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PDBsum entry 1gge

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1gge
Jmol
Contents
Protein chains
727 a.a. *
Ligands
HDD ×4
Waters ×3208
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          16-AUG-00   1GGE
TITLE     CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI,
TITLE    2 NATIVE STRUCTURE AT 1.9 A RESOLUTION.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (CATALASE HPII);
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 1.11.1.6;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PAMKATE72
KEYWDS    BETA BARREL, ALPHA HELICAL DOMAIN, FLAVODOXIN LIKE DOMAIN,
KEYWDS   2 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.R.MELIK-ADAMYAN,J.BRAVO,X.CARPENA,J.SWITALA,M.J.MATE,
AUTHOR   2 I.FITA,P.C.LOEWEN
REVDAT   4   24-FEB-09 1GGE    1       VERSN
REVDAT   3   01-APR-03 1GGE    1       JRNL
REVDAT   2   22-AUG-01 1GGE    1       JRNL   REMARK
REVDAT   1   30-AUG-00 1GGE    0
JRNL        AUTH   W.MELIK-ADAMYAN,J.BRAVO,X.CARPENA,J.SWITALA,
JRNL        AUTH 2 M.J.MATE,I.FITA,P.C.LOEWEN
JRNL        TITL   SUBSTRATE FLOW IN CATALASES DEDUCED FROM THE
JRNL        TITL 2 CRYSTAL STRUCTURES OF ACTIVE SITE VARIANTS OF HPII
JRNL        TITL 3 FROM ESCHERICHIA COLI.
JRNL        REF    PROTEINS                      V.  44   270 2001
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   11455600
JRNL        DOI    10.1002/PROT.1092
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.BRAVO,N.VERDAGUER,J.TORMO,C.BETZEL,J.SWITALA,
REMARK   1  AUTH 2 P.C.LOEWEN,I.FITA
REMARK   1  TITL   CRYSTAL STRUCTURE OF CATALASE HPII FROM
REMARK   1  TITL 2 ESCHERICHIA COLI
REMARK   1  REF    STRUCTURE                     V.   3   491 1995
REMARK   1  REFN                   ISSN 0969-2126
REMARK   1 REFERENCE 2
REMARK   1  AUTH   G.N.MURSHUDOV,A.I.GREBENKO,V.BARYNIN,Z.DAUTER,
REMARK   1  AUTH 2 K.S.WILSON,B.K.VAINSHTEIN,W.R.MELIK-ADAMYAN,
REMARK   1  AUTH 3 J.BRAVO,J.M.FERRAN,J.C.FERRER,J.SWITALA,P.C.LOEWEN,
REMARK   1  AUTH 4 I.FITA
REMARK   1  TITL   STRUCTURE OF THE HEME D OF PENICILLIUM VITALE AND
REMARK   1  TITL 2 ESCHERICHIA COLI CATALASES
REMARK   1  REF    J.BIOL.CHEM.                  V. 271  8863 1996
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  DOI    10.1074/JBC.271.15.8863
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.BRAVO,M.J.MATE,T.SCHNEIDER,J.SWITALA,K.S.WILSON,
REMARK   1  AUTH 2 P.C.LOEWEN,I.FITA
REMARK   1  TITL   STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI
REMARK   1  TITL 2 AT 1.9 A RESOLUTION
REMARK   1  REF    PROTEINS:                     V.  34   155 1999
REMARK   1  REF  2 STRUCT.,FUNCT.,GENET.
REMARK   1  REFN                   ISSN 0887-3585
REMARK   1  DOI    10.1002/(SICI)1097-0134(19990201)34:2<155::AID-PROT
REMARK   1  DOI  2 1>3.0.CO;2-P
REMARK   2
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.60
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 203615
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.163
REMARK   3   FREE R VALUE                     : 0.202
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 10774
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 22984
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 176
REMARK   3   SOLVENT ATOMS            : 3208
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 19.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.007 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 0.023 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: REFMAC, WEIGHT MATRIX 0.2.  X-PLOR
REMARK   3  WAS ALSO USED FOR REFINEMENT.
REMARK   4
REMARK   4 1GGE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-00.
REMARK 100 THE RCSB ID CODE IS RCSB001490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-96
REMARK 200  TEMPERATURE           (KELVIN) : 120.0
REMARK 200  PH                             : 9.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 214389
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.960
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LICL, TRIS-HCL, PH 9.00,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297.0K
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       66.17000
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 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: 58600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -267.0 KCAL/MOL
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     SER A     2
REMARK 465     GLN A     3
REMARK 465     HIS A     4
REMARK 465     ASN A     5
REMARK 465     GLU A     6
REMARK 465     LYS A     7
REMARK 465     ASN A     8
REMARK 465     PRO A     9
REMARK 465     HIS A    10
REMARK 465     GLN A    11
REMARK 465     HIS A    12
REMARK 465     GLN A    13
REMARK 465     SER A    14
REMARK 465     PRO A    15
REMARK 465     LEU A    16
REMARK 465     HIS A    17
REMARK 465     ASP A    18
REMARK 465     SER A    19
REMARK 465     SER A    20
REMARK 465     GLU A    21
REMARK 465     ALA A    22
REMARK 465     LYS A    23
REMARK 465     PRO A    24
REMARK 465     GLY A    25
REMARK 465     MET A    26
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     GLN B     3
REMARK 465     HIS B     4
REMARK 465     ASN B     5
REMARK 465     GLU B     6
REMARK 465     LYS B     7
REMARK 465     ASN B     8
REMARK 465     PRO B     9
REMARK 465     HIS B    10
REMARK 465     GLN B    11
REMARK 465     HIS B    12
REMARK 465     GLN B    13
REMARK 465     SER B    14
REMARK 465     PRO B    15
REMARK 465     LEU B    16
REMARK 465     HIS B    17
REMARK 465     ASP B    18
REMARK 465     SER B    19
REMARK 465     SER B    20
REMARK 465     GLU B    21
REMARK 465     ALA B    22
REMARK 465     LYS B    23
REMARK 465     PRO B    24
REMARK 465     GLY B    25
REMARK 465     MET B    26
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     GLN C     3
REMARK 465     HIS C     4
REMARK 465     ASN C     5
REMARK 465     GLU C     6
REMARK 465     LYS C     7
REMARK 465     ASN C     8
REMARK 465     PRO C     9
REMARK 465     HIS C    10
REMARK 465     GLN C    11
REMARK 465     HIS C    12
REMARK 465     GLN C    13
REMARK 465     SER C    14
REMARK 465     PRO C    15
REMARK 465     LEU C    16
REMARK 465     HIS C    17
REMARK 465     ASP C    18
REMARK 465     SER C    19
REMARK 465     SER C    20
REMARK 465     GLU C    21
REMARK 465     ALA C    22
REMARK 465     LYS C    23
REMARK 465     PRO C    24
REMARK 465     GLY C    25
REMARK 465     MET C    26
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     GLN D     3
REMARK 465     HIS D     4
REMARK 465     ASN D     5
REMARK 465     GLU D     6
REMARK 465     LYS D     7
REMARK 465     ASN D     8
REMARK 465     PRO D     9
REMARK 465     HIS D    10
REMARK 465     GLN D    11
REMARK 465     HIS D    12
REMARK 465     GLN D    13
REMARK 465     SER D    14
REMARK 465     PRO D    15
REMARK 465     LEU D    16
REMARK 465     HIS D    17
REMARK 465     ASP D    18
REMARK 465     SER D    19
REMARK 465     SER D    20
REMARK 465     GLU D    21
REMARK 465     ALA D    22
REMARK 465     LYS D    23
REMARK 465     PRO D    24
REMARK 465     GLY D    25
REMARK 465     MET D    26
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    ARG A 121   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG A 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ARG A 130   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ARG A 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A 278   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 497   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES
REMARK 500    SER B  28   N   -  CA  -  CB  ANGL. DEV. =  13.1 DEGREES
REMARK 500    ARG B 377   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG B 422   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG B 521   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG B 601   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG C  61   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP C  70   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG C 111   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG C 111   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG C 121   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ASP C 725   N   -  CA  -  CB  ANGL. DEV. =  11.7 DEGREES
REMARK 500    GLY C 726   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES
REMARK 500    ARG D  61   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES
REMARK 500    ARG D  61   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG D  61   NE  -  CZ  -  NH2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG D 125   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG D 125   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG D 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG D 320   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG D 377   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG D 445   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    HIS D 449   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES
REMARK 500    ARG D 521   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG D 612   CG  -  CD  -  NE  ANGL. DEV. =  13.4 DEGREES
REMARK 500    ARG D 612   CD  -  NE  -  CZ  ANGL. DEV. =  15.4 DEGREES
REMARK 500    ARG D 740   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES
REMARK 500    ARG D 740   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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  28       88.26     -5.59
REMARK 500    SER A  75      -42.33   -168.77
REMARK 500    THR A 178       41.91    -88.49
REMARK 500    ILE A 274      -63.47     73.63
REMARK 500    ASP A 314       88.49   -153.37
REMARK 500    ASP A 405      118.57    -39.92
REMARK 500    ASP A 446     -146.71     64.70
REMARK 500    LYS A 584      159.35    177.63
REMARK 500    ASP A 595       17.41   -147.96
REMARK 500    GLU A 610       58.11   -149.54
REMARK 500    PRO A 658      159.81    -49.22
REMARK 500    LYS A 709       63.36     18.20
REMARK 500    ALA A 711      150.64     61.09
REMARK 500    ASP A 712      -35.68   -130.16
REMARK 500    ASP A 725     -164.26   -127.02
REMARK 500    HIS A 739      -67.32     69.67
REMARK 500    SER B  28       86.05   -176.58
REMARK 500    SER B  35        0.60    -69.19
REMARK 500    SER B  75      -37.55   -166.53
REMARK 500    THR B 178       36.97    -84.30
REMARK 500    ILE B 274      -62.00     73.25
REMARK 500    ASP B 314       86.78   -156.14
REMARK 500    ASP B 330       55.22    -92.01
REMARK 500    ASP B 446     -149.50     65.30
REMARK 500    LYS B 584      164.02    168.52
REMARK 500    ASP B 595       17.53   -153.32
REMARK 500    ARG B 612       89.44    -69.79
REMARK 500    LYS B 709       59.67     39.78
REMARK 500    ALA B 724       32.16    -91.15
REMARK 500    ASP B 725     -171.16    -47.52
REMARK 500    HIS B 739      -66.35     76.70
REMARK 500    SER C  75      -39.21   -167.67
REMARK 500    THR C 178       42.42    -88.64
REMARK 500    ILE C 274      -61.70     68.17
REMARK 500    PHE C 277     -169.26   -114.87
REMARK 500    ASP C 446     -152.90     65.19
REMARK 500    LYS C 584      153.86    173.81
REMARK 500    ASP C 595       34.69   -144.55
REMARK 500    GLU C 610       53.62   -150.08
REMARK 500    ALA C 724       40.48    -79.86
REMARK 500    ASP C 725     -142.00   -164.97
REMARK 500    HIS C 739      -64.53     67.65
REMARK 500    SER D  28       63.86    122.70
REMARK 500    SER D  75      -39.90   -162.90
REMARK 500    THR D 178       42.96    -85.55
REMARK 500    ILE D 274      -62.43     72.37
REMARK 500    ASP D 314       86.82   -155.11
REMARK 500    ASP D 446     -145.77     62.76
REMARK 500    LYS D 584      156.51    170.53
REMARK 500    ASP D 595       32.89   -145.84
REMARK 500    GLU D 610       59.81   -153.40
REMARK 500    HIS D 739      -65.00     75.80
REMARK 500    LYS D 750     -121.41    -75.19
REMARK 500    ILE D 751      109.12     48.32
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 B1323        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH A1541        DISTANCE =  5.63 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                             HDD A 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415   OH
REMARK 620 2 HOH A1417   O   167.3
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDD B 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415   OH
REMARK 620 2 HOH B1380   O   163.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HDD C 760  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415   OH
REMARK 620 2 HOH C1396   O   155.1
REMARK 620 N                    1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD A 760
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD B 760
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD C 760
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD D 760
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IPH   RELATED DB: PDB
REMARK 900 1IPH CONTAINS THE STRUCTURE OF NATIVE PROTEIN AT 2.8 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1CF9   RELATED DB: PDB
REMARK 900 1CF9 CONTAINS THE STRUCTURE OF VAL169CYS VARIANT AT 1.8 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1QF7   RELATED DB: PDB
REMARK 900 1QF7 CONTAINS THE STRUCTURE OF HIS992GLN VARIANT AT 1.9 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1GG9   RELATED DB: PDB
REMARK 900 1GG9 CONTAINS THE STRUCTURE OF HIS128ASN VARIANT AT 1.9 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1GGF   RELATED DB: PDB
REMARK 900 1GGF CONTAINS THE STRUCTURE OF HIS128ASN VARIANT COMPLEX
REMARK 900 WITH HYDROGEN PEROXIDE AT 2.28 A RESOLUTION.
REMARK 900 RELATED ID: 1GGH   RELATED DB: PDB
REMARK 900 1GGH CONTAINS THE STRUCTURE OF HIS128ALA VARIANT AT 2.15 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1GGJ   RELATED DB: PDB
REMARK 900 1GGJ CONTAINS THE STRUCTURE OF ASN201ALA VARIANT COMPLEX
REMARK 900 WITH CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE AT 1.92 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 1GGK   RELATED DB: PDB
REMARK 900 1GGK CONTAINS THE STRUCTURE OF ASN201HIS VARIANT AT 2.26 A
REMARK 900 RESOLUTION.
DBREF  1GGE A    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  1GGE B    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  1GGE C    1   753  UNP    P21179   CATE_ECOLI       1    753
DBREF  1GGE D    1   753  UNP    P21179   CATE_ECOLI       1    753
SEQRES   1 A  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 A  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 A  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 A  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 A  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 A  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 A  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 A  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 A  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 A  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 A  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 A  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 A  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 A  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 A  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 A  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 A  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 A  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 A  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 A  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 A  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 A  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 A  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 A  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 A  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 A  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 A  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 A  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 A  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 A  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 A  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 A  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 A  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 A  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 A  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 A  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 A  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 A  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 A  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 A  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 A  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 A  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 A  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 A  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 A  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 A  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 A  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 A  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 A  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 A  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 A  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 A  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 A  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 A  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 A  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 A  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 A  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 A  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES   1 B  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 B  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 B  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 B  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 B  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 B  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 B  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 B  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 B  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 B  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 B  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 B  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 B  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 B  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 B  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 B  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 B  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 B  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 B  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 B  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 B  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 B  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 B  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 B  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 B  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 B  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 B  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 B  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 B  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 B  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 B  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 B  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 B  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 B  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 B  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 B  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 B  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 B  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 B  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 B  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 B  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 B  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 B  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 B  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 B  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 B  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 B  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 B  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 B  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 B  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 B  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 B  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 B  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 B  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 B  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 B  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 B  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 B  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES   1 C  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 C  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 C  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 C  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 C  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 C  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 C  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 C  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 C  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 C  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 C  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 C  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 C  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 C  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 C  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 C  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 C  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 C  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 C  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 C  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 C  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 C  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 C  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 C  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 C  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 C  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 C  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 C  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 C  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 C  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 C  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 C  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 C  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 C  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 C  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 C  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 C  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 C  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 C  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 C  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 C  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 C  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 C  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 C  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 C  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 C  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 C  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 C  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 C  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 C  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 C  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 C  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 C  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 C  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 C  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 C  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 C  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 C  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES   1 D  753  MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES   2 D  753  SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES   3 D  753  ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES   4 D  753  ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES   5 D  753  GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES   6 D  753  ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES   7 D  753  ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES   8 D  753  GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES   9 D  753  LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES  10 D  753  ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES  11 D  753  GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES  12 D  753  LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES  13 D  753  ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES  14 D  753  GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES  15 D  753  ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES  16 D  753  PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES  17 D  753  GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES  18 D  753  LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN SER
SEQRES  19 D  753  ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES  20 D  753  GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES  21 D  753  GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES  22 D  753  ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES  23 D  753  THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES  24 D  753  ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES  25 D  753  ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES  26 D  753  ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES  27 D  753  GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES  28 D  753  ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES  29 D  753  VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES  30 D  753  ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES  31 D  753  PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES  32 D  753  ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES  33 D  753  ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES  34 D  753  GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES  35 D  753  PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES  36 D  753  ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES  37 D  753  TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES  38 D  753  PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES  39 D  753  ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES  40 D  753  PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES  41 D  753  ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES  42 D  753  VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES  43 D  753  LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES  44 D  753  LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES  45 D  753  ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES  46 D  753  PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES  47 D  753  LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES  48 D  753  ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES  49 D  753  ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES  50 D  753  GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES  51 D  753  ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES  52 D  753  ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES  53 D  753  ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES  54 D  753  LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES  55 D  753  LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES  56 D  753  GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES  57 D  753  MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES  58 D  753  TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
HET    HDD  A 760      44
HET    HDD  B 760      44
HET    HDD  C 760      44
HET    HDD  D 760      44
HETNAM     HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE
HETSYN     HDD HEME
FORMUL   5  HDD    4(C34 H32 FE N4 O5)
FORMUL   9  HOH   *3208(H2 O)
HELIX    1   1 PRO A   52  ALA A   57  1                                   6
HELIX    2   2 ASN A   62  LEU A   68  1                                   7
HELIX    3   3 ASP A  107  HIS A  119  1                                  13
HELIX    4   4 ALA A  150  SER A  154  5                                   5
HELIX    5   5 ASP A  210  HIS A  212  5                                   3
HELIX    6   6 LYS A  213  LYS A  222  1                                  10
HELIX    7   7 HIS A  236  GLN A  246  1                                  11
HELIX    8   8 THR A  249  SER A  258  1                                  10
HELIX    9   9 ASP A  259  ILE A  262  5                                   4
HELIX   10  10 SER A  265  MET A  269  5                                   5
HELIX   11  11 VAL A  303  ASP A  314  1                                  12
HELIX   12  12 ASP A  316  ALA A  328  1                                  13
HELIX   13  13 GLU A  344  GLU A  346  5                                   3
HELIX   14  14 ASN A  381  ASN A  386  1                                   6
HELIX   15  15 ASP A  405  LEU A  423  1                                  19
HELIX   16  16 ASN A  427  ILE A  431  5                                   5
HELIX   17  17 ILE A  431  ARG A  435  5                                   5
HELIX   18  18 SER A  498  GLY A  502  5                                   5
HELIX   19  19 TYR A  505  GLN A  515  1                                  11
HELIX   20  20 THR A  516  LYS A  533  1                                  18
HELIX   21  21 ARG A  536  HIS A  549  1                                  14
HELIX   22  22 ASP A  551  GLY A  563  1                                  13
HELIX   23  23 THR A  567  ASN A  572  1                                   6
HELIX   24  24 ASP A  585  SER A  589  5                                   5
HELIX   25  25 ARG A  612  LYS A  626  1                                  15
HELIX   26  26 PRO A  658  VAL A  662  5                                   5
HELIX   27  27 ILE A  672  ASP A  677  1                                   6
HELIX   28  28 ASN A  678  HIS A  691  1                                  14
HELIX   29  29 ASP A  700  THR A  707  5                                   8
HELIX   30  30 ASP A  725  ALA A  738  1                                  14
HELIX   31  31 VAL A  741  SER A  743  5                                   3
HELIX   32  32 ARG A  744  ASP A  749  1                                   6
HELIX   33  33 PRO B   52  ALA B   57  1                                   6
HELIX   34  34 ASN B   62  LEU B   68  1                                   7
HELIX   35  35 ASP B  107  HIS B  119  1                                  13
HELIX   36  36 ALA B  150  SER B  154  5                                   5
HELIX   37  37 ASP B  210  HIS B  212  5                                   3
HELIX   38  38 LYS B  213  LYS B  222  1                                  10
HELIX   39  39 HIS B  236  GLN B  246  1                                  11
HELIX   40  40 THR B  249  SER B  258  1                                  10
HELIX   41  41 ASP B  259  ILE B  262  5                                   4
HELIX   42  42 SER B  265  MET B  269  5                                   5
HELIX   43  43 VAL B  303  ASP B  314  1                                  12
HELIX   44  44 ASP B  316  GLY B  329  1                                  14
HELIX   45  45 GLU B  344  GLU B  346  5                                   3
HELIX   46  46 ASN B  381  ASN B  386  1                                   6
HELIX   47  47 ASP B  405  THR B  418  1                                  14
HELIX   48  48 THR B  418  LEU B  423  1                                   6
HELIX   49  49 ASN B  427  ILE B  431  5                                   5
HELIX   50  50 ILE B  431  ARG B  435  5                                   5
HELIX   51  51 SER B  498  GLY B  502  5                                   5
HELIX   52  52 TYR B  505  GLN B  515  1                                  11
HELIX   53  53 THR B  516  LYS B  533  1                                  18
HELIX   54  54 ARG B  536  ASP B  551  1                                  16
HELIX   55  55 ASP B  551  LEU B  562  1                                  12
HELIX   56  56 THR B  567  ASN B  572  1                                   6
HELIX   57  57 ASP B  585  SER B  589  5                                   5
HELIX   58  58 ARG B  612  LYS B  626  1                                  15
HELIX   59  59 PRO B  658  VAL B  662  5                                   5
HELIX   60  60 ASN B  671  ASP B  677  1                                   7
HELIX   61  61 ASN B  678  HIS B  691  1                                  14
HELIX   62  62 ASP B  700  THR B  707  5                                   8
HELIX   63  63 ASP B  725  ALA B  738  1                                  14
HELIX   64  64 VAL B  741  SER B  743  5                                   3
HELIX   65  65 ARG B  744  ASP B  749  1                                   6
HELIX   66  66 PRO C   52  ALA C   57  1                                   6
HELIX   67  67 ASN C   62  LEU C   68  1                                   7
HELIX   68  68 ASP C  107  HIS C  119  1                                  13
HELIX   69  69 ALA C  150  SER C  154  5                                   5
HELIX   70  70 ASP C  210  HIS C  212  5                                   3
HELIX   71  71 LYS C  213  LYS C  222  1                                  10
HELIX   72  72 HIS C  236  GLN C  246  1                                  11
HELIX   73  73 THR C  249  SER C  258  1                                  10
HELIX   74  74 ASP C  259  ILE C  262  5                                   4
HELIX   75  75 SER C  265  MET C  269  5                                   5
HELIX   76  76 VAL C  303  ASP C  314  1                                  12
HELIX   77  77 ASP C  316  GLY C  329  1                                  14
HELIX   78  78 GLU C  344  GLU C  346  5                                   3
HELIX   79  79 ASN C  381  ASN C  386  1                                   6
HELIX   80  80 ASP C  405  LEU C  423  1                                  19
HELIX   81  81 ASN C  427  ILE C  431  5                                   5
HELIX   82  82 ILE C  431  ARG C  435  5                                   5
HELIX   83  83 SER C  498  GLY C  502  5                                   5
HELIX   84  84 TYR C  505  SER C  514  1                                  10
HELIX   85  85 THR C  516  LYS C  533  1                                  18
HELIX   86  86 ARG C  536  HIS C  549  1                                  14
HELIX   87  87 ASP C  551  LEU C  562  1                                  12
HELIX   88  88 THR C  567  ASN C  572  1                                   6
HELIX   89  89 ASP C  585  SER C  589  5                                   5
HELIX   90  90 ARG C  612  LYS C  626  1                                  15
HELIX   91  91 PRO C  658  VAL C  662  5                                   5
HELIX   92  92 ASN C  671  ILE C  675  5                                   5
HELIX   93  93 ASN C  678  HIS C  691  1                                  14
HELIX   94  94 ASP C  700  THR C  707  5                                   8
HELIX   95  95 SER C  727  ALA C  738  1                                  12
HELIX   96  96 VAL C  741  SER C  743  5                                   3
HELIX   97  97 ARG C  744  ASP C  749  1                                   6
HELIX   98  98 PRO D   52  ALA D   57  1                                   6
HELIX   99  99 ASN D   62  LEU D   68  1                                   7
HELIX  100 100 ASP D  107  HIS D  119  1                                  13
HELIX  101 101 ALA D  150  SER D  154  5                                   5
HELIX  102 102 ASP D  210  HIS D  212  5                                   3
HELIX  103 103 LYS D  213  LYS D  222  1                                  10
HELIX  104 104 HIS D  236  GLN D  246  1                                  11
HELIX  105 105 THR D  249  SER D  258  1                                  10
HELIX  106 106 ASP D  259  ILE D  262  5                                   4
HELIX  107 107 SER D  265  MET D  269  5                                   5
HELIX  108 108 VAL D  303  ASP D  314  1                                  12
HELIX  109 109 ASP D  316  GLY D  329  1                                  14
HELIX  110 110 GLU D  344  GLU D  346  5                                   3
HELIX  111 111 ASN D  381  ASN D  386  1                                   6
HELIX  112 112 ASP D  405  LEU D  423  1                                  19
HELIX  113 113 ASN D  427  ILE D  431  5                                   5
HELIX  114 114 ILE D  431  ARG D  435  5                                   5
HELIX  115 115 SER D  498  GLY D  502  5                                   5
HELIX  116 116 TYR D  505  GLN D  515  1                                  11
HELIX  117 117 THR D  516  LYS D  533  1                                  18
HELIX  118 118 ARG D  536  HIS D  549  1                                  14
HELIX  119 119 ASP D  551  LEU D  562  1                                  12
HELIX  120 120 THR D  567  ASN D  572  1                                   6
HELIX  121 121 ASP D  585  SER D  589  5                                   5
HELIX  122 122 ARG D  612  LYS D  626  1                                  15
HELIX  123 123 PRO D  658  VAL D  662  5                                   5
HELIX  124 124 ILE D  672  ASP D  677  1                                   6
HELIX  125 125 ASN D  678  HIS D  691  1                                  14
HELIX  126 126 ASP D  700  THR D  707  5                                   8
HELIX  127 127 SER D  727  ALA D  738  1                                  12
HELIX  128 128 VAL D  741  SER D  743  5                                   3
HELIX  129 129 ARG D  744  ASP D  749  1                                   6
SHEET    1   A 2 ARG A  72  LYS A  73  0
SHEET    2   A 2 ILE C 453  ASP C 454  1  O  ILE C 453   N  LYS A  73
SHEET    1   B 4 LEU A  95  ALA A  97  0
SHEET    2   B 4 ARG D 488  ARG D 495 -1  N  VAL D 494   O  ARG A  96
SHEET    3   B 4 ARG C 488  ARG C 495 -1  N  VAL C 489   O  GLY D 491
SHEET    4   B 4 LEU B  95  ALA B  97 -1  N  ARG B  96   O  VAL C 494
SHEET    1   C11 LEU A 400  ASP A 401  0
SHEET    2   C11 PHE A 277  ILE A 280 -1  N  ARG A 278   O  ASP A 401
SHEET    3   C11 ALA A 286  PRO A 295 -1  N  THR A 287   O  LEU A 279
SHEET    4   C11 GLU A 333  PRO A 342 -1  N  GLU A 335   O  LYS A 294
SHEET    5   C11 VAL A 367  ARG A 377 -1  N  GLN A 368   O  PHE A 338
SHEET    6   C11 GLY A 131  PRO A 140 -1  N  HIS A 135   O  ARG A 377
SHEET    7   C11 THR A 160  SER A 167 -1  N  THR A 160   O  PHE A 138
SHEET    8   C11 GLY A 184  THR A 191 -1  N  GLY A 184   O  SER A 167
SHEET    9   C11 GLY A 194  ASN A 201 -1  N  GLY A 194   O  THR A 191
SHEET   10   C11 GLY A 271  PHE A 272 -1  N  PHE A 272   O  ASN A 201
SHEET   11   C11 ALA A 286  PRO A 295 -1  N  TRP A 293   O  GLY A 271
SHEET    1   D 2 ILE A 453  ASP A 454  0
SHEET    2   D 2 ARG C  72  LYS C  73  1  N  LYS C  73   O  ILE A 453
SHEET    1   E 4 LEU D  95  ALA D  97  0
SHEET    2   E 4 ARG A 488  ARG A 495 -1  O  VAL A 494   N  ARG D  96
SHEET    3   E 4 ARG B 488  ARG B 495 -1  N  VAL B 489   O  GLY A 491
SHEET    4   E 4 LEU C  95  ALA C  97 -1  O  ARG C  96   N  VAL B 494
SHEET    1   F 6 ALA A 652  THR A 653  0
SHEET    2   F 6 HIS A 629  TYR A 634  1  O  LEU A 632   N  ALA A 652
SHEET    3   F 6 VAL A 602  LEU A 606  1  N  VAL A 603   O  HIS A 629
SHEET    4   F 6 ALA A 664  VAL A 667  1  O  ALA A 664   N  ALA A 604
SHEET    5   F 6 ILE A 695  ALA A 698  1  N  ALA A 696   O  VAL A 665
SHEET    6   F 6 ILE A 718  ALA A 721  1  O  VAL A 719   N  LEU A 697
SHEET    1   G 2 GLU A 639  THR A 641  0
SHEET    2   G 2 VAL A 647  PRO A 649 -1  N  LEU A 648   O  VAL A 640
SHEET    1   H 2 ARG B  72  LYS B  73  0
SHEET    2   H 2 ILE D 453  ASP D 454  1  O  ILE D 453   N  LYS B  73
SHEET    1   I11 LEU B 400  ASP B 401  0
SHEET    2   I11 PHE B 277  ILE B 280 -1  N  ARG B 278   O  ASP B 401
SHEET    3   I11 ALA B 286  PRO B 295 -1  O  THR B 287   N  LEU B 279
SHEET    4   I11 GLU B 333  PRO B 342 -1  N  GLU B 335   O  LYS B 294
SHEET    5   I11 VAL B 367  ARG B 377 -1  N  GLN B 368   O  PHE B 338
SHEET    6   I11 GLY B 131  PRO B 140 -1  N  HIS B 135   O  ARG B 377
SHEET    7   I11 THR B 160  SER B 167 -1  N  THR B 160   O  PHE B 138
SHEET    8   I11 GLY B 184  THR B 191 -1  N  GLY B 184   O  SER B 167
SHEET    9   I11 GLY B 194  ASN B 201 -1  N  GLY B 194   O  THR B 191
SHEET   10   I11 GLY B 271  PHE B 272 -1  N  PHE B 272   O  ASN B 201
SHEET   11   I11 ALA B 286  PRO B 295 -1  N  TRP B 293   O  GLY B 271
SHEET    1   J 2 ILE B 453  ASP B 454  0
SHEET    2   J 2 ARG D  72  LYS D  73  1  N  LYS D  73   O  ILE B 453
SHEET    1   K 6 ALA B 652  THR B 653  0
SHEET    2   K 6 HIS B 629  TYR B 634  1  O  LEU B 632   N  ALA B 652
SHEET    3   K 6 VAL B 602  LEU B 606  1  N  VAL B 603   O  HIS B 629
SHEET    4   K 6 ALA B 664  VAL B 667  1  O  ALA B 664   N  ALA B 604
SHEET    5   K 6 ILE B 695  ALA B 698  1  N  ALA B 696   O  VAL B 665
SHEET    6   K 6 ILE B 718  ALA B 721  1  O  VAL B 719   N  LEU B 697
SHEET    1   L 2 GLU B 639  THR B 641  0
SHEET    2   L 2 VAL B 647  PRO B 649 -1  N  LEU B 648   O  VAL B 640
SHEET    1   M11 LEU C 400  ASP C 401  0
SHEET    2   M11 PHE C 277  ILE C 280 -1  N  ARG C 278   O  ASP C 401
SHEET    3   M11 ALA C 286  PRO C 295 -1  N  THR C 287   O  LEU C 279
SHEET    4   M11 GLU C 333  PRO C 342 -1  N  GLU C 335   O  LYS C 294
SHEET    5   M11 VAL C 367  ARG C 377 -1  N  GLN C 368   O  PHE C 338
SHEET    6   M11 GLY C 131  PRO C 140 -1  N  HIS C 135   O  ARG C 377
SHEET    7   M11 THR C 160  SER C 167 -1  O  THR C 160   N  PHE C 138
SHEET    8   M11 GLY C 184  THR C 191 -1  N  GLY C 184   O  SER C 167
SHEET    9   M11 GLY C 194  ASN C 201 -1  O  GLY C 194   N  THR C 191
SHEET   10   M11 GLY C 271  PHE C 272 -1  N  PHE C 272   O  ASN C 201
SHEET   11   M11 ALA C 286  PRO C 295 -1  N  TRP C 293   O  GLY C 271
SHEET    1   N 6 ALA C 652  THR C 653  0
SHEET    2   N 6 HIS C 629  TYR C 634  1  O  LEU C 632   N  ALA C 652
SHEET    3   N 6 VAL C 602  LEU C 606  1  N  VAL C 603   O  HIS C 629
SHEET    4   N 6 ALA C 664  VAL C 667  1  O  ALA C 664   N  ALA C 604
SHEET    5   N 6 ILE C 695  ALA C 698  1  N  ALA C 696   O  VAL C 665
SHEET    6   N 6 ILE C 718  ALA C 721  1  N  VAL C 719   O  ILE C 695
SHEET    1   O 2 GLU C 639  THR C 641  0
SHEET    2   O 2 VAL C 647  PRO C 649 -1  N  LEU C 648   O  VAL C 640
SHEET    1   P11 LEU D 400  ASP D 401  0
SHEET    2   P11 PHE D 277  ILE D 280 -1  N  ARG D 278   O  ASP D 401
SHEET    3   P11 ALA D 286  PRO D 295 -1  O  THR D 287   N  LEU D 279
SHEET    4   P11 GLU D 333  PRO D 342 -1  N  GLU D 335   O  LYS D 294
SHEET    5   P11 GLN D 368  ARG D 377 -1  N  GLN D 368   O  PHE D 338
SHEET    6   P11 GLY D 131  PRO D 140 -1  N  HIS D 135   O  ARG D 377
SHEET    7   P11 THR D 160  SER D 167 -1  N  THR D 160   O  PHE D 138
SHEET    8   P11 GLY D 184  THR D 191 -1  N  GLY D 184   O  SER D 167
SHEET    9   P11 GLY D 194  ASN D 201 -1  N  GLY D 194   O  THR D 191
SHEET   10   P11 GLY D 271  PHE D 272 -1  N  PHE D 272   O  ASN D 201
SHEET   11   P11 ALA D 286  PRO D 295 -1  N  TRP D 293   O  GLY D 271
SHEET    1   Q 6 ALA D 652  THR D 653  0
SHEET    2   Q 6 HIS D 629  TYR D 634  1  O  LEU D 632   N  ALA D 652
SHEET    3   Q 6 VAL D 602  LEU D 606  1  N  VAL D 603   O  HIS D 629
SHEET    4   Q 6 ALA D 664  VAL D 667  1  O  ALA D 664   N  ALA D 604
SHEET    5   Q 6 ILE D 695  ALA D 698  1  O  ALA D 696   N  VAL D 667
SHEET    6   Q 6 ILE D 718  ALA D 721  1  N  VAL D 719   O  ILE D 695
LINK        FE   HDD A 760                 OH  TYR A 415     1555   1555  2.10
LINK         ND1 HIS A 392                 CB  TYR A 415     1555   1555  2.05
LINK        FE   HDD B 760                 OH  TYR B 415     1555   1555  1.98
LINK         ND1 HIS B 392                 CB  TYR B 415     1555   1555  2.05
LINK        FE   HDD C 760                 OH  TYR C 415     1555   1555  2.03
LINK         ND1 HIS C 392                 CB  TYR C 415     1555   1555  2.05
LINK        FE   HDD D 760                 OH  TYR D 415     1555   1555  1.99
LINK         ND1 HIS D 392                 CB  TYR D 415     1555   1555  2.06
LINK        FE   HDD A 760                 O   HOH A1417     1555   1555  2.39
LINK        FE   HDD B 760                 O   HOH B1380     1555   1555  2.45
LINK        FE   HDD C 760                 O   HOH C1396     1555   1555  2.58
CISPEP   1 ILE A  229    PRO A  230          0         0.04
CISPEP   2 GLU A  461    PRO A  462          0         3.22
CISPEP   3 TRP A  469    PRO A  470          0        -4.54
CISPEP   4 ILE B  229    PRO B  230          0         2.14
CISPEP   5 GLU B  461    PRO B  462          0         0.33
CISPEP   6 TRP B  469    PRO B  470          0        -6.65
CISPEP   7 ILE C  229    PRO C  230          0         3.35
CISPEP   8 GLU C  461    PRO C  462          0         3.46
CISPEP   9 TRP C  469    PRO C  470          0        -5.28
CISPEP  10 ILE D  229    PRO D  230          0        -0.98
CISPEP  11 GLU D  461    PRO D  462          0         2.04
CISPEP  12 TRP D  469    PRO D  470          0        -3.04
SITE     1 AC1 22 ARG A 125  VAL A 127  HIS A 128  ARG A 165
SITE     2 AC1 22 GLY A 184  VAL A 199  GLY A 200  ASN A 201
SITE     3 AC1 22 PHE A 206  PHE A 214  HIS A 275  PHE A 391
SITE     4 AC1 22 LEU A 407  ARG A 411  SER A 414  TYR A 415
SITE     5 AC1 22 THR A 418  GLN A 419  HOH A 784  HOH A 832
SITE     6 AC1 22 HOH A 860  HOH A1417
SITE     1 AC2 22 ARG B 125  VAL B 127  HIS B 128  ARG B 165
SITE     2 AC2 22 GLY B 184  VAL B 199  GLY B 200  ASN B 201
SITE     3 AC2 22 PHE B 214  HIS B 275  PHE B 391  LEU B 407
SITE     4 AC2 22 ARG B 411  SER B 414  TYR B 415  THR B 418
SITE     5 AC2 22 GLN B 419  HOH B 833  HOH B 880  HOH B 909
SITE     6 AC2 22 HOH B1380  ASP C 118
SITE     1 AC3 22 ARG C 125  VAL C 127  HIS C 128  ARG C 165
SITE     2 AC3 22 GLY C 184  VAL C 199  GLY C 200  ASN C 201
SITE     3 AC3 22 PHE C 206  PHE C 214  ILE C 274  HIS C 275
SITE     4 AC3 22 PHE C 391  LEU C 407  ARG C 411  SER C 414
SITE     5 AC3 22 TYR C 415  THR C 418  GLN C 419  HOH C 875
SITE     6 AC3 22 HOH C 921  HOH C1396
SITE     1 AC4 20 ARG D 125  VAL D 127  HIS D 128  ARG D 165
SITE     2 AC4 20 GLY D 184  VAL D 199  GLY D 200  ASN D 201
SITE     3 AC4 20 PHE D 206  PHE D 214  HIS D 275  PHE D 391
SITE     4 AC4 20 LEU D 407  ARG D 411  SER D 414  TYR D 415
SITE     5 AC4 20 THR D 418  GLN D 419  HOH D 936  HOH D 985
CRYST1   93.040  132.340  121.200  90.00 109.63  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      0.010748  0.000000  0.003834        0.00000
SCALE2      0.000000  0.007556  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008760        0.00000
      
PROCHECK
Go to PROCHECK summary
 References