HEADER OXIDOREDUCTASE 12-JUL-10 2XKR
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS CYP142: A NOVEL
TITLE 2 CHOLESTEROL OXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE CYTOCHROME P450 142;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYP142;
COMPND 5 EC: 1.14.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: POLYETHYLENE GLYCOL BOUND TO HEME IRON
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 10 OTHER_DETAILS: INSTITUT PASTEUR
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.DRISCOLL,K.J.MCLEAN,C.W.LEVY,P.LAFITE,N.MAST,I.A.PIKULEVA,
AUTHOR 2 S.E.J.RIGBY,D.LEYS,A.W.MUNRO
REVDAT 5 20-DEC-23 2XKR 1 REMARK
REVDAT 4 10-APR-19 2XKR 1 SOURCE REMARK
REVDAT 3 08-DEC-10 2XKR 1 JRNL
REVDAT 2 13-OCT-10 2XKR 1 JRNL
REVDAT 1 29-SEP-10 2XKR 0
JRNL AUTH M.D.DRISCOLL,K.J.MCLEAN,C.W.LEVY,N.MAST,I.A.PIKULEVA,
JRNL AUTH 2 P.LAFITE,S.E.J.RIGBY,D.LEYS,A.W.MUNRO
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS CYP142: EVIDENCE FOR MULTIPLE CHOLESTEROL
JRNL TITL 3 27-HYDROXYLASE ACTIVITIES IN A HUMAN PATHOGEN.
JRNL REF J.BIOL.CHEM. V. 285 38270 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20889498
JRNL DOI 10.1074/JBC.M110.164293
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 62544
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3169
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 40.1764 - 4.5510 0.99 2780 136 0.1724 0.1751
REMARK 3 2 4.5510 - 3.6130 1.00 2642 158 0.1419 0.1629
REMARK 3 3 3.6130 - 3.1565 1.00 2622 150 0.1666 0.1917
REMARK 3 4 3.1565 - 2.8680 1.00 2609 150 0.1817 0.2337
REMARK 3 5 2.8680 - 2.6625 1.00 2622 126 0.1737 0.1887
REMARK 3 6 2.6625 - 2.5055 1.00 2586 135 0.1686 0.2069
REMARK 3 7 2.5055 - 2.3800 1.00 2611 128 0.1638 0.1879
REMARK 3 8 2.3800 - 2.2764 1.00 2599 133 0.1600 0.1862
REMARK 3 9 2.2764 - 2.1888 1.00 2552 150 0.1546 0.1901
REMARK 3 10 2.1888 - 2.1133 1.00 2604 122 0.1533 0.1629
REMARK 3 11 2.1133 - 2.0472 1.00 2524 141 0.1571 0.1946
REMARK 3 12 2.0472 - 1.9887 1.00 2581 139 0.1629 0.1893
REMARK 3 13 1.9887 - 1.9363 1.00 2594 139 0.1620 0.1940
REMARK 3 14 1.9363 - 1.8891 1.00 2557 151 0.1676 0.1995
REMARK 3 15 1.8891 - 1.8462 1.00 2544 127 0.1634 0.2123
REMARK 3 16 1.8462 - 1.8069 1.00 2580 125 0.1746 0.2144
REMARK 3 17 1.8069 - 1.7707 1.00 2553 148 0.1715 0.2285
REMARK 3 18 1.7707 - 1.7373 1.00 2552 130 0.1772 0.1827
REMARK 3 19 1.7373 - 1.7063 1.00 2570 135 0.1804 0.2026
REMARK 3 20 1.7063 - 1.6774 1.00 2524 139 0.1817 0.2301
REMARK 3 21 1.6774 - 1.6503 1.00 2570 142 0.1853 0.2326
REMARK 3 22 1.6503 - 1.6249 1.00 2536 143 0.1945 0.2266
REMARK 3 23 1.6249 - 1.6010 0.97 2463 122 0.2067 0.2503
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 : 0.36
REMARK 3 B_SOL : 50.64
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27080
REMARK 3 B22 (A**2) : 1.92050
REMARK 3 B33 (A**2) : -2.19130
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 : 0.005 3180
REMARK 3 ANGLE : 1.032 4334
REMARK 3 CHIRALITY : 0.067 482
REMARK 3 PLANARITY : 0.005 574
REMARK 3 DIHEDRAL : 12.630 1177
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 2XKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1290044583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-10
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 : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62547
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
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: PDB ENTRY 2WM4
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 550MME WITH 100 MM POTASSIUM
REMARK 280 THIOCYANATE AND 0.1 M SODIUM ACETATE AT A PH RANGE OF 5.0-6.0.,
REMARK 280 PH 7.5
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 27.65500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.73500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.73000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.73500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.65500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.73000
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 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 THR A 2
REMARK 465 GLU A 3
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 ARG A 96 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 97 CG CD CE NZ
REMARK 470 HIS A 166 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 169 CG CD OE1 NE2
REMARK 470 GLU A 170 CG CD OE1 OE2
REMARK 470 ASP A 196 CG OD1 OD2
REMARK 470 ASP A 369 CG OD1 OD2
REMARK 470 ARG A 376 CG CD NE CZ NH1 NH2
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 GLN A 31 79.66 -157.50
REMARK 500 LEU A 129 -54.10 -128.09
REMARK 500 THR A 198 -152.91 -116.83
REMARK 500 ASP A 232 -79.17 -89.46
REMARK 500 ALA A 275 65.87 31.37
REMARK 500 PHE A 380 -68.38 -124.81
REMARK 500 MET A 387 82.39 -153.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2014 DISTANCE = 6.42 ANGSTROMS
REMARK 525 HOH A2028 DISTANCE = 5.99 ANGSTROMS
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 A1400 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 340 SG
REMARK 620 2 HEM A1400 NA 98.4
REMARK 620 3 HEM A1400 NB 88.5 89.3
REMARK 620 4 HEM A1400 NC 86.8 174.7 89.8
REMARK 620 5 HEM A1400 ND 96.5 90.5 175.0 90.0
REMARK 620 6 PG4 A1399 O3 174.2 84.8 86.6 89.9 88.4
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 PG4 A 1399
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 1400
DBREF 2XKR A 1 398 UNP O53563 CP142_MYCTU 1 398
SEQRES 1 A 398 MET THR GLU ALA PRO ASP VAL ASP LEU ALA ASP GLY ASN
SEQRES 2 A 398 PHE TYR ALA SER ARG GLU ALA ARG ALA ALA TYR ARG TRP
SEQRES 3 A 398 MET ARG ALA ASN GLN PRO VAL PHE ARG ASP ARG ASN GLY
SEQRES 4 A 398 LEU ALA ALA ALA SER THR TYR GLN ALA VAL ILE ASP ALA
SEQRES 5 A 398 GLU ARG GLN PRO GLU LEU PHE SER ASN ALA GLY GLY ILE
SEQRES 6 A 398 ARG PRO ASP GLN PRO ALA LEU PRO MET MET ILE ASP MET
SEQRES 7 A 398 ASP ASP PRO ALA HIS LEU LEU ARG ARG LYS LEU VAL ASN
SEQRES 8 A 398 ALA GLY PHE THR ARG LYS ARG VAL LYS ASP LYS GLU ALA
SEQRES 9 A 398 SER ILE ALA ALA LEU CYS ASP THR LEU ILE ASP ALA VAL
SEQRES 10 A 398 CYS GLU ARG GLY GLU CYS ASP PHE VAL ARG ASP LEU ALA
SEQRES 11 A 398 ALA PRO LEU PRO MET ALA VAL ILE GLY ASP MET LEU GLY
SEQRES 12 A 398 VAL ARG PRO GLU GLN ARG ASP MET PHE LEU ARG TRP SER
SEQRES 13 A 398 ASP ASP LEU VAL THR PHE LEU SER SER HIS VAL SER GLN
SEQRES 14 A 398 GLU ASP PHE GLN ILE THR MET ASP ALA PHE ALA ALA TYR
SEQRES 15 A 398 ASN ASP PHE THR ARG ALA THR ILE ALA ALA ARG ARG ALA
SEQRES 16 A 398 ASP PRO THR ASP ASP LEU VAL SER VAL LEU VAL SER SER
SEQRES 17 A 398 GLU VAL ASP GLY GLU ARG LEU SER ASP ASP GLU LEU VAL
SEQRES 18 A 398 MET GLU THR LEU LEU ILE LEU ILE GLY GLY ASP GLU THR
SEQRES 19 A 398 THR ARG HIS THR LEU SER GLY GLY THR GLU GLN LEU LEU
SEQRES 20 A 398 ARG ASN ARG ASP GLN TRP ASP LEU LEU GLN ARG ASP PRO
SEQRES 21 A 398 SER LEU LEU PRO GLY ALA ILE GLU GLU MET LEU ARG TRP
SEQRES 22 A 398 THR ALA PRO VAL LYS ASN MET CYS ARG VAL LEU THR ALA
SEQRES 23 A 398 ASP THR GLU PHE HIS GLY THR ALA LEU CYS ALA GLY GLU
SEQRES 24 A 398 LYS MET MET LEU LEU PHE GLU SER ALA ASN PHE ASP GLU
SEQRES 25 A 398 ALA VAL PHE CYS GLU PRO GLU LYS PHE ASP VAL GLN ARG
SEQRES 26 A 398 ASN PRO ASN SER HIS LEU ALA PHE GLY PHE GLY THR HIS
SEQRES 27 A 398 PHE CYS LEU GLY ASN GLN LEU ALA ARG LEU GLU LEU SER
SEQRES 28 A 398 LEU MET THR GLU ARG VAL LEU ARG ARG LEU PRO ASP LEU
SEQRES 29 A 398 ARG LEU VAL ALA ASP ASP SER VAL LEU PRO LEU ARG PRO
SEQRES 30 A 398 ALA ASN PHE VAL SER GLY LEU GLU SER MET PRO VAL VAL
SEQRES 31 A 398 PHE THR PRO SER PRO PRO LEU GLY
HET HEM A1400 43
HET PG4 A1399 7
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 PG4 C8 H18 O5
FORMUL 4 HOH *510(H2 O)
HELIX 1 1 ASP A 11 ALA A 16 1 6
HELIX 2 2 GLU A 19 GLN A 31 1 13
HELIX 3 3 THR A 45 ARG A 54 1 10
HELIX 4 4 MET A 74 MET A 78 5 5
HELIX 5 5 PRO A 81 ASN A 91 1 11
HELIX 6 6 ALA A 92 PHE A 94 5 3
HELIX 7 7 THR A 95 ASP A 101 1 7
HELIX 8 8 LYS A 102 ALA A 116 1 15
HELIX 9 9 PHE A 125 LEU A 129 1 5
HELIX 10 10 ALA A 131 GLY A 143 1 13
HELIX 11 11 ARG A 145 GLU A 147 5 3
HELIX 12 12 GLN A 148 SER A 164 1 17
HELIX 13 13 SER A 168 ASP A 196 1 29
HELIX 14 14 ASP A 200 SER A 208 1 9
HELIX 15 15 SER A 216 ASP A 232 1 17
HELIX 16 16 ASP A 232 ASN A 249 1 18
HELIX 17 17 ASN A 249 ASP A 259 1 11
HELIX 18 18 LEU A 262 ALA A 275 1 14
HELIX 19 19 PHE A 305 PHE A 310 1 6
HELIX 20 20 GLY A 342 LEU A 361 1 20
SHEET 1 AA 5 VAL A 33 ARG A 35 0
SHEET 2 AA 5 ALA A 41 ALA A 43 -1 O ALA A 42 N PHE A 34
SHEET 3 AA 5 LYS A 300 LEU A 304 1 O LYS A 300 N ALA A 41
SHEET 4 AA 5 ASN A 279 LEU A 284 -1 O MET A 280 N LEU A 303
SHEET 5 AA 5 PHE A 59 SER A 60 -1 O SER A 60 N VAL A 283
SHEET 1 AB 3 GLU A 122 ASP A 124 0
SHEET 2 AB 3 PRO A 388 VAL A 390 -1 O VAL A 389 N CYS A 123
SHEET 3 AB 3 ARG A 365 LEU A 366 -1 O ARG A 365 N VAL A 390
SHEET 1 AC 2 THR A 288 PHE A 290 0
SHEET 2 AC 2 THR A 293 LEU A 295 -1 O THR A 293 N PHE A 290
LINK SG CYS A 340 FE HEM A1400 1555 1555 2.33
LINK O3 PG4 A1399 FE HEM A1400 1555 1555 2.21
CISPEP 1 ASP A 80 PRO A 81 0 7.35
CISPEP 2 ASN A 326 PRO A 327 0 -0.31
SITE 1 AC1 4 LEU A 163 LEU A 226 GLY A 230 HEM A1400
SITE 1 AC2 24 GLU A 53 MET A 75 ILE A 76 HIS A 83
SITE 2 AC2 24 ARG A 87 PHE A 94 ILE A 227 GLY A 230
SITE 3 AC2 24 GLY A 231 THR A 234 THR A 235 THR A 238
SITE 4 AC2 24 VAL A 277 ARG A 282 ALA A 332 PHE A 333
SITE 5 AC2 24 GLY A 334 PHE A 335 THR A 337 HIS A 338
SITE 6 AC2 24 CYS A 340 GLY A 342 PG4 A1399 HOH A2510
CRYST1 55.310 65.460 129.470 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 0.018080 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007724 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
