HEADER OXIDOREDUCTASE 24-JUN-14 4TUV
TITLE X-RAY CRYSTAL STRUCTURE OF CYP119 FROM SULFOLOBUS ACIDOCALDARIUS,
TITLE 2 COMPLEXED WITH 4-(4-CHLOROPHENYL)IMIDAZOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 119;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PEROXIDASE;
COMPND 5 EC: 1.14.-.-,1.11.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_TAXID: 330779;
SOURCE 4 STRAIN: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
SOURCE 5 GENE: CYP119, SACI_2081;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MADRONA
REVDAT 4 27-DEC-23 4TUV 1 REMARK
REVDAT 3 25-DEC-19 4TUV 1 REMARK
REVDAT 2 20-SEP-17 4TUV 1 SOURCE JRNL REMARK
REVDAT 1 18-FEB-15 4TUV 0
JRNL AUTH D.BASUDHAR,Y.MADRONA,P.R.ORTIZ DE MONTELLANO
JRNL TITL NMR AND X-RAY ANALYSIS OF CYP119 LIGAND DEPENDENT
JRNL TITL 2 CONFORMATIONAL CHANGES.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 21708
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1108
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 36.6760 - 4.9987 1.00 2782 127 0.1721 0.2394
REMARK 3 2 4.9987 - 3.9692 1.00 2621 129 0.1509 0.1585
REMARK 3 3 3.9692 - 3.4679 1.00 2562 155 0.1804 0.2438
REMARK 3 4 3.4679 - 3.1510 1.00 2542 148 0.2046 0.2490
REMARK 3 5 3.1510 - 2.9252 1.00 2538 137 0.2222 0.2847
REMARK 3 6 2.9252 - 2.7528 1.00 2524 145 0.2420 0.2907
REMARK 3 7 2.7528 - 2.6150 1.00 2504 147 0.2386 0.3311
REMARK 3 8 2.6150 - 2.5010 1.00 2527 120 0.2678 0.3363
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.600
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 : 0.010 3158
REMARK 3 ANGLE : 1.212 4278
REMARK 3 CHIRALITY : 0.047 462
REMARK 3 PLANARITY : 0.005 545
REMARK 3 DIHEDRAL : 16.080 1196
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 4TUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000202305.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-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 : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.127092
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21711
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 36.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.4800
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1-1.5M AMMONIUM SULFATE, 80MM SODIUM
REMARK 280 ACETATE PH 4.5, 20MM SODIUM ACETATE PH 5.6, 20% GLYCEROL, 340MM
REMARK 280 NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.93000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 37.93000
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 37.93000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.93000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.93000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.93000
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 GLU A 368
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 ASN A 19 -60.70 -123.16
REMARK 500 TYR A 66 77.74 -117.32
REMARK 500 THR A 70 51.29 -111.86
REMARK 500 GLU A 114 121.35 -170.77
REMARK 500 LYS A 157 77.29 -106.37
REMARK 500 LEU A 164 -148.19 -94.45
REMARK 500 ASN A 303 117.06 -171.75
REMARK 500 CYS A 317 119.45 -32.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 365 SER A 366 -146.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 HEM A 401
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 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 317 SG
REMARK 620 2 HEM A 401 NA 97.2
REMARK 620 3 HEM A 401 NB 85.5 89.6
REMARK 620 4 HEM A 401 NC 87.4 174.5 87.6
REMARK 620 5 HEM A 401 ND 99.2 86.9 174.5 95.5
REMARK 620 6 CPZ A 402 N1 174.3 87.0 90.6 88.3 84.9
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CPZ A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TT5 RELATED DB: PDB
REMARK 900 4TT5 IS THE SAME PROTEIN COMPLEXED WITH 4-4-(4-BROMOPHENYL)-1H-
REMARK 900 IMIDAZOLE
DBREF 4TUV A 1 368 UNP Q55080 CP119_SULAC 1 368
SEQRES 1 A 368 MET TYR ASP TRP PHE SER GLU MET ARG LYS LYS ASP PRO
SEQRES 2 A 368 VAL TYR TYR ASP GLY ASN ILE TRP GLN VAL PHE SER TYR
SEQRES 3 A 368 ARG TYR THR LYS GLU VAL LEU ASN ASN PHE SER LYS PHE
SEQRES 4 A 368 SER SER ASP LEU THR GLY TYR HIS GLU ARG LEU GLU ASP
SEQRES 5 A 368 LEU ARG ASN GLY LYS ILE ARG PHE ASP ILE PRO THR ARG
SEQRES 6 A 368 TYR THR MET LEU THR SER ASP PRO PRO LEU HIS ASP GLU
SEQRES 7 A 368 LEU ARG SER MET SER ALA ASP ILE PHE SER PRO GLN LYS
SEQRES 8 A 368 LEU GLN THR LEU GLU THR PHE ILE ARG GLU THR THR ARG
SEQRES 9 A 368 SER LEU LEU ASP SER ILE ASP PRO ARG GLU ASP ASP ILE
SEQRES 10 A 368 VAL LYS LYS LEU ALA VAL PRO LEU PRO ILE ILE VAL ILE
SEQRES 11 A 368 SER LYS ILE LEU GLY LEU PRO ILE GLU ASP LYS GLU LYS
SEQRES 12 A 368 PHE LYS GLU TRP SER ASP LEU VAL ALA PHE ARG LEU GLY
SEQRES 13 A 368 LYS PRO GLY GLU ILE PHE GLU LEU GLY LYS LYS TYR LEU
SEQRES 14 A 368 GLU LEU ILE GLY TYR VAL LYS ASP HIS LEU ASN SER GLY
SEQRES 15 A 368 THR GLU VAL VAL SER ARG VAL VAL ASN SER ASN LEU SER
SEQRES 16 A 368 ASP ILE GLU LYS LEU GLY TYR ILE ILE LEU LEU LEU ILE
SEQRES 17 A 368 ALA GLY ASN GLU THR THR THR ASN LEU ILE SER ASN SER
SEQRES 18 A 368 VAL ILE ASP PHE THR ARG PHE ASN LEU TRP GLN ARG ILE
SEQRES 19 A 368 ARG GLU GLU ASN LEU TYR LEU LYS ALA ILE GLU GLU ALA
SEQRES 20 A 368 LEU ARG TYR SER PRO PRO VAL MET ARG THR VAL ARG LYS
SEQRES 21 A 368 THR LYS GLU ARG VAL LYS LEU GLY ASP GLN THR ILE GLU
SEQRES 22 A 368 GLU GLY GLU TYR VAL ARG VAL TRP ILE ALA SER ALA ASN
SEQRES 23 A 368 ARG ASP GLU GLU VAL PHE HIS ASP GLY GLU LYS PHE ILE
SEQRES 24 A 368 PRO ASP ARG ASN PRO ASN PRO HIS LEU SER PHE GLY SER
SEQRES 25 A 368 GLY ILE HIS LEU CYS LEU GLY ALA PRO LEU ALA ARG LEU
SEQRES 26 A 368 GLU ALA ARG ILE ALA ILE GLU GLU PHE SER LYS ARG PHE
SEQRES 27 A 368 ARG HIS ILE GLU ILE LEU ASP THR GLU LYS VAL PRO ASN
SEQRES 28 A 368 GLU VAL LEU ASN GLY TYR LYS ARG LEU VAL VAL ARG LEU
SEQRES 29 A 368 LYS SER ASN GLU
HET HEM A 401 42
HET CPZ A 402 12
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CPZ 4-(4-CHLOROPHENYL)IMIDAZOLE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 CPZ C9 H7 CL N2
FORMUL 4 HOH *66(H2 O)
HELIX 1 AA1 MET A 1 ASP A 12 1 12
HELIX 2 AA2 SER A 25 ASN A 35 1 11
HELIX 3 AA3 GLY A 45 ASN A 55 1 11
HELIX 4 AA4 ILE A 62 TYR A 66 5 5
HELIX 5 AA5 THR A 67 SER A 71 5 5
HELIX 6 AA6 PRO A 74 SER A 81 1 8
HELIX 7 AA7 SER A 88 GLN A 93 1 6
HELIX 8 AA8 LEU A 95 SER A 109 1 15
HELIX 9 AA9 ILE A 117 LEU A 121 1 5
HELIX 10 AB1 VAL A 123 GLY A 135 1 13
HELIX 11 AB2 ASP A 140 ASP A 149 1 10
HELIX 12 AB3 GLY A 165 ASP A 177 1 13
HELIX 13 AB4 HIS A 178 GLY A 182 5 5
HELIX 14 AB5 THR A 183 SER A 192 1 10
HELIX 15 AB6 SER A 195 ALA A 209 1 15
HELIX 16 AB7 GLY A 210 PHE A 228 1 19
HELIX 17 AB8 LEU A 230 GLU A 237 1 8
HELIX 18 AB9 LEU A 239 SER A 251 1 13
HELIX 19 AC1 TRP A 281 ASN A 286 1 6
HELIX 20 AC2 SER A 312 LEU A 316 5 5
HELIX 21 AC3 GLY A 319 PHE A 338 1 20
SHEET 1 AA1 5 VAL A 14 TYR A 16 0
SHEET 2 AA1 5 TRP A 21 VAL A 23 -1 O GLN A 22 N TYR A 15
SHEET 3 AA1 5 TYR A 277 VAL A 280 1 O ARG A 279 N TRP A 21
SHEET 4 AA1 5 THR A 257 THR A 261 -1 N THR A 257 O VAL A 280
SHEET 5 AA1 5 PHE A 39 SER A 40 -1 N SER A 40 O LYS A 260
SHEET 1 AA2 3 ASP A 115 ASP A 116 0
SHEET 2 AA2 3 TYR A 357 LYS A 365 -1 O VAL A 362 N ASP A 115
SHEET 3 AA2 3 HIS A 340 LYS A 348 -1 N GLU A 347 O LYS A 358
SHEET 1 AA3 2 VAL A 265 LEU A 267 0
SHEET 2 AA3 2 GLN A 270 ILE A 272 -1 O ILE A 272 N VAL A 265
LINK SG CYS A 317 FE HEM A 401 1555 1555 2.32
LINK FE HEM A 401 N1 CPZ A 402 1555 1555 1.91
CISPEP 1 PRO A 73 PRO A 74 0 1.49
CISPEP 2 LEU A 155 GLY A 156 0 -25.87
CISPEP 3 ASN A 303 PRO A 304 0 8.06
SITE 1 AC1 24 MET A 68 LEU A 69 HIS A 76 ARG A 80
SITE 2 AC1 24 LEU A 205 LEU A 206 GLY A 210 THR A 213
SITE 3 AC1 24 THR A 214 LEU A 217 VAL A 254 THR A 257
SITE 4 AC1 24 ARG A 259 SER A 309 PHE A 310 GLY A 311
SITE 5 AC1 24 ILE A 314 HIS A 315 CYS A 317 GLY A 319
SITE 6 AC1 24 ALA A 323 CPZ A 402 HOH A 523 HOH A 541
SITE 1 AC2 6 VAL A 151 PHE A 153 ALA A 209 THR A 213
SITE 2 AC2 6 VAL A 353 HEM A 401
CRYST1 165.800 165.800 75.860 90.00 90.00 120.00 P 63 2 2 12
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 0.006031 0.003482 0.000000 0.00000
SCALE2 0.000000 0.006964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013182 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
