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PDBsum entry 2j2m

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
2j2m
Jmol
Contents
Protein chains
480 a.a.
Ligands
HEM ×4
Waters ×536
HEADER    OXIDOREDUCTASE                          17-AUG-06   2J2M
TITLE     CRYSTAL STRUCTURE ANALYSIS OF CATALASE FROM EXIGUOBACTERIUM
TITLE    2 OXIDOTOLERANS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CATALASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 1.11.1.6
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: EXIGUOBACTERIUM OXIDOTOLERANS;
SOURCE   3 ORGANISM_TAXID: 223958;
SOURCE   4 STRAIN: T-2-2T
KEYWDS    FUNCTIONAL CLASS, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    I.HARA,N.ICHISE,K.KOJIMA,H.KONDO,S.OHGIYA,H.MATSUYAMA,
AUTHOR   2 I.YUMOTO
REVDAT   2   24-FEB-09 2J2M    1       VERSN
REVDAT   1   16-JAN-07 2J2M    0
JRNL        AUTH   I.HARA,N.ICHISE,K.KOJIMA,H.KONDO,S.OHGIYA,
JRNL        AUTH 2 H.MATSUYAMA,I.YUMOTO
JRNL        TITL   RELATIONSHIP BETWEEN THE SIZE OF THE BOTTLENECK 15
JRNL        TITL 2 A FROM IRON IN THE MAIN CHANNEL AND THE REACTIVITY
JRNL        TITL 3 OF CATALASE CORRESPONDING TO THE MOLECULAR SIZE OF
JRNL        TITL 4 SUBSTRATES.
JRNL        REF    BIOCHEMISTRY                  V.  46    11 2007
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   17198371
JRNL        DOI    10.1021/BI061519W
REMARK   2
REMARK   2 RESOLUTION.    2.4  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   NUMBER OF REFLECTIONS             : 94615
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 + TEST SET) : 0.201
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.230
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4994
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6822
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010
REMARK   3   BIN FREE R VALUE SET COUNT          : 321
REMARK   3   BIN FREE R VALUE                    : 0.2570
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 15576
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 172
REMARK   3   SOLVENT ATOMS            : 536
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 23.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.64
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.60000
REMARK   3    B22 (A**2) : -0.27000
REMARK   3    B33 (A**2) : 1.11000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.39000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.363
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.234
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.151
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.259
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.907
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16188 ; 0.013 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22024 ; 1.430 ; 1.970
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1916 ; 6.423 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   892 ;38.395 ;24.529
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2620 ;18.062 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   108 ;18.705 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2260 ; 0.104 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12880 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7846 ; 0.209 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10792 ; 0.305 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1052 ; 0.140 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    27 ; 0.144 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.078 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9891 ; 0.620 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15584 ; 1.000 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7164 ; 1.648 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6432 ; 2.474 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2J2M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-AUG-06.
REMARK 100 THE PDBE ID CODE IS EBI-29727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-03
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTONFACTORY
REMARK 200  BEAMLINE                       : AR-NW12A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : SI (111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 99632
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.06000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 10.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 8CAT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH6.0,
REMARK 280  12-13%(W/V)PEG10000, 5%(W/V)PEG400 AND 20%(W/V)GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.96750
REMARK 290   SMTRY3   2  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 GENERATING THE BIOMOLECULE
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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     ASN A     2
REMARK 465     GLU A     3
REMARK 465     ASN A     4
REMARK 465     GLU A     5
REMARK 465     LEU A   486
REMARK 465     GLN A   487
REMARK 465     GLN A   488
REMARK 465     MET A   489
REMARK 465     GLN A   490
REMARK 465     LYS A   491
REMARK 465     MET B     1
REMARK 465     ASN B     2
REMARK 465     GLU B     3
REMARK 465     ASN B     4
REMARK 465     GLU B     5
REMARK 465     LEU B   486
REMARK 465     GLN B   487
REMARK 465     GLN B   488
REMARK 465     MET B   489
REMARK 465     GLN B   490
REMARK 465     LYS B   491
REMARK 465     MET C     1
REMARK 465     ASN C     2
REMARK 465     GLU C     3
REMARK 465     ASN C     4
REMARK 465     GLU C     5
REMARK 465     LEU C   486
REMARK 465     GLN C   487
REMARK 465     GLN C   488
REMARK 465     MET C   489
REMARK 465     GLN C   490
REMARK 465     LYS C   491
REMARK 465     MET D     1
REMARK 465     ASN D     2
REMARK 465     GLU D     3
REMARK 465     ASN D     4
REMARK 465     GLU D     5
REMARK 465     LEU D   486
REMARK 465     GLN D   487
REMARK 465     GLN D   488
REMARK 465     MET D   489
REMARK 465     GLN D   490
REMARK 465     LYS D   491
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   O    THR A   101  -  O    THR B   101              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU A 278   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    ARG B 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B 216   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG B 216   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG C 216   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
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 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    ARG A 170       72.69   -118.71
REMARK 500    VAL A 198      -56.58     66.83
REMARK 500    GLU A 309      -70.80   -113.70
REMARK 500    ASP A 329      116.27    -31.61
REMARK 500    VAL B  97      -62.48   -122.55
REMARK 500    VAL B 198      -59.12     62.80
REMARK 500    GLU B 309      -77.81   -110.78
REMARK 500    ASP B 329      116.06    -38.81
REMARK 500    ASN B 419       59.96     37.21
REMARK 500    ASN C  11       -7.24    -59.99
REMARK 500    ASP C  35       80.73    -68.62
REMARK 500    VAL C  97      -55.78   -123.29
REMARK 500    VAL C 198      -62.57     66.20
REMARK 500    GLU C 309      -72.28   -107.75
REMARK 500    PRO C 484     -100.83    -80.80
REMARK 500    ASP D  35       78.30    -67.29
REMARK 500    VAL D  97      -58.89   -121.27
REMARK 500    ASP D 109      143.15   -172.75
REMARK 500    ASN D 156       30.18     72.38
REMARK 500    ARG D 170       71.78   -118.86
REMARK 500    VAL D 198      -60.61     62.71
REMARK 500    GLU D 309      -74.57   -115.89
REMARK 500    PRO D 484     -104.31    -79.09
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 LEU A  478     ASN A  479                  -39.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    LEU A 478        21.2      L          L   OUTSIDE RANGE
REMARK 500    LEU B 478        18.9      L          L   OUTSIDE RANGE
REMARK 500    LEU C 478        22.8      L          L   OUTSIDE RANGE
REMARK 500    LEU D 478        22.7      L          L   OUTSIDE RANGE
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 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 339   OH
REMARK 620 2 HEM A 501   NB   92.6
REMARK 620 3 HEM A 501   NC  102.5  88.4
REMARK 620 4 HEM A 501   NA   93.0  86.1 163.8
REMARK 620 5 HEM A 501   ND  104.3 163.0  89.9  91.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 501  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEM B 501   NB
REMARK 620 2 HEM B 501   NC   90.8
REMARK 620 3 TYR B 339   OH   88.3 100.5
REMARK 620 4 HEM B 501   NA   87.2 169.6  89.6
REMARK 620 5 HEM B 501   ND  167.8  88.7 103.8  91.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 501  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEM C 501   NA
REMARK 620 2 HEM C 501   ND   89.2
REMARK 620 3 TYR C 339   OH   89.1 103.1
REMARK 620 4 HEM C 501   NB   91.4 171.5  85.4
REMARK 620 5 HEM C 501   NC  170.8  90.6  99.9  87.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 501  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 339   OH
REMARK 620 2 HEM D 501   NA   92.1
REMARK 620 3 HEM D 501   NB   91.5  91.5
REMARK 620 4 HEM D 501   NC  101.5 166.4  89.1
REMARK 620 5 HEM D 501   ND  102.3  86.0 166.1  90.2
REMARK 620 N                    1     2     3     4
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
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 HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 501
REMARK 999
REMARK 999 SEQUENCE
REMARK 999  THE SEQUENCE OF THIS CATALASE HAS BEEN DEPOSITED TO DDBJ
REMARK 999  WITH ACCESSION NUMBER OF AB266484
DBREF  2J2M A    1   491  PDB    2J2M     2J2M             1    491
DBREF  2J2M B    1   491  PDB    2J2M     2J2M             1    491
DBREF  2J2M C    1   491  PDB    2J2M     2J2M             1    491
DBREF  2J2M D    1   491  PDB    2J2M     2J2M             1    491
SEQRES   1 A  491  MET ASN GLU ASN GLU LYS LYS LEU THR THR ASN GLN GLY
SEQRES   2 A  491  VAL PRO ILE GLY ASP ASN GLN ASN SER ARG THR ALA GLY
SEQRES   3 A  491  ARG ARG GLY PRO THR LEU LEU GLU ASP TYR GLN LEU ILE
SEQRES   4 A  491  GLU LYS ILE ALA HIS PHE ASP ARG GLU ARG VAL PRO GLU
SEQRES   5 A  491  ARG VAL VAL HIS ALA ARG GLY PHE GLY ALA HIS GLY VAL
SEQRES   6 A  491  PHE LYS VAL LYS ASN SER MET LYS LYS TYR THR LYS ALA
SEQRES   7 A  491  ALA PHE LEU GLN GLU GLU GLY THR GLU VAL PRO VAL PHE
SEQRES   8 A  491  ALA ARG PHE SER THR VAL ILE HIS GLY THR HIS SER PRO
SEQRES   9 A  491  GLU THR LEU ARG ASP PRO ARG GLY PHE SER VAL LYS PHE
SEQRES  10 A  491  TYR THR GLU GLU GLY ASN TRP ASP PHE VAL GLY ASN ASN
SEQRES  11 A  491  LEU PRO VAL PHE PHE ILE ARG ASP ALA MET LYS PHE PRO
SEQRES  12 A  491  ASP MET VAL HIS SER LEU LYS PRO ASP PRO ARG THR ASN
SEQRES  13 A  491  ILE GLN ASP PRO ASP ARG TYR TRP ASP PHE MET THR LEU
SEQRES  14 A  491  ARG PRO GLU SER THR ASN MET LEU MET HIS ILE PHE THR
SEQRES  15 A  491  ASP GLU GLY ILE PRO ALA SER TYR ARG LYS MET ARG GLY
SEQRES  16 A  491  SER SER VAL HIS SER PHE LYS TRP VAL ASN ALA HIS GLY
SEQRES  17 A  491  ASN THR VAL TYR ILE LYS LEU ARG TRP VAL PRO LYS GLU
SEQRES  18 A  491  GLY VAL HIS ASN LEU SER ALA ASP GLU ALA THR GLU VAL
SEQRES  19 A  491  GLN GLY LYS ASP PHE ASN HIS ALA SER ASN ASP THR PHE
SEQRES  20 A  491  GLN ALA ILE GLU ASN GLY ASP PHE PRO GLU TRP ASP LEU
SEQRES  21 A  491  PHE VAL GLN VAL LEU ASP PRO ALA ASP VAL GLU ASN PHE
SEQRES  22 A  491  ASP PHE ASP PRO LEU ASP ALA THR LYS ASP TRP PHE GLU
SEQRES  23 A  491  ASP VAL ILE PRO PHE GLN HIS VAL GLY THR MET THR LEU
SEQRES  24 A  491  ASN LYS ASN VAL ASP ASN TYR PHE ALA GLU THR GLU SER
SEQRES  25 A  491  VAL GLY PHE ASN PRO GLY VAL LEU VAL PRO GLY MET LEU
SEQRES  26 A  491  PRO SER GLU ASP LYS LEU LEU GLN GLY ARG LEU PHE SER
SEQRES  27 A  491  TYR SER ASP THR GLN ARG HIS ARG ILE GLY PRO ASN TYR
SEQRES  28 A  491  GLN GLN LEU PRO ILE ASN CYS PRO PHE ALA GLN VAL ASN
SEQRES  29 A  491  ASN TYR GLN ARG ASP GLY ALA MET PRO PHE LYS GLN GLN
SEQRES  30 A  491  THR SER SER VAL ASN TYR GLU PRO ASN ARG TYR GLN ASP
SEQRES  31 A  491  GLU PRO LYS GLN THR PRO GLU TYR THR GLU ASP THR GLN
SEQRES  32 A  491  PRO LEU HIS ASP ASP ILE HIS GLY ARG LEU GLU ILE GLU
SEQRES  33 A  491  LYS THR ASN ASN PHE GLY GLN ALA GLY GLU VAL TYR ARG
SEQRES  34 A  491  ARG MET THR GLU GLU GLU GLN MET ALA LEU LEU ASN ASN
SEQRES  35 A  491  LEU VAL ASN ASP LEU GLN GLN VAL ARG HIS GLU ASN THR
SEQRES  36 A  491  VAL LEU LEU ALA ILE CYS ASN PHE TYR ARG ALA ASP ALA
SEQRES  37 A  491  SER LEU GLY GLU LYS LEU SER GLU ALA LEU ASN VAL ASP
SEQRES  38 A  491  ILE LYS PRO PHE LEU GLN GLN MET GLN LYS
SEQRES   1 B  491  MET ASN GLU ASN GLU LYS LYS LEU THR THR ASN GLN GLY
SEQRES   2 B  491  VAL PRO ILE GLY ASP ASN GLN ASN SER ARG THR ALA GLY
SEQRES   3 B  491  ARG ARG GLY PRO THR LEU LEU GLU ASP TYR GLN LEU ILE
SEQRES   4 B  491  GLU LYS ILE ALA HIS PHE ASP ARG GLU ARG VAL PRO GLU
SEQRES   5 B  491  ARG VAL VAL HIS ALA ARG GLY PHE GLY ALA HIS GLY VAL
SEQRES   6 B  491  PHE LYS VAL LYS ASN SER MET LYS LYS TYR THR LYS ALA
SEQRES   7 B  491  ALA PHE LEU GLN GLU GLU GLY THR GLU VAL PRO VAL PHE
SEQRES   8 B  491  ALA ARG PHE SER THR VAL ILE HIS GLY THR HIS SER PRO
SEQRES   9 B  491  GLU THR LEU ARG ASP PRO ARG GLY PHE SER VAL LYS PHE
SEQRES  10 B  491  TYR THR GLU GLU GLY ASN TRP ASP PHE VAL GLY ASN ASN
SEQRES  11 B  491  LEU PRO VAL PHE PHE ILE ARG ASP ALA MET LYS PHE PRO
SEQRES  12 B  491  ASP MET VAL HIS SER LEU LYS PRO ASP PRO ARG THR ASN
SEQRES  13 B  491  ILE GLN ASP PRO ASP ARG TYR TRP ASP PHE MET THR LEU
SEQRES  14 B  491  ARG PRO GLU SER THR ASN MET LEU MET HIS ILE PHE THR
SEQRES  15 B  491  ASP GLU GLY ILE PRO ALA SER TYR ARG LYS MET ARG GLY
SEQRES  16 B  491  SER SER VAL HIS SER PHE LYS TRP VAL ASN ALA HIS GLY
SEQRES  17 B  491  ASN THR VAL TYR ILE LYS LEU ARG TRP VAL PRO LYS GLU
SEQRES  18 B  491  GLY VAL HIS ASN LEU SER ALA ASP GLU ALA THR GLU VAL
SEQRES  19 B  491  GLN GLY LYS ASP PHE ASN HIS ALA SER ASN ASP THR PHE
SEQRES  20 B  491  GLN ALA ILE GLU ASN GLY ASP PHE PRO GLU TRP ASP LEU
SEQRES  21 B  491  PHE VAL GLN VAL LEU ASP PRO ALA ASP VAL GLU ASN PHE
SEQRES  22 B  491  ASP PHE ASP PRO LEU ASP ALA THR LYS ASP TRP PHE GLU
SEQRES  23 B  491  ASP VAL ILE PRO PHE GLN HIS VAL GLY THR MET THR LEU
SEQRES  24 B  491  ASN LYS ASN VAL ASP ASN TYR PHE ALA GLU THR GLU SER
SEQRES  25 B  491  VAL GLY PHE ASN PRO GLY VAL LEU VAL PRO GLY MET LEU
SEQRES  26 B  491  PRO SER GLU ASP LYS LEU LEU GLN GLY ARG LEU PHE SER
SEQRES  27 B  491  TYR SER ASP THR GLN ARG HIS ARG ILE GLY PRO ASN TYR
SEQRES  28 B  491  GLN GLN LEU PRO ILE ASN CYS PRO PHE ALA GLN VAL ASN
SEQRES  29 B  491  ASN TYR GLN ARG ASP GLY ALA MET PRO PHE LYS GLN GLN
SEQRES  30 B  491  THR SER SER VAL ASN TYR GLU PRO ASN ARG TYR GLN ASP
SEQRES  31 B  491  GLU PRO LYS GLN THR PRO GLU TYR THR GLU ASP THR GLN
SEQRES  32 B  491  PRO LEU HIS ASP ASP ILE HIS GLY ARG LEU GLU ILE GLU
SEQRES  33 B  491  LYS THR ASN ASN PHE GLY GLN ALA GLY GLU VAL TYR ARG
SEQRES  34 B  491  ARG MET THR GLU GLU GLU GLN MET ALA LEU LEU ASN ASN
SEQRES  35 B  491  LEU VAL ASN ASP LEU GLN GLN VAL ARG HIS GLU ASN THR
SEQRES  36 B  491  VAL LEU LEU ALA ILE CYS ASN PHE TYR ARG ALA ASP ALA
SEQRES  37 B  491  SER LEU GLY GLU LYS LEU SER GLU ALA LEU ASN VAL ASP
SEQRES  38 B  491  ILE LYS PRO PHE LEU GLN GLN MET GLN LYS
SEQRES   1 C  491  MET ASN GLU ASN GLU LYS LYS LEU THR THR ASN GLN GLY
SEQRES   2 C  491  VAL PRO ILE GLY ASP ASN GLN ASN SER ARG THR ALA GLY
SEQRES   3 C  491  ARG ARG GLY PRO THR LEU LEU GLU ASP TYR GLN LEU ILE
SEQRES   4 C  491  GLU LYS ILE ALA HIS PHE ASP ARG GLU ARG VAL PRO GLU
SEQRES   5 C  491  ARG VAL VAL HIS ALA ARG GLY PHE GLY ALA HIS GLY VAL
SEQRES   6 C  491  PHE LYS VAL LYS ASN SER MET LYS LYS TYR THR LYS ALA
SEQRES   7 C  491  ALA PHE LEU GLN GLU GLU GLY THR GLU VAL PRO VAL PHE
SEQRES   8 C  491  ALA ARG PHE SER THR VAL ILE HIS GLY THR HIS SER PRO
SEQRES   9 C  491  GLU THR LEU ARG ASP PRO ARG GLY PHE SER VAL LYS PHE
SEQRES  10 C  491  TYR THR GLU GLU GLY ASN TRP ASP PHE VAL GLY ASN ASN
SEQRES  11 C  491  LEU PRO VAL PHE PHE ILE ARG ASP ALA MET LYS PHE PRO
SEQRES  12 C  491  ASP MET VAL HIS SER LEU LYS PRO ASP PRO ARG THR ASN
SEQRES  13 C  491  ILE GLN ASP PRO ASP ARG TYR TRP ASP PHE MET THR LEU
SEQRES  14 C  491  ARG PRO GLU SER THR ASN MET LEU MET HIS ILE PHE THR
SEQRES  15 C  491  ASP GLU GLY ILE PRO ALA SER TYR ARG LYS MET ARG GLY
SEQRES  16 C  491  SER SER VAL HIS SER PHE LYS TRP VAL ASN ALA HIS GLY
SEQRES  17 C  491  ASN THR VAL TYR ILE LYS LEU ARG TRP VAL PRO LYS GLU
SEQRES  18 C  491  GLY VAL HIS ASN LEU SER ALA ASP GLU ALA THR GLU VAL
SEQRES  19 C  491  GLN GLY LYS ASP PHE ASN HIS ALA SER ASN ASP THR PHE
SEQRES  20 C  491  GLN ALA ILE GLU ASN GLY ASP PHE PRO GLU TRP ASP LEU
SEQRES  21 C  491  PHE VAL GLN VAL LEU ASP PRO ALA ASP VAL GLU ASN PHE
SEQRES  22 C  491  ASP PHE ASP PRO LEU ASP ALA THR LYS ASP TRP PHE GLU
SEQRES  23 C  491  ASP VAL ILE PRO PHE GLN HIS VAL GLY THR MET THR LEU
SEQRES  24 C  491  ASN LYS ASN VAL ASP ASN TYR PHE ALA GLU THR GLU SER
SEQRES  25 C  491  VAL GLY PHE ASN PRO GLY VAL LEU VAL PRO GLY MET LEU
SEQRES  26 C  491  PRO SER GLU ASP LYS LEU LEU GLN GLY ARG LEU PHE SER
SEQRES  27 C  491  TYR SER ASP THR GLN ARG HIS ARG ILE GLY PRO ASN TYR
SEQRES  28 C  491  GLN GLN LEU PRO ILE ASN CYS PRO PHE ALA GLN VAL ASN
SEQRES  29 C  491  ASN TYR GLN ARG ASP GLY ALA MET PRO PHE LYS GLN GLN
SEQRES  30 C  491  THR SER SER VAL ASN TYR GLU PRO ASN ARG TYR GLN ASP
SEQRES  31 C  491  GLU PRO LYS GLN THR PRO GLU TYR THR GLU ASP THR GLN
SEQRES  32 C  491  PRO LEU HIS ASP ASP ILE HIS GLY ARG LEU GLU ILE GLU
SEQRES  33 C  491  LYS THR ASN ASN PHE GLY GLN ALA GLY GLU VAL TYR ARG
SEQRES  34 C  491  ARG MET THR GLU GLU GLU GLN MET ALA LEU LEU ASN ASN
SEQRES  35 C  491  LEU VAL ASN ASP LEU GLN GLN VAL ARG HIS GLU ASN THR
SEQRES  36 C  491  VAL LEU LEU ALA ILE CYS ASN PHE TYR ARG ALA ASP ALA
SEQRES  37 C  491  SER LEU GLY GLU LYS LEU SER GLU ALA LEU ASN VAL ASP
SEQRES  38 C  491  ILE LYS PRO PHE LEU GLN GLN MET GLN LYS
SEQRES   1 D  491  MET ASN GLU ASN GLU LYS LYS LEU THR THR ASN GLN GLY
SEQRES   2 D  491  VAL PRO ILE GLY ASP ASN GLN ASN SER ARG THR ALA GLY
SEQRES   3 D  491  ARG ARG GLY PRO THR LEU LEU GLU ASP TYR GLN LEU ILE
SEQRES   4 D  491  GLU LYS ILE ALA HIS PHE ASP ARG GLU ARG VAL PRO GLU
SEQRES   5 D  491  ARG VAL VAL HIS ALA ARG GLY PHE GLY ALA HIS GLY VAL
SEQRES   6 D  491  PHE LYS VAL LYS ASN SER MET LYS LYS TYR THR LYS ALA
SEQRES   7 D  491  ALA PHE LEU GLN GLU GLU GLY THR GLU VAL PRO VAL PHE
SEQRES   8 D  491  ALA ARG PHE SER THR VAL ILE HIS GLY THR HIS SER PRO
SEQRES   9 D  491  GLU THR LEU ARG ASP PRO ARG GLY PHE SER VAL LYS PHE
SEQRES  10 D  491  TYR THR GLU GLU GLY ASN TRP ASP PHE VAL GLY ASN ASN
SEQRES  11 D  491  LEU PRO VAL PHE PHE ILE ARG ASP ALA MET LYS PHE PRO
SEQRES  12 D  491  ASP MET VAL HIS SER LEU LYS PRO ASP PRO ARG THR ASN
SEQRES  13 D  491  ILE GLN ASP PRO ASP ARG TYR TRP ASP PHE MET THR LEU
SEQRES  14 D  491  ARG PRO GLU SER THR ASN MET LEU MET HIS ILE PHE THR
SEQRES  15 D  491  ASP GLU GLY ILE PRO ALA SER TYR ARG LYS MET ARG GLY
SEQRES  16 D  491  SER SER VAL HIS SER PHE LYS TRP VAL ASN ALA HIS GLY
SEQRES  17 D  491  ASN THR VAL TYR ILE LYS LEU ARG TRP VAL PRO LYS GLU
SEQRES  18 D  491  GLY VAL HIS ASN LEU SER ALA ASP GLU ALA THR GLU VAL
SEQRES  19 D  491  GLN GLY LYS ASP PHE ASN HIS ALA SER ASN ASP THR PHE
SEQRES  20 D  491  GLN ALA ILE GLU ASN GLY ASP PHE PRO GLU TRP ASP LEU
SEQRES  21 D  491  PHE VAL GLN VAL LEU ASP PRO ALA ASP VAL GLU ASN PHE
SEQRES  22 D  491  ASP PHE ASP PRO LEU ASP ALA THR LYS ASP TRP PHE GLU
SEQRES  23 D  491  ASP VAL ILE PRO PHE GLN HIS VAL GLY THR MET THR LEU
SEQRES  24 D  491  ASN LYS ASN VAL ASP ASN TYR PHE ALA GLU THR GLU SER
SEQRES  25 D  491  VAL GLY PHE ASN PRO GLY VAL LEU VAL PRO GLY MET LEU
SEQRES  26 D  491  PRO SER GLU ASP LYS LEU LEU GLN GLY ARG LEU PHE SER
SEQRES  27 D  491  TYR SER ASP THR GLN ARG HIS ARG ILE GLY PRO ASN TYR
SEQRES  28 D  491  GLN GLN LEU PRO ILE ASN CYS PRO PHE ALA GLN VAL ASN
SEQRES  29 D  491  ASN TYR GLN ARG ASP GLY ALA MET PRO PHE LYS GLN GLN
SEQRES  30 D  491  THR SER SER VAL ASN TYR GLU PRO ASN ARG TYR GLN ASP
SEQRES  31 D  491  GLU PRO LYS GLN THR PRO GLU TYR THR GLU ASP THR GLN
SEQRES  32 D  491  PRO LEU HIS ASP ASP ILE HIS GLY ARG LEU GLU ILE GLU
SEQRES  33 D  491  LYS THR ASN ASN PHE GLY GLN ALA GLY GLU VAL TYR ARG
SEQRES  34 D  491  ARG MET THR GLU GLU GLU GLN MET ALA LEU LEU ASN ASN
SEQRES  35 D  491  LEU VAL ASN ASP LEU GLN GLN VAL ARG HIS GLU ASN THR
SEQRES  36 D  491  VAL LEU LEU ALA ILE CYS ASN PHE TYR ARG ALA ASP ALA
SEQRES  37 D  491  SER LEU GLY GLU LYS LEU SER GLU ALA LEU ASN VAL ASP
SEQRES  38 D  491  ILE LYS PRO PHE LEU GLN GLN MET GLN LYS
HET    HEM  A 501      43
HET    HEM  B 501      43
HET    HEM  C 501      43
HET    HEM  D 501      43
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN     HEM [DIHYDROGEN 3,7,12,17-TETRAMETHYL-8,13-
HETSYN   2 HEM  DIVINYL-2,18-PORPHINEDIPROPIONATO(2-)]IRON
FORMUL   5  HEM    4(C34 H32 FE N4 O4)
FORMUL   9  HOH   *536(H2 O1)
HELIX    1   1 ASP A   35  ASP A   46  1                                  12
HELIX    2   2 ALA A   78  GLN A   82  5                                   5
HELIX    3   3 ASP A  138  MET A  140  5                                   3
HELIX    4   4 LYS A  141  LYS A  150  1                                  10
HELIX    5   5 ASP A  159  ARG A  170  1                                  12
HELIX    6   6 SER A  173  PHE A  181  1                                   9
HELIX    7   7 THR A  182  ILE A  186  5                                   5
HELIX    8   8 SER A  189  MET A  193  5                                   5
HELIX    9   9 SER A  227  ASP A  238  1                                  12
HELIX   10  10 ASN A  240  ASN A  252  1                                  13
HELIX   11  11 ASP A  266  PHE A  273  5                                   8
HELIX   12  12 TYR A  306  SER A  312  0                                   7
HELIX   13  13 ASP A  329  ILE A  347  1                                  19
HELIX   14  14 ASN A  350  LEU A  354  5                                   5
HELIX   15  15 THR A  395  THR A  399  5                                   5
HELIX   16  16 PHE A  421  MET A  431  1                                  11
HELIX   17  17 THR A  432  GLN A  448  1                                  17
HELIX   18  18 HIS A  452  ASP A  467  1                                  16
HELIX   19  19 ASP A  467  LEU A  478  1                                  12
HELIX   20  20 ASP B   35  ASP B   46  1                                  12
HELIX   21  21 ALA B   78  GLN B   82  5                                   5
HELIX   22  22 ASP B  138  MET B  140  5                                   3
HELIX   23  23 LYS B  141  LYS B  150  1                                  10
HELIX   24  24 ASP B  159  ARG B  170  1                                  12
HELIX   25  25 SER B  173  PHE B  181  1                                   9
HELIX   26  26 THR B  182  ILE B  186  5                                   5
HELIX   27  27 SER B  189  MET B  193  5                                   5
HELIX   28  28 SER B  227  ASP B  238  1                                  12
HELIX   29  29 ASN B  240  ASN B  252  1                                  13
HELIX   30  30 ASP B  266  PHE B  273  5                                   8
HELIX   31  31 TYR B  306  SER B  312  0                                   7
HELIX   32  32 ASP B  329  ILE B  347  1                                  19
HELIX   33  33 ASN B  350  LEU B  354  5                                   5
HELIX   34  34 THR B  395  THR B  399  5                                   5
HELIX   35  35 PHE B  421  MET B  431  1                                  11
HELIX   36  36 THR B  432  GLN B  448  1                                  17
HELIX   37  37 HIS B  452  ASP B  467  1                                  16
HELIX   38  38 ASP B  467  ASN B  479  1                                  13
HELIX   39  39 ASP C   35  ASP C   46  1                                  12
HELIX   40  40 ALA C   78  GLN C   82  5                                   5
HELIX   41  41 ASP C  138  MET C  140  5                                   3
HELIX   42  42 LYS C  141  LYS C  150  1                                  10
HELIX   43  43 ASP C  159  ARG C  170  1                                  12
HELIX   44  44 SER C  173  PHE C  181  1                                   9
HELIX   45  45 THR C  182  ILE C  186  5                                   5
HELIX   46  46 SER C  189  MET C  193  5                                   5
HELIX   47  47 SER C  227  ASP C  238  1                                  12
HELIX   48  48 ASN C  240  ASN C  252  1                                  13
HELIX   49  49 ASP C  266  VAL C  270  5                                   5
HELIX   50  50 ASN C  305  THR C  310  1                                   6
HELIX   51  51 ASP C  329  ILE C  347  1                                  19
HELIX   52  52 ASN C  350  LEU C  354  5                                   5
HELIX   53  53 THR C  395  THR C  399  5                                   5
HELIX   54  54 PHE C  421  MET C  431  1                                  11
HELIX   55  55 THR C  432  GLN C  448  1                                  17
HELIX   56  56 HIS C  452  ASP C  467  1                                  16
HELIX   57  57 ASP C  467  ASN C  479  1                                  13
HELIX   58  58 ASP D   35  ASP D   46  1                                  12
HELIX   59  59 ALA D   78  GLN D   82  5                                   5
HELIX   60  60 ASP D  138  MET D  140  5                                   3
HELIX   61  61 LYS D  141  LYS D  150  1                                  10
HELIX   62  62 ASP D  159  ARG D  170  1                                  12
HELIX   63  63 SER D  173  PHE D  181  1                                   9
HELIX   64  64 THR D  182  ILE D  186  5                                   5
HELIX   65  65 SER D  189  MET D  193  5                                   5
HELIX   66  66 SER D  227  ASP D  238  1                                  12
HELIX   67  67 ASN D  240  ASN D  252  1                                  13
HELIX   68  68 ASP D  266  VAL D  270  5                                   5
HELIX   69  69 ASN D  305  THR D  310  1                                   6
HELIX   70  70 LEU D  331  ILE D  347  1                                  17
HELIX   71  71 ASN D  350  LEU D  354  5                                   5
HELIX   72  72 THR D  395  THR D  399  5                                   5
HELIX   73  73 PHE D  421  MET D  431  1                                  11
HELIX   74  74 THR D  432  GLN D  448  1                                  17
HELIX   75  75 HIS D  452  ASP D  467  1                                  16
HELIX   76  76 ASP D  467  ASN D  479  1                                  13
SHEET    1  AA 3 ARG A  23  THR A  24  0
SHEET    2  AA 3 ILE B 409  ARG B 412 -1  O  GLY B 411   N  THR A  24
SHEET    3  AA 3 GLN C 403  PRO C 404 -1  O  GLN C 403   N  HIS B 410
SHEET    1  AB11 GLY A  59  VAL A  68  0
SHEET    2  AB11 GLU A  87  SER A  95 -1  O  VAL A  88   N  PHE A  66
SHEET    3  AB11 GLY A 112  THR A 119 -1  O  GLY A 112   N  SER A  95
SHEET    4  AB11 GLY A 122  ASN A 129 -1  O  GLY A 122   N  THR A 119
SHEET    5  AB11 GLY A 195  SER A 196 -1  O  SER A 196   N  ASN A 129
SHEET    6  AB11 THR A 210  PRO A 219 -1  O  TRP A 217   N  GLY A 195
SHEET    7  AB11 GLU A 257  LEU A 265 -1  O  ASP A 259   N  VAL A 218
SHEET    8  AB11 GLN A 292  ASN A 302 -1  O  GLN A 292   N  VAL A 262
SHEET    9  AB11 GLY A  59  VAL A  68 -1  O  HIS A  63   N  LYS A 301
SHEET   10  AB11 GLU A  87  SER A  95 -1  O  VAL A  88   N  PHE A  66
SHEET   11  AB11 GLY A  59  VAL A  68 -1  O  PHE A  60   N  PHE A  94
SHEET    1  AC 3 GLN A 403  PRO A 404  0
SHEET    2  AC 3 ILE D 409  ARG D 412 -1  O  HIS D 410   N  GLN A 403
SHEET    3  AC 3 ARG C  23  THR C  24 -1  N  THR C  24   O  GLY D 411
SHEET    1  BA 3 ARG B  23  THR B  24  0
SHEET    2  BA 3 ILE A 409  ARG A 412 -1  O  GLY A 411   N  THR B  24
SHEET    3  BA 3 GLN D 403  PRO D 404 -1  O  GLN D 403   N  HIS A 410
SHEET    1  BB11 GLY B  59  VAL B  68  0
SHEET    2  BB11 GLU B  87  SER B  95 -1  O  VAL B  88   N  PHE B  66
SHEET    3  BB11 GLY B 112  THR B 119 -1  O  GLY B 112   N  SER B  95
SHEET    4  BB11 GLY B 122  ASN B 129 -1  O  GLY B 122   N  THR B 119
SHEET    5  BB11 GLY B 195  SER B 196 -1  O  SER B 196   N  ASN B 129
SHEET    6  BB11 THR B 210  PRO B 219 -1  O  TRP B 217   N  GLY B 195
SHEET    7  BB11 GLU B 257  LEU B 265 -1  O  ASP B 259   N  VAL B 218
SHEET    8  BB11 GLN B 292  ASN B 302 -1  O  GLN B 292   N  VAL B 262
SHEET    9  BB11 GLY B  59  VAL B  68 -1  O  HIS B  63   N  LYS B 301
SHEET   10  BB11 GLU B  87  SER B  95 -1  O  VAL B  88   N  PHE B  66
SHEET   11  BB11 GLY B  59  VAL B  68 -1  O  PHE B  60   N  PHE B  94
SHEET    1  BC 3 GLN B 403  PRO B 404  0
SHEET    2  BC 3 ILE C 409  ARG C 412 -1  O  HIS C 410   N  GLN B 403
SHEET    3  BC 3 ARG D  23  THR D  24 -1  O  THR D  24   N  GLY C 411
SHEET    1  CA22 GLY C  59  VAL C  68  0
SHEET    2  CA22 GLU C  87  SER C  95 -1  O  VAL C  88   N  PHE C  66
SHEET    3  CA22 GLY C 112  THR C 119 -1  O  GLY C 112   N  SER C  95
SHEET    4  CA22 GLY C 122  ASN C 129 -1  O  GLY C 122   N  THR C 119
SHEET    5  CA22 GLU C  87  SER C  95
SHEET    6  CA22 GLY C  59  VAL C  68 -1  O  PHE C  60   N  PHE C  94
SHEET    7  CA22 GLY C 112  THR C 119
SHEET    8  CA22 GLU C  87  SER C  95 -1  O  PRO C  89   N  TYR C 118
SHEET    9  CA22 GLY C 122  ASN C 129
SHEET   10  CA22 GLY C 112  THR C 119 -1  O  PHE C 113   N  GLY C 128
SHEET   11  CA22 GLY C 195  SER C 196
SHEET   12  CA22 GLY C 122  ASN C 129 -1  O  ASN C 129   N  SER C 196
SHEET   13  CA22 PHE C 201  VAL C 204
SHEET   14  CA22 THR C 210  PRO C 219 -1  O  VAL C 211   N  TRP C 203
SHEET   15  CA22 THR C 210  PRO C 219
SHEET   16  CA22 GLY C 195  SER C 196 -1  O  GLY C 195   N  TRP C 217
SHEET   17  CA22 GLU C 257  LEU C 265
SHEET   18  CA22 THR C 210  PRO C 219 -1  O  TYR C 212   N  LEU C 265
SHEET   19  CA22 GLN C 292  ASN C 302
SHEET   20  CA22 GLY C  59  VAL C  68 -1  O  HIS C  63   N  LYS C 301
SHEET   21  CA22 MET C 324  PRO C 326
SHEET   22  CA22 PHE C 201  VAL C 204 -1  O  LYS C 202   N  LEU C 325
SHEET    1  DA20 GLY D  59  VAL D  68  0
SHEET    2  DA20 GLU D  87  SER D  95 -1  O  VAL D  88   N  PHE D  66
SHEET    3  DA20 GLU D  87  SER D  95
SHEET    4  DA20 GLY D  59  VAL D  68 -1  O  PHE D  60   N  PHE D  94
SHEET    5  DA20 GLY D 112  THR D 119
SHEET    6  DA20 GLU D  87  SER D  95 -1  O  PRO D  89   N  TYR D 118
SHEET    7  DA20 GLY D 122  ASN D 129
SHEET    8  DA20 GLY D 112  THR D 119 -1  O  PHE D 113   N  GLY D 128
SHEET    9  DA20 GLY D 195  SER D 196
SHEET   10  DA20 GLY D 122  ASN D 129 -1  O  ASN D 129   N  SER D 196
SHEET   11  DA20 PHE D 201  VAL D 204
SHEET   12  DA20 THR D 210  PRO D 219 -1  O  VAL D 211   N  TRP D 203
SHEET   13  DA20 THR D 210  PRO D 219
SHEET   14  DA20 GLY D 195  SER D 196 -1  O  GLY D 195   N  TRP D 217
SHEET   15  DA20 GLU D 257  LEU D 265
SHEET   16  DA20 THR D 210  PRO D 219 -1  O  TYR D 212   N  LEU D 265
SHEET   17  DA20 PHE D 291  ASN D 302
SHEET   18  DA20 GLY D  59  VAL D  68 -1  O  HIS D  63   N  LYS D 301
SHEET   19  DA20 MET D 324  PRO D 326
SHEET   20  DA20 PHE D 201  VAL D 204 -1  O  LYS D 202   N  LEU D 325
LINK         OH  TYR A 339                FE   HEM A 501     1555   1555  1.89
LINK         OH  TYR B 339                FE   HEM B 501     1555   1555  1.93
LINK         OH  TYR C 339                FE   HEM C 501     1555   1555  1.91
LINK         OH  TYR D 339                FE   HEM D 501     1555   1555  1.77
CISPEP   1 GLU A  384    PRO A  385          0        -3.17
CISPEP   2 GLU B  384    PRO B  385          0         1.57
CISPEP   3 LEU B  478    ASN B  479          0       -14.24
CISPEP   4 GLU C  384    PRO C  385          0         7.59
CISPEP   5 LEU C  478    ASN C  479          0       -11.14
CISPEP   6 GLU D  384    PRO D  385          0         5.61
CISPEP   7 LEU D  478    ASN D  479          0         1.08
SITE     1 AC1 26 ARG A  53  VAL A  54  VAL A  55  HIS A  56
SITE     2 AC1 26 ARG A  93  GLY A 112  SER A 114  GLY A 128
SITE     3 AC1 26 ASN A 129  PHE A 134  PHE A 142  VAL A 198
SITE     4 AC1 26 HIS A 199  PHE A 315  LEU A 331  GLY A 334
SITE     5 AC1 26 ARG A 335  SER A 338  TYR A 339  THR A 342
SITE     6 AC1 26 GLN A 343  ARG A 346  HOH A2038  HOH A2161
SITE     7 AC1 26 HOH A2162  ASP B  46
SITE     1 AC2 27 ASP A  46  ARG B  53  VAL B  54  VAL B  55
SITE     2 AC2 27 HIS B  56  ARG B  93  GLY B 112  PHE B 113
SITE     3 AC2 27 SER B 114  GLY B 128  ASN B 129  PHE B 134
SITE     4 AC2 27 PHE B 142  VAL B 198  HIS B 199  PHE B 315
SITE     5 AC2 27 LEU B 331  GLY B 334  ARG B 335  SER B 338
SITE     6 AC2 27 TYR B 339  THR B 342  GLN B 343  ARG B 346
SITE     7 AC2 27 HOH B2153  HOH B2154  HOH B2155
SITE     1 AC3 26 ARG C  53  VAL C  54  VAL C  55  HIS C  56
SITE     2 AC3 26 ARG C  93  GLY C 112  PHE C 113  SER C 114
SITE     3 AC3 26 GLY C 128  ASN C 129  PHE C 134  PHE C 142
SITE     4 AC3 26 VAL C 198  HIS C 199  PHE C 315  LEU C 331
SITE     5 AC3 26 ARG C 335  SER C 338  TYR C 339  THR C 342
SITE     6 AC3 26 GLN C 343  ARG C 346  HOH C2031  HOH C2108
SITE     7 AC3 26 ILE D  42  ASP D  46
SITE     1 AC4 26 ASP C  46  ARG D  53  VAL D  54  VAL D  55
SITE     2 AC4 26 HIS D  56  ARG D  93  GLY D 112  SER D 114
SITE     3 AC4 26 GLY D 128  ASN D 129  PHE D 134  PHE D 142
SITE     4 AC4 26 VAL D 198  HIS D 199  PHE D 315  LEU D 331
SITE     5 AC4 26 GLY D 334  ARG D 335  SER D 338  TYR D 339
SITE     6 AC4 26 THR D 342  GLN D 343  ARG D 346  HOH D2066
SITE     7 AC4 26 HOH D2076  HOH D2111
CRYST1   94.267  131.935  110.642  90.00 107.61  90.00 P 1 21 1      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      0.010608  0.000000  0.003367        0.00000
SCALE2      0.000000  0.007579  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009483        0.00000
      
PROCHECK
Go to PROCHECK summary
 References