HEADER OXIDOREDUCTASE 12-AUG-08 3E4Y
TITLE CRYSTAL STRUCTURE OF A 33KDA CATALASE-RELATED PROTEIN FROM
TITLE 2 MYCOBACTERIUM AVIUM SUBSP. PARATUBERCULOSIS. I2(1)2(1)2(1) CRYSTAL
TITLE 3 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM AVIUM SUBSP. PARATUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1770;
SOURCE 4 GENE: MAP_2744C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS HEME ENZYME, CATALASE, PEROXIDASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PAKHOMOVA,M.E.NEWCOMER
REVDAT 4 30-AUG-23 3E4Y 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3E4Y 1 VERSN
REVDAT 2 08-DEC-09 3E4Y 1 JRNL
REVDAT 1 18-AUG-09 3E4Y 0
JRNL AUTH S.PAKHOMOVA,B.GAO,W.E.BOEGLIN,A.R.BRASH,M.E.NEWCOMER
JRNL TITL THE STRUCTURE AND PEROXIDASE ACTIVITY OF A 33-KDA
JRNL TITL 2 CATALASE-RELATED PROTEIN FROM MYCOBACTERIUM AVIUM SSP.
JRNL TITL 3 PARATUBERCULOSIS.
JRNL REF PROTEIN SCI. V. 18 2559 2009
JRNL REFN ISSN 0961-8368
JRNL PMID 19827095
JRNL DOI 10.1002/PRO.265
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.5
REMARK 3 NUMBER OF REFLECTIONS : 14446
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) : 0.202
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 997
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2266
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.46000
REMARK 3 B22 (A**2) : 13.80000
REMARK 3 B33 (A**2) : -11.34000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.37
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) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.49
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.810
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3E4Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000048880.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CAMD
REMARK 200 BEAMLINE : GCPCC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5896
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15361
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 43.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 3E4W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M 1,6-HEXANEDIOL, 0.1 M NA
REMARK 280 CITRATE, 13-15 % PEG 20000, 2.5-6.5 % GLYCEROL, PH 6.9, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 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 -1.000000 0.000000 0.000000 34.80200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.74950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.74950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.80200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.34000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.80200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.34000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 82.74950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.34000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.80200
REMARK 290 SMTRY2 7 0.000000 1.000000 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 82.74950
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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 305
REMARK 465 ARG A 306
REMARK 465 GLY A 307
REMARK 465 ALA A 308
REMARK 465 GLN A 309
REMARK 465 ALA A 310
REMARK 465 PRO A 311
REMARK 465 PRO A 312
REMARK 465 VAL A 313
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 LEU A 124 -106.60 -19.03
REMARK 500 LEU A 130 24.63 -79.40
REMARK 500 ALA A 131 -39.00 -135.72
REMARK 500 ARG A 139 -36.69 -27.37
REMARK 500 LEU A 144 -49.37 -26.02
REMARK 500 LEU A 165 -54.95 61.50
REMARK 500 PRO A 237 2.19 -69.86
REMARK 500 GLU A 262 40.26 70.69
REMARK 500 VAL A 275 -159.98 -85.44
REMARK 500 ASP A 283 44.57 -75.77
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 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 294 OH
REMARK 620 2 HEM A 501 NA 85.7
REMARK 620 3 HEM A 501 NB 98.4 88.0
REMARK 620 4 HEM A 501 NC 93.5 178.5 90.9
REMARK 620 5 HEM A 501 ND 82.8 89.6 177.2 91.5
REMARK 620 N 1 2 3 4
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 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 710
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E4W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A 33KDA CATALASE-RELATED PROTEIN FROM
REMARK 900 MYCOBACTERIUM AVIUM SUBSP. PARATUBERCULOSIS. P2(1)2(1)2(1) CRYSTAL
REMARK 900 FORM.
DBREF 3E4Y A 1 313 UNP Q73WB6 Q73WB6_MYCPA 1 313
SEQADV 3E4Y MET A -6 UNP Q73WB6 EXPRESSION TAG
SEQADV 3E4Y HIS A -5 UNP Q73WB6 EXPRESSION TAG
SEQADV 3E4Y HIS A -4 UNP Q73WB6 EXPRESSION TAG
SEQADV 3E4Y HIS A -3 UNP Q73WB6 EXPRESSION TAG
SEQADV 3E4Y HIS A -2 UNP Q73WB6 EXPRESSION TAG
SEQADV 3E4Y HIS A -1 UNP Q73WB6 EXPRESSION TAG
SEQADV 3E4Y HIS A 0 UNP Q73WB6 EXPRESSION TAG
SEQRES 1 A 320 MET HIS HIS HIS HIS HIS HIS MET SER GLY GLY LEU THR
SEQRES 2 A 320 PRO ASP GLN ALA ILE ASP ALA ILE ARG GLY THR GLY GLY
SEQRES 3 A 320 ALA GLN PRO GLY CYS ARG ALA LEU HIS ALA LYS GLY THR
SEQRES 4 A 320 LEU TYR ARG GLY THR PHE THR ALA THR ARG ASP ALA VAL
SEQRES 5 A 320 MET LEU SER ALA ALA PRO HIS LEU ASP GLY SER THR VAL
SEQRES 6 A 320 PRO ALA LEU ILE ARG PHE SER ASN GLY SER GLY ASN PRO
SEQRES 7 A 320 LYS GLN ARG ASP GLY ALA PRO GLY VAL ARG GLY MET ALA
SEQRES 8 A 320 VAL LYS PHE THR LEU PRO ASP GLY SER THR THR ASP VAL
SEQRES 9 A 320 SER ALA GLN THR ALA ARG LEU LEU VAL SER SER THR PRO
SEQRES 10 A 320 GLU GLY PHE ILE ASP LEU LEU LYS ALA MET ARG PRO GLY
SEQRES 11 A 320 LEU THR THR PRO LEU ARG LEU ALA THR HIS LEU LEU THR
SEQRES 12 A 320 HIS PRO ARG LEU LEU GLY ALA LEU PRO LEU LEU ARG GLU
SEQRES 13 A 320 ALA ASN ARG ILE PRO ALA SER TYR ALA THR THR GLU TYR
SEQRES 14 A 320 HIS GLY LEU HIS ALA PHE ARG TRP ILE ALA ALA ASP GLY
SEQRES 15 A 320 SER ALA ARG PHE VAL ARG TYR HIS LEU VAL PRO THR ALA
SEQRES 16 A 320 ALA GLU GLU TYR LEU SER ALA SER ASP ALA ARG GLY LYS
SEQRES 17 A 320 ASP PRO ASP PHE LEU THR ASP GLU LEU ALA ALA ARG LEU
SEQRES 18 A 320 GLN ASP GLY PRO VAL ARG PHE ASP PHE ARG VAL GLN ILE
SEQRES 19 A 320 ALA GLY PRO THR ASP SER THR VAL ASP PRO SER SER ALA
SEQRES 20 A 320 TRP GLN SER THR GLN ILE VAL THR VAL GLY THR VAL THR
SEQRES 21 A 320 ILE THR GLY PRO ASP THR GLU ARG GLU HIS GLY GLY ASP
SEQRES 22 A 320 ILE VAL VAL PHE ASP PRO MET ARG VAL THR ASP GLY ILE
SEQRES 23 A 320 GLU PRO SER ASP ASP PRO VAL LEU ARG PHE ARG THR LEU
SEQRES 24 A 320 VAL TYR SER ALA SER VAL LYS LEU ARG THR GLY VAL ASP
SEQRES 25 A 320 ARG GLY ALA GLN ALA PRO PRO VAL
HET HEM A 501 43
HET GOL A 610 6
HET GOL A 620 6
HET PO4 A 710 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 PO4 O4 P 3-
FORMUL 6 HOH *122(H2 O)
HELIX 1 1 THR A 6 GLY A 16 1 11
HELIX 2 2 ASP A 43 LEU A 47 5 5
HELIX 3 3 ALA A 50 ASP A 54 5 5
HELIX 4 4 THR A 109 ALA A 119 1 11
HELIX 5 5 THR A 125 HIS A 137 1 13
HELIX 6 6 PRO A 138 GLY A 142 5 5
HELIX 7 7 ALA A 143 ALA A 150 1 8
HELIX 8 8 SER A 156 THR A 160 5 5
HELIX 9 9 SER A 194 LYS A 201 1 8
HELIX 10 10 ASP A 204 GLY A 217 1 14
HELIX 11 11 ASP A 284 VAL A 304 1 21
SHEET 1 A10 ILE A 279 PRO A 281 0
SHEET 2 A10 TYR A 162 ILE A 171 -1 N ARG A 169 O GLU A 280
SHEET 3 A10 ALA A 177 PRO A 186 -1 O ARG A 178 N TRP A 170
SHEET 4 A10 VAL A 219 ILE A 227 -1 O ARG A 224 N HIS A 183
SHEET 5 A10 ILE A 246 PRO A 257 -1 O VAL A 252 N PHE A 221
SHEET 6 A10 GLY A 31 ALA A 40 -1 N ARG A 35 O GLY A 256
SHEET 7 A10 THR A 57 ASN A 66 -1 O ALA A 60 N GLY A 36
SHEET 8 A10 ARG A 81 THR A 88 -1 O GLY A 82 N SER A 65
SHEET 9 A10 THR A 94 GLN A 100 -1 O ALA A 99 N MET A 83
SHEET 10 A10 TYR A 162 ILE A 171 -1 O HIS A 163 N GLN A 100
SHEET 1 B 2 ILE A 153 PRO A 154 0
SHEET 2 B 2 TYR A 192 LEU A 193 -1 O LEU A 193 N ILE A 153
LINK OH TYR A 294 FE HEM A 501 1555 1555 2.47
SITE 1 AC1 20 ARG A 25 ALA A 26 LEU A 27 HIS A 28
SITE 2 AC1 20 ARG A 63 SER A 98 ALA A 99 GLN A 100
SITE 3 AC1 20 LEU A 105 PHE A 113 HIS A 163 GLY A 164
SITE 4 AC1 20 PHE A 270 ARG A 290 TYR A 294 SER A 297
SITE 5 AC1 20 ARG A 301 GOL A 610 HOH A 721 HOH A 773
SITE 1 AC2 4 HIS A 28 GLN A 100 LEU A 105 HEM A 501
SITE 1 AC3 5 ARG A 103 HIS A 183 THR A 187 ALA A 189
SITE 2 AC3 5 ARG A 224
SITE 1 AC4 3 HIS A 263 GLY A 264 HOH A 828
CRYST1 69.604 92.680 165.499 90.00 90.00 90.00 I 21 21 21 8
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 0.014367 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006042 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
