HEADER OXIDOREDUCTASE 14-JUL-04 1U13
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE C37L/C151T/C442A-TRIPLE MUTANT OF
TITLE 2 CYP51 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 51;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYPLI, P450-LIA1, STEROL 14- ALPHA DEMETHYLASE, LANOSTEROL
COMPND 5 14-ALPHA DEMETHYLASE, P450-14DM;
COMPND 6 EC: 1.14.13.70;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: NAME=CYP51; ORDEREDLOCUSNAMES=RV0764C, MT0788, MB0787C;
SOURCE 5 ORFNAMES=MTCY369.09C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS ALPHA-BETA, HEME CO-FACTOR, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.PODUST,L.V.YERMALITSKAYA,Y.KIM,M.R.WATERMAN
REVDAT 4 23-AUG-23 1U13 1 REMARK
REVDAT 3 27-OCT-21 1U13 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1U13 1 VERSN
REVDAT 1 27-JUL-04 1U13 0
JRNL AUTH L.M.PODUST,L.V.YERMALITSKAYA,Y.KIM,M.R.WATERMAN
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF THE C37L/C151T/C442A-TRIPLE
JRNL TITL 2 MUTANT OF CYP51 FROM MYCOBACTERIUM TUBERCULOSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 195159.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 28398
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2829
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3579
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 397
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3433
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.66000
REMARK 3 B22 (A**2) : -4.37000
REMARK 3 B33 (A**2) : -2.28000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.190 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.820 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.940 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 36.83
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : HEM.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : HEM.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-04
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 : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 46.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1E9X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, HEPES, ISOPROPANOL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING 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 23.14700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.23200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.56650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.23200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.14700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.56650
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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 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 GLU A 85
REMARK 465 GLY A 86
REMARK 465 VAL A 87
REMARK 465 VAL A 88
REMARK 465 PHE A 89
REMARK 465 ASP A 90
REMARK 465 ALA A 91
REMARK 465 SER A 92
REMARK 465 PRO A 93
REMARK 465 GLU A 94
REMARK 465 PRO A 217
REMARK 465 THR A 218
REMARK 465 ASP A 219
REMARK 465 LYS A 220
REMARK 465 SER A 221
REMARK 465 GLY A 450
REMARK 465 VAL A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
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 SER A 2 OG
REMARK 470 ARG A 95 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 96 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 222 CG OD1 OD2
REMARK 470 GLU A 235 CG CD OE1 OE2
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 HIS A 16 42.39 -107.40
REMARK 500 ASP A 25 71.77 -152.37
REMARK 500 ALA A 46 -121.98 59.23
REMARK 500 HIS A 101 -59.56 -120.24
REMARK 500 ASN A 102 -66.88 -16.50
REMARK 500 ASP A 183 119.77 -168.24
REMARK 500 ARG A 223 142.30 -34.00
REMARK 500 ASP A 224 -169.66 -127.65
REMARK 500 ALA A 234 -93.62 -78.55
REMARK 500 GLU A 235 -42.90 -143.90
REMARK 500 GLN A 375 53.30 38.10
REMARK 500 ASN A 380 65.17 -103.30
REMARK 500 ALA A 441 58.99 -142.74
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 460 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 394 SG
REMARK 620 2 HEM A 460 NA 95.0
REMARK 620 3 HEM A 460 NB 84.0 90.6
REMARK 620 4 HEM A 460 NC 85.4 179.4 89.9
REMARK 620 5 HEM A 460 ND 96.8 88.3 178.6 91.3
REMARK 620 6 HOH A 500 O 171.9 83.1 88.1 96.6 91.0
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 460
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E9X RELATED DB: PDB
REMARK 900 4-PHENYLIMIDAZOLE-BOUND CYP51
REMARK 900 RELATED ID: 1EA1 RELATED DB: PDB
REMARK 900 FLUCONAZOLE-BOUND CYP51
REMARK 900 RELATED ID: 1H5Z RELATED DB: PDB
REMARK 900 LIGAND-FREE WILD TYPE CYP51
DBREF 1U13 A 1 451 UNP P0A512 CP51_MYCTU 1 451
SEQADV 1U13 LEU A 37 UNP P0A512 CYS 37 ENGINEERED MUTATION
SEQADV 1U13 THR A 151 UNP P0A512 CYS 151 ENGINEERED MUTATION
SEQADV 1U13 ALA A 442 UNP P0A512 CYS 442 ENGINEERED MUTATION
SEQADV 1U13 HIS A 452 UNP P0A512 EXPRESSION TAG
SEQADV 1U13 HIS A 453 UNP P0A512 EXPRESSION TAG
SEQADV 1U13 HIS A 454 UNP P0A512 EXPRESSION TAG
SEQADV 1U13 HIS A 455 UNP P0A512 EXPRESSION TAG
SEQRES 1 A 455 MET SER ALA VAL ALA LEU PRO ARG VAL SER GLY GLY HIS
SEQRES 2 A 455 ASP GLU HIS GLY HIS LEU GLU GLU PHE ARG THR ASP PRO
SEQRES 3 A 455 ILE GLY LEU MET GLN ARG VAL ARG ASP GLU LEU GLY ASP
SEQRES 4 A 455 VAL GLY THR PHE GLN LEU ALA GLY LYS GLN VAL VAL LEU
SEQRES 5 A 455 LEU SER GLY SER HIS ALA ASN GLU PHE PHE PHE ARG ALA
SEQRES 6 A 455 GLY ASP ASP ASP LEU ASP GLN ALA LYS ALA TYR PRO PHE
SEQRES 7 A 455 MET THR PRO ILE PHE GLY GLU GLY VAL VAL PHE ASP ALA
SEQRES 8 A 455 SER PRO GLU ARG ARG LYS GLU MET LEU HIS ASN ALA ALA
SEQRES 9 A 455 LEU ARG GLY GLU GLN MET LYS GLY HIS ALA ALA THR ILE
SEQRES 10 A 455 GLU ASP GLN VAL ARG ARG MET ILE ALA ASP TRP GLY GLU
SEQRES 11 A 455 ALA GLY GLU ILE ASP LEU LEU ASP PHE PHE ALA GLU LEU
SEQRES 12 A 455 THR ILE TYR THR SER SER ALA THR LEU ILE GLY LYS LYS
SEQRES 13 A 455 PHE ARG ASP GLN LEU ASP GLY ARG PHE ALA LYS LEU TYR
SEQRES 14 A 455 HIS GLU LEU GLU ARG GLY THR ASP PRO LEU ALA TYR VAL
SEQRES 15 A 455 ASP PRO TYR LEU PRO ILE GLU SER PHE ARG ARG ARG ASP
SEQRES 16 A 455 GLU ALA ARG ASN GLY LEU VAL ALA LEU VAL ALA ASP ILE
SEQRES 17 A 455 MET ASN GLY ARG ILE ALA ASN PRO PRO THR ASP LYS SER
SEQRES 18 A 455 ASP ARG ASP MET LEU ASP VAL LEU ILE ALA VAL LYS ALA
SEQRES 19 A 455 GLU THR GLY THR PRO ARG PHE SER ALA ASP GLU ILE THR
SEQRES 20 A 455 GLY MET PHE ILE SER MET MET PHE ALA GLY HIS HIS THR
SEQRES 21 A 455 SER SER GLY THR ALA SER TRP THR LEU ILE GLU LEU MET
SEQRES 22 A 455 ARG HIS ARG ASP ALA TYR ALA ALA VAL ILE ASP GLU LEU
SEQRES 23 A 455 ASP GLU LEU TYR GLY ASP GLY ARG SER VAL SER PHE HIS
SEQRES 24 A 455 ALA LEU ARG GLN ILE PRO GLN LEU GLU ASN VAL LEU LYS
SEQRES 25 A 455 GLU THR LEU ARG LEU HIS PRO PRO LEU ILE ILE LEU MET
SEQRES 26 A 455 ARG VAL ALA LYS GLY GLU PHE GLU VAL GLN GLY HIS ARG
SEQRES 27 A 455 ILE HIS GLU GLY ASP LEU VAL ALA ALA SER PRO ALA ILE
SEQRES 28 A 455 SER ASN ARG ILE PRO GLU ASP PHE PRO ASP PRO HIS ASP
SEQRES 29 A 455 PHE VAL PRO ALA ARG TYR GLU GLN PRO ARG GLN GLU ASP
SEQRES 30 A 455 LEU LEU ASN ARG TRP THR TRP ILE PRO PHE GLY ALA GLY
SEQRES 31 A 455 ARG HIS ARG CYS VAL GLY ALA ALA PHE ALA ILE MET GLN
SEQRES 32 A 455 ILE LYS ALA ILE PHE SER VAL LEU LEU ARG GLU TYR GLU
SEQRES 33 A 455 PHE GLU MET ALA GLN PRO PRO GLU SER TYR ARG ASN ASP
SEQRES 34 A 455 HIS SER LYS MET VAL VAL GLN LEU ALA GLN PRO ALA ALA
SEQRES 35 A 455 VAL ARG TYR ARG ARG ARG THR GLY VAL HIS HIS HIS HIS
HET HEM A 460 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 HOH *209(H2 O)
HELIX 1 1 HIS A 18 ASP A 25 1 8
HELIX 2 2 ASP A 25 GLY A 38 1 14
HELIX 3 3 SER A 54 ALA A 65 1 12
HELIX 4 4 TYR A 76 PHE A 78 5 3
HELIX 5 5 MET A 79 GLY A 84 1 6
HELIX 6 6 ARG A 95 ALA A 103 1 9
HELIX 7 7 ARG A 106 ALA A 126 1 21
HELIX 8 8 LEU A 136 ILE A 153 1 18
HELIX 9 9 GLY A 154 GLN A 160 1 7
HELIX 10 10 ASP A 162 GLY A 175 1 14
HELIX 11 11 THR A 176 VAL A 182 5 7
HELIX 12 12 ILE A 188 ASN A 215 1 28
HELIX 13 13 ASP A 224 VAL A 232 1 9
HELIX 14 14 SER A 242 HIS A 275 1 34
HELIX 15 15 HIS A 275 TYR A 290 1 16
HELIX 16 16 GLY A 291 GLY A 293 5 3
HELIX 17 17 SER A 295 ALA A 300 1 6
HELIX 18 18 ILE A 304 HIS A 318 1 15
HELIX 19 19 SER A 348 ASN A 353 1 6
HELIX 20 20 VAL A 366 GLU A 371 5 6
HELIX 21 21 GLN A 375 ASN A 380 1 6
HELIX 22 22 ALA A 389 ARG A 393 5 5
HELIX 23 23 GLY A 396 GLU A 414 1 19
HELIX 24 24 PRO A 422 TYR A 426 5 5
SHEET 1 A 5 VAL A 40 LEU A 45 0
SHEET 2 A 5 LYS A 48 LEU A 53 -1 O VAL A 50 N PHE A 43
SHEET 3 A 5 LEU A 344 ALA A 347 1 O ALA A 346 N LEU A 53
SHEET 4 A 5 LEU A 324 ALA A 328 -1 N ARG A 326 O VAL A 345
SHEET 5 A 5 LEU A 70 ASP A 71 -1 N ASP A 71 O VAL A 327
SHEET 1 B 3 ALA A 131 ASP A 135 0
SHEET 2 B 3 ALA A 442 ARG A 447 -1 O VAL A 443 N ILE A 134
SHEET 3 B 3 TYR A 415 MET A 419 -1 N GLU A 418 O ARG A 444
SHEET 1 C 2 PHE A 332 VAL A 334 0
SHEET 2 C 2 HIS A 337 ILE A 339 -1 O ILE A 339 N PHE A 332
SHEET 1 D 2 ASN A 428 ASP A 429 0
SHEET 2 D 2 GLN A 436 LEU A 437 -1 O GLN A 436 N ASP A 429
LINK SG CYS A 394 FE HEM A 460 1555 1555 2.47
LINK FE HEM A 460 O HOH A 500 1555 1555 2.38
CISPEP 1 GLN A 439 PRO A 440 0 0.14
SITE 1 AC1 19 GLN A 72 TYR A 76 LYS A 97 HIS A 101
SITE 2 AC1 19 LEU A 105 ALA A 256 GLY A 257 THR A 260
SITE 3 AC1 19 PRO A 320 ARG A 326 PRO A 386 PHE A 387
SITE 4 AC1 19 GLY A 388 HIS A 392 CYS A 394 VAL A 395
SITE 5 AC1 19 GLY A 396 ALA A 400 HOH A 500
CRYST1 46.294 85.133 110.464 90.00 90.00 90.00 P 21 21 21 4
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 0.021601 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011746 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009053 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
