HEADER OXIDOREDUCTASE 04-MAY-09 3HB6
TITLE INACTIVE MUTANT H54F OF PROTEUS MIRABILIS CATALASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.11.1.6;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE 3 ORGANISM_TAXID: 584;
SOURCE 4 GENE: KATA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PALTER-CAT
KEYWDS BETA-BARREL, HEME, HYDROGEN PEROXIDE, IRON, METAL-BINDING, NADP,
KEYWDS 2 OXIDATION, OXIDOREDUCTASE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.ANDEOLETTI,H.M.JOUVE,P.GOUET
REVDAT 5 06-SEP-23 3HB6 1 REMARK
REVDAT 4 13-OCT-21 3HB6 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3HB6 1 VERSN
REVDAT 2 21-JUL-09 3HB6 1 JRNL
REVDAT 1 12-MAY-09 3HB6 0
JRNL AUTH P.ANDREOLETTI,J.M.MOUESCA,P.GOUET,M.JAQUINOD,
JRNL AUTH 2 C.CAPEILLERE-BLANDIN,H.M.JOUVE
JRNL TITL VERDOHEME FORMATION IN PROTEUS MIRABILIS CATALASE.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1790 741 2009
JRNL REFN ISSN 0006-3002
JRNL PMID 19394409
JRNL DOI 10.1016/J.BBAGEN.2009.04.010
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2883366.320
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 39529
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) : 0.203
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1986
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6136
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 323
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3869
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 476
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.69000
REMARK 3 B22 (A**2) : 8.69000
REMARK 3 B33 (A**2) : -17.38000
REMARK 3 B12 (A**2) : 2.19000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.28
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.600
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) : 1.080 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.700 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.760 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.510 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 13.53
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : PARAM19.CHROMO
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052919.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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 1M85
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M TRIS-MALATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 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+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 166.06667
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 83.03333
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 0.00000
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 166.06667
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 83.03333
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 166.06667
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 83.03333
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 166.06667
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 0.00000
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 83.03333
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 39250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -181.8 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 109.30000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 109.30000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A 493 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 562 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 708 LIES ON A SPECIAL POSITION.
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 2
REMARK 465 LYS A 3
REMARK 465 GLY A 480
REMARK 465 LYS A 481
REMARK 465 ASP A 482
REMARK 465 ALA A 483
REMARK 465 LYS A 484
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 32 0.22 -65.82
REMARK 500 LYS A 148 -158.73 -98.76
REMARK 500 SER A 196 -56.37 65.32
REMARK 500 TYR A 199 -168.06 -119.08
REMARK 500 VAL A 292 -56.46 -124.32
REMARK 500 ASN A 348 37.40 -93.49
REMARK 500 ASP A 367 -132.99 56.98
REMARK 500 ASN A 375 -174.87 73.88
REMARK 500 HIS A 464 130.45 -170.61
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 485 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 337 OH
REMARK 620 2 HEM A 485 NA 103.9
REMARK 620 3 HEM A 485 NB 101.2 88.0
REMARK 620 4 HEM A 485 NC 88.1 168.0 91.2
REMARK 620 5 HEM A 485 ND 83.9 90.6 174.9 89.1
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 485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 489
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 494
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M85 RELATED DB: PDB
REMARK 900 PROTEUS MIRABILIS CATALASE, NATIVE FORM
REMARK 900 RELATED ID: 1MQF RELATED DB: PDB
REMARK 900 COMPOUND I FROM PROTEUS MIRABILIS CATALASE
REMARK 900 RELATED ID: 1NM0 RELATED DB: PDB
REMARK 900 PROTEUS MIRABILIS CATALASE IN COMPLEX WITH FORMATE
REMARK 900 RELATED ID: 2CAG RELATED DB: PDB
REMARK 900 CATALASE COMPOUND II
REMARK 900 RELATED ID: 2CAH RELATED DB: PDB
REMARK 900 PROTEUS MIRABILIS PR CATALASE, NATIVE FORM (E-FE(III)) COMPLEXED
REMARK 900 WITH NADPH
REMARK 900 RELATED ID: 1E93 RELATED DB: PDB
REMARK 900 RECOMBINANT CATALASE DEPLETED IN IRON
REMARK 900 RELATED ID: 1H6N RELATED DB: PDB
REMARK 900 TYROSYL RADICAL INTERMEDIATE IN PROTEUS MIRABILIS CATALASE
REMARK 900 RELATED ID: 1H7K RELATED DB: PDB
REMARK 900 TYROSYL RADICAL INTERMEDIATE IN PROTEUS MIRABILIS CATALASE
DBREF 3HB6 A 1 484 UNP P42321 CATA_PROMI 1 484
SEQADV 3HB6 PHE A 54 UNP P42321 HIS 54 ENGINEERED MUTATION
SEQRES 1 A 484 MET GLU LYS LYS LYS LEU THR THR ALA ALA GLY ALA PRO
SEQRES 2 A 484 VAL VAL ASP ASN ASN ASN VAL ILE THR ALA GLY PRO ARG
SEQRES 3 A 484 GLY PRO MET LEU LEU GLN ASP VAL TRP PHE LEU GLU LYS
SEQRES 4 A 484 LEU ALA HIS PHE ASP ARG GLU VAL ILE PRO GLU ARG ARG
SEQRES 5 A 484 MET PHE ALA LYS GLY SER GLY ALA PHE GLY THR PHE THR
SEQRES 6 A 484 VAL THR HIS ASP ILE THR LYS TYR THR ARG ALA LYS ILE
SEQRES 7 A 484 PHE SER GLU VAL GLY LYS LYS THR GLU MET PHE ALA ARG
SEQRES 8 A 484 PHE SER THR VAL ALA GLY GLU ARG GLY ALA ALA ASP ALA
SEQRES 9 A 484 GLU ARG ASP ILE ARG GLY PHE ALA LEU LYS PHE TYR THR
SEQRES 10 A 484 GLU GLU GLY ASN TRP ASP MET VAL GLY ASN ASN THR PRO
SEQRES 11 A 484 VAL PHE TYR LEU ARG ASP PRO LEU LYS PHE PRO ASP LEU
SEQRES 12 A 484 ASN HIS ILE VAL LYS ARG ASP PRO ARG THR ASN MET ARG
SEQRES 13 A 484 ASN MET ALA TYR LYS TRP ASP PHE PHE SER HIS LEU PRO
SEQRES 14 A 484 GLU SER LEU HIS GLN LEU THR ILE ASP MET SER ASP ARG
SEQRES 15 A 484 GLY LEU PRO LEU SER TYR ARG PHE VAL HIS GLY PHE GLY
SEQRES 16 A 484 SER HIS THR TYR SER PHE ILE ASN LYS ASP ASN GLU ARG
SEQRES 17 A 484 PHE TRP VAL LYS PHE HIS PHE ARG CYS GLN GLN GLY ILE
SEQRES 18 A 484 LYS ASN LEU MET ASP ASP GLU ALA GLU ALA LEU VAL GLY
SEQRES 19 A 484 LYS ASP ARG GLU SER SER GLN ARG ASP LEU PHE GLU ALA
SEQRES 20 A 484 ILE GLU ARG GLY ASP TYR PRO ARG TRP LYS LEU GLN ILE
SEQRES 21 A 484 GLN ILE MET PRO GLU LYS GLU ALA SER THR VAL PRO TYR
SEQRES 22 A 484 ASN PRO PHE ASP LEU THR LYS VAL TRP PRO HIS ALA ASP
SEQRES 23 A 484 TYR PRO LEU MET ASP VAL GLY TYR PHE GLU LEU ASN ARG
SEQRES 24 A 484 ASN PRO ASP ASN TYR PHE SER ASP VAL GLU GLN ALA ALA
SEQRES 25 A 484 PHE SER PRO ALA ASN ILE VAL PRO GLY ILE SER PHE SER
SEQRES 26 A 484 PRO ASP LYS MET LEU GLN GLY ARG LEU PHE SER TYR GLY
SEQRES 27 A 484 ASP ALA HIS ARG TYR ARG LEU GLY VAL ASN HIS HIS GLN
SEQRES 28 A 484 ILE PRO VAL ASN ALA PRO LYS CYS PRO PHE HIS ASN TYR
SEQRES 29 A 484 HIS ARG ASP GLY ALA MET ARG VAL ASP GLY ASN SER GLY
SEQRES 30 A 484 ASN GLY ILE THR TYR GLU PRO ASN SER GLY GLY VAL PHE
SEQRES 31 A 484 GLN GLU GLN PRO ASP PHE LYS GLU PRO PRO LEU SER ILE
SEQRES 32 A 484 GLU GLY ALA ALA ASP HIS TRP ASN HIS ARG GLU ASP GLU
SEQRES 33 A 484 ASP TYR PHE SER GLN PRO ARG ALA LEU TYR GLU LEU LEU
SEQRES 34 A 484 SER ASP ASP GLU HIS GLN ARG MET PHE ALA ARG ILE ALA
SEQRES 35 A 484 GLY GLU LEU SER GLN ALA SER LYS GLU THR GLN GLN ARG
SEQRES 36 A 484 GLN ILE ASP LEU PHE THR LYS VAL HIS PRO GLU TYR GLY
SEQRES 37 A 484 ALA GLY VAL GLU LYS ALA ILE LYS VAL LEU GLU GLY LYS
SEQRES 38 A 484 ASP ALA LYS
HET HEM A 485 43
HET SO4 A 486 5
HET SO4 A 487 5
HET SO4 A 488 5
HET SO4 A 489 5
HET SO4 A 490 5
HET SO4 A 491 5
HET SO4 A 492 5
HET SO4 A 493 5
HET GOL A 494 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 11 GOL C3 H8 O3
FORMUL 12 HOH *476(H2 O)
HELIX 1 1 ASP A 33 ASP A 44 1 12
HELIX 2 2 ASP A 136 LEU A 138 5 3
HELIX 3 3 LYS A 139 LYS A 148 1 10
HELIX 4 4 ASN A 157 HIS A 167 1 11
HELIX 5 5 LEU A 168 GLU A 170 5 3
HELIX 6 6 SER A 171 SER A 180 1 10
HELIX 7 7 ASP A 181 LEU A 184 5 4
HELIX 8 8 SER A 187 VAL A 191 5 5
HELIX 9 9 MET A 225 ASP A 236 1 12
HELIX 10 10 GLU A 238 ARG A 250 1 13
HELIX 11 11 LYS A 266 THR A 270 5 5
HELIX 12 12 ASN A 303 VAL A 308 1 6
HELIX 13 13 ASP A 327 LEU A 345 1 19
HELIX 14 14 ASN A 348 ILE A 352 5 5
HELIX 15 15 GLN A 393 LYS A 397 5 5
HELIX 16 16 ASN A 411 ASP A 415 5 5
HELIX 17 17 PHE A 419 LEU A 429 1 11
HELIX 18 18 SER A 430 SER A 446 1 17
HELIX 19 19 SER A 449 HIS A 464 1 16
HELIX 20 20 HIS A 464 GLU A 479 1 16
SHEET 1 A11 ILE A 322 SER A 323 0
SHEET 2 A11 TYR A 199 ILE A 202 -1 N SER A 200 O SER A 323
SHEET 3 A11 ARG A 208 CYS A 217 -1 O PHE A 209 N PHE A 201
SHEET 4 A11 ARG A 255 PRO A 264 -1 O MET A 263 N TRP A 210
SHEET 5 A11 MET A 290 ARG A 299 -1 O MET A 290 N ILE A 260
SHEET 6 A11 GLY A 57 VAL A 66 -1 N PHE A 61 O ARG A 299
SHEET 7 A11 LYS A 85 SER A 93 -1 O THR A 86 N PHE A 64
SHEET 8 A11 GLY A 110 THR A 117 -1 O LYS A 114 N PHE A 89
SHEET 9 A11 GLY A 120 ASN A 127 -1 O TRP A 122 N PHE A 115
SHEET 10 A11 GLY A 193 PHE A 194 -1 O PHE A 194 N ASN A 127
SHEET 11 A11 ARG A 208 CYS A 217 -1 O PHE A 215 N GLY A 193
LINK OH TYR A 337 FE HEM A 485 1555 1555 2.02
CISPEP 1 GLU A 383 PRO A 384 0 0.35
SITE 1 AC1 23 LEU A 40 ASP A 44 ARG A 51 PHE A 54
SITE 2 AC1 23 ARG A 91 GLY A 110 VAL A 125 GLY A 126
SITE 3 AC1 23 ASN A 127 PHE A 140 GLY A 195 SER A 196
SITE 4 AC1 23 HIS A 197 PHE A 313 MET A 329 ARG A 333
SITE 5 AC1 23 SER A 336 TYR A 337 HIS A 341 ARG A 344
SITE 6 AC1 23 HOH A 495 HOH A 641 HOH A 645
SITE 1 AC2 4 ARG A 182 HIS A 192 ARG A 216 HOH A 883
SITE 1 AC3 6 ASP A 417 ARG A 423 HOH A 553 HOH A 835
SITE 2 AC3 6 HOH A 851 HOH A 910
SITE 1 AC4 3 SER A 430 GLU A 433 ARG A 436
SITE 1 AC5 2 ARG A 182 ASN A 223
SITE 1 AC6 4 PRO A 283 HIS A 284 ALA A 285 HOH A 886
SITE 1 AC7 2 ARG A 216 GLN A 218
SITE 1 AC8 2 GLN A 447 HOH A 811
SITE 1 AC9 4 ARG A 45 ARG A 342 TYR A 343 HOH A 659
SITE 1 BC1 6 GLU A 38 HIS A 42 ARG A 342 HIS A 349
SITE 2 BC1 6 HOH A 592 HOH A 624
CRYST1 109.300 109.300 249.100 90.00 90.00 120.00 P 62 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 0.009149 0.005282 0.000000 0.00000
SCALE2 0.000000 0.010565 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004014 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
