HEADER HYDROLASE/HYDROLASE INHIBITOR 17-JUN-11 3SHY
TITLE CRYSTAL STRUCTURE OF THE PDE5A1 CATALYTIC DOMAIN IN COMPLEX WITH NOVEL
TITLE 2 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 535-860;
COMPND 5 SYNONYM: PDE5A1, CGMP-BINDING CGMP-SPECIFIC PHOSPHODIESTERASE, CGB-
COMPND 6 PDE;
COMPND 7 EC: 3.1.4.35;
COMPND 8 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: PDE5, PDE5A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PDE5A INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.T.CHEN,T.CHEN,Y.C.XU
REVDAT 3 20-MAR-24 3SHY 1 REMARK SEQADV LINK
REVDAT 2 08-NOV-17 3SHY 1 REMARK
REVDAT 1 24-AUG-11 3SHY 0
JRNL AUTH Z.XU,Z.LIU,T.CHEN,T.T.CHEN,Z.WANG,G.TIAN,J.SHI,X.WANG,Y.LU,
JRNL AUTH 2 X.YAN,G.WANG,H.JIANG,K.CHEN,S.WANG,Y.XU,J.SHEN,W.ZHU
JRNL TITL UTILIZATION OF HALOGEN BOND IN LEAD OPTIMIZATION: A CASE
JRNL TITL 2 STUDY OF RATIONAL DESIGN OF POTENT PHOSPHODIESTERASE TYPE 5
JRNL TITL 3 (PDE5) INHIBITORS.
JRNL REF J.MED.CHEM. V. 54 5607 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21714539
JRNL DOI 10.1021/JM200644R
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 12511
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 608
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 36.3344 - 4.1997 0.99 3137 162 0.2103 0.2522
REMARK 3 2 4.1997 - 3.3342 0.99 3040 162 0.1831 0.2501
REMARK 3 3 3.3342 - 2.9129 0.97 2927 150 0.2361 0.2686
REMARK 3 4 2.9129 - 2.6467 0.93 2799 134 0.2645 0.3097
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 51.95
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.51540
REMARK 3 B22 (A**2) : 2.51540
REMARK 3 B33 (A**2) : -5.03080
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.009 2354
REMARK 3 ANGLE : 1.191 3192
REMARK 3 CHIRALITY : 0.071 368
REMARK 3 PLANARITY : 0.005 403
REMARK 3 DIHEDRAL : 14.740 827
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3SHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-11
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12774
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.647
REMARK 200 RESOLUTION RANGE LOW (A) : 36.331
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19-20%(W/V) PEG 3350, 200MM MGSO4,
REMARK 280 100MM TRIS-HCL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.97533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 87.95067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 87.95067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 43.97533
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 514
REMARK 465 GLY A 515
REMARK 465 SER A 516
REMARK 465 SER A 517
REMARK 465 HIS A 518
REMARK 465 HIS A 519
REMARK 465 HIS A 520
REMARK 465 HIS A 521
REMARK 465 HIS A 522
REMARK 465 HIS A 523
REMARK 465 SER A 524
REMARK 465 SER A 525
REMARK 465 GLY A 526
REMARK 465 LEU A 527
REMARK 465 VAL A 528
REMARK 465 PRO A 529
REMARK 465 ARG A 530
REMARK 465 GLY A 531
REMARK 465 SER A 532
REMARK 465 HIS A 533
REMARK 465 MET A 534
REMARK 465 GLU A 535
REMARK 465 HIS A 670
REMARK 465 PRO A 671
REMARK 465 LEU A 672
REMARK 465 ALA A 673
REMARK 465 GLN A 674
REMARK 465 LEU A 675
REMARK 465 TYR A 676
REMARK 465 CYS A 677
REMARK 465 GLY A 790
REMARK 465 ASP A 791
REMARK 465 ARG A 792
REMARK 465 GLU A 793
REMARK 465 ARG A 794
REMARK 465 LYS A 795
REMARK 465 GLU A 796
REMARK 465 LEU A 797
REMARK 465 ASN A 798
REMARK 465 ILE A 799
REMARK 465 GLU A 800
REMARK 465 PRO A 801
REMARK 465 THR A 802
REMARK 465 ASP A 803
REMARK 465 LEU A 804
REMARK 465 MET A 805
REMARK 465 ASN A 806
REMARK 465 ARG A 807
REMARK 465 GLU A 808
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 GLU A 536 CG CD OE1 OE2
REMARK 470 ARG A 538 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 540 CG CD1 CD2
REMARK 470 GLN A 541 CG CD OE1 NE2
REMARK 470 LEU A 543 CD1 CD2
REMARK 470 GLN A 589 OE1 NE2
REMARK 470 LYS A 591 CD CE NZ
REMARK 470 GLU A 593 CG CD OE1 OE2
REMARK 470 ARG A 597 CZ NH1 NH2
REMARK 470 LYS A 604 CD CE NZ
REMARK 470 LYS A 608 CD CE NZ
REMARK 470 LYS A 633 CE NZ
REMARK 470 ASN A 636 CG OD1 ND2
REMARK 470 ASN A 662 OD1 ND2
REMARK 470 SER A 663 OG
REMARK 470 TYR A 664 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 665 CB CG1 CG2 CD1
REMARK 470 GLN A 666 CB CG CD OE1 NE2
REMARK 470 ARG A 667 CB CG CD NE CZ NH1 NH2
REMARK 470 SER A 668 CB OG
REMARK 470 GLU A 669 CB CG CD OE1 OE2
REMARK 470 ILE A 706 CD1
REMARK 470 GLU A 707 CG CD OE1 OE2
REMARK 470 LYS A 714 CG CD CE NZ
REMARK 470 LEU A 727 CD1 CD2
REMARK 470 LYS A 730 CD CE NZ
REMARK 470 LYS A 741 CG CD CE NZ
REMARK 470 ASN A 742 CG OD1 ND2
REMARK 470 GLN A 743 CD OE1 NE2
REMARK 470 LEU A 746 CG CD1 CD2
REMARK 470 GLU A 747 CG CD OE1 OE2
REMARK 470 LYS A 809 CG CD CE NZ
REMARK 470 LYS A 810 CG CD CE NZ
REMARK 470 ASN A 811 CG OD1 ND2
REMARK 470 LYS A 812 CG CD CE NZ
REMARK 470 ILE A 824 CD1
REMARK 470 LEU A 826 CD1 CD2
REMARK 470 GLU A 837 CG CD OE1 OE2
REMARK 470 GLN A 851 CD OE1 NE2
REMARK 470 GLN A 859 CG CD OE1 NE2
REMARK 470 GLN A 860 OE1 NE2
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 PHE A 561 150.50 -44.58
REMARK 500 ASN A 583 17.35 84.25
REMARK 500 GLN A 586 -72.67 -54.16
REMARK 500 LYS A 630 -76.11 -85.87
REMARK 500 ASN A 661 32.30 -95.46
REMARK 500 ARG A 667 -114.55 41.45
REMARK 500 ILE A 700 1.56 -62.07
REMARK 500 ASN A 742 10.24 43.92
REMARK 500 PRO A 841 -19.52 -48.92
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 MG A 862 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 11 O
REMARK 620 2 HOH A 864 O 150.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 861 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 617 NE2
REMARK 620 2 HIS A 653 NE2 88.2
REMARK 620 3 ASP A 654 OD2 88.9 81.4
REMARK 620 4 ASP A 764 OD1 76.3 83.0 158.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5FO A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 862
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T9R RELATED DB: PDB
REMARK 900 PDE5A CATALYTIC DOMAIN COMPLEX WITH INHIBITORS
REMARK 900 RELATED ID: 3SHZ RELATED DB: PDB
REMARK 900 RELATED ID: 3SIE RELATED DB: PDB
DBREF 3SHY A 535 860 UNP O76074 PDE5A_HUMAN 535 860
SEQADV 3SHY MET A 514 UNP O76074 EXPRESSION TAG
SEQADV 3SHY GLY A 515 UNP O76074 EXPRESSION TAG
SEQADV 3SHY SER A 516 UNP O76074 EXPRESSION TAG
SEQADV 3SHY SER A 517 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 518 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 519 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 520 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 521 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 522 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 523 UNP O76074 EXPRESSION TAG
SEQADV 3SHY SER A 524 UNP O76074 EXPRESSION TAG
SEQADV 3SHY SER A 525 UNP O76074 EXPRESSION TAG
SEQADV 3SHY GLY A 526 UNP O76074 EXPRESSION TAG
SEQADV 3SHY LEU A 527 UNP O76074 EXPRESSION TAG
SEQADV 3SHY VAL A 528 UNP O76074 EXPRESSION TAG
SEQADV 3SHY PRO A 529 UNP O76074 EXPRESSION TAG
SEQADV 3SHY ARG A 530 UNP O76074 EXPRESSION TAG
SEQADV 3SHY GLY A 531 UNP O76074 EXPRESSION TAG
SEQADV 3SHY SER A 532 UNP O76074 EXPRESSION TAG
SEQADV 3SHY HIS A 533 UNP O76074 EXPRESSION TAG
SEQADV 3SHY MET A 534 UNP O76074 EXPRESSION TAG
SEQRES 1 A 347 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 347 LEU VAL PRO ARG GLY SER HIS MET GLU GLU THR ARG GLU
SEQRES 3 A 347 LEU GLN SER LEU ALA ALA ALA VAL VAL PRO SER ALA GLN
SEQRES 4 A 347 THR LEU LYS ILE THR ASP PHE SER PHE SER ASP PHE GLU
SEQRES 5 A 347 LEU SER ASP LEU GLU THR ALA LEU CYS THR ILE ARG MET
SEQRES 6 A 347 PHE THR ASP LEU ASN LEU VAL GLN ASN PHE GLN MET LYS
SEQRES 7 A 347 HIS GLU VAL LEU CYS ARG TRP ILE LEU SER VAL LYS LYS
SEQRES 8 A 347 ASN TYR ARG LYS ASN VAL ALA TYR HIS ASN TRP ARG HIS
SEQRES 9 A 347 ALA PHE ASN THR ALA GLN CYS MET PHE ALA ALA LEU LYS
SEQRES 10 A 347 ALA GLY LYS ILE GLN ASN LYS LEU THR ASP LEU GLU ILE
SEQRES 11 A 347 LEU ALA LEU LEU ILE ALA ALA LEU SER HIS ASP LEU ASP
SEQRES 12 A 347 HIS ARG GLY VAL ASN ASN SER TYR ILE GLN ARG SER GLU
SEQRES 13 A 347 HIS PRO LEU ALA GLN LEU TYR CYS HIS SER ILE MET GLU
SEQRES 14 A 347 HIS HIS HIS PHE ASP GLN CYS LEU MET ILE LEU ASN SER
SEQRES 15 A 347 PRO GLY ASN GLN ILE LEU SER GLY LEU SER ILE GLU GLU
SEQRES 16 A 347 TYR LYS THR THR LEU LYS ILE ILE LYS GLN ALA ILE LEU
SEQRES 17 A 347 ALA THR ASP LEU ALA LEU TYR ILE LYS ARG ARG GLY GLU
SEQRES 18 A 347 PHE PHE GLU LEU ILE ARG LYS ASN GLN PHE ASN LEU GLU
SEQRES 19 A 347 ASP PRO HIS GLN LYS GLU LEU PHE LEU ALA MET LEU MET
SEQRES 20 A 347 THR ALA CYS ASP LEU SER ALA ILE THR LYS PRO TRP PRO
SEQRES 21 A 347 ILE GLN GLN ARG ILE ALA GLU LEU VAL ALA THR GLU PHE
SEQRES 22 A 347 PHE ASP GLN GLY ASP ARG GLU ARG LYS GLU LEU ASN ILE
SEQRES 23 A 347 GLU PRO THR ASP LEU MET ASN ARG GLU LYS LYS ASN LYS
SEQRES 24 A 347 ILE PRO SER MET GLN VAL GLY PHE ILE ASP ALA ILE CYS
SEQRES 25 A 347 LEU GLN LEU TYR GLU ALA LEU THR HIS VAL SER GLU ASP
SEQRES 26 A 347 CYS PHE PRO LEU LEU ASP GLY CYS ARG LYS ASN ARG GLN
SEQRES 27 A 347 LYS TRP GLN ALA LEU ALA GLU GLN GLN
HET 5FO A 1 30
HET ZN A 861 1
HET MG A 862 1
HET MG A 2 1
HET MG A 3 1
HETNAM 5FO 6-ETHYL-5-FLUORO-2-{5-[(4-METHYLPIPERAZIN-1-YL)
HETNAM 2 5FO SULFONYL]-2-PROPOXYPHENYL}PYRIMIDIN-4(3H)-ONE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 2 5FO C20 H27 F N4 O4 S
FORMUL 3 ZN ZN 2+
FORMUL 4 MG 3(MG 2+)
FORMUL 7 HOH *12(H2 O)
HELIX 1 1 THR A 537 ALA A 546 1 10
HELIX 2 2 SER A 550 LYS A 555 1 6
HELIX 3 3 SER A 567 LEU A 582 1 16
HELIX 4 4 ASN A 583 GLN A 589 1 7
HELIX 5 5 LYS A 591 ASN A 605 1 15
HELIX 6 6 ASN A 614 LYS A 630 1 17
HELIX 7 7 ILE A 634 LEU A 638 5 5
HELIX 8 8 THR A 639 HIS A 653 1 15
HELIX 9 9 SER A 679 ASN A 694 1 16
HELIX 10 10 SER A 705 THR A 723 1 19
HELIX 11 11 ASP A 724 LYS A 741 1 18
HELIX 12 12 ASP A 748 LEU A 765 1 18
HELIX 13 13 SER A 766 LYS A 770 5 5
HELIX 14 14 PRO A 771 GLN A 789 1 19
HELIX 15 15 LYS A 812 ILE A 824 1 13
HELIX 16 16 ILE A 824 SER A 836 1 13
HELIX 17 17 CYS A 839 GLN A 860 1 22
LINK O HOH A 11 MG MG A 862 1555 1555 2.61
LINK NE2 HIS A 617 ZN ZN A 861 1555 1555 2.40
LINK NE2 HIS A 653 ZN ZN A 861 1555 1555 2.38
LINK OD2 ASP A 654 ZN ZN A 861 1555 1555 2.21
LINK OD1 ASP A 764 ZN ZN A 861 1555 1555 2.27
LINK MG MG A 862 O HOH A 864 1555 1555 2.64
SITE 1 AC1 8 SER A 668 ALA A 779 PHE A 786 ILE A 813
SITE 2 AC1 8 MET A 816 GLN A 817 PHE A 820 HOH A 865
SITE 1 AC2 6 HIS A 617 HIS A 653 ASP A 654 ASP A 764
SITE 2 AC2 6 MG A 862 HOH A 864
SITE 1 AC3 5 HOH A 11 HIS A 613 ASP A 654 ZN A 861
SITE 2 AC3 5 HOH A 864
SITE 1 AC4 1 ASP A 568
CRYST1 74.458 74.458 131.926 90.00 90.00 120.00 P 31 2 1 6
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 0.013430 0.007754 0.000000 0.00000
SCALE2 0.000000 0.015508 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007580 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
