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PDBsum entry 1pth

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1pth
Jmol
Contents
Protein chains
551 a.a.
Ligands
NAG ×4
NAG-NAG ×2
BOG ×2
HEM ×2
SAL ×2
Waters ×1
HEADER    OXIDOREDUCTASE                          11-APR-95   1PTH
TITLE     THE STRUCTURAL BASIS OF ASPIRIN ACTIVITY INFERRED FROM THE CRYSTAL
TITLE    2 STRUCTURE OF INACTIVATED PROSTAGLANDIN H2 SYNTHASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN H2 SYNTHASE-1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CYCLOOXYGENASE I;
COMPND   5 EC: 1.14.99.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 ORGANELLE: SEMINAL VESICLES
KEYWDS    DIOXYGENASE, PEROXIDASE, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.J.LOLL,D.PICOT,R.M.GARAVITO
REVDAT   3   13-JUL-11 1PTH    1       VERSN
REVDAT   2   24-FEB-09 1PTH    1       VERSN
REVDAT   1   11-APR-96 1PTH    0
JRNL        AUTH   P.J.LOLL,D.PICOT,R.M.GARAVITO
JRNL        TITL   THE STRUCTURAL BASIS OF ASPIRIN ACTIVITY INFERRED FROM THE
JRNL        TITL 2 CRYSTAL STRUCTURE OF INACTIVATED PROSTAGLANDIN H2 SYNTHASE.
JRNL        REF    NAT.STRUCT.BIOL.              V.   2   637 1995
JRNL        REFN                   ISSN 1072-8368
JRNL        PMID   7552725
JRNL        DOI    10.1038/NSB0895-637
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   D.PICOT,P.J.LOLL,R.M.GARAVITO
REMARK   1  TITL   THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN
REMARK   1  TITL 2 PROSTAGLANDIN H2 SYNTHASE-1
REMARK   1  REF    NATURE                        V. 367   243 1994
REMARK   1  REFN                   ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 75.5
REMARK   3   NUMBER OF REFLECTIONS             : 23789
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 SET) : 0.186
REMARK   3   FREE R VALUE                     : 0.227
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8962
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 258
REMARK   3   SOLVENT ATOMS            : 1
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.00
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.013
REMARK   3   BOND ANGLES            (DEGREES) : 1.89
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.69
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : 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  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1PTH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : JUN-93
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
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                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27154
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.0
REMARK 200  DATA REDUNDANCY                : 2.700
REMARK 200  R MERGE                    (I) : 0.09500
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) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 73.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.78500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      104.90000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      117.50000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       49.78500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      104.90000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      117.50000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.78500
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      104.90000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      117.50000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       49.78500
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      104.90000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      117.50000
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 300 REMARK: MTRIX
REMARK 300  THE TRANSFORMATION PRESENTED ON MTRIX RECORDS BELOW
REMARK 300  DESCRIBES THE NON-CRYSTALLOGRAPHIC RELATIONSHIP TO CREATE
REMARK 300  THE SECOND SUBUNIT OF THE PGHS-1 DIMER.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 400
REMARK 400 COMPOUND
REMARK 400 COMPND
REMARK 400   MOLECULE: PROSTAGLANDIN H2 SYNTHASE-1. ACETYLATED BY THE
REMARK 400   ASPIRIN ANALOG 2-BROMOACETOXY BENZOIC ACID.
REMARK 400
REMARK 400 THE SIDE CHAIN OXYGEN OG OF SER 530 IS ESTERIFIED WITH A
REMARK 400 2-BROMOACETYL GROUP:
REMARK 400
REMARK 400                       |
REMARK 400              SER 530  CH-CH2-O-CO-CH2BR
REMARK 400                       |
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     ALA A    25
REMARK 465     ASP A    26
REMARK 465     PRO A    27
REMARK 465     GLY A    28
REMARK 465     ALA A    29
REMARK 465     PRO A    30
REMARK 465     ALA A    31
REMARK 465     PRO A    32
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     ARG A   586
REMARK 465     GLN A   587
REMARK 465     GLU A   588
REMARK 465     ASP A   589
REMARK 465     ARG A   590
REMARK 465     PRO A   591
REMARK 465     GLY A   592
REMARK 465     VAL A   593
REMARK 465     GLU A   594
REMARK 465     ARG A   595
REMARK 465     PRO A   596
REMARK 465     PRO A   597
REMARK 465     THR A   598
REMARK 465     GLU A   599
REMARK 465     LEU A   600
REMARK 465     ALA B    25
REMARK 465     ASP B    26
REMARK 465     PRO B    27
REMARK 465     GLY B    28
REMARK 465     ALA B    29
REMARK 465     PRO B    30
REMARK 465     ALA B    31
REMARK 465     PRO B    32
REMARK 465     ASP B   584
REMARK 465     PRO B   585
REMARK 465     ARG B   586
REMARK 465     GLN B   587
REMARK 465     GLU B   588
REMARK 465     ASP B   589
REMARK 465     ARG B   590
REMARK 465     PRO B   591
REMARK 465     GLY B   592
REMARK 465     VAL B   593
REMARK 465     GLU B   594
REMARK 465     ARG B   595
REMARK 465     PRO B   596
REMARK 465     PRO B   597
REMARK 465     THR B   598
REMARK 465     GLU B   599
REMARK 465     LEU B   600
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   CE1  PHE A   409     NH1  ARG B   277     8456     2.18
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    PRO A 392   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES
REMARK 500    ARG A 433   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    PRO B 392   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES
REMARK 500    ARG B 433   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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    GLN A  44       17.59     83.32
REMARK 500    ASP A  53     -122.32    -91.79
REMARK 500    ARG A  54      163.52     35.09
REMARK 500    CYS A  59       35.43    -96.28
REMARK 500    THR A 129      -92.50   -110.24
REMARK 500    ASP A 135       49.83    -95.85
REMARK 500    PRO A 153      152.78    -49.83
REMARK 500    PRO A 162        0.85    -67.16
REMARK 500    ASN A 195     -167.46   -104.98
REMARK 500    LYS A 211       61.45   -163.82
REMARK 500    ASP A 249       15.10     55.25
REMARK 500    PRO A 270       77.39    -64.37
REMARK 500    VAL A 287      -30.24   -139.70
REMARK 500    GLU A 290      -49.49    -26.21
REMARK 500    PHE A 292      -17.59    -44.09
REMARK 500    LEU A 295       99.55    157.29
REMARK 500    HIS A 320       77.41   -112.62
REMARK 500    ASP A 325      -77.92    -48.54
REMARK 500    GLU A 347      -60.02   -105.80
REMARK 500    TYR A 348      -70.16    -56.75
REMARK 500    ASP A 362       89.70   -151.23
REMARK 500    PRO A 363       -6.76    -53.16
REMARK 500    TRP A 387       41.13    -83.10
REMARK 500    VAL A 397       72.45   -108.52
REMARK 500    LEU A 408      -27.62    -32.22
REMARK 500    ASN A 410       95.11    -49.06
REMARK 500    GLU A 486      -80.75    -62.23
REMARK 500    PRO A 514      -71.61      4.11
REMARK 500    VAL A 554      -76.75    -60.98
REMARK 500    PRO A 576     -167.26   -100.20
REMARK 500    GLN B  44       17.59     83.34
REMARK 500    ASP B  53     -122.36    -91.77
REMARK 500    ARG B  54      163.56     35.12
REMARK 500    CYS B  59       35.39    -96.30
REMARK 500    THR B 129      -92.48   -110.25
REMARK 500    ASP B 135       49.80    -95.85
REMARK 500    PRO B 153      152.79    -49.86
REMARK 500    PRO B 162        0.79    -67.09
REMARK 500    ASN B 195     -167.43   -104.93
REMARK 500    LYS B 211       61.43   -163.81
REMARK 500    ASP B 249       15.05     55.31
REMARK 500    PRO B 270       77.37    -64.40
REMARK 500    VAL B 287      -30.28   -139.70
REMARK 500    GLU B 290      -49.48    -26.25
REMARK 500    PHE B 292      -17.52    -44.17
REMARK 500    LEU B 295       99.60    157.29
REMARK 500    HIS B 320       77.46   -112.63
REMARK 500    ASP B 325      -77.90    -48.54
REMARK 500    TYR B 348      -70.17    -56.73
REMARK 500    ASP B 362       89.71   -151.21
REMARK 500
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A 136         0.07    SIDE CHAIN
REMARK 500    TYR A 348         0.07    SIDE CHAIN
REMARK 500    TYR B 136         0.07    SIDE CHAIN
REMARK 500    TYR B 348         0.07    SIDE CHAIN
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    VAL A 145        24.9      L          L   OUTSIDE RANGE
REMARK 500    VAL A 287        23.9      L          L   OUTSIDE RANGE
REMARK 500    LEU A 408        19.3      L          L   OUTSIDE RANGE
REMARK 500    VAL B 145        24.9      L          L   OUTSIDE RANGE
REMARK 500    VAL B 287        23.9      L          L   OUTSIDE RANGE
REMARK 500    LEU B 408        19.3      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 601   NA   95.2
REMARK 620 3 HEM A 601   NB   84.8  92.7
REMARK 620 4 HEM A 601   NC   80.5 175.7  87.6
REMARK 620 5 HEM A 601   ND   87.2  88.5 172.0  90.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 602  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 602   NA   95.3
REMARK 620 3 HEM B 602   NB   84.8  92.7
REMARK 620 4 HEM B 602   NC   80.5 175.7  87.6
REMARK 620 5 HEM B 602   ND   87.2  88.5 172.0  90.6
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 NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAL A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SAL B 711
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEQUENCE IS FOUND IN ENTRY 1PRH.  THE NUMBERING IS
REMARK 999 DERIVED FROM THE PRE-PROTEIN, WHICH CONTAINS A 24-RESIDUE
REMARK 999 SIGNAL SEQUENCE WHICH IS CLEAVED DURING MATURATION.
DBREF  1PTH A   25   600  PIR    A29947   A29947          24    599
DBREF  1PTH B   25   600  PIR    A29947   A29947          24    599
SEQRES   1 A  576  ALA ASP PRO GLY ALA PRO ALA PRO VAL ASN PRO CYS CYS
SEQRES   2 A  576  TYR TYR PRO CYS GLN HIS GLN GLY ILE CYS VAL ARG PHE
SEQRES   3 A  576  GLY LEU ASP ARG TYR GLN CYS ASP CYS THR ARG THR GLY
SEQRES   4 A  576  TYR SER GLY PRO ASN CYS THR ILE PRO GLU ILE TRP THR
SEQRES   5 A  576  TRP LEU ARG THR THR LEU ARG PRO SER PRO SER PHE ILE
SEQRES   6 A  576  HIS PHE LEU LEU THR HIS GLY ARG TRP LEU TRP ASP PHE
SEQRES   7 A  576  VAL ASN ALA THR PHE ILE ARG ASP THR LEU MET ARG LEU
SEQRES   8 A  576  VAL LEU THR VAL ARG SER ASN LEU ILE PRO SER PRO PRO
SEQRES   9 A  576  THR TYR ASN ILE ALA HIS ASP TYR ILE SER TRP GLU SER
SEQRES  10 A  576  PHE SER ASN VAL SER TYR TYR THR ARG ILE LEU PRO SER
SEQRES  11 A  576  VAL PRO ARG ASP CYS PRO THR PRO MET GLY THR LYS GLY
SEQRES  12 A  576  LYS LYS GLN LEU PRO ASP ALA GLU PHE LEU SER ARG ARG
SEQRES  13 A  576  PHE LEU LEU ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY
SEQRES  14 A  576  THR ASN LEU MET PHE ALA PHE PHE ALA GLN HIS PHE THR
SEQRES  15 A  576  HIS GLN PHE PHE LYS THR SER GLY LYS MET GLY PRO GLY
SEQRES  16 A  576  PHE THR LYS ALA LEU GLY HIS GLY VAL ASP LEU GLY HIS
SEQRES  17 A  576  ILE TYR GLY ASP ASN LEU GLU ARG GLN TYR GLN LEU ARG
SEQRES  18 A  576  LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN MET LEU ASN
SEQRES  19 A  576  GLY GLU VAL TYR PRO PRO SER VAL GLU GLU ALA PRO VAL
SEQRES  20 A  576  LEU MET HIS TYR PRO ARG GLY ILE PRO PRO GLN SER GLN
SEQRES  21 A  576  MET ALA VAL GLY GLN GLU VAL PHE GLY LEU LEU PRO GLY
SEQRES  22 A  576  LEU MET LEU TYR ALA THR ILE TRP LEU ARG GLU HIS ASN
SEQRES  23 A  576  ARG VAL CYS ASP LEU LEU LYS ALA GLU HIS PRO THR TRP
SEQRES  24 A  576  GLY ASP GLU GLN LEU PHE GLN THR ALA ARG LEU ILE LEU
SEQRES  25 A  576  ILE GLY GLU THR ILE LYS ILE VAL ILE GLU GLU TYR VAL
SEQRES  26 A  576  GLN GLN LEU SER GLY TYR PHE LEU GLN LEU LYS PHE ASP
SEQRES  27 A  576  PRO GLU LEU LEU PHE GLY ALA GLN PHE GLN TYR ARG ASN
SEQRES  28 A  576  ARG ILE ALA MET GLU PHE ASN GLN LEU TYR HIS TRP HIS
SEQRES  29 A  576  PRO LEU MET PRO ASP SER PHE ARG VAL GLY PRO GLN ASP
SEQRES  30 A  576  TYR SER TYR GLU GLN PHE LEU PHE ASN THR SER MET LEU
SEQRES  31 A  576  VAL ASP TYR GLY VAL GLU ALA LEU VAL ASP ALA PHE SER
SEQRES  32 A  576  ARG GLN PRO ALA GLY ARG ILE GLY GLY GLY ARG ASN ILE
SEQRES  33 A  576  ASP HIS HIS ILE LEU HIS VAL ALA VAL ASP VAL ILE LYS
SEQRES  34 A  576  GLU SER ARG VAL LEU ARG LEU GLN PRO PHE ASN GLU TYR
SEQRES  35 A  576  ARG LYS ARG PHE GLY MET LYS PRO TYR THR SER PHE GLN
SEQRES  36 A  576  GLU LEU THR GLY GLU LYS GLU MET ALA ALA GLU LEU GLU
SEQRES  37 A  576  GLU LEU TYR GLY ASP ILE ASP ALA LEU GLU PHE TYR PRO
SEQRES  38 A  576  GLY LEU LEU LEU GLU LYS CYS HIS PRO ASN SER ILE PHE
SEQRES  39 A  576  GLY GLU SER MET ILE GLU MET GLY ALA PRO PHE 0AH LEU
SEQRES  40 A  576  LYS GLY LEU LEU GLY ASN PRO ILE CYS SER PRO GLU TYR
SEQRES  41 A  576  TRP LYS ALA SER THR PHE GLY GLY GLU VAL GLY PHE ASN
SEQRES  42 A  576  LEU VAL LYS THR ALA THR LEU LYS LYS LEU VAL CYS LEU
SEQRES  43 A  576  ASN THR LYS THR CYS PRO TYR VAL SER PHE HIS VAL PRO
SEQRES  44 A  576  ASP PRO ARG GLN GLU ASP ARG PRO GLY VAL GLU ARG PRO
SEQRES  45 A  576  PRO THR GLU LEU
SEQRES   1 B  576  ALA ASP PRO GLY ALA PRO ALA PRO VAL ASN PRO CYS CYS
SEQRES   2 B  576  TYR TYR PRO CYS GLN HIS GLN GLY ILE CYS VAL ARG PHE
SEQRES   3 B  576  GLY LEU ASP ARG TYR GLN CYS ASP CYS THR ARG THR GLY
SEQRES   4 B  576  TYR SER GLY PRO ASN CYS THR ILE PRO GLU ILE TRP THR
SEQRES   5 B  576  TRP LEU ARG THR THR LEU ARG PRO SER PRO SER PHE ILE
SEQRES   6 B  576  HIS PHE LEU LEU THR HIS GLY ARG TRP LEU TRP ASP PHE
SEQRES   7 B  576  VAL ASN ALA THR PHE ILE ARG ASP THR LEU MET ARG LEU
SEQRES   8 B  576  VAL LEU THR VAL ARG SER ASN LEU ILE PRO SER PRO PRO
SEQRES   9 B  576  THR TYR ASN ILE ALA HIS ASP TYR ILE SER TRP GLU SER
SEQRES  10 B  576  PHE SER ASN VAL SER TYR TYR THR ARG ILE LEU PRO SER
SEQRES  11 B  576  VAL PRO ARG ASP CYS PRO THR PRO MET GLY THR LYS GLY
SEQRES  12 B  576  LYS LYS GLN LEU PRO ASP ALA GLU PHE LEU SER ARG ARG
SEQRES  13 B  576  PHE LEU LEU ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY
SEQRES  14 B  576  THR ASN LEU MET PHE ALA PHE PHE ALA GLN HIS PHE THR
SEQRES  15 B  576  HIS GLN PHE PHE LYS THR SER GLY LYS MET GLY PRO GLY
SEQRES  16 B  576  PHE THR LYS ALA LEU GLY HIS GLY VAL ASP LEU GLY HIS
SEQRES  17 B  576  ILE TYR GLY ASP ASN LEU GLU ARG GLN TYR GLN LEU ARG
SEQRES  18 B  576  LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN MET LEU ASN
SEQRES  19 B  576  GLY GLU VAL TYR PRO PRO SER VAL GLU GLU ALA PRO VAL
SEQRES  20 B  576  LEU MET HIS TYR PRO ARG GLY ILE PRO PRO GLN SER GLN
SEQRES  21 B  576  MET ALA VAL GLY GLN GLU VAL PHE GLY LEU LEU PRO GLY
SEQRES  22 B  576  LEU MET LEU TYR ALA THR ILE TRP LEU ARG GLU HIS ASN
SEQRES  23 B  576  ARG VAL CYS ASP LEU LEU LYS ALA GLU HIS PRO THR TRP
SEQRES  24 B  576  GLY ASP GLU GLN LEU PHE GLN THR ALA ARG LEU ILE LEU
SEQRES  25 B  576  ILE GLY GLU THR ILE LYS ILE VAL ILE GLU GLU TYR VAL
SEQRES  26 B  576  GLN GLN LEU SER GLY TYR PHE LEU GLN LEU LYS PHE ASP
SEQRES  27 B  576  PRO GLU LEU LEU PHE GLY ALA GLN PHE GLN TYR ARG ASN
SEQRES  28 B  576  ARG ILE ALA MET GLU PHE ASN GLN LEU TYR HIS TRP HIS
SEQRES  29 B  576  PRO LEU MET PRO ASP SER PHE ARG VAL GLY PRO GLN ASP
SEQRES  30 B  576  TYR SER TYR GLU GLN PHE LEU PHE ASN THR SER MET LEU
SEQRES  31 B  576  VAL ASP TYR GLY VAL GLU ALA LEU VAL ASP ALA PHE SER
SEQRES  32 B  576  ARG GLN PRO ALA GLY ARG ILE GLY GLY GLY ARG ASN ILE
SEQRES  33 B  576  ASP HIS HIS ILE LEU HIS VAL ALA VAL ASP VAL ILE LYS
SEQRES  34 B  576  GLU SER ARG VAL LEU ARG LEU GLN PRO PHE ASN GLU TYR
SEQRES  35 B  576  ARG LYS ARG PHE GLY MET LYS PRO TYR THR SER PHE GLN
SEQRES  36 B  576  GLU LEU THR GLY GLU LYS GLU MET ALA ALA GLU LEU GLU
SEQRES  37 B  576  GLU LEU TYR GLY ASP ILE ASP ALA LEU GLU PHE TYR PRO
SEQRES  38 B  576  GLY LEU LEU LEU GLU LYS CYS HIS PRO ASN SER ILE PHE
SEQRES  39 B  576  GLY GLU SER MET ILE GLU MET GLY ALA PRO PHE 0AH LEU
SEQRES  40 B  576  LYS GLY LEU LEU GLY ASN PRO ILE CYS SER PRO GLU TYR
SEQRES  41 B  576  TRP LYS ALA SER THR PHE GLY GLY GLU VAL GLY PHE ASN
SEQRES  42 B  576  LEU VAL LYS THR ALA THR LEU LYS LYS LEU VAL CYS LEU
SEQRES  43 B  576  ASN THR LYS THR CYS PRO TYR VAL SER PHE HIS VAL PRO
SEQRES  44 B  576  ASP PRO ARG GLN GLU ASP ARG PRO GLY VAL GLU ARG PRO
SEQRES  45 B  576  PRO THR GLU LEU
MODRES 1PTH ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 1PTH ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 1PTH ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 1PTH ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 1PTH ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 1PTH ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 1PTH 0AH A  530  SER  O-(BROMOACETYL)-L-SERINE
MODRES 1PTH 0AH B  530  SER  O-(BROMOACETYL)-L-SERINE
HET    0AH  A 530      10
HET    0AH  B 530      10
HET    NAG  A 661      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 681      14
HET    BOG  A 702      20
HET    NAG  B 661      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 681      14
HET    BOG  B 702      20
HET    HEM  A 601      43
HET    SAL  A 710      10
HET    HEM  B 602      43
HET    SAL  B 711      10
HETNAM     0AH O-(BROMOACETYL)-L-SERINE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     SAL 2-HYDROXYBENZOIC ACID
HETSYN     HEM HEME
HETSYN     SAL SALICYLIC ACID
FORMUL   1  0AH    2(C5 H8 BR N O4)
FORMUL   3  NAG    8(C8 H15 N O6)
FORMUL   6  BOG    2(C14 H28 O6)
FORMUL  11  HEM    2(C34 H32 FE N4 O4)
FORMUL  12  SAL    2(C7 H6 O3)
FORMUL  15  HOH   *(H2 O)
HELIX    1   1 PRO A   35  TYR A   38  5                                   4
HELIX    2   2 ILE A   74  LEU A   82  1                                   9
HELIX    3   3 PRO A   86  THR A   94  1                                   9
HELIX    4   4 ARG A   97  ALA A  105  1                                   9
HELIX    5   5 ILE A  108  LEU A  123  1                                  16
HELIX    6   6 TRP A  139  SER A  143  1                                   5
HELIX    7   7 ALA A  174  PHE A  181  1                                   8
HELIX    8   8 LEU A  196  GLN A  208  1                                  13
HELIX    9   9 GLY A  231  TYR A  234  1                                   4
HELIX   10  10 LEU A  238  LEU A  244  1                                   7
HELIX   11  11 PRO A  281  SER A  283  5                                   3
HELIX   12  12 GLU A  290  GLY A  293  5                                   4
HELIX   13  13 PRO A  296  GLU A  319  1                                  24
HELIX   14  14 ASP A  325  GLU A  346  1                                  22
HELIX   15  15 TYR A  348  SER A  353  1                                   6
HELIX   16  16 PRO A  363  LEU A  366  5                                   4
HELIX   17  17 MET A  379  LEU A  384  1                                   6
HELIX   18  18 HIS A  388  LEU A  390  5                                   3
HELIX   19  19 TYR A  404  PHE A  407  1                                   4
HELIX   20  20 MET A  413  TYR A  417  1                                   5
HELIX   21  21 VAL A  419  ARG A  428  1                                  10
HELIX   22  22 HIS A  442  LEU A  458  5                                  17
HELIX   23  23 PHE A  463  ARG A  469  1                                   7
HELIX   24  24 PHE A  478  LEU A  481  1                                   4
HELIX   25  25 GLU A  486  TYR A  495  1                                  10
HELIX   26  26 ILE A  498  ALA A  500  5                                   3
HELIX   27  27 PHE A  503  LEU A  509  1                                   7
HELIX   28  28 GLU A  520  LEU A  535  1                                  16
HELIX   29  29 PRO A  538  CYS A  540  5                                   3
HELIX   30  30 GLU A  553  THR A  561  1                                   9
HELIX   31  31 LEU A  564  ASN A  571  1                                   8
HELIX   32  32 PRO B   35  TYR B   38  5                                   4
HELIX   33  33 ILE B   74  LEU B   82  1                                   9
HELIX   34  34 PRO B   86  THR B   94  1                                   9
HELIX   35  35 ARG B   97  ALA B  105  1                                   9
HELIX   36  36 ILE B  108  LEU B  123  1                                  16
HELIX   37  37 TRP B  139  SER B  143  1                                   5
HELIX   38  38 ALA B  174  PHE B  181  1                                   8
HELIX   39  39 LEU B  196  GLN B  208  1                                  13
HELIX   40  40 GLY B  231  TYR B  234  1                                   4
HELIX   41  41 LEU B  238  LEU B  244  1                                   7
HELIX   42  42 PRO B  281  SER B  283  5                                   3
HELIX   43  43 GLU B  290  GLY B  293  5                                   4
HELIX   44  44 PRO B  296  GLU B  319  1                                  24
HELIX   45  45 ASP B  325  GLU B  346  1                                  22
HELIX   46  46 TYR B  348  SER B  353  1                                   6
HELIX   47  47 PRO B  363  LEU B  366  5                                   4
HELIX   48  48 MET B  379  LEU B  384  1                                   6
HELIX   49  49 HIS B  388  LEU B  390  5                                   3
HELIX   50  50 TYR B  404  PHE B  407  1                                   4
HELIX   51  51 MET B  413  TYR B  417  1                                   5
HELIX   52  52 VAL B  419  ARG B  428  1                                  10
HELIX   53  53 HIS B  442  LEU B  458  5                                  17
HELIX   54  54 PHE B  463  ARG B  469  1                                   7
HELIX   55  55 PHE B  478  LEU B  481  1                                   4
HELIX   56  56 GLU B  486  TYR B  495  1                                  10
HELIX   57  57 ILE B  498  ALA B  500  5                                   3
HELIX   58  58 PHE B  503  LEU B  509  1                                   7
HELIX   59  59 GLU B  520  LEU B  535  1                                  16
HELIX   60  60 PRO B  538  CYS B  540  5                                   3
HELIX   61  61 GLU B  553  THR B  561  1                                   9
HELIX   62  62 LEU B  564  ASN B  571  1                                   8
SHEET    1   A 2 ILE A  46  ARG A  49  0
SHEET    2   A 2 TYR A  55  ASP A  58 -1  N  ASP A  58   O  ILE A  46
SHEET    1   B 2 GLN A 255  LEU A 257  0
SHEET    2   B 2 GLU A 260  TYR A 262 -1  N  TYR A 262   O  GLN A 255
SHEET    1   C 2 PHE A 395  VAL A 397  0
SHEET    2   C 2 GLN A 400  TYR A 402 -1  N  TYR A 402   O  PHE A 395
SHEET    1   D 2 ILE B  46  ARG B  49  0
SHEET    2   D 2 TYR B  55  ASP B  58 -1  N  ASP B  58   O  ILE B  46
SHEET    1   E 2 GLN B 255  LEU B 257  0
SHEET    2   E 2 GLU B 260  TYR B 262 -1  N  TYR B 262   O  GLN B 255
SHEET    1   F 2 PHE B 395  VAL B 397  0
SHEET    2   F 2 GLN B 400  TYR B 402 -1  N  TYR B 402   O  PHE B 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.01
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.02
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.02
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.04
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.01
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.02
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.02
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.46
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.39
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.46
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.45
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.39
LINK         NE2 HIS A 388                FE   HEM A 601     1555   1555  2.08
LINK         NE2 HIS B 388                FE   HEM B 602     1555   1555  2.08
LINK         C   PHE A 529                 N   0AH A 530     1555   1555  1.33
LINK         C   0AH A 530                 N   LEU A 531     1555   1555  1.33
LINK         C   PHE B 529                 N   0AH B 530     1555   1555  1.33
LINK         C   0AH B 530                 N   LEU B 531     1555   1555  1.33
CISPEP   1 SER A  126    PRO A  127          0        -0.10
CISPEP   2 SER B  126    PRO B  127          0        -0.17
SITE     1 AC1  2 TYR A  55  ASN A  68
SITE     1 AC2  4 GLU A 140  ASN A 144  TYR A 147  NAG A 672
SITE     1 AC3  4 MET A 216  NAG A 671  GLU B 239  TYR B 242
SITE     1 AC4  9 TYR A 402  GLN A 406  ASN A 410  MET A 413
SITE     2 AC4  9 ASP A 416  TYR A 417  GLY B 278  PRO B 280
SITE     3 AC4  9 GLN B 282
SITE     1 AC5  7 ARG A  83  PRO A  84  LEU A 115  VAL A 119
SITE     2 AC5  7 ARG A 120  LEU A 123  GLU A 524
SITE     1 AC6  2 TYR B  55  ASN B  68
SITE     1 AC7  4 GLU B 140  ASN B 144  TYR B 147  NAG B 672
SITE     1 AC8  4 GLU A 239  TYR A 242  MET B 216  NAG B 671
SITE     1 AC9  7 GLN A 282  TYR B 402  GLN B 406  ASN B 410
SITE     2 AC9  7 MET B 413  ASP B 416  TYR B 417
SITE     1 BC1  7 ARG B  83  PRO B  84  LEU B 115  VAL B 119
SITE     2 BC1  7 ARG B 120  LEU B 123  GLU B 524
SITE     1 BC2 17 TYR A 148  ALA A 199  GLN A 203  HIS A 207
SITE     2 BC2 17 PHE A 210  LYS A 211  THR A 212  LEU A 295
SITE     3 BC2 17 ASN A 382  TYR A 385  HIS A 386  TRP A 387
SITE     4 BC2 17 HIS A 388  MET A 391  ILE A 444  VAL A 447
SITE     5 BC2 17 ASP A 450
SITE     1 BC3  6 ARG A 120  VAL A 349  TYR A 355  ALA A 527
SITE     2 BC3  6 0AH A 530  LEU A 531
SITE     1 BC4 17 TYR B 148  ALA B 199  GLN B 203  HIS B 207
SITE     2 BC4 17 PHE B 210  LYS B 211  THR B 212  LEU B 295
SITE     3 BC4 17 ASN B 382  TYR B 385  HIS B 386  TRP B 387
SITE     4 BC4 17 HIS B 388  MET B 391  ILE B 444  VAL B 447
SITE     5 BC4 17 ASP B 450
SITE     1 BC5  6 ARG B 120  VAL B 349  TYR B 355  ALA B 527
SITE     2 BC5  6 0AH B 530  LEU B 531
CRYST1   99.570  209.800  235.000  90.00  90.00  90.00 I 2 2 2      16
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      0.010043  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004766  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004255        0.00000
MTRIX1   1 -0.995361 -0.058518  0.076371       81.63500    1
MTRIX2   1 -0.059985 -0.243176 -0.968126      236.00490    1
MTRIX3   1  0.075225 -0.968215  0.238537      179.50690    1
      
PROCHECK
Go to PROCHECK summary
 References