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PDBsum entry 1qwm

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1qwm
Jmol
Contents
Protein chains
490 a.a. *
Ligands
AZI
HEM-FMT
FMT ×35
HEM
Waters ×933
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          02-SEP-03   1QWM
TITLE     STRUCTURE OF HELICOBACTER PYLORI CATALASE WITH FORMIC ACID BOUND
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: KATA CATALASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 1.11.1.6;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE   3 ORGANISM_TAXID: 210;
SOURCE   4 GENE: KATA (HP0875);
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: UM255;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PSO100
KEYWDS    BETA BARREL, AZIDE COMPLEX, FORMATE COMPLEX, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.C.LOEWEN,X.CARPENA,R.PEREZ-LUQUE,C.ROVIRA,R.HAAS,S.ODENBREIT,
AUTHOR   2 P.NICHOLLS,I.FITA
REVDAT   3   13-JUL-11 1QWM    1       VERSN
REVDAT   2   24-FEB-09 1QWM    1       VERSN
REVDAT   1   30-MAR-04 1QWM    0
JRNL        AUTH   P.C.LOEWEN,X.CARPENA,C.ROVIRA,A.IVANCICH,R.PEREZ-LUQUE,
JRNL        AUTH 2 R.HAAS,S.OBENBREIT,P.NICHOLLS,I.FITA
JRNL        TITL   STRUCTURE OF HELICOBACTER PYLORI CATALASE, WITH AND WITHOUT
JRNL        TITL 2 FORMIC ACID BOUND, AT 1.6 A RESOLUTION
JRNL        REF    BIOCHEMISTRY                  V.  43  3089 2004
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15023060
JRNL        DOI    10.1021/BI035663I
REMARK   2
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
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) : 1.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.88
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 118512
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) : 0.196
REMARK   3   R VALUE            (WORKING SET) : 0.194
REMARK   3   FREE R VALUE                     : 0.227
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6282
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) : 1.60
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8128
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2140
REMARK   3   BIN FREE R VALUE SET COUNT          : 429
REMARK   3   BIN FREE R VALUE                    : 0.2650
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8040
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 197
REMARK   3   SOLVENT ATOMS            : 933
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.15
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.94000
REMARK   3    B22 (A**2) : -0.19000
REMARK   3    B33 (A**2) : -0.75000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.103
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.698
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.921
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8503 ; 0.017 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11480 ; 1.612 ; 1.960
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   980 ; 6.067 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1128 ; 0.118 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6641 ; 0.009 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4021 ; 0.213 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ; 0.150 ; 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):   369 ; 0.202 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):   126 ; 0.239 ; 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):  4976 ; 0.924 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7948 ; 1.453 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3527 ; 2.319 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3532 ; 3.540 ; 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 : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A     490      6
REMARK   3           1     B      1       B     490      6
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   1    A    (A):   4017 ;  0.21 ;  5.00
REMARK   3   LOOSE THERMAL      1    A (A**2):   4017 ;  1.41 ; 10.00
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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1QWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-SEP-03.
REMARK 100 THE RCSB ID CODE IS RCSB020156.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-SEP-02
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 5.6
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) : 0.9330
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118512
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.900
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04700
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.17900
REMARK 200   FOR SHELL         : NULL
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 1QWL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG MME 550, 0.1 M SODIUM CITRATE,
REMARK 280  10 MM ZNSO4, 3 MM NAN3, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       32.37800
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.48050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.37800
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       77.48050
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 62380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -266.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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       64.75600
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      154.96100
REMARK 350   BIOMT3   2  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     LYS A   491
REMARK 465     ASP A   492
REMARK 465     MET A   493
REMARK 465     HIS A   494
REMARK 465     GLY A   495
REMARK 465     LYS A   496
REMARK 465     ASP A   497
REMARK 465     MET A   498
REMARK 465     HIS A   499
REMARK 465     HIS A   500
REMARK 465     THR A   501
REMARK 465     LYS A   502
REMARK 465     LYS A   503
REMARK 465     LYS A   504
REMARK 465     LYS A   505
REMARK 465     LYS B   491
REMARK 465     ASP B   492
REMARK 465     MET B   493
REMARK 465     HIS B   494
REMARK 465     GLY B   495
REMARK 465     LYS B   496
REMARK 465     ASP B   497
REMARK 465     MET B   498
REMARK 465     HIS B   499
REMARK 465     HIS B   500
REMARK 465     THR B   501
REMARK 465     LYS B   502
REMARK 465     LYS B   503
REMARK 465     LYS B   504
REMARK 465     LYS B   505
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   O1   FMT A  1714     O    HOH A  2694              1.83
REMARK 500   O    HOH A  2935     O    HOH A  3018              1.84
REMARK 500   O    HOH A  2812     O    HOH A  3011              2.09
REMARK 500   OE1  GLU A    89     O    HOH A  2763              2.10
REMARK 500   O    ARG B   101     O2   FMT B  1720              2.13
REMARK 500   O    HOH B  2022     O    HOH B  2201              2.17
REMARK 500   OH   TYR A   371     O2   FMT A  1730              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NE2  GLN A   154     O    HOH A  2849     2665     1.45
REMARK 500   O    HOH A  2930     O    HOH B  2217     1554     1.91
REMARK 500   O2   FMT B  1721     O    HOH B  2177     2665     1.94
REMARK 500   O    HOH B  2009     O    HOH B  2128     2665     2.17
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  32   CA  -  CB  -  CG  ANGL. DEV. = -16.2 DEGREES
REMARK 500    ASP A 109   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 446   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP B  18   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP B 109   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP B 125   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG B 184   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP B 279   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP B 399   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 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
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    SER A  35       76.05    -69.69
REMARK 500    LYS A 150     -137.40   -104.78
REMARK 500    SER A 198      -63.32     68.86
REMARK 500    ASN A 300       10.19   -140.61
REMARK 500    PRO A 328       27.41    -78.48
REMARK 500    ASP A 369     -146.27     72.60
REMARK 500    LYS B 150     -143.13    -99.03
REMARK 500    SER B 198      -65.62     73.91
REMARK 500    ASN B 300       11.44   -144.17
REMARK 500    PRO B 328       25.71    -79.89
REMARK 500    ASP B 369     -147.21     74.37
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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    ARG A 101        20.6      L          L   OUTSIDE RANGE
REMARK 500    ARG B 101        20.5      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 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A2809        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A2875        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH B1945        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH B1956        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH B1976        DISTANCE =  6.60 ANGSTROMS
REMARK 525    HOH B2127        DISTANCE =  6.02 ANGSTROMS
REMARK 525    HOH B2131        DISTANCE =  5.72 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 550  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 339   OH
REMARK 620 2 HEM A 550   NA   98.4
REMARK 620 3 HEM A 550   NB   96.4  90.5
REMARK 620 4 HEM A 550   NC   88.9 172.5  87.5
REMARK 620 5 HEM A 550   ND   91.0  89.6 172.5  91.4
REMARK 620 6 FMT A1701   O2  162.7  96.9  91.4  75.9  81.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 550  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 339   OH
REMARK 620 2 HEM B 550   NA   99.2
REMARK 620 3 HEM B 550   NB   97.2  91.3
REMARK 620 4 HEM B 550   NC   89.6 171.2  86.6
REMARK 620 5 HEM B 550   ND   92.3  89.1 170.3  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 AZI A 2600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 550
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1708
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1714
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1715
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1716
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1717
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1718
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1719
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1720
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1721
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1722
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1723
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1724
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1725
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1726
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1727
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1728
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1729
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1730
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1731
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1732
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1733
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1734
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1735
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 1736
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QWL   RELATED DB: PDB
REMARK 900 STRUCTURE OF HELICOBACTER PYLORI CATALASE
DBREF  1QWM A    1   505  UNP    P77872   CATA_HELPY       1    505
DBREF  1QWM B    1   505  UNP    P77872   CATA_HELPY       1    505
SEQRES   1 A  505  MET VAL ASN LYS ASP VAL LYS GLN THR THR ALA PHE GLY
SEQRES   2 A  505  ALA PRO VAL TRP ASP ASP ASN ASN VAL ILE THR ALA GLY
SEQRES   3 A  505  PRO ARG GLY PRO VAL LEU LEU GLN SER THR TRP PHE LEU
SEQRES   4 A  505  GLU LYS LEU ALA ALA PHE ASP ARG GLU ARG ILE PRO GLU
SEQRES   5 A  505  ARG VAL VAL HIS ALA LYS GLY SER GLY ALA TYR GLY THR
SEQRES   6 A  505  PHE THR VAL THR LYS ASP ILE THR LYS TYR THR LYS ALA
SEQRES   7 A  505  LYS ILE PHE SER LYS VAL GLY LYS LYS THR GLU CYS PHE
SEQRES   8 A  505  PHE ARG PHE SER THR VAL ALA GLY GLU ARG GLY SER ALA
SEQRES   9 A  505  ASP ALA VAL ARG ASP PRO ARG GLY PHE ALA MET LYS TYR
SEQRES  10 A  505  TYR THR GLU GLU GLY ASN TRP ASP LEU VAL GLY ASN ASN
SEQRES  11 A  505  THR PRO VAL PHE PHE ILE ARG ASP ALA ILE LYS PHE PRO
SEQRES  12 A  505  ASP PHE ILE HIS THR GLN LYS ARG ASP PRO GLN THR ASN
SEQRES  13 A  505  LEU PRO ASN HIS ASP MET VAL TRP ASP PHE TRP SER ASN
SEQRES  14 A  505  VAL PRO GLU SER LEU TYR GLN VAL THR TRP VAL MET SER
SEQRES  15 A  505  ASP ARG GLY ILE PRO LYS SER PHE ARG HIS MET ASP GLY
SEQRES  16 A  505  PHE GLY SER HIS THR PHE SER LEU ILE ASN ALA LYS GLY
SEQRES  17 A  505  GLU ARG PHE TRP VAL LYS PHE HIS PHE HIS THR MET GLN
SEQRES  18 A  505  GLY VAL LYS HIS LEU THR ASN GLU GLU ALA ALA GLU ILE
SEQRES  19 A  505  ARG LYS HIS ASP PRO ASP SER ASN GLN ARG ASP LEU PHE
SEQRES  20 A  505  ASP ALA ILE ALA ARG GLY ASP TYR PRO LYS TRP LYS LEU
SEQRES  21 A  505  SER ILE GLN VAL MET PRO GLU GLU ASP ALA LYS LYS TYR
SEQRES  22 A  505  ARG PHE HIS PRO PHE ASP VAL THR LYS ILE TRP TYR THR
SEQRES  23 A  505  GLN ASP TYR PRO LEU MET GLU VAL GLY ILE VAL GLU LEU
SEQRES  24 A  505  ASN LYS ASN PRO GLU ASN TYR PHE ALA GLU VAL GLU GLN
SEQRES  25 A  505  ALA ALA PHE THR PRO ALA ASN VAL VAL PRO GLY ILE GLY
SEQRES  26 A  505  TYR SER PRO ASP ARG MET LEU GLN GLY ARG LEU PHE SER
SEQRES  27 A  505  TYR GLY ASP THR HIS ARG TYR ARG LEU GLY VAL ASN TYR
SEQRES  28 A  505  PRO GLN ILE PRO VAL ASN LYS PRO ARG CYS PRO PHE HIS
SEQRES  29 A  505  SER SER SER ARG ASP GLY TYR MET GLN ASN GLY TYR TYR
SEQRES  30 A  505  GLY SER LEU GLN ASN TYR THR PRO SER SER LEU PRO GLY
SEQRES  31 A  505  TYR LYS GLU ASP LYS SER ALA ARG ASP PRO LYS PHE ASN
SEQRES  32 A  505  LEU ALA HIS ILE GLU LYS GLU PHE GLU VAL TRP ASN TRP
SEQRES  33 A  505  ASP TYR ARG ALA ASP ASP SER ASP TYR TYR THR GLN PRO
SEQRES  34 A  505  GLY ASP TYR TYR ARG SER LEU PRO ALA ASP GLU LYS GLU
SEQRES  35 A  505  ARG LEU HIS ASP THR ILE GLY GLU SER LEU ALA HIS VAL
SEQRES  36 A  505  THR HIS LYS GLU ILE VAL ASP LYS GLN LEU GLU HIS PHE
SEQRES  37 A  505  LYS LYS ALA ASP PRO LYS TYR ALA GLU GLY VAL LYS LYS
SEQRES  38 A  505  ALA LEU GLU LYS HIS GLN LYS MET MET LYS ASP MET HIS
SEQRES  39 A  505  GLY LYS ASP MET HIS HIS THR LYS LYS LYS LYS
SEQRES   1 B  505  MET VAL ASN LYS ASP VAL LYS GLN THR THR ALA PHE GLY
SEQRES   2 B  505  ALA PRO VAL TRP ASP ASP ASN ASN VAL ILE THR ALA GLY
SEQRES   3 B  505  PRO ARG GLY PRO VAL LEU LEU GLN SER THR TRP PHE LEU
SEQRES   4 B  505  GLU LYS LEU ALA ALA PHE ASP ARG GLU ARG ILE PRO GLU
SEQRES   5 B  505  ARG VAL VAL HIS ALA LYS GLY SER GLY ALA TYR GLY THR
SEQRES   6 B  505  PHE THR VAL THR LYS ASP ILE THR LYS TYR THR LYS ALA
SEQRES   7 B  505  LYS ILE PHE SER LYS VAL GLY LYS LYS THR GLU CYS PHE
SEQRES   8 B  505  PHE ARG PHE SER THR VAL ALA GLY GLU ARG GLY SER ALA
SEQRES   9 B  505  ASP ALA VAL ARG ASP PRO ARG GLY PHE ALA MET LYS TYR
SEQRES  10 B  505  TYR THR GLU GLU GLY ASN TRP ASP LEU VAL GLY ASN ASN
SEQRES  11 B  505  THR PRO VAL PHE PHE ILE ARG ASP ALA ILE LYS PHE PRO
SEQRES  12 B  505  ASP PHE ILE HIS THR GLN LYS ARG ASP PRO GLN THR ASN
SEQRES  13 B  505  LEU PRO ASN HIS ASP MET VAL TRP ASP PHE TRP SER ASN
SEQRES  14 B  505  VAL PRO GLU SER LEU TYR GLN VAL THR TRP VAL MET SER
SEQRES  15 B  505  ASP ARG GLY ILE PRO LYS SER PHE ARG HIS MET ASP GLY
SEQRES  16 B  505  PHE GLY SER HIS THR PHE SER LEU ILE ASN ALA LYS GLY
SEQRES  17 B  505  GLU ARG PHE TRP VAL LYS PHE HIS PHE HIS THR MET GLN
SEQRES  18 B  505  GLY VAL LYS HIS LEU THR ASN GLU GLU ALA ALA GLU ILE
SEQRES  19 B  505  ARG LYS HIS ASP PRO ASP SER ASN GLN ARG ASP LEU PHE
SEQRES  20 B  505  ASP ALA ILE ALA ARG GLY ASP TYR PRO LYS TRP LYS LEU
SEQRES  21 B  505  SER ILE GLN VAL MET PRO GLU GLU ASP ALA LYS LYS TYR
SEQRES  22 B  505  ARG PHE HIS PRO PHE ASP VAL THR LYS ILE TRP TYR THR
SEQRES  23 B  505  GLN ASP TYR PRO LEU MET GLU VAL GLY ILE VAL GLU LEU
SEQRES  24 B  505  ASN LYS ASN PRO GLU ASN TYR PHE ALA GLU VAL GLU GLN
SEQRES  25 B  505  ALA ALA PHE THR PRO ALA ASN VAL VAL PRO GLY ILE GLY
SEQRES  26 B  505  TYR SER PRO ASP ARG MET LEU GLN GLY ARG LEU PHE SER
SEQRES  27 B  505  TYR GLY ASP THR HIS ARG TYR ARG LEU GLY VAL ASN TYR
SEQRES  28 B  505  PRO GLN ILE PRO VAL ASN LYS PRO ARG CYS PRO PHE HIS
SEQRES  29 B  505  SER SER SER ARG ASP GLY TYR MET GLN ASN GLY TYR TYR
SEQRES  30 B  505  GLY SER LEU GLN ASN TYR THR PRO SER SER LEU PRO GLY
SEQRES  31 B  505  TYR LYS GLU ASP LYS SER ALA ARG ASP PRO LYS PHE ASN
SEQRES  32 B  505  LEU ALA HIS ILE GLU LYS GLU PHE GLU VAL TRP ASN TRP
SEQRES  33 B  505  ASP TYR ARG ALA ASP ASP SER ASP TYR TYR THR GLN PRO
SEQRES  34 B  505  GLY ASP TYR TYR ARG SER LEU PRO ALA ASP GLU LYS GLU
SEQRES  35 B  505  ARG LEU HIS ASP THR ILE GLY GLU SER LEU ALA HIS VAL
SEQRES  36 B  505  THR HIS LYS GLU ILE VAL ASP LYS GLN LEU GLU HIS PHE
SEQRES  37 B  505  LYS LYS ALA ASP PRO LYS TYR ALA GLU GLY VAL LYS LYS
SEQRES  38 B  505  ALA LEU GLU LYS HIS GLN LYS MET MET LYS ASP MET HIS
SEQRES  39 B  505  GLY LYS ASP MET HIS HIS THR LYS LYS LYS LYS
HET    AZI  A2600       3
HET    HEM  A 550      43
HET    HEM  B 550      43
HET    FMT  A1701       3
HET    FMT  B1702       3
HET    FMT  B1703       3
HET    FMT  A1704       3
HET    FMT  B1705       3
HET    FMT  A1706       3
HET    FMT  B1707       3
HET    FMT  B1708       3
HET    FMT  A1709       3
HET    FMT  A1710       3
HET    FMT  A1711       3
HET    FMT  B1712       3
HET    FMT  A1713       3
HET    FMT  A1714       3
HET    FMT  A1715       3
HET    FMT  A1716       3
HET    FMT  B1717       3
HET    FMT  A1718       3
HET    FMT  A1719       3
HET    FMT  B1720       3
HET    FMT  B1721       3
HET    FMT  A1722       3
HET    FMT  A1723       3
HET    FMT  A1724       3
HET    FMT  A1725       3
HET    FMT  B1726       3
HET    FMT  B1727       3
HET    FMT  B1728       3
HET    FMT  B1729       3
HET    FMT  A1730       3
HET    FMT  B1731       3
HET    FMT  A1732       3
HET    FMT  A1733       3
HET    FMT  A1734       3
HET    FMT  A1735       3
HET    FMT  B1736       3
HETNAM     AZI AZIDE ION
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     FMT FORMIC ACID
HETSYN     HEM HEME
FORMUL   3  AZI    N3 1-
FORMUL   4  HEM    2(C34 H32 FE N4 O4)
FORMUL   6  FMT    36(C H2 O2)
FORMUL  42  HOH   *933(H2 O)
HELIX    1   1 SER A   35  ASP A   46  1                                  12
HELIX    2   2 ALA A   78  SER A   82  5                                   5
HELIX    3   3 ASP A  138  ILE A  140  5                                   3
HELIX    4   4 LYS A  141  LYS A  150  1                                  10
HELIX    5   5 ASN A  159  VAL A  170  1                                  12
HELIX    6   6 SER A  173  SER A  182  1                                  10
HELIX    7   7 ASP A  183  ILE A  186  5                                   4
HELIX    8   8 SER A  189  MET A  193  5                                   5
HELIX    9   9 THR A  227  ASP A  238  1                                  12
HELIX   10  10 ASP A  240  ARG A  252  1                                  13
HELIX   11  11 GLU A  268  ALA A  270  5                                   3
HELIX   12  12 ASN A  305  VAL A  310  1                                   6
HELIX   13  13 ASP A  329  GLY A  348  1                                  20
HELIX   14  14 ASN A  350  LYS A  358  5                                   9
HELIX   15  15 ASP A  394  ARG A  398  5                                   5
HELIX   16  16 ASN A  403  ILE A  407  5                                   5
HELIX   17  17 ASP A  417  ASP A  422  1                                   6
HELIX   18  18 TYR A  426  LEU A  436  1                                  11
HELIX   19  19 PRO A  437  ALA A  453  1                                  17
HELIX   20  20 HIS A  457  ASP A  472  1                                  16
HELIX   21  21 ASP A  472  MET A  490  1                                  19
HELIX   22  22 SER B   35  ASP B   46  1                                  12
HELIX   23  23 ALA B   78  SER B   82  5                                   5
HELIX   24  24 ASP B  138  ILE B  140  5                                   3
HELIX   25  25 LYS B  141  LYS B  150  1                                  10
HELIX   26  26 ASN B  159  VAL B  170  1                                  12
HELIX   27  27 SER B  173  SER B  182  1                                  10
HELIX   28  28 ASP B  183  ILE B  186  5                                   4
HELIX   29  29 SER B  189  MET B  193  5                                   5
HELIX   30  30 THR B  227  ASP B  238  1                                  12
HELIX   31  31 ASP B  240  ARG B  252  1                                  13
HELIX   32  32 GLU B  268  ALA B  270  5                                   3
HELIX   33  33 ASN B  305  VAL B  310  1                                   6
HELIX   34  34 ASP B  329  GLY B  348  1                                  20
HELIX   35  35 ASN B  350  LYS B  358  5                                   9
HELIX   36  36 ASP B  394  ARG B  398  5                                   5
HELIX   37  37 ASN B  403  ILE B  407  5                                   5
HELIX   38  38 ASP B  417  ASP B  422  1                                   6
HELIX   39  39 TYR B  426  LEU B  436  1                                  11
HELIX   40  40 PRO B  437  ALA B  453  1                                  17
HELIX   41  41 HIS B  457  ASP B  472  1                                  16
HELIX   42  42 ASP B  472  MET B  490  1                                  19
SHEET    1   A11 ILE A 324  GLY A 325  0
SHEET    2   A11 PHE A 201  ILE A 204 -1  N  SER A 202   O  GLY A 325
SHEET    3   A11 ARG A 210  THR A 219 -1  O  PHE A 211   N  LEU A 203
SHEET    4   A11 LYS A 257  PRO A 266 -1  O  MET A 265   N  TRP A 212
SHEET    5   A11 MET A 292  LYS A 301 -1  O  VAL A 294   N  LEU A 260
SHEET    6   A11 GLY A  59  VAL A  68 -1  N  THR A  67   O  ILE A 296
SHEET    7   A11 LYS A  87  SER A  95 -1  O  PHE A  92   N  ALA A  62
SHEET    8   A11 GLY A 112  THR A 119 -1  O  ALA A 114   N  ARG A  93
SHEET    9   A11 GLY A 122  ASN A 129 -1  O  GLY A 128   N  PHE A 113
SHEET   10   A11 GLY A 195  PHE A 196 -1  O  PHE A 196   N  ASN A 129
SHEET   11   A11 ARG A 210  THR A 219 -1  O  PHE A 217   N  GLY A 195
SHEET    1   B11 ILE B 324  GLY B 325  0
SHEET    2   B11 PHE B 201  ILE B 204 -1  N  SER B 202   O  GLY B 325
SHEET    3   B11 ARG B 210  THR B 219 -1  O  PHE B 211   N  LEU B 203
SHEET    4   B11 LYS B 257  PRO B 266 -1  O  MET B 265   N  TRP B 212
SHEET    5   B11 MET B 292  LYS B 301 -1  O  VAL B 294   N  LEU B 260
SHEET    6   B11 GLY B  59  VAL B  68 -1  N  TYR B  63   O  LYS B 301
SHEET    7   B11 LYS B  87  SER B  95 -1  O  PHE B  94   N  SER B  60
SHEET    8   B11 GLY B 112  THR B 119 -1  O  ALA B 114   N  ARG B  93
SHEET    9   B11 GLY B 122  ASN B 129 -1  O  TRP B 124   N  TYR B 117
SHEET   10   B11 GLY B 195  PHE B 196 -1  O  PHE B 196   N  ASN B 129
SHEET   11   B11 ARG B 210  THR B 219 -1  O  PHE B 217   N  GLY B 195
LINK         OH  TYR A 339                FE   HEM A 550     1555   1555  1.87
LINK         OH  TYR B 339                FE   HEM B 550     1555   1555  1.93
LINK         O  BARG A 101                 O2  FMT A1710     1555   1555  1.96
LINK        FE   HEM A 550                 O2  FMT A1701     1555   1555  2.64
LINK         O1  FMT A1735                 N1  AZI A2600     1555   1555  1.73
CISPEP   1 THR A  384    PRO A  385          0        -8.72
CISPEP   2 THR B  384    PRO B  385          0        -3.10
SITE     1 AC1  6 ARG A  47  ARG A 344  FMT A1713  FMT A1735
SITE     2 AC1  6 ARG B  47  TYR B 345
SITE     1 AC2 27 ASP A  46  ARG A  53  VAL A  54  VAL A  55
SITE     2 AC2 27 HIS A  56  ARG A  93  GLY A 112  VAL A 127
SITE     3 AC2 27 GLY A 128  ASN A 129  ALA A 139  PHE A 142
SITE     4 AC2 27 GLY A 197  SER A 198  HIS A 199  PHE A 315
SITE     5 AC2 27 MET A 331  ARG A 335  SER A 338  TYR A 339
SITE     6 AC2 27 THR A 342  HIS A 343  ARG A 346  FMT A1701
SITE     7 AC2 27 HOH A2606  HOH A2629  HOH A2668
SITE     1 AC3 28 ASP B  46  ARG B  53  VAL B  54  VAL B  55
SITE     2 AC3 28 HIS B  56  ARG B  93  GLY B 112  PHE B 113
SITE     3 AC3 28 ALA B 114  VAL B 127  GLY B 128  ASN B 129
SITE     4 AC3 28 ALA B 139  PHE B 142  GLY B 197  SER B 198
SITE     5 AC3 28 PHE B 315  MET B 331  ARG B 335  SER B 338
SITE     6 AC3 28 TYR B 339  THR B 342  HIS B 343  ARG B 346
SITE     7 AC3 28 FMT B1702  HOH B1739  HOH B1745  HOH B1792
SITE     1 AC4  5 HIS A  56  ASN A 129  PHE A 134  PHE A 142
SITE     2 AC4  5 HEM A 550
SITE     1 AC5  5 HIS B  56  VAL B  97  ASN B 129  PHE B 134
SITE     2 AC5  5 HEM B 550
SITE     1 AC6  6 ARG B 108  ASP B 109  PRO B 110  PHE B 135
SITE     2 AC6  6 GLN B 149  VAL B 180
SITE     1 AC7  5 GLN A 149  VAL A 163  TRP A 167  MET A 181
SITE     2 AC7  5 HOH A3041
SITE     1 AC8  7 GLN B 149  PRO B 158  VAL B 163  FMT B1707
SITE     2 AC8  7 HOH B1827  HOH B2015  HOH B2224
SITE     1 AC9  4 PRO A 158  HIS A 160  HOH A2784  HOH A2855
SITE     1 BC1  3 FMT B1705  HOH B1977  HOH B2112
SITE     1 BC2  6 HIS B 160  GLU B 450  SER B 451  HIS B 454
SITE     2 BC2  6 HOH B1817  HOH B1986
SITE     1 BC3  6 ASP A 183  ARG A 184  VAL A 223  GLU A 440
SITE     2 BC3  6 HOH A2717  HOH A2732
SITE     1 BC4  8 LYS A  58  ARG A 101  GLY A 102  ARG A 151
SITE     2 BC4  8 ASN A 156  FMT A1734  HOH A2845  HOH A2890
SITE     1 BC5  5 LYS A 150  ARG A 151  HOH A2607  HOH A2652
SITE     2 BC5  5 HOH A3040
SITE     1 BC6  8 ALA B  57  LYS B  58  GLY B  59  ARG B 101
SITE     2 BC6  8 TYR B 306  GLU B 311  FMT B1720  HOH B2207
SITE     1 BC7  5 ARG A  47  TYR A 345  AZI A2600  HOH A2654
SITE     2 BC7  5 ARG B 344
SITE     1 BC8  5 ASN A 130  TRP A 179  ARG A 184  ASP A 194
SITE     2 BC8  5 HOH A2694
SITE     1 BC9  2 TYR A 371  TYR B 371
SITE     1 CC1  7 PRO A 352  GLN A 353  PRO A 359  PHE A 363
SITE     2 CC1  7 HOH A2791  HOH A2860  ALA B  11
SITE     1 CC2  3 TYR B 285  THR B 286  HOH B2133
SITE     1 CC3  4 PHE A 247  ALA A 251  ASN A 302  HOH A2725
SITE     1 CC4  5 LYS A  77  GLY A 323  SER A 396  ALA A 397
SITE     2 CC4  5 ARG A 398
SITE     1 CC5  8 LYS B  58  ARG B 101  GLY B 102  ARG B 151
SITE     2 CC5  8 ASN B 156  FMT B1712  HOH B2050  HOH B2207
SITE     1 CC6  8 HOH A2634  ARG B  49  ARG B 101  HOH B1801
SITE     2 CC6  8 HOH B1916  HOH B2050  HOH B2085  HOH B2177
SITE     1 CC7  4 ASP A 194  HIS A 218  THR A 219  HOH A2928
SITE     1 CC8  4 VAL A 223  LYS A 224  HOH A2688  HOH A2978
SITE     1 CC9  3 LYS A 188  HOH A2688  HOH A2925
SITE     1 DC1  4 LYS A 188  LEU A 226  HOH A2925  HOH A2956
SITE     1 DC2  3 VAL B 223  LYS B 224  HOH B1830
SITE     1 DC3  3 ASP B 183  HIS B 225  GLU B 440
SITE     1 DC4  4 LYS B 188  LYS B 224  HOH B1830  HOH B2143
SITE     1 DC5  9 SER B 182  ASP B 183  ARG B 184  TYR B 432
SITE     2 DC5  9 LEU B 436  GLU B 440  HOH B1897  HOH B2000
SITE     3 DC5  9 HOH B2225
SITE     1 DC6  4 TYR A 371  FMT A1735  PRO B  51  TYR B 345
SITE     1 DC7  5 LEU B 336  PHE B 337  ASP B 341  ARG B 344
SITE     2 DC7  5 FMT B1736
SITE     1 DC8  4 LEU A 336  PHE A 337  ARG A 344  FMT A1733
SITE     1 DC9  9 ALA A 318  ARG A 344  FMT A1732  HOH A2787
SITE     2 DC9  9 THR B  36  LEU B  39  GLU B  40  HOH B1800
SITE     3 DC9  9 HOH B2160
SITE     1 EC1  8 ALA A  57  LYS A  58  GLY A  59  ARG A 101
SITE     2 EC1  8 TYR A 306  GLU A 311  FMT A1710  HOH A2845
SITE     1 EC2  7 ARG A 344  FMT A1730  AZI A2600  HOH A2727
SITE     2 EC2  7 HOH A2867  ARG B  47  TYR B 345
SITE     1 EC3  9 THR A  36  LEU A  39  GLU A  40  ALA B 318
SITE     2 EC3  9 ARG B 344  FMT B1731  HOH B1917  HOH B2011
SITE     3 EC3  9 HOH B2179
CRYST1   64.756  154.961   96.163  90.00  90.00  90.00 P 21 21 2     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      0.015443  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006453  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010399        0.00000
      
PROCHECK
Go to PROCHECK summary
 References