: 0.2241 T22: 0.2517 REMARK 3 T33: 0.3826 T12: -0.0372 REMARK 3 T13: -0.0262 T23: -0.0030 REMARK 3 L TENSOR REMARK 3 L11: 0.4810 L22: 0.3484 REMARK 3 L33: 1.1410 L12: -0.0222 REMARK 3 L13: -0.3094 L23: -0.0474 REMARK 3 S TENSOR REMARK 3 S11: 0.0379 S12: -0.0538 S13: 0.1690 REMARK 3 S21: 0.0651 S22: -0.0028 S23: -0.1357 REMARK 3 S31: -0.2479 S32: 0.0719 S33: -0.0135 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9CB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000285101. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-JUL-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03317 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 V722 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 V722 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56511 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 48.430 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8 REMARK 200 DATA REDUNDANCY : 6.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.22600 REMARK 200 FOR THE DATA SET : 7.3800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.98500 REMARK 200 FOR SHELL : 0.890 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX 1.21.1_5286 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.5, 20% PEG 8000, 3% REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.62650 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 92.62950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.33000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 92.62950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.62650 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.33000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 8110 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 32200 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, G, I 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 350 REMARK 350 BIOMOLECULE: 2 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: 8710 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 31940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, H 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 GLY A 301 REMARK 465 GLN A 471 REMARK 465 ASP A 472 REMARK 465 TYR A 473 REMARK 465 ARG A 474 REMARK 465 GLY A 475 REMARK 465 GLY A 476 REMARK 465 LYS A 477 REMARK 465 ASN A 478 REMARK 465 SER A 479 REMARK 465 THR A 480 REMARK 465 TRP A 481 REMARK 465 SER A 482 REMARK 465 GLY A 483 REMARK 465 GLU A 484 REMARK 465 SER A 485 REMARK 465 LYS A 486 REMARK 465 THR A 487 REMARK 465 LEU A 488 REMARK 465 VAL A 489 REMARK 465 LEU A 490 REMARK 465 SER A 491 REMARK 465 ASN A 492 REMARK 465 LEU A 493 REMARK 465 SER A 494 REMARK 465 TYR A 495 REMARK 465 SER A 496 REMARK 465 ALA A 497 REMARK 465 THR A 498 REMARK 465 GLU A 499 REMARK 465 GLU A 500 REMARK 465 THR A 501 REMARK 465 LEU A 502 REMARK 465 GLN A 503 REMARK 465 GLU A 504 REMARK 465 VAL A 505 REMARK 465 PHE A 506 REMARK 465 GLU A 507 REMARK 465 LYS A 508 REMARK 465 ALA A 509 REMARK 465 THR A 510 REMARK 465 PHE A 511 REMARK 465 ILE A 512 REMARK 465 LYS A 513 REMARK 465 VAL A 514 REMARK 465 PRO A 515 REMARK 465 GLN A 516 REMARK 465 ASN A 517 REMARK 465 GLN A 518 REMARK 465 ASN A 519 REMARK 465 GLY A 520 REMARK 465 LYS A 521 REMARK 465 SER A 522 REMARK 465 LYS A 523 REMARK 465 GLY A 524 REMARK 465 TYR A 525 REMARK 465 ALA A 526 REMARK 465 PHE A 527 REMARK 465 ILE A 528 REMARK 465 GLU A 529 REMARK 465 PHE A 530 REMARK 465 ALA A 531 REMARK 465 SER A 532 REMARK 465 PHE A 533 REMARK 465 GLU A 534 REMARK 465 ASP A 535 REMARK 465 ALA A 536 REMARK 465 LYS A 537 REMARK 465 GLU A 538 REMARK 465 ALA A 539 REMARK 465 LEU A 540 REMARK 465 ASN A 541 REMARK 465 SER A 542 REMARK 465 SER A 543 REMARK 465 ASN A 544 REMARK 465 LYS A 545 REMARK 465 ARG A 546 REMARK 465 GLU A 547 REMARK 465 ILE A 548 REMARK 465 GLU A 549 REMARK 465 GLY A 550 REMARK 465 ARG A 551 REMARK 465 ALA A 552 REMARK 465 ILE A 553 REMARK 465 ARG A 554 REMARK 465 LEU A 555 REMARK 465 GLU A 556 REMARK 465 LEU A 557 REMARK 465 GLN A 558 REMARK 465 GLY A 559 REMARK 465 PRO A 560 REMARK 465 ARG A 561 REMARK 465 GLY A 562 REMARK 465 SER A 563 REMARK 465 PRO A 564 REMARK 465 ASN A 565 REMARK 465 ALA A 566 REMARK 465 ARG A 567 REMARK 465 SER A 568 REMARK 465 GLN A 569 REMARK 465 PRO A 570 REMARK 465 SER A 571 REMARK 465 LYS A 572 REMARK 465 THR A 573 REMARK 465 LEU A 574 REMARK 465 PHE A 575 REMARK 465 VAL A 576 REMARK 465 LYS A 577 REMARK 465 GLY A 578 REMARK 465 LEU A 579 REMARK 465 SER A 580 REMARK 465 GLU A 581 REMARK 465 ASP A 582 REMARK 465 THR A 583 REMARK 465 THR A 584 REMARK 465 GLU A 585 REMARK 465 GLU A 586 REMARK 465 THR A 587 REMARK 465 LEU A 588 REMARK 465 LYS A 589 REMARK 465 GLU A 590 REMARK 465 SER A 591 REMARK 465 PHE A 592 REMARK 465 ASP A 593 REMARK 465 GLY A 594 REMARK 465 SER A 595 REMARK 465 VAL A 596 REMARK 465 ARG A 597 REMARK 465 ALA A 598 REMARK 465 ARG A 599 REMARK 465 ILE A 600 REMARK 465 VAL A 601 REMARK 465 THR A 602 REMARK 465 ASP A 603 REMARK 465 ARG A 604 REMARK 465 GLU A 605 REMARK 465 THR A 606 REMARK 465 GLY A 607 REMARK 465 SER A 608 REMARK 465 SER A 609 REMARK 465 LYS A 610 REMARK 465 GLY A 611 REMARK 465 PHE A 612 REMARK 465 GLY A 613 REMARK 465 PHE A 614 REMARK 465 VAL A 615 REMARK 465 ASP A 616 REMARK 465 PHE A 617 REMARK 465 ASN A 618 REMARK 465 SER A 619 REMARK 465 GLU A 620 REMARK 465 GLU A 621 REMARK 465 ASP A 622 REMARK 465 ALA A 623 REMARK 465 LYS A 624 REMARK 465 ALA A 625 REMARK 465 ALA A 626 REMARK 465 LYS A 627 REMARK 465 GLU A 628 REMARK 465 ALA A 629 REMARK 465 MET A 630 REMARK 465 GLU A 631 REMARK 465 ASP A 632 REMARK 465 GLY A 633 REMARK 465 GLU A 634 REMARK 465 ILE A 635 REMARK 465 ASP A 636 REMARK 465 GLY A 637 REMARK 465 ASN A 638 REMARK 465 LYS A 639 REMARK 465 VAL A 640 REMARK 465 THR A 641 REMARK 465 LEU A 642 REMARK 465 ASP A 643 REMARK 465 TRP A 644 REMARK 465 ALA A 645 REMARK 465 LYS A 646 REMARK 465 PRO A 647 REMARK 465 GLY B 301 REMARK 465 TYR B 473 REMARK 465 ARG B 474 REMARK 465 GLY B 475 REMARK 465 GLY B 476 REMARK 465 LYS B 477 REMARK 465 ASN B 478 REMARK 465 SER B 479 REMARK 465 THR B 480 REMARK 465 TRP B 481 REMARK 465 SER B 482 REMARK 465 GLY B 483 REMARK 465 GLU B 484 REMARK 465 SER B 485 REMARK 465 LYS B 486 REMARK 465 THR B 487 REMARK 465 LEU B 488 REMARK 465 VAL B 489 REMARK 465 LEU B 490 REMARK 465 SER B 491 REMARK 465 ASN B 492 REMARK 465 LEU B 493 REMARK 465 SER B 494 REMARK 465 TYR B 495 REMARK 465 SER B 496 REMARK 465 ALA B 497 REMARK 465 THR B 498 REMARK 465 GLU B 499 REMARK 465 GLU B 500 REMARK 465 THR B 501 REMARK 465 LEU B 502 REMARK 465 GLN B 503 REMARK 465 GLU B 504 REMARK 465 VAL B 505 REMARK 465 PHE B 506 REMARK 465 GLU B 507 REMARK 465 LYS B 508 REMARK 465 ALA B 509 REMARK 465 THR B 510 REMARK 465 PHE B 511 REMARK 465 ILE B 512 REMARK 465 LYS B 513 REMARK 465 VAL B 514 REMARK 465 PRO B 515 REMARK 465 GLN B 516 REMARK 465 ASN B 517 REMARK 465 GLN B 518 REMARK 465 ASN B 519 REMARK 465 GLY B 520 REMARK 465 LYS B 521 REMARK 465 SER B 522 REMARK 465 LYS B 523 REMARK 465 GLY B 524 REMARK 465 TYR B 525 REMARK 465 ALA B 526 REMARK 465 PHE B 527 REMARK 465 ILE B 528 REMARK 465 GLU B 529 REMARK 465 PHE B 530 REMARK 465 ALA B 531 REMARK 465 SER B 532 REMARK 465 PHE B 533 REMARK 465 GLU B 534 REMARK 465 ASP B 535 REMARK 465 ALA B 536 REMARK 465 LYS B 537 REMARK 465 GLU B 538 REMARK 465 ALA B 539 REMARK 465 LEU B 540 REMARK 465 ASN B 541 REMARK 465 SER B 542 REMARK 465 SER B 543 REMARK 465 ASN B 544 REMARK 465 LYS B 545 REMARK 465 ARG B 546 REMARK 465 GLU B 547 REMARK 465 ILE B 548 REMARK 465 GLU B 549 REMARK 465 GLY B 550 REMARK 465 ARG B 551 REMARK 465 ALA B 552 REMARK 465 ILE B 553 REMARK 465 ARG B 554 REMARK 465 LEU B 555 REMARK 465 GLU B 556 REMARK 465 LEU B 557 REMARK 465 GLN B 558 REMARK 465 GLY B 559 REMARK 465 PRO B 560 REMARK 465 ARG B 561 REMARK 465 GLY B 562 REMARK 465 SER B 563 REMARK 465 PRO B 564 REMARK 465 ASN B 565 REMARK 465 ALA B 566 REMARK 465 ARG B 567 REMARK 465 SER B 568 REMARK 465 GLN B 569 REMARK 465 PRO B 570 REMARK 465 SER B 571 REMARK 465 LYS B 572 REMARK 465 THR B 573 REMARK 465 LEU B 574 REMARK 465 PHE B 575 REMARK 465 VAL B 576 REMARK 465 LYS B 577 REMARK 465 GLY B 578 REMARK 465 LEU B 579 REMARK 465 SER B 580 REMARK 465 GLU B 581 REMARK 465 ASP B 582 REMARK 465 THR B 583 REMARK 465 THR B 584 REMARK 465 GLU B 585 REMARK 465 GLU B 586 REMARK 465 THR B 587 REMARK 465 LEU B 588 REMARK 465 LYS B 589 REMARK 465 GLU B 590 REMARK 465 SER B 591 REMARK 465 PHE B 592 REMARK 465 ASP B 593 REMARK 465 GLY B 594 REMARK 465 SER B 595 REMARK 465 VAL B 596 REMARK 465 ARG B 597 REMARK 465 ALA B 598 REMARK 465 ARG B 599 REMARK 465 ILE B 600 REMARK 465 VAL B 601 REMARK 465 THR B 602 REMARK 465 ASP B 603 REMARK 465 ARG B 604 REMARK 465 GLU B 605 REMARK 465 THR B 606 REMARK 465 GLY B 607 REMARK 465 SER B 608 REMARK 465 SER B 609 REMARK 465 LYS B 610 REMARK 465 GLY B 611 REMARK 465 PHE B 612 REMARK 465 GLY B 613 REMARK 465 PHE B 614 REMARK 465 VAL B 615 REMARK 465 ASP B 616 REMARK 465 PHE B 617 REMARK 465 ASN B 618 REMARK 465 SER B 619 REMARK 465 GLU B 620 REMARK 465 GLU B 621 REMARK 465 ASP B 622 REMARK 465 ALA B 623 REMARK 465 LYS B 624 REMARK 465 ALA B 625 REMARK 465 ALA B 626 REMARK 465 LYS B 627 REMARK 465 GLU B 628 REMARK 465 ALA B 629 REMARK 465 MET B 630 REMARK 465 GLU B 631 REMARK 465 ASP B 632 REMARK 465 GLY B 633 REMARK 465 GLU B 634 REMARK 465 ILE B 635 REMARK 465 ASP B 636 REMARK 465 GLY B 637 REMARK 465 ASN B 638 REMARK 465 LYS B 639 REMARK 465 VAL B 640 REMARK 465 THR B 641 REMARK 465 LEU B 642 REMARK 465 ASP B 643 REMARK 465 TRP B 644 REMARK 465 ALA B 645 REMARK 465 LYS B 646 REMARK 465 PRO B 647 REMARK 465 GLU D -1 REMARK 465 THR D 234 REMARK 465 HIS D 235 REMARK 465 THR D 236 REMARK 465 SER D 237 REMARK 465 ARG D 238 REMARK 465 HIS D 239 REMARK 465 HIS D 240 REMARK 465 HIS D 241 REMARK 465 HIS D 242 REMARK 465 HIS D 243 REMARK 465 HIS D 244 REMARK 465 DA F -4 REMARK 465 DT F -3 REMARK 465 DC F -2 REMARK 465 DG F -1 REMARK 465 DC F 0 REMARK 465 ASP G 232 REMARK 465 LYS G 233 REMARK 465 THR G 234 REMARK 465 HIS G 235 REMARK 465 THR G 236 REMARK 465 SER G 237 REMARK 465 ARG G 238 REMARK 465 HIS G 239 REMARK 465 HIS G 240 REMARK 465 HIS G 241 REMARK 465 HIS G 242 REMARK 465 HIS G 243 REMARK 465 HIS G 244 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 LYS A 333 CG CD CE NZ REMARK 470 LYS A 388 CG CD CE NZ REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2 REMARK 470 THR A 394 OG1 CG2 REMARK 470 LEU A 396 CG CD1 CD2 REMARK 470 LYS A 398 CG CD CE NZ REMARK 470 ASN A 399 CG OD1 ND2 REMARK 470 LEU A 400 CG CD1 CD2 REMARK 470 PRO A 401 CG CD REMARK 470 TYR A 402 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 403 CG CD CE NZ REMARK 470 VAL A 404 CG1 CG2 REMARK 470 THR A 405 OG1 CG2 REMARK 470 ASP A 407 CG OD1 OD2 REMARK 470 GLU A 408 CG CD OE1 OE2 REMARK 470 LEU A 409 CG CD1 CD2 REMARK 470 LYS A 410 CG CD CE NZ REMARK 470 GLU A 411 CG CD OE1 OE2 REMARK 470 VAL A 412 CG1 CG2 REMARK 470 PHE A 413 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 414 CG CD OE1 OE2 REMARK 470 ASP A 415 CG OD1 OD2 REMARK 470 GLU A 418 CG CD OE1 OE2 REMARK 470 ILE A 419 CG1 CG2 CD1 REMARK 470 ARG A 420 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 421 CG CD1 CD2 REMARK 470 VAL A 422 CG1 CG2 REMARK 470 SER A 423 OG REMARK 470 LYS A 424 CG CD CE NZ REMARK 470 ASP A 425 CG OD1 OD2 REMARK 470 LYS A 427 CG CD CE NZ REMARK 470 SER A 428 OG REMARK 470 LYS A 429 CG CD CE NZ REMARK 470 ILE A 431 CG1 CG2 CD1 REMARK 470 TYR A 433 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE A 434 CG1 CG2 CD1 REMARK 470 GLU A 435 CG CD OE1 OE2 REMARK 470 PHE A 436 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 437 CG CD CE NZ REMARK 470 THR A 438 OG1 CG2 REMARK 470 GLU A 439 CG CD OE1 OE2 REMARK 470 ASP A 441 CG OD1 OD2 REMARK 470 GLU A 443 CG CD OE1 OE2 REMARK 470 LYS A 444 CG CD CE NZ REMARK 470 THR A 445 OG1 CG2 REMARK 470 PHE A 446 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU A 447 CG CD OE1 OE2 REMARK 470 GLU A 448 CG CD OE1 OE2 REMARK 470 LYS A 449 CG CD CE NZ REMARK 470 THR A 452 OG1 CG2 REMARK 470 GLU A 453 CG CD OE1 OE2 REMARK 470 ASP A 455 CG OD1 OD2 REMARK 470 ARG A 457 CG CD NE CZ NH1 NH2 REMARK 470 SER A 458 OG REMARK 470 ILE A 459 CG1 CG2 CD1 REMARK 470 SER A 460 OG REMARK 470 LEU A 461 CG CD1 CD2 REMARK 470 TYR A 462 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 463 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR A 464 OG1 CG2 REMARK 470 GLU A 466 CG CD OE1 OE2 REMARK 470 LYS A 467 CG CD CE NZ REMARK 470 GLN A 469 CG CD OE1 NE2 REMARK 470 ASN A 470 CG OD1 ND2 REMARK 470 ASP B 472 CG OD1 OD2 REMARK 470 ILE D 0 CG1 CG2 CD1 REMARK 470 SER D 145 OG REMARK 470 THR D 146 OG1 CG2 REMARK 470 SER D 147 OG REMARK 470 SER D 201 OG REMARK 470 LYS D 225 CG CD CE NZ REMARK 470 LYS D 229 CG CD CE NZ REMARK 470 SER D 230 OG REMARK 470 CYS D 231 SG REMARK 470 ASP D 232 CG OD1 OD2 REMARK 470 LYS D 233 CG CD CE NZ REMARK 470 LEU G 139 CG CD1 CD2 REMARK 470 SER G 142 OG REMARK 470 LYS G 144 CG CD CE NZ REMARK 470 SER G 145 OG REMARK 470 THR G 146 OG1 CG2 REMARK 470 SER G 147 OG REMARK 470 THR G 150 OG1 CG2 REMARK 470 LEU G 153 CG CD1 CD2 REMARK 470 SER G 201 OG REMARK 470 THR G 206 OG1 CG2 REMARK 470 GLN G 207 CG CD OE1 NE2 REMARK 470 THR G 208 OG1 CG2 REMARK 470 TYR G 209 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN G 212 CG OD1 ND2 REMARK 470 VAL G 213 CG1 CG2 REMARK 470 ASN G 219 CG OD1 ND2 REMARK 470 THR G 220 OG1 CG2 REMARK 470 LYS G 225 CG CD CE NZ REMARK 470 VAL G 226 CG1 CG2 REMARK 470 LYS G 229 CG CD CE NZ REMARK 470 SER G 230 OG REMARK 470 LEU H 123 CG CD1 CD2 REMARK 470 ASP H 149 CG OD1 OD2 REMARK 470 GLN H 153 CG CD OE1 NE2 REMARK 470 LYS H 186 CG CD CE NZ REMARK 470 LYS H 188 CG CD CE NZ REMARK 470 ARG H 209 CG CD NE CZ NH1 NH2 REMARK 470 GLU H 211 CG CD OE1 OE2 REMARK 470 SER I 28 OG REMARK 470 SER I 121 OG REMARK 470 GLN I 122 CG CD OE1 NE2 REMARK 470 LEU I 123 CG CD1 CD2 REMARK 470 LYS I 124 CG CD CE NZ REMARK 470 GLN I 145 CG CD OE1 NE2 REMARK 470 LYS I 147 CG CD CE NZ REMARK 470 VAL I 148 CG1 CG2 REMARK 470 ASN I 150 CG OD1 ND2 REMARK 470 LEU I 152 CG CD1 CD2 REMARK 470 SER I 154 OG REMARK 470 LYS I 167 CG CD CE NZ REMARK 470 LYS I 186 CG CD CE NZ REMARK 470 LYS I 188 CG CD CE NZ REMARK 470 THR I 195 OG1 CG2 REMARK 470 GLN I 197 CG CD OE1 NE2 REMARK 470 PHE I 207 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU I 211 CG CD OE1 OE2 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 NH2 ARG A 342 O4 DT F 10 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 DA F 15 O4' - C1' - N9 ANGL. DEV. = 3.4 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 LYS A 382 49.32 -79.44 REMARK 500 SER A 386 -165.18 -79.48 REMARK 500 LYS A 387 5.51 -61.47 REMARK 500 ASP A 391 -8.23 72.12 REMARK 500 LEU A 400 68.16 -109.14 REMARK 500 PRO A 401 -90.47 -169.19 REMARK 500 TYR A 402 -166.64 -160.96 REMARK 500 ALA A 416 147.06 -170.19 REMARK 500 ASP A 441 -154.37 52.06 REMARK 500 LYS B 382 -168.09 -116.46 REMARK 500 LYS B 403 31.90 -97.16 REMARK 500 TYR D 113 -163.97 59.64 REMARK 500 THR D 146 -107.71 61.59 REMARK 500 THR D 208 -10.46 73.05 REMARK 500 CYS D 231 -62.57 155.03 REMARK 500 TYR G 113 -179.66 65.26 REMARK 500 PHE G 137 -107.43 -117.60 REMARK 500 THR G 166 119.70 -38.08 REMARK 500 THR G 175 -8.52 -58.21 REMARK 500 GLN G 207 -146.49 47.57 REMARK 500 THR G 208 -96.70 167.07 REMARK 500 PRO G 217 37.25 -86.47 REMARK 500 SER H 28 -124.43 52.43 REMARK 500 ALA H 49 -9.45 72.54 REMARK 500 ALA H 82 -169.68 -165.12 REMARK 500 PRO H 139 -167.37 -77.80 REMARK 500 ASP H 149 -95.75 50.57 REMARK 500 SER H 154 49.35 -141.18 REMARK 500 ASN H 208 -76.18 -82.95 REMARK 500 ARG H 209 112.90 -167.71 REMARK 500 ASP I -1 -3.46 69.48 REMARK 500 SER I 7 -2.02 70.85 REMARK 500 SER I 8 133.61 -175.91 REMARK 500 SER I 28 -97.63 60.93 REMARK 500 ALA I 49 -5.55 73.67 REMARK 500 SER I 50 0.90 -151.49 REMARK 500 PRO I 118 -177.44 -61.84 REMARK 500 ASP I 120 -15.59 64.33 REMARK 500 ASP I 149 -23.08 66.56 REMARK 500 ASN I 150 -18.06 -149.72 REMARK 500 SER I 166 44.64 -87.08 REMARK 500 VAL I 189 105.27 63.30 REMARK 500 ARG I 209 -155.88 -147.27 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 K C 101 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 DG C 3 O6 REMARK 620 2 DG C 4 O6 71.2 REMARK 620 3 DG C 7 O6 74.0 84.9 REMARK 620 4 DG C 8 O6 126.4 65.7 71.9 REMARK 620 5 DG C 16 O6 119.5 152.4 75.2 89.8 REMARK 620 6 DG C 17 O6 157.2 106.6 128.8 68.7 73.3 REMARK 620 7 DG C 20 O6 81.0 133.7 122.4 152.7 73.8 85.5 REMARK 620 8 DG C 21 O6 81.4 71.4 150.2 111.9 132.9 76.6 68.4 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K C 102 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 DG C 4 O6 REMARK 620 2 DG C 5 O6 71.5 REMARK 620 3 DG C 8 O6 67.9 89.0 REMARK 620 4 DG C 9 O6 130.7 76.4 75.2 REMARK 620 5 DG C 17 O6 110.8 157.8 72.5 86.9 REMARK 620 6 DG C 18 O6 158.4 116.4 129.7 70.5 70.1 REMARK 620 7 DG C 21 O6 67.8 124.7 107.9 158.1 73.9 92.6 REMARK 620 8 DG C 22 O6 91.7 68.9 154.2 110.4 131.8 74.2 76.6 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K F 101 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 DG F 3 O6 REMARK 620 2 DG F 4 O6 75.8 REMARK 620 3 DG F 7 O6 64.3 90.9 REMARK 620 4 DG F 8 O6 130.3 76.5 75.8 REMARK 620 5 DG F 16 O6 107.9 163.0 76.5 89.2 REMARK 620 6 DG F 17 O6 158.6 114.5 131.1 71.1 68.2 REMARK 620 7 DG F 20 O6 71.1 133.2 103.1 150.2 62.1 89.4 REMARK 620 8 DG F 21 O6 96.1 80.8 160.1 119.0 114.7 68.6 71.0 REMARK 620 N 1 2 3 4 5 6 7 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K F 102 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 DG F 4 O6 REMARK 620 2 DG F 5 O6 66.2 REMARK 620 3 DG F 8 O6 69.7 87.1 REMARK 620 4 DG F 9 O6 130.9 80.2 74.1 REMARK 620 5 DG F 17 O6 106.4 155.6 68.8 89.6 REMARK 620 6 DG F 18 O6 158.9 122.5 126.8 69.9 73.1 REMARK 620 7 DG F 21 O6 73.1 128.3 107.6 151.2 65.7 88.2 REMARK 620 8 DG F 22 O6 88.6 69.5 153.3 112.6 134.7 78.3 79.3 REMARK 620 N 1 2 3 4 5 6 7 DBREF 9CB5 A 307 647 UNP P19338 NUCL_HUMAN 307 647 DBREF 9CB5 B 307 647 UNP P19338 NUCL_HUMAN 307 647 DBREF 9CB5 C -4 23 PDB 9CB5 9CB5 -4 23 DBREF 9CB5 D -1 244 PDB 9CB5 9CB5 -1 244 DBREF 9CB5 F -4 23 PDB 9CB5 9CB5 -4 23 DBREF 9CB5 G -1 244 PDB 9CB5 9CB5 -1 244 DBREF 9CB5 H -2 212 PDB 9CB5 9CB5 -2 212 DBREF 9CB5 I -2 212 PDB 9CB5 9CB5 -2 212 SEQADV 9CB5 GLY A 301 UNP P19338 EXPRESSION TAG SEQADV 9CB5 GLY A 302 UNP P19338 EXPRESSION TAG SEQADV 9CB5 GLY A 303 UNP P19338 EXPRESSION TAG SEQADV 9CB5 GLY A 304 UNP P19338 EXPRESSION TAG SEQADV 9CB5 HIS A 305 UNP P19338 EXPRESSION TAG SEQADV 9CB5 MET A 306 UNP P19338 EXPRESSION TAG SEQADV 9CB5 SER A 543 UNP P19338 CYS 543 CONFLICT SEQADV 9CB5 GLY B 301 UNP P19338 EXPRESSION TAG SEQADV 9CB5 GLY B 302 UNP P19338 EXPRESSION TAG SEQADV 9CB5 GLY B 303 UNP P19338 EXPRESSION TAG SEQADV 9CB5 GLY B 304 UNP P19338 EXPRESSION TAG SEQADV 9CB5 HIS B 305 UNP P19338 EXPRESSION TAG SEQADV 9CB5 MET B 306 UNP P19338 EXPRESSION TAG SEQADV 9CB5 SER B 543 UNP P19338 CYS 543 CONFLICT SEQRES 1 A 347 GLY GLY GLY GLY HIS MET PHE ASN LEU PHE VAL GLY ASN SEQRES 2 A 347 LEU ASN PHE ASN LYS SER ALA PRO GLU LEU LYS THR GLY SEQRES 3 A 347 ILE SER ASP VAL PHE ALA LYS ASN ASP LEU ALA VAL VAL SEQRES 4 A 347 ASP VAL ARG ILE GLY MET THR ARG LYS PHE GLY TYR VAL SEQRES 5 A 347 ASP PHE GLU SER ALA GLU ASP LEU GLU LYS ALA LEU GLU SEQRES 6 A 347 LEU THR GLY LEU LYS VAL PHE GLY ASN GLU ILE LYS LEU SEQRES 7 A 347 GLU LYS PRO LYS GLY LYS ASP SER LYS LYS GLU ARG ASP SEQRES 8 A 347 ALA ARG THR LEU LEU ALA LYS ASN LEU PRO TYR LYS VAL SEQRES 9 A 347 THR GLN ASP GLU LEU LYS GLU VAL PHE GLU ASP ALA ALA SEQRES 10 A 347 GLU ILE ARG LEU VAL SER LYS ASP GLY LYS SER LYS GLY SEQRES 11 A 347 ILE ALA TYR ILE GLU PHE LYS THR GLU ALA ASP ALA GLU SEQRES 12 A 347 LYS THR PHE GLU GLU LYS GLN GLY THR GLU ILE ASP GLY SEQRES 13 A 347 ARG SER ILE SER LEU TYR TYR THR GLY GLU LYS GLY GLN SEQRES 14 A 347 ASN GLN ASP TYR ARG GLY GLY LYS ASN SER THR TRP SER SEQRES 15 A 347 GLY GLU SER LYS THR LEU VAL LEU SER ASN LEU SER TYR SEQRES 16 A 347 SER ALA THR GLU GLU THR LEU GLN GLU VAL PHE GLU LYS SEQRES 17 A 347 ALA THR PHE ILE LYS VAL PRO GLN ASN GLN ASN GLY LYS SEQRES 18 A 347 SER LYS GLY TYR ALA PHE ILE GLU PHE ALA SER PHE GLU SEQRES 19 A 347 ASP ALA LYS GLU ALA LEU ASN SER SER ASN LYS ARG GLU SEQRES 20 A 347 ILE GLU GLY ARG ALA ILE ARG LEU GLU LEU GLN GLY PRO SEQRES 21 A 347 ARG GLY SER PRO ASN ALA ARG SER GLN PRO SER LYS THR SEQRES 22 A 347 LEU PHE VAL LYS GLY LEU SER GLU ASP THR THR GLU GLU SEQRES 23 A 347 THR LEU LYS GLU SER PHE ASP GLY SER VAL ARG ALA ARG SEQRES 24 A 347 ILE VAL THR ASP ARG GLU THR GLY SER SER LYS GLY PHE SEQRES 25 A 347 GLY PHE VAL ASP PHE ASN SER GLU GLU ASP ALA LYS ALA SEQRES 26 A 347 ALA LYS GLU ALA MET GLU ASP GLY GLU ILE ASP GLY ASN SEQRES 27 A 347 LYS VAL THR LEU ASP TRP ALA LYS PRO SEQRES 1 B 347 GLY GLY GLY GLY HIS MET PHE ASN LEU PHE VAL GLY ASN SEQRES 2 B 347 LEU ASN PHE ASN LYS SER ALA PRO GLU LEU LYS THR GLY SEQRES 3 B 347 ILE SER ASP VAL PHE ALA LYS ASN ASP LEU ALA VAL VAL SEQRES 4 B 347 ASP VAL ARG ILE GLY MET THR ARG LYS PHE GLY TYR VAL SEQRES 5 B 347 ASP PHE GLU SER ALA GLU ASP LEU GLU LYS ALA LEU GLU SEQRES 6 B 347 LEU THR GLY LEU LYS VAL PHE GLY ASN GLU ILE LYS LEU SEQRES 7 B 347 GLU LYS PRO LYS GLY LYS ASP SER LYS LYS GLU ARG ASP SEQRES 8 B 347 ALA ARG THR LEU LEU ALA LYS ASN LEU PRO TYR LYS VAL SEQRES 9 B 347 THR GLN ASP GLU LEU LYS GLU VAL PHE GLU ASP ALA ALA SEQRES 10 B 347 GLU ILE ARG LEU VAL SER LYS ASP GLY LYS SER LYS GLY SEQRES 11 B 347 ILE ALA TYR ILE GLU PHE LYS THR GLU ALA ASP ALA GLU SEQRES 12 B 347 LYS THR PHE GLU GLU LYS GLN GLY THR GLU ILE ASP GLY SEQRES 13 B 347 ARG SER ILE SER LEU TYR TYR THR GLY GLU LYS GLY GLN SEQRES 14 B 347 ASN GLN ASP TYR ARG GLY GLY LYS ASN SER THR TRP SER SEQRES 15 B 347 GLY GLU SER LYS THR LEU VAL LEU SER ASN LEU SER TYR SEQRES 16 B 347 SER ALA THR GLU GLU THR LEU GLN GLU VAL PHE GLU LYS SEQRES 17 B 347 ALA THR PHE ILE LYS VAL PRO GLN ASN GLN ASN GLY LYS SEQRES 18 B 347 SER LYS GLY TYR ALA PHE ILE GLU PHE ALA SER PHE GLU SEQRES 19 B 347 ASP ALA LYS GLU ALA LEU ASN SER SER ASN LYS ARG GLU SEQRES 20 B 347 ILE GLU GLY ARG ALA ILE ARG LEU GLU LEU GLN GLY PRO SEQRES 21 B 347 ARG GLY SER PRO ASN ALA ARG SER GLN PRO SER LYS THR SEQRES 22 B 347 LEU PHE VAL LYS GLY LEU SER GLU ASP THR THR GLU GLU SEQRES 23 B 347 THR LEU LYS GLU SER PHE ASP GLY SER VAL ARG ALA ARG SEQRES 24 B 347 ILE VAL THR ASP ARG GLU THR GLY SER SER LYS GLY PHE SEQRES 25 B 347 GLY PHE VAL ASP PHE ASN SER GLU GLU ASP ALA LYS ALA SEQRES 26 B 347 ALA LYS GLU ALA MET GLU ASP GLY GLU ILE ASP GLY ASN SEQRES 27 B 347 LYS VAL THR LEU ASP TRP ALA LYS PRO SEQRES 1 C 28 DA DT DC DG DC DT DA DG DG DG DA DG DG SEQRES 2 C 28 DG DT DT DT DT DT DA DG DG DG DT DG DG SEQRES 3 C 28 DG DT SEQRES 1 D 246 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 D 246 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 D 246 ALA SER GLY PHE ASN ILE TYR TYR TYR SER ILE HIS TRP SEQRES 4 D 246 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 D 246 SER ILE SER PRO SER TYR GLY TYR THR SER TYR ALA ASP SEQRES 6 D 246 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 D 246 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 D 246 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TRP SER ARG SEQRES 9 D 246 TRP ALA TYR SER TYR TRP SER TYR LYS SER TYR GLY MET SEQRES 10 D 246 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 11 D 246 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 D 246 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 D 246 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 D 246 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 D 246 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 D 246 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 D 246 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 D 246 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 19 D 246 LYS THR HIS THR SER ARG HIS HIS HIS HIS HIS HIS SEQRES 1 F 28 DA DT DC DG DC DT DA DG DG DG DA DG DG SEQRES 2 F 28 DG DT DT DT DT DT DA DG DG DG DT DG DG SEQRES 3 F 28 DG DT SEQRES 1 G 246 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 G 246 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 G 246 ALA SER GLY PHE ASN ILE TYR TYR TYR SER ILE HIS TRP SEQRES 4 G 246 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 G 246 SER ILE SER PRO SER TYR GLY TYR THR SER TYR ALA ASP SEQRES 6 G 246 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 G 246 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 G 246 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TRP SER ARG SEQRES 9 G 246 TRP ALA TYR SER TYR TRP SER TYR LYS SER TYR GLY MET SEQRES 10 G 246 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 11 G 246 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 G 246 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 G 246 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 G 246 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 G 246 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 G 246 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 G 246 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 G 246 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 19 G 246 LYS THR HIS THR SER ARG HIS HIS HIS HIS HIS HIS SEQRES 1 H 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 H 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 H 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 H 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 H 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 H 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 H 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 H 215 SER GLY GLY GLY PRO ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 H 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 H 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 H 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 H 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 H 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 H 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 H 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 H 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 H 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 I 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 I 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 I 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 I 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 I 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 I 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 I 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 I 215 SER GLY GLY GLY PRO ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 I 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 I 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 I 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 I 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 I 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 I 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 I 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 I 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 I 215 SER PHE ASN ARG GLY GLU CYS HET K C 101 1 HET K C 102 1 HET K F 101 1 HET K F 102 1 HETNAM K POTASSIUM ION FORMUL 9 K 4(K 1+) FORMUL 13 HOH *189(H2 O) HELIX 1 AA1 SER A 319 ASN A 334 1 16 HELIX 2 AA2 SER A 356 GLU A 365 1 10 HELIX 3 AA3 ALA A 442 GLU A 447 1 6 HELIX 4 AA4 SER B 319 ASN B 334 1 16 HELIX 5 AA5 SER B 356 GLU B 365 1 10 HELIX 6 AA6 LYS B 384 ALA B 392 1 9 HELIX 7 AA7 THR B 405 PHE B 413 1 9 HELIX 8 AA8 THR B 438 LYS B 449 1 12 HELIX 9 AA9 ASN D 29 TYR D 33 5 5 HELIX 10 AB1 ARG D 88 THR D 92 5 5 HELIX 11 AB2 SER D 106 SER D 112 5 7 HELIX 12 AB3 SER D 142 THR D 146 5 5 HELIX 13 AB4 SER D 171 ALA D 173 5 3 HELIX 14 AB5 SER D 202 THR D 206 5 5 HELIX 15 AB6 LYS D 216 ASN D 219 5 4 HELIX 16 AB7 ASN G 29 TYR G 33 5 5 HELIX 17 AB8 ARG G 88 THR G 92 5 5 HELIX 18 AB9 SER G 106 SER G 112 5 7 HELIX 19 AC1 HIS G 215 ASN G 219 5 5 HELIX 20 AC2 GLN H 77 PHE H 81 5 5 HELIX 21 AC3 SER H 119 LYS H 124 1 6 HELIX 22 AC4 SER H 180 GLU H 185 1 6 HELIX 23 AC5 GLN I 77 PHE I 81 5 5 HELIX 24 AC6 LYS I 181 LYS I 186 1 6 SHEET 1 AA1 3 PHE A 349 ASP A 353 0 SHEET 2 AA1 3 ASN A 308 GLY A 312 -1 N LEU A 309 O VAL A 352 SHEET 3 AA1 3 LYS A 377 GLU A 379 -1 O GLU A 379 N PHE A 310 SHEET 1 AA2 2 LYS A 370 VAL A 371 0 SHEET 2 AA2 2 ASN A 374 GLU A 375 -1 O ASN A 374 N VAL A 371 SHEET 1 AA3 2 LEU A 395 LEU A 396 0 SHEET 2 AA3 2 TYR A 462 TYR A 463 -1 O TYR A 462 N LEU A 396 SHEET 1 AA4 4 ASP B 340 ILE B 343 0 SHEET 2 AA4 4 PHE B 349 ASP B 353 -1 O TYR B 351 N ARG B 342 SHEET 3 AA4 4 ASN B 308 GLY B 312 -1 N LEU B 309 O VAL B 352 SHEET 4 AA4 4 LYS B 377 GLU B 379 -1 O LYS B 377 N GLY B 312 SHEET 1 AA5 2 LYS B 370 VAL B 371 0 SHEET 2 AA5 2 ASN B 374 GLU B 375 -1 O ASN B 374 N VAL B 371 SHEET 1 AA6 4 GLU B 418 LYS B 424 0 SHEET 2 AA6 4 LYS B 427 GLU B 435 -1 O GLU B 435 N GLU B 418 SHEET 3 AA6 4 THR B 394 LYS B 398 -1 N LEU B 395 O ILE B 434 SHEET 4 AA6 4 SER B 460 TYR B 463 -1 O TYR B 462 N LEU B 396 SHEET 1 AA7 2 GLU B 453 ILE B 454 0 SHEET 2 AA7 2 ARG B 457 SER B 458 -1 O ARG B 457 N ILE B 454 SHEET 1 AA8 4 GLN D 4 SER D 8 0 SHEET 2 AA8 4 LEU D 19 SER D 26 -1 O ALA D 24 N VAL D 6 SHEET 3 AA8 4 THR D 79 MET D 84 -1 O ALA D 80 N CYS D 23 SHEET 4 AA8 4 PHE D 69 ASP D 74 -1 N SER D 72 O TYR D 81 SHEET 1 AA9 6 GLY D 11 VAL D 13 0 SHEET 2 AA9 6 THR D 122 VAL D 126 1 O THR D 125 N GLY D 11 SHEET 3 AA9 6 ALA D 93 TRP D 100 -1 N TYR D 95 O THR D 122 SHEET 4 AA9 6 ILE D 35 GLN D 40 -1 N VAL D 38 O TYR D 96 SHEET 5 AA9 6 LEU D 46 SER D 53 -1 O VAL D 49 N TRP D 37 SHEET 6 AA9 6 TYR D 58 TYR D 61 -1 O TYR D 58 N SER D 53 SHEET 1 AB1 4 GLY D 11 VAL D 13 0 SHEET 2 AB1 4 THR D 122 VAL D 126 1 O THR D 125 N GLY D 11 SHEET 3 AB1 4 ALA D 93 TRP D 100 -1 N TYR D 95 O THR D 122 SHEET 4 AB1 4 MET D 115 TRP D 118 -1 O TYR D 117 N ARG D 99 SHEET 1 AB2 4 SER D 135 LEU D 139 0 SHEET 2 AB2 4 ALA D 151 TYR D 160 -1 O LEU D 156 N PHE D 137 SHEET 3 AB2 4 TYR D 191 VAL D 199 -1 O LEU D 193 N VAL D 157 SHEET 4 AB2 4 HIS D 179 LEU D 185 -1 N HIS D 179 O VAL D 196 SHEET 1 AB3 3 THR D 166 TRP D 169 0 SHEET 2 AB3 3 CYS D 211 HIS D 215 -1 O ASN D 212 N SER D 168 SHEET 3 AB3 3 THR D 220 VAL D 222 -1 O THR D 220 N HIS D 215 SHEET 1 AB4 4 GLN G 4 SER G 8 0 SHEET 2 AB4 4 LEU G 19 SER G 26 -1 O ALA G 24 N VAL G 6 SHEET 3 AB4 4 THR G 79 MET G 84 -1 O MET G 84 N LEU G 19 SHEET 4 AB4 4 PHE G 69 ASP G 74 -1 N SER G 72 O TYR G 81 SHEET 1 AB5 6 LEU G 12 VAL G 13 0 SHEET 2 AB5 6 THR G 122 VAL G 126 1 O THR G 125 N VAL G 13 SHEET 3 AB5 6 ALA G 93 TRP G 100 -1 N TYR G 95 O THR G 122 SHEET 4 AB5 6 ILE G 35 GLN G 40 -1 N VAL G 38 O TYR G 96 SHEET 5 AB5 6 LEU G 46 SER G 53 -1 O ALA G 50 N TRP G 37 SHEET 6 AB5 6 TYR G 58 TYR G 61 -1 O TYR G 58 N SER G 53 SHEET 1 AB6 4 LEU G 12 VAL G 13 0 SHEET 2 AB6 4 THR G 122 VAL G 126 1 O THR G 125 N VAL G 13 SHEET 3 AB6 4 ALA G 93 TRP G 100 -1 N TYR G 95 O THR G 122 SHEET 4 AB6 4 MET G 115 TRP G 118 -1 O ASP G 116 N ARG G 99 SHEET 1 AB7 2 ALA G 151 ALA G 152 0 SHEET 2 AB7 2 THR G 198 VAL G 199 -1 O VAL G 199 N ALA G 151 SHEET 1 AB8 3 CYS G 155 TYR G 160 0 SHEET 2 AB8 3 TYR G 191 VAL G 196 -1 O LEU G 193 N VAL G 157 SHEET 3 AB8 3 HIS G 179 THR G 180 -1 N HIS G 179 O VAL G 196 SHEET 1 AB9 3 CYS G 155 TYR G 160 0 SHEET 2 AB9 3 TYR G 191 VAL G 196 -1 O LEU G 193 N VAL G 157 SHEET 3 AB9 3 VAL G 184 LEU G 185 -1 N VAL G 184 O SER G 192 SHEET 1 AC1 2 SER G 168 TRP G 169 0 SHEET 2 AC1 2 CYS G 211 ASN G 212 -1 O ASN G 212 N SER G 168 SHEET 1 AC2 4 MET H 2 SER H 5 0 SHEET 2 AC2 4 VAL H 17 ALA H 23 -1 O ARG H 22 N THR H 3 SHEET 3 AC2 4 ASP H 68 ILE H 73 -1 O LEU H 71 N ILE H 19 SHEET 4 AC2 4 PHE H 60 SER H 65 -1 N SER H 65 O ASP H 68 SHEET 1 AC3 6 SER H 8 ALA H 11 0 SHEET 2 AC3 6 THR H 100 ILE H 104 1 O GLU H 103 N LEU H 9 SHEET 3 AC3 6 THR H 83 GLN H 88 -1 N TYR H 84 O THR H 100 SHEET 4 AC3 6 VAL H 31 GLN H 36 -1 N TYR H 34 O TYR H 85 SHEET 5 AC3 6 LYS H 43 TYR H 47 -1 O LEU H 45 N TRP H 33 SHEET 6 AC3 6 SER H 51 LEU H 52 -1 O SER H 51 N TYR H 47 SHEET 1 AC4 4 SER H 8 ALA H 11 0 SHEET 2 AC4 4 THR H 100 ILE H 104 1 O GLU H 103 N LEU H 9 SHEET 3 AC4 4 THR H 83 GLN H 88 -1 N TYR H 84 O THR H 100 SHEET 4 AC4 4 THR H 95 PHE H 96 -1 O THR H 95 N GLN H 88 SHEET 1 AC5 4 SER H 112 PHE H 116 0 SHEET 2 AC5 4 ALA H 128 PHE H 137 -1 O LEU H 133 N PHE H 114 SHEET 3 AC5 4 TYR H 171 LEU H 179 -1 O LEU H 177 N VAL H 130 SHEET 4 AC5 4 SER H 157 VAL H 161 -1 N GLN H 158 O THR H 176 SHEET 1 AC6 4 ALA H 151 LEU H 152 0 SHEET 2 AC6 4 ALA H 142 VAL H 148 -1 N VAL H 148 O ALA H 151 SHEET 3 AC6 4 TYR H 190 HIS H 196 -1 O GLU H 193 N GLN H 145 SHEET 4 AC6 4 VAL H 203 PHE H 207 -1 O VAL H 203 N VAL H 194 SHEET 1 AC7 4 MET I 2 SER I 5 0 SHEET 2 AC7 4 VAL I 17 ALA I 23 -1 O ARG I 22 N THR I 3 SHEET 3 AC7 4 ASP I 68 ILE I 73 -1 O PHE I 69 N CYS I 21 SHEET 4 AC7 4 PHE I 60 ARG I 64 -1 N SER I 61 O THR I 72 SHEET 1 AC8 6 SER I 8 ALA I 11 0 SHEET 2 AC8 6 THR I 100 ILE I 104 1 O LYS I 101 N LEU I 9 SHEET 3 AC8 6 THR I 83 GLN I 88 -1 N TYR I 84 O THR I 100 SHEET 4 AC8 6 VAL I 31 GLN I 36 -1 N TYR I 34 O TYR I 85 SHEET 5 AC8 6 LYS I 43 TYR I 47 -1 O LEU I 45 N TRP I 33 SHEET 6 AC8 6 SER I 51 LEU I 52 -1 O SER I 51 N TYR I 47 SHEET 1 AC9 4 SER I 8 ALA I 11 0 SHEET 2 AC9 4 THR I 100 ILE I 104 1 O LYS I 101 N LEU I 9 SHEET 3 AC9 4 THR I 83 GLN I 88 -1 N TYR I 84 O THR I 100 SHEET 4 AC9 4 THR I 95 PHE I 96 -1 O THR I 95 N GLN I 88 SHEET 1 AD1 4 PHE I 114 PHE I 116 0 SHEET 2 AD1 4 THR I 127 PHE I 137 -1 O VAL I 131 N PHE I 116 SHEET 3 AD1 4 TYR I 171 SER I 180 -1 O LEU I 173 N LEU I 134 SHEET 4 AD1 4 SER I 157 VAL I 161 -1 N GLN I 158 O THR I 176 SHEET 1 AD2 4 ALA I 151 LEU I 152 0 SHEET 2 AD2 4 VAL I 144 VAL I 148 -1 N VAL I 148 O ALA I 151 SHEET 3 AD2 4 TYR I 190 VAL I 194 -1 O GLU I 193 N GLN I 145 SHEET 4 AD2 4 THR I 204 PHE I 207 -1 O LYS I 205 N CYS I 192 SSBOND 1 CYS D 23 CYS D 97 1555 1555 2.03 SSBOND 2 CYS D 155 CYS D 211 1555 1555 2.04 SSBOND 3 CYS G 23 CYS G 97 1555 1555 2.03 SSBOND 4 CYS G 155 CYS G 211 1555 1555 2.03 SSBOND 5 CYS G 231 CYS I 212 1555 1555 2.03 SSBOND 6 CYS H 21 CYS H 86 1555 1555 2.03 SSBOND 7 CYS H 132 CYS H 192 1555 1555 2.03 SSBOND 8 CYS I 21 CYS I 86 1555 1555 2.03 SSBOND 9 CYS I 132 CYS I 192 1555 1555 2.03 LINK O6 DG C 3 K K C 101 1555 1555 2.68 LINK O6 DG C 4 K K C 101 1555 1555 2.86 LINK O6 DG C 4 K K C 102 1555 1555 2.83 LINK O6 DG C 5 K K C 102 1555 1555 2.78 LINK O6 DG C 7 K K C 101 1555 1555 2.82 LINK O6 DG C 8 K K C 101 1555 1555 2.85 LINK O6 DG C 8 K K C 102 1555 1555 2.71 LINK O6 DG C 9 K K C 102 1555 1555 2.66 LINK O6 DG C 16 K K C 101 1555 1555 2.75 LINK O6 DG C 17 K K C 101 1555 1555 2.87 LINK O6 DG C 17 K K C 102 1555 1555 2.75 LINK O6 DG C 18 K K C 102 1555 1555 2.87 LINK O6 DG C 20 K K C 101 1555 1555 2.75 LINK O6 DG C 21 K K C 101 1555 1555 2.84 LINK O6 DG C 21 K K C 102 1555 1555 3.11 LINK O6 DG C 22 K K C 102 1555 1555 2.81 LINK O6 DG F 3 K K F 101 1555 1555 2.72 LINK O6 DG F 4 K K F 101 1555 1555 2.75 LINK O6 DG F 4 K K F 102 1555 1555 3.04 LINK O6 DG F 5 K K F 102 1555 1555 2.81 LINK O6 DG F 7 K K F 101 1555 1555 3.14 LINK O6 DG F 8 K K F 101 1555 1555 2.79 LINK O6 DG F 8 K K F 102 1555 1555 2.96 LINK O6 DG F 9 K K F 102 1555 1555 2.78 LINK O6 DG F 16 K K F 101 1555 1555 2.60 LINK O6 DG F 17 K K F 101 1555 1555 2.79 LINK O6 DG F 17 K K F 102 1555 1555 2.77 LINK O6 DG F 18 K K F 102 1555 1555 2.70 LINK O6 DG F 20 K K F 101 1555 1555 3.18 LINK O6 DG F 21 K K F 101 1555 1555 2.93 LINK O6 DG F 21 K K F 102 1555 1555 3.15 LINK O6 DG F 22 K K F 102 1555 1555 2.66 CISPEP 1 PHE D 161 PRO D 162 0 -3.79 CISPEP 2 GLU D 163 PRO D 164 0 0.71 CISPEP 3 PHE G 161 PRO G 162 0 -5.24 CISPEP 4 GLU G 163 PRO G 164 0 10.71 CISPEP 5 SER H 5 PRO H 6 0 -4.34 CISPEP 6 TYR H 138 PRO H 139 0 1.91 CISPEP 7 SER I 5 PRO I 6 0 1.74 CISPEP 8 TYR I 138 PRO I 139 0 2.50 CRYST1 75.253 134.660 185.259 90.00 90.00 90.00 P 21 21 21 8 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 0.013289 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007426 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005398 0.00000