HEADER OXIDOREDUCTASE 11-AUG-14 4UAX
TITLE X-RAY CRYSTAL STRUCTURE OF LIGAND FREE CYP142A2 FROM MYCOBACTERIUM
TITLE 2 SMEGMATIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P450 HEME-THIOLATE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 5 GENE: MSMEG_5918;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS CYTOCHROME P450, OXIDOREDUCTASE, HEMOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MADRONA
REVDAT 6 27-SEP-23 4UAX 1 REMARK
REVDAT 5 27-NOV-19 4UAX 1 REMARK
REVDAT 4 06-SEP-17 4UAX 1 SOURCE JRNL REMARK
REVDAT 3 12-NOV-14 4UAX 1 JRNL
REVDAT 2 24-SEP-14 4UAX 1 JRNL
REVDAT 1 17-SEP-14 4UAX 0
JRNL AUTH D.J.FRANK,Y.MADRONA,P.R.ORTIZ DE MONTELLANO
JRNL TITL CHOLESTEROL ESTER OXIDATION BY MYCOBACTERIAL CYTOCHROME
JRNL TITL 2 P450.
JRNL REF J.BIOL.CHEM. V. 289 30417 2014
JRNL REFN ESSN 1083-351X
JRNL PMID 25210044
JRNL DOI 10.1074/JBC.M114.602771
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 42890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2148
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 19.5924 - 4.3736 0.99 2896 182 0.1515 0.1737
REMARK 3 2 4.3736 - 3.4778 1.00 2824 152 0.1383 0.1550
REMARK 3 3 3.4778 - 3.0400 1.00 2812 142 0.1584 0.1857
REMARK 3 4 3.0400 - 2.7629 1.00 2783 139 0.1742 0.2230
REMARK 3 5 2.7629 - 2.5654 1.00 2746 157 0.1730 0.2184
REMARK 3 6 2.5654 - 2.4144 1.00 2781 143 0.1706 0.2042
REMARK 3 7 2.4144 - 2.2937 1.00 2732 139 0.1648 0.1982
REMARK 3 8 2.2937 - 2.1940 1.00 2768 119 0.1605 0.1711
REMARK 3 9 2.1940 - 2.1096 1.00 2746 152 0.1633 0.2004
REMARK 3 10 2.1096 - 2.0369 1.00 2700 156 0.1782 0.1930
REMARK 3 11 2.0369 - 1.9733 1.00 2744 144 0.1726 0.2098
REMARK 3 12 1.9733 - 1.9169 0.99 2727 136 0.1863 0.2125
REMARK 3 13 1.9169 - 1.8665 1.00 2728 130 0.2006 0.2559
REMARK 3 14 1.8665 - 1.8210 0.96 2581 154 0.2185 0.2617
REMARK 3 15 1.8210 - 1.7796 0.80 2174 103 0.2461 0.2491
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.990
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 3267
REMARK 3 ANGLE : 1.083 4442
REMARK 3 CHIRALITY : 0.043 489
REMARK 3 PLANARITY : 0.005 586
REMARK 3 DIHEDRAL : 13.443 1216
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 4UAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1000203052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JAN-14
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) : 1.115869
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42943
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 19.591
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 2.790
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.35
REMARK 200 R MERGE FOR SHELL (I) : 0.49300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
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 3ZBY
REMARK 200
REMARK 200 REMARK: RECTANGULAR
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.27 M SODIUM CITRATE DIBASIC, 60 MM
REMARK 280 CALCIUM CHLORIDE, 100 MM BIS-TRIS PROPANE, PH 6.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 28.32500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.25050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.75900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.25050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.32500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.75900
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 TOTAL BURIED SURFACE AREA: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
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 HIS A 404
REMARK 465 HIS A 405
REMARK 465 HIS A 406
REMARK 465 HIS A 407
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 NH1 ARG A 368 O HOH A 1138 2.14
REMARK 500 NH1 ARG A 7 OE1 GLU A 34 2.19
REMARK 500 OD1 ASP A 372 O HOH A 1109 2.19
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 GLU A 34 69.58 -159.84
REMARK 500 PRO A 76 43.03 -82.73
REMARK 500 ILE A 132 -56.04 -124.77
REMARK 500 THR A 201 -158.75 -120.91
REMARK 500 ASP A 235 -79.58 -94.96
REMARK 500 SER A 278 64.31 33.04
REMARK 500 CYS A 343 119.76 -39.94
REMARK 500 PHE A 382 -71.02 -118.75
REMARK 500 MET A 389 80.67 -164.23
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 A 980 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A1091 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A1124 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A1149 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH A1189 DISTANCE = 5.90 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 A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 343 SG
REMARK 620 2 HEM A 501 NA 100.1
REMARK 620 3 HEM A 501 NB 92.5 88.6
REMARK 620 4 HEM A 501 NC 88.6 171.2 90.5
REMARK 620 5 HEM A 501 ND 97.4 90.1 170.1 89.3
REMARK 620 6 HOH A 770 O 172.7 79.2 80.2 92.0 89.9
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 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TRI RELATED DB: PDB
REMARK 900 CYP142A2 COMPLEXED WITH CHOLESTEROL SULFATE
DBREF 4UAX A 1 401 UNP A0R4Q6 A0R4Q6_MYCS2 1 401
SEQADV 4UAX HIS A 402 UNP A0R4Q6 EXPRESSION TAG
SEQADV 4UAX HIS A 403 UNP A0R4Q6 EXPRESSION TAG
SEQADV 4UAX HIS A 404 UNP A0R4Q6 EXPRESSION TAG
SEQADV 4UAX HIS A 405 UNP A0R4Q6 EXPRESSION TAG
SEQADV 4UAX HIS A 406 UNP A0R4Q6 EXPRESSION TAG
SEQADV 4UAX HIS A 407 UNP A0R4Q6 EXPRESSION TAG
SEQRES 1 A 407 MET THR GLN MET LEU THR ARG PRO ASP VAL ASP LEU VAL
SEQRES 2 A 407 ASN GLY MET PHE TYR ALA ASP GLY GLY ALA ARG GLU ALA
SEQRES 3 A 407 TYR ARG TRP MET ARG ALA ASN GLU PRO VAL PHE ARG ASP
SEQRES 4 A 407 ARG ASN GLY LEU ALA ALA ALA THR THR TYR GLN ALA VAL
SEQRES 5 A 407 LEU ASP ALA GLU ARG ASN PRO GLU LEU PHE SER SER THR
SEQRES 6 A 407 GLY GLY ILE ARG PRO ASP GLN PRO GLY MET PRO TYR MET
SEQRES 7 A 407 ILE ASP MET ASP ASP PRO GLN HIS LEU LEU ARG ARG LYS
SEQRES 8 A 407 LEU VAL ASN ALA GLY PHE THR ARG LYS ARG VAL MET ASP
SEQRES 9 A 407 LYS VAL ASP SER ILE GLY ARG LEU CYS ASP THR LEU ILE
SEQRES 10 A 407 ASP ALA VAL CYS GLU ARG GLY GLU CYS ASP PHE VAL ARG
SEQRES 11 A 407 ASP ILE ALA ALA PRO LEU PRO MET ALA VAL ILE GLY ASP
SEQRES 12 A 407 MET LEU GLY VAL LEU PRO THR GLU ARG ASP MET LEU LEU
SEQRES 13 A 407 LYS TRP SER ASP ASP LEU VAL CYS GLY LEU SER SER HIS
SEQRES 14 A 407 VAL ASP GLU ALA ALA ILE GLN LYS LEU MET ASP THR PHE
SEQRES 15 A 407 ALA ALA TYR THR GLU PHE THR LYS ASP VAL ILE THR LYS
SEQRES 16 A 407 ARG ARG ALA GLU PRO THR ASP ASP LEU PHE SER VAL LEU
SEQRES 17 A 407 VAL ASN SER GLU VAL GLU GLY GLN ARG MET SER ASP ASP
SEQRES 18 A 407 GLU ILE VAL PHE GLU THR LEU LEU ILE LEU ILE GLY GLY
SEQRES 19 A 407 ASP GLU THR THR ARG HIS THR LEU SER GLY GLY THR GLU
SEQRES 20 A 407 GLN LEU LEU ARG HIS ARG ASP GLN TRP ASP ALA LEU VAL
SEQRES 21 A 407 ALA ASP VAL ASP LEU LEU PRO GLY ALA ILE GLU GLU MET
SEQRES 22 A 407 LEU ARG TRP THR SER PRO VAL LYS ASN MET CYS ARG THR
SEQRES 23 A 407 LEU THR ALA ASP THR VAL PHE HIS GLY THR GLU LEU ARG
SEQRES 24 A 407 ALA GLY GLU LYS ILE MET LEU MET PHE GLU SER ALA ASN
SEQRES 25 A 407 PHE ASP GLU SER VAL PHE GLY ASP PRO ASP ASN PHE ARG
SEQRES 26 A 407 ILE ASP ARG ASN PRO ASN SER HIS VAL ALA PHE GLY PHE
SEQRES 27 A 407 GLY THR HIS PHE CYS LEU GLY ASN GLN LEU ALA ARG LEU
SEQRES 28 A 407 GLU LEU ARG LEU MET THR GLU ARG VAL LEU ARG ARG LEU
SEQRES 29 A 407 PRO ASP LEU ARG LEU ALA ASP ASP ALA PRO VAL PRO LEU
SEQRES 30 A 407 ARG PRO ALA ASN PHE VAL SER GLY PRO GLU SER MET PRO
SEQRES 31 A 407 VAL VAL PHE THR PRO SER ALA PRO VAL LEU ALA HIS HIS
SEQRES 32 A 407 HIS HIS HIS HIS
HET HEM A 501 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 HOH *589(H2 O)
HELIX 1 AA1 ASN A 14 ALA A 19 5 6
HELIX 2 AA2 GLY A 22 GLU A 34 1 13
HELIX 3 AA3 THR A 48 ASN A 58 1 11
HELIX 4 AA4 TYR A 77 MET A 81 5 5
HELIX 5 AA5 PRO A 84 ALA A 95 1 12
HELIX 6 AA6 THR A 98 ASP A 104 1 7
HELIX 7 AA7 LYS A 105 ALA A 119 1 15
HELIX 8 AA8 PHE A 128 ILE A 132 1 5
HELIX 9 AA9 ALA A 134 GLY A 146 1 13
HELIX 10 AB1 LEU A 148 SER A 168 1 21
HELIX 11 AB2 ASP A 171 GLU A 199 1 29
HELIX 12 AB3 ASP A 203 SER A 211 1 9
HELIX 13 AB4 SER A 219 ASP A 235 1 17
HELIX 14 AB5 ASP A 235 HIS A 252 1 18
HELIX 15 AB6 HIS A 252 ASP A 262 1 11
HELIX 16 AB7 LEU A 265 SER A 278 1 14
HELIX 17 AB8 PHE A 308 PHE A 313 1 6
HELIX 18 AB9 ASP A 314 GLY A 319 1 6
HELIX 19 AC1 PHE A 338 PHE A 342 5 5
HELIX 20 AC2 GLY A 345 LEU A 364 1 20
SHEET 1 AA1 5 VAL A 36 ARG A 38 0
SHEET 2 AA1 5 ALA A 44 ALA A 46 -1 O ALA A 45 N PHE A 37
SHEET 3 AA1 5 LYS A 303 MET A 307 1 O MET A 305 N ALA A 46
SHEET 4 AA1 5 ASN A 282 LEU A 287 -1 N MET A 283 O LEU A 306
SHEET 5 AA1 5 PHE A 62 SER A 63 -1 N SER A 63 O THR A 286
SHEET 1 AA2 3 GLU A 125 ASP A 127 0
SHEET 2 AA2 3 PRO A 390 VAL A 392 -1 O VAL A 391 N CYS A 126
SHEET 3 AA2 3 ARG A 368 LEU A 369 -1 N ARG A 368 O VAL A 392
SHEET 1 AA3 2 GLU A 212 VAL A 213 0
SHEET 2 AA3 2 GLN A 216 ARG A 217 -1 O GLN A 216 N VAL A 213
SHEET 1 AA4 2 THR A 291 PHE A 293 0
SHEET 2 AA4 2 THR A 296 LEU A 298 -1 O LEU A 298 N THR A 291
LINK SG CYS A 343 FE HEM A 501 1555 1555 2.26
LINK FE HEM A 501 O HOH A 770 1555 1555 2.57
CISPEP 1 ASP A 83 PRO A 84 0 6.83
CISPEP 2 ASN A 329 PRO A 330 0 -0.26
SITE 1 AC1 22 GLU A 56 MET A 78 ILE A 79 HIS A 86
SITE 2 AC1 22 ARG A 90 PHE A 97 GLY A 233 GLY A 234
SITE 3 AC1 22 THR A 237 THR A 238 THR A 241 VAL A 280
SITE 4 AC1 22 ARG A 285 ALA A 335 PHE A 336 GLY A 337
SITE 5 AC1 22 PHE A 338 HIS A 341 CYS A 343 GLY A 345
SITE 6 AC1 22 HOH A 770 HOH A 777
CRYST1 56.650 83.518 94.501 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 0.017652 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011973 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010582 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
