HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 12-NOV-15 5EQB
TITLE CRYSTAL STRUCTURE OF LANOSTEROL 14-ALPHA DEMETHYLASE WITH INTACT
TITLE 2 TRANSMEMBRANE DOMAIN BOUND TO ITRACONAZOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LANOSTEROL 14-ALPHA DEMETHYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYPLI,CYTOCHROME P450 51,CYTOCHROME P450-14DM,CYTOCHROME
COMPND 5 P450-LIA1,STEROL 14-ALPHA DEMETHYLASE;
COMPND 6 EC: 1.14.13.70;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: ERG11, CYP51, YHR007C;
SOURCE 8 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS STEROL ANTIFUNGAL MEMBRANE CYTOCHROME, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, CENTER FOR STRUCTURES OF MEMBRANE
KEYWDS 3 PROTEINS, CSMP, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.MONK,T.M.TOMASIAK,M.V.KENIYA,F.U.HUSCHMANN,J.D.A.TYNDALL,
AUTHOR 2 J.D.O'CONNELL III,R.D.CANNON,J.FINER-MORRE,R.M.STROUD,CENTER FOR
AUTHOR 3 STRUCTURES OF MEMBRANE PROTEINS (CSMP)
REVDAT 2 06-MAR-24 5EQB 1 JRNL REMARK
REVDAT 1 13-JAN-16 5EQB 0
SPRSDE 13-JAN-16 5EQB 4K0F
JRNL AUTH B.C.MONK,T.M.TOMASIAK,M.V.KENIYA,F.U.HUSCHMANN,J.D.TYNDALL,
JRNL AUTH 2 J.D.O'CONNELL,R.D.CANNON,J.G.MCDONALD,A.RODRIGUEZ,
JRNL AUTH 3 J.S.FINER-MOORE,R.M.STROUD
JRNL TITL ARCHITECTURE OF A SINGLE MEMBRANE SPANNING CYTOCHROME P450
JRNL TITL 2 SUGGESTS CONSTRAINTS THAT ORIENT THE CATALYTIC DOMAIN
JRNL TITL 3 RELATIVE TO A BILAYER.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 3865 2014
JRNL REFN ESSN 1091-6490
JRNL PMID 24613931
JRNL DOI 10.1073/PNAS.1324245111
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1664
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 42460
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2139
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 29.8778 - 5.3831 0.91 2625 140 0.1856 0.2056
REMARK 3 2 5.3831 - 4.2767 0.94 2668 140 0.1604 0.1747
REMARK 3 3 4.2767 - 3.7373 0.95 2626 161 0.1736 0.2149
REMARK 3 4 3.7373 - 3.3961 0.96 2690 134 0.1879 0.2140
REMARK 3 5 3.3961 - 3.1530 0.97 2697 152 0.2090 0.2708
REMARK 3 6 3.1530 - 2.9673 0.97 2679 157 0.2107 0.2601
REMARK 3 7 2.9673 - 2.8188 0.98 2712 141 0.2003 0.2488
REMARK 3 8 2.8188 - 2.6962 0.98 2737 132 0.2018 0.2580
REMARK 3 9 2.6962 - 2.5924 0.98 2731 130 0.1960 0.2381
REMARK 3 10 2.5924 - 2.5030 0.98 2713 147 0.1951 0.2296
REMARK 3 11 2.5030 - 2.4248 0.99 2738 146 0.1958 0.2327
REMARK 3 12 2.4248 - 2.3555 0.99 2778 121 0.2127 0.2730
REMARK 3 13 2.3555 - 2.2935 0.99 2713 150 0.2257 0.2817
REMARK 3 14 2.2935 - 2.2376 0.99 2726 144 0.2384 0.3001
REMARK 3 15 2.2376 - 2.1867 0.91 2488 144 0.2675 0.3035
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.011 4532
REMARK 3 ANGLE : 1.181 6159
REMARK 3 CHIRALITY : 0.050 648
REMARK 3 PLANARITY : 0.007 811
REMARK 3 DIHEDRAL : 13.938 1699
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 5EQB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000211385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42829
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
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: NULL
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 (%): 65.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 45% PEG 400, 0.1M GLYCINE, PH 9.3,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 33.92250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 LYS A 5
REMARK 465 HIS A 537
REMARK 465 HIS A 538
REMARK 465 HIS A 539
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 OE1 GLU A 249 NH1 ARG A 252 2.03
REMARK 500 OH TYR A 293 O HOH A 701 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 ARG A 489 NE - CZ - NH2 ANGL. DEV. = -3.5 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 TRP A 65 -48.59 70.03
REMARK 500 LYS A 75 70.92 -150.77
REMARK 500 ILE A 139 -112.72 58.44
REMARK 500 LEU A 158 57.99 -111.27
REMARK 500 PHE A 184 -80.70 -127.36
REMARK 500 GLN A 279 -147.06 -118.87
REMARK 500 SER A 291 19.25 -152.50
REMARK 500 MET A 363 72.47 -119.56
REMARK 500 ASP A 434 58.49 -159.82
REMARK 500 THR A 511 49.95 -81.08
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 HEM A 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 470 SG
REMARK 620 2 HEM A 601 NA 96.3
REMARK 620 3 HEM A 601 NB 87.1 84.6
REMARK 620 4 HEM A 601 NC 84.1 174.0 89.4
REMARK 620 5 HEM A 601 ND 92.5 93.8 178.4 92.2
REMARK 620 6 1YN A 602 N39 172.1 90.4 97.6 89.6 83.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1YN A 602
DBREF 5EQB A 1 530 UNP P10614 CP51_YEAST 1 530
SEQADV 5EQB ASN A 433 UNP P10614 LYS 433 CONFLICT
SEQADV 5EQB GLY A 531 UNP P10614 EXPRESSION TAG
SEQADV 5EQB GLY A 532 UNP P10614 EXPRESSION TAG
SEQADV 5EQB ARG A 533 UNP P10614 EXPRESSION TAG
SEQADV 5EQB HIS A 534 UNP P10614 EXPRESSION TAG
SEQADV 5EQB HIS A 535 UNP P10614 EXPRESSION TAG
SEQADV 5EQB HIS A 536 UNP P10614 EXPRESSION TAG
SEQADV 5EQB HIS A 537 UNP P10614 EXPRESSION TAG
SEQADV 5EQB HIS A 538 UNP P10614 EXPRESSION TAG
SEQADV 5EQB HIS A 539 UNP P10614 EXPRESSION TAG
SEQRES 1 A 539 MET SER ALA THR LYS SER ILE VAL GLY GLU ALA LEU GLU
SEQRES 2 A 539 TYR VAL ASN ILE GLY LEU SER HIS PHE LEU ALA LEU PRO
SEQRES 3 A 539 LEU ALA GLN ARG ILE SER LEU ILE ILE ILE ILE PRO PHE
SEQRES 4 A 539 ILE TYR ASN ILE VAL TRP GLN LEU LEU TYR SER LEU ARG
SEQRES 5 A 539 LYS ASP ARG PRO PRO LEU VAL PHE TYR TRP ILE PRO TRP
SEQRES 6 A 539 VAL GLY SER ALA VAL VAL TYR GLY MET LYS PRO TYR GLU
SEQRES 7 A 539 PHE PHE GLU GLU CYS GLN LYS LYS TYR GLY ASP ILE PHE
SEQRES 8 A 539 SER PHE VAL LEU LEU GLY ARG VAL MET THR VAL TYR LEU
SEQRES 9 A 539 GLY PRO LYS GLY HIS GLU PHE VAL PHE ASN ALA LYS LEU
SEQRES 10 A 539 ALA ASP VAL SER ALA GLU ALA ALA TYR ALA HIS LEU THR
SEQRES 11 A 539 THR PRO VAL PHE GLY LYS GLY VAL ILE TYR ASP CYS PRO
SEQRES 12 A 539 ASN SER ARG LEU MET GLU GLN LYS LYS PHE VAL LYS GLY
SEQRES 13 A 539 ALA LEU THR LYS GLU ALA PHE LYS SER TYR VAL PRO LEU
SEQRES 14 A 539 ILE ALA GLU GLU VAL TYR LYS TYR PHE ARG ASP SER LYS
SEQRES 15 A 539 ASN PHE ARG LEU ASN GLU ARG THR THR GLY THR ILE ASP
SEQRES 16 A 539 VAL MET VAL THR GLN PRO GLU MET THR ILE PHE THR ALA
SEQRES 17 A 539 SER ARG SER LEU LEU GLY LYS GLU MET ARG ALA LYS LEU
SEQRES 18 A 539 ASP THR ASP PHE ALA TYR LEU TYR SER ASP LEU ASP LYS
SEQRES 19 A 539 GLY PHE THR PRO ILE ASN PHE VAL PHE PRO ASN LEU PRO
SEQRES 20 A 539 LEU GLU HIS TYR ARG LYS ARG ASP HIS ALA GLN LYS ALA
SEQRES 21 A 539 ILE SER GLY THR TYR MET SER LEU ILE LYS GLU ARG ARG
SEQRES 22 A 539 LYS ASN ASN ASP ILE GLN ASP ARG ASP LEU ILE ASP SER
SEQRES 23 A 539 LEU MET LYS ASN SER THR TYR LYS ASP GLY VAL LYS MET
SEQRES 24 A 539 THR ASP GLN GLU ILE ALA ASN LEU LEU ILE GLY VAL LEU
SEQRES 25 A 539 MET GLY GLY GLN HIS THR SER ALA ALA THR SER ALA TRP
SEQRES 26 A 539 ILE LEU LEU HIS LEU ALA GLU ARG PRO ASP VAL GLN GLN
SEQRES 27 A 539 GLU LEU TYR GLU GLU GLN MET ARG VAL LEU ASP GLY GLY
SEQRES 28 A 539 LYS LYS GLU LEU THR TYR ASP LEU LEU GLN GLU MET PRO
SEQRES 29 A 539 LEU LEU ASN GLN THR ILE LYS GLU THR LEU ARG MET HIS
SEQRES 30 A 539 HIS PRO LEU HIS SER LEU PHE ARG LYS VAL MET LYS ASP
SEQRES 31 A 539 MET HIS VAL PRO ASN THR SER TYR VAL ILE PRO ALA GLY
SEQRES 32 A 539 TYR HIS VAL LEU VAL SER PRO GLY TYR THR HIS LEU ARG
SEQRES 33 A 539 ASP GLU TYR PHE PRO ASN ALA HIS GLN PHE ASN ILE HIS
SEQRES 34 A 539 ARG TRP ASN ASN ASP SER ALA SER SER TYR SER VAL GLY
SEQRES 35 A 539 GLU GLU VAL ASP TYR GLY PHE GLY ALA ILE SER LYS GLY
SEQRES 36 A 539 VAL SER SER PRO TYR LEU PRO PHE GLY GLY GLY ARG HIS
SEQRES 37 A 539 ARG CYS ILE GLY GLU HIS PHE ALA TYR CYS GLN LEU GLY
SEQRES 38 A 539 VAL LEU MET SER ILE PHE ILE ARG THR LEU LYS TRP HIS
SEQRES 39 A 539 TYR PRO GLU GLY LYS THR VAL PRO PRO PRO ASP PHE THR
SEQRES 40 A 539 SER MET VAL THR LEU PRO THR GLY PRO ALA LYS ILE ILE
SEQRES 41 A 539 TRP GLU LYS ARG ASN PRO GLU GLN LYS ILE GLY GLY ARG
SEQRES 42 A 539 HIS HIS HIS HIS HIS HIS
HET HEM A 601 43
HET 1YN A 602 49
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 1YN 2-[(2R)-BUTAN-2-YL]-4-{4-[4-(4-{[(2R,4S)-2-(2,4-
HETNAM 2 1YN DICHLOROPHENYL)-2-(1H-1,2,4-TRIAZOL-1-YLMETHYL)-1,3-
HETNAM 3 1YN DIOXOLAN-4-YL]METHOXY}PHENYL)PIPERAZIN-1-YL]PHENYL}-2,
HETNAM 4 1YN 4-DIHYDRO-3H-1,2,4-TRIAZOL-3-ONE
HETSYN HEM HEME
HETSYN 1YN ITRACONAZOLE
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 1YN C35 H38 CL2 N8 O4
FORMUL 4 HOH *124(H2 O)
HELIX 1 AA1 VAL A 8 LEU A 25 1 18
HELIX 2 AA2 PRO A 26 SER A 50 1 25
HELIX 3 AA3 SER A 68 LYS A 75 1 8
HELIX 4 AA4 LYS A 75 GLY A 88 1 14
HELIX 5 AA5 LEU A 104 ASN A 114 1 11
HELIX 6 AA6 ALA A 122 GLY A 135 1 14
HELIX 7 AA7 PRO A 143 ALA A 157 1 15
HELIX 8 AA8 THR A 159 SER A 181 1 23
HELIX 9 AA9 VAL A 196 LEU A 213 1 18
HELIX 10 AB1 GLY A 214 LEU A 221 1 8
HELIX 11 AB2 ASP A 222 ASP A 224 5 3
HELIX 12 AB3 PHE A 225 LYS A 234 1 10
HELIX 13 AB4 GLY A 235 THR A 237 5 3
HELIX 14 AB5 PRO A 238 PHE A 243 1 6
HELIX 15 AB6 LEU A 248 ASN A 275 1 28
HELIX 16 AB7 ASP A 282 ASN A 290 1 9
HELIX 17 AB8 THR A 300 ALA A 331 1 32
HELIX 18 AB9 ARG A 333 LEU A 348 1 16
HELIX 19 AC1 ASP A 349 LYS A 352 5 4
HELIX 20 AC2 THR A 356 GLN A 361 1 6
HELIX 21 AC3 MET A 363 HIS A 377 1 15
HELIX 22 AC4 SER A 409 HIS A 414 1 6
HELIX 23 AC5 ASN A 427 ASN A 432 5 6
HELIX 24 AC6 GLY A 465 ARG A 469 5 5
HELIX 25 AC7 GLY A 472 THR A 490 1 19
SHEET 1 AA1 5 ILE A 90 LEU A 95 0
SHEET 2 AA1 5 ARG A 98 TYR A 103 -1 O MET A 100 N PHE A 93
SHEET 3 AA1 5 HIS A 405 VAL A 408 1 O HIS A 405 N THR A 101
SHEET 4 AA1 5 LEU A 383 VAL A 387 -1 N LEU A 383 O VAL A 408
SHEET 5 AA1 5 VAL A 120 SER A 121 -1 N SER A 121 O LYS A 386
SHEET 1 AA2 3 THR A 191 ASP A 195 0
SHEET 2 AA2 3 LYS A 518 LYS A 523 -1 O ILE A 519 N ILE A 194
SHEET 3 AA2 3 LEU A 491 HIS A 494 -1 N HIS A 494 O ILE A 520
SHEET 1 AA3 2 MET A 391 HIS A 392 0
SHEET 2 AA3 2 VAL A 399 ILE A 400 -1 O ILE A 400 N MET A 391
SHEET 1 AA4 2 GLU A 444 ASP A 446 0
SHEET 2 AA4 2 ALA A 451 SER A 453 -1 O ILE A 452 N VAL A 445
LINK SG CYS A 470 FE HEM A 601 1555 1555 2.31
LINK FE HEM A 601 N39 1YN A 602 1555 1555 2.11
CISPEP 1 PRO A 394 ASN A 395 0 -7.49
CISPEP 2 GLY A 515 PRO A 516 0 -9.51
SITE 1 AC1 18 PHE A 113 TYR A 126 TYR A 140 LYS A 151
SITE 2 AC1 18 GLY A 315 THR A 318 PRO A 379 LEU A 383
SITE 3 AC1 18 ARG A 385 PRO A 462 PHE A 463 GLY A 464
SITE 4 AC1 18 HIS A 468 CYS A 470 GLY A 472 ALA A 476
SITE 5 AC1 18 1YN A 602 HOH A 729
SITE 1 AC2 19 ALA A 69 TYR A 72 GLY A 73 TYR A 126
SITE 2 AC2 19 PHE A 134 ILE A 139 TYR A 140 PHE A 236
SITE 3 AC2 19 PRO A 238 GLY A 310 GLY A 314 HIS A 381
SITE 4 AC2 19 SER A 382 PHE A 384 THR A 507 SER A 508
SITE 5 AC2 19 MET A 509 HEM A 601 HOH A 764
CRYST1 79.630 67.845 80.705 90.00 99.75 90.00 P 1 21 1 2
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 0.012558 0.000000 0.002158 0.00000
SCALE2 0.000000 0.014739 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012572 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
