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PDBsum entry 3rr3

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase/oxidoreductase inhibitor PDB id
3rr3
Jmol
Contents
Protein chains
552 a.a.
Ligands
NAG ×16
HEM ×4
FLR ×4
BOG ×6
Waters ×241
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 28-APR-11   3RR3
TITLE     STRUCTURE OF (R)-FLURBIPROFEN BOUND TO MCOX-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED
COMPND   5 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-
COMPND   6 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2
COMPND   7 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE
COMPND   8 SYNTHASE 2, TIS10 PROTEIN;
COMPND   9 EC: 1.14.99.1;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    FLURBIPROFEN, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.C.DUGGAN,D.J.HERMANSON,J.MUSEE,J.J.PRUSAKIEWICZ,J.SCHEIB,
AUTHOR   2 B.D.CARTER,S.BANERJEE,J.A.OATES,L.J.MARNETT
REVDAT   2   21-MAR-12 3RR3    1       JRNL
REVDAT   1   09-NOV-11 3RR3    0
JRNL        AUTH   K.C.DUGGAN,D.J.HERMANSON,J.MUSEE,J.J.PRUSAKIEWICZ,
JRNL        AUTH 2 J.L.SCHEIB,B.D.CARTER,S.BANERJEE,J.A.OATES,L.J.MARNETT
JRNL        TITL   (R)-PROFENS ARE SUBSTRATE-SELECTIVE INHIBITORS OF
JRNL        TITL 2 ENDOCANNABINOID OXYGENATION BY COX-2.
JRNL        REF    NAT.CHEM.BIOL.                V.   7   803 2011
JRNL        REFN                   ISSN 1552-4450
JRNL        PMID   22053353
JRNL        DOI    10.1038/NCHEMBIO.663
REMARK   2
REMARK   2 RESOLUTION.    2.84 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.93
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5
REMARK   3   NUMBER OF REFLECTIONS             : 62160
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.244
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040
REMARK   3   FREE R VALUE TEST SET COUNT      : 3131
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 29.9266 -  7.9158    0.93     3084   139  0.2373 0.2655
REMARK   3     2  7.9158 -  6.3023    0.96     3030   161  0.1757 0.2298
REMARK   3     3  6.3023 -  5.5113    0.95     2977   150  0.1857 0.2490
REMARK   3     4  5.5113 -  5.0099    0.96     2961   162  0.1701 0.2158
REMARK   3     5  5.0099 -  4.6522    0.96     2966   161  0.1465 0.1674
REMARK   3     6  4.6522 -  4.3788    0.96     2939   163  0.1406 0.1980
REMARK   3     7  4.3788 -  4.1601    0.95     2918   171  0.1461 0.1984
REMARK   3     8  4.1601 -  3.9795    0.94     2847   162  0.1507 0.1813
REMARK   3     9  3.9795 -  3.8266    0.92     2807   159  0.1544 0.1848
REMARK   3    10  3.8266 -  3.6948    0.90     2758   136  0.1675 0.2097
REMARK   3    11  3.6948 -  3.5795    0.90     2733   147  0.1813 0.2426
REMARK   3    12  3.5795 -  3.4773    0.89     2706   151  0.2066 0.2769
REMARK   3    13  3.4773 -  3.3859    0.87     2646   124  0.2190 0.2794
REMARK   3    14  3.3859 -  3.3034    0.87     2613   140  0.2286 0.2724
REMARK   3    15  3.3034 -  3.2284    0.85     2590   129  0.2399 0.2909
REMARK   3    16  3.2284 -  3.1598    0.84     2531   145  0.2512 0.3442
REMARK   3    17  3.1598 -  3.0966    0.82     2515   132  0.2589 0.3004
REMARK   3    18  3.0966 -  3.0382    0.79     2393   112  0.2714 0.3174
REMARK   3    19  3.0382 -  2.9840    0.79     2352   142  0.2615 0.3537
REMARK   3    20  2.9840 -  2.9335    0.78     2367   107  0.2779 0.2948
REMARK   3    21  2.9335 -  2.8862    0.76     2299   124  0.2938 0.3930
REMARK   3    22  2.8862 -  2.8420    0.66     1999   114  0.3093 0.4076
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.83
REMARK   3   K_SOL              : 0.24
REMARK   3   B_SOL              : 1.87
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.380
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -22.02690
REMARK   3    B22 (A**2) : 23.19750
REMARK   3    B33 (A**2) : -1.17060
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : -0.00000
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.009          19044
REMARK   3   ANGLE     :  1.232          25842
REMARK   3   CHIRALITY :  0.082           2742
REMARK   3   PLANARITY :  0.005           3296
REMARK   3   DIHEDRAL  : 18.525           7070
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : 1
REMARK   3   NCS GROUP : 1
REMARK   3    NCS OPERATOR : 1
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 33:583 )
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 33:583 )
REMARK   3     ATOM PAIRS NUMBER  : 4474
REMARK   3     RMSD               : 0.041
REMARK   3    NCS OPERATOR : 2
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 33:583 )
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 33:583 )
REMARK   3     ATOM PAIRS NUMBER  : 4474
REMARK   3     RMSD               : 0.034
REMARK   3    NCS OPERATOR : 3
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 33:583 )
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 33:583 )
REMARK   3     ATOM PAIRS NUMBER  : 4474
REMARK   3     RMSD               : 0.040
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3RR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065274.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 24-ID-E
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62162
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.842
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.925
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
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) : 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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       90.30750
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.27450
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.30750
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.27450
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 11810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     ASP B   584
REMARK 465     PRO B   585
REMARK 465     GLN B   586
REMARK 465     PRO B   587
REMARK 465     THR B   588
REMARK 465     LYS B   589
REMARK 465     THR B   590
REMARK 465     ALA B   591
REMARK 465     ASP C   584
REMARK 465     PRO C   585
REMARK 465     GLN C   586
REMARK 465     PRO C   587
REMARK 465     THR C   588
REMARK 465     LYS C   589
REMARK 465     THR C   590
REMARK 465     ALA C   591
REMARK 465     ASP D   584
REMARK 465     PRO D   585
REMARK 465     GLN D   586
REMARK 465     PRO D   587
REMARK 465     THR D   588
REMARK 465     LYS D   589
REMARK 465     THR D   590
REMARK 465     ALA D   591
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    THR D   578     O    HOH D   628              1.96
REMARK 500   O4   NAG B   671     O5   NAG B     9              2.08
REMARK 500   O    PHE A   142     NH2  ARG A   376              2.15
REMARK 500   N    GLY C   219     O    HOH C   619              2.19
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    ASN A  34      108.28    -47.78
REMARK 500    ARG A  44        4.91     83.92
REMARK 500    THR A  50       54.58   -119.58
REMARK 500    TYR A 130      132.22     51.84
REMARK 500    SER A 138      142.47     36.44
REMARK 500    LEU A 183      154.53    -49.93
REMARK 500    ARG A 185      -75.93    -89.37
REMARK 500    ASN A 195     -162.75   -103.94
REMARK 500    ALA A 286      -67.63    -96.31
REMARK 500    VAL A 287      -42.31     59.30
REMARK 500    ASP A 347      -53.74   -120.67
REMARK 500    TRP A 387       47.81    -89.42
REMARK 500    GLU A 398      117.03     -1.72
REMARK 500    ASP A 399      -63.45    118.54
REMARK 500    TYR A 409       34.98     38.57
REMARK 500    PHE A 422      -69.10    125.92
REMARK 500    SER A 496      -37.14     82.50
REMARK 500    ASP A 499        2.14    -69.63
REMARK 500    PRO A 514      -95.94    -22.46
REMARK 500    ASP A 515       43.88    -98.75
REMARK 500    ASN B  34      108.51    -48.63
REMARK 500    ARG B  44        4.87     84.00
REMARK 500    ARG B  61       14.81     59.61
REMARK 500    TYR B 130      133.22     49.81
REMARK 500    SER B 138      145.23     36.19
REMARK 500    ARG B 185      -76.18    -88.88
REMARK 500    ASN B 195     -165.00   -104.55
REMARK 500    ALA B 286      -64.92    -95.27
REMARK 500    VAL B 287      -40.90     56.72
REMARK 500    TRP B 387       46.92    -90.76
REMARK 500    GLU B 398      116.29     -4.73
REMARK 500    ASP B 399      -60.94    120.34
REMARK 500    TYR B 409       34.84     38.75
REMARK 500    ASN B 410       76.40   -119.98
REMARK 500    PHE B 422      -67.31    126.29
REMARK 500    SER B 496      -37.29     80.24
REMARK 500    ASP B 499        1.71    -69.08
REMARK 500    PRO B 514      -97.04    -22.73
REMARK 500    ASP B 515       44.61    -99.43
REMARK 500    ASN C  34      109.83    -48.10
REMARK 500    ARG C  44        3.80     83.41
REMARK 500    ARG C  61       13.39     57.73
REMARK 500    TYR C 130      133.75     52.39
REMARK 500    SER C 138      143.05     35.72
REMARK 500    PRO C 172      150.92    -48.80
REMARK 500    ARG C 185      -76.11    -89.15
REMARK 500    ASN C 195     -163.94   -106.16
REMARK 500    ALA C 286      -64.63    -96.28
REMARK 500    VAL C 287      -40.35     54.28
REMARK 500    ASP C 347      -54.74   -121.41
REMARK 500
REMARK 500 THIS ENTRY HAS      81 RAMACHANDRAN OUTLIERS.
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 B 287        24.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A  12        DISTANCE =  6.55 ANGSTROMS
REMARK 525    HOH A 593        DISTANCE =  6.71 ANGSTROMS
REMARK 525    HOH A 609        DISTANCE =  6.87 ANGSTROMS
REMARK 525    HOH A 623        DISTANCE =  6.33 ANGSTROMS
REMARK 525    HOH A 624        DISTANCE =  6.55 ANGSTROMS
REMARK 525    HOH A 629        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH A 631        DISTANCE =  5.59 ANGSTROMS
REMARK 525    HOH A 634        DISTANCE =  6.05 ANGSTROMS
REMARK 525    HOH A 638        DISTANCE =  6.80 ANGSTROMS
REMARK 525    HOH A 640        DISTANCE =  8.20 ANGSTROMS
REMARK 525    HOH B  30        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH B 596        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH B 597        DISTANCE =  9.90 ANGSTROMS
REMARK 525    HOH B 601        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH B 603        DISTANCE =  6.86 ANGSTROMS
REMARK 525    HOH B 604        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH B 605        DISTANCE =  9.09 ANGSTROMS
REMARK 525    HOH B 621        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH B 643        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH C 592        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH C 596        DISTANCE =  8.01 ANGSTROMS
REMARK 525    HOH C 597        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH C 598        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH C 616        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH C 636        DISTANCE = 10.32 ANGSTROMS
REMARK 525    HOH C 638        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH D 602        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH D 605        DISTANCE =  8.26 ANGSTROMS
REMARK 525    HOH D 606        DISTANCE =  7.08 ANGSTROMS
REMARK 525    HOH D 636        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH D 643        DISTANCE =  8.60 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NAG A  661
REMARK 610     NAG A  671
REMARK 610     NAG A  681
REMARK 610     NAG A    9
REMARK 610     NAG B  661
REMARK 610     NAG B  671
REMARK 610     NAG B  681
REMARK 610     NAG B    9
REMARK 610     NAG C  661
REMARK 610     NAG C  671
REMARK 610     NAG C  681
REMARK 610     NAG C    9
REMARK 610     NAG D  661
REMARK 610     NAG D  671
REMARK 610     NAG D  681
REMARK 610     NAG D    9
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 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 682   NA   90.7
REMARK 620 3 HEM A 682   NB   96.3  87.5
REMARK 620 4 HEM A 682   NC   98.7 170.3  89.1
REMARK 620 5 HEM A 682   ND   90.7  91.2 172.9  91.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 388   NE2
REMARK 620 2 HEM C 682   NA   90.4
REMARK 620 3 HEM C 682   NB   97.2  87.5
REMARK 620 4 HEM C 682   NC   95.5 173.8  89.9
REMARK 620 5 HEM C 682   ND   87.7  92.6 175.1  89.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 388   NE2
REMARK 620 2 HEM D 682   NA   87.9
REMARK 620 3 HEM D 682   NB   87.7  88.2
REMARK 620 4 HEM D 682   NC   90.9 177.2  89.2
REMARK 620 5 HEM D 682   ND   89.7  91.0 177.4  91.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 682   NA   84.8
REMARK 620 3 HEM B 682   NB   86.0  85.8
REMARK 620 4 HEM B 682   NC   89.3 174.0  92.4
REMARK 620 5 HEM B 682   ND   88.3  91.9 174.0  89.2
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 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR C 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FLR D 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 9
DBREF  3RR3 A   33   591  UNP    Q05769   PGH2_MOUSE      18    577
DBREF  3RR3 B   33   591  UNP    Q05769   PGH2_MOUSE      18    577
DBREF  3RR3 C   33   591  UNP    Q05769   PGH2_MOUSE      18    577
DBREF  3RR3 D   33   591  UNP    Q05769   PGH2_MOUSE      18    577
SEQRES   1 A  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 A  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 A  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 A  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 A  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 A  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 A  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 A  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 A  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 A  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 A  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 A  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 A  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 A  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 A  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 A  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 A  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 A  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 A  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 A  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 A  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 A  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 A  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 A  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 A  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 A  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 A  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 A  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 A  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 A  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 A  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 A  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 A  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 A  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 A  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 A  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 A  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 A  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 A  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 A  560  ALA
SEQRES   1 B  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 B  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 B  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 B  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 B  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 B  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 B  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 B  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 B  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 B  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 B  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 B  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 B  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 B  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 B  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 B  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 B  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 B  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 B  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 B  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 B  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 B  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 B  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 B  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 B  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 B  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 B  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 B  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 B  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 B  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 B  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 B  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 B  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 B  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 B  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 B  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 B  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 B  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 B  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 B  560  ALA
SEQRES   1 C  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 C  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 C  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 C  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 C  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 C  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 C  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 C  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 C  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 C  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 C  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 C  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 C  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 C  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 C  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 C  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 C  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 C  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 C  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 C  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 C  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 C  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 C  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 C  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 C  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 C  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 C  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 C  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 C  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 C  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 C  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 C  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 C  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 C  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 C  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 C  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 C  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 C  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 C  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 C  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 C  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 C  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 C  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 C  560  ALA
SEQRES   1 D  560  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 D  560  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 D  560  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 D  560  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 D  560  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 D  560  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 D  560  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 D  560  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 D  560  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 D  560  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 D  560  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 D  560  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 D  560  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 D  560  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 D  560  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 D  560  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 D  560  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 D  560  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 D  560  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 D  560  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 D  560  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 D  560  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 D  560  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 D  560  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 D  560  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 D  560  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 D  560  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 D  560  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 D  560  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 D  560  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 D  560  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 D  560  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 D  560  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 D  560  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 D  560  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 D  560  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 D  560  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 D  560  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 D  560  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 D  560  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 D  560  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 D  560  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 D  560  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 D  560  ALA
HET    NAG  A 661      14
HET    NAG  A 671      14
HET    NAG  A 681      14
HET    HEM  A 682      43
HET    FLR  A 700      18
HET    BOG  A   3      20
HET    BOG  A   6      20
HET    NAG  A   9      14
HET    NAG  B 661      14
HET    NAG  B 671      14
HET    NAG  B 681      14
HET    HEM  B 682      43
HET    FLR  B 700      18
HET    BOG  B   3      20
HET    NAG  B   9      14
HET    NAG  C 661      14
HET    NAG  C 671      14
HET    NAG  C 681      14
HET    FLR  C 700      18
HET    HEM  C 682      43
HET    BOG  C   3      20
HET    BOG  C   6      20
HET    NAG  C   9      14
HET    NAG  D 661      14
HET    NAG  D 671      14
HET    FLR  D 700      18
HET    NAG  D 681      14
HET    HEM  D 682      43
HET    BOG  D   3      20
HET    NAG  D   9      14
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     FLR (2R)-2-(3-FLUORO-4-PHENYL-PHENYL)PROPANOIC ACID
HETNAM     BOG B-OCTYLGLUCOSIDE
HETSYN     HEM HEME
HETSYN     FLR FLURBIRPROFEN, R-FORM
FORMUL   5  NAG    16(C8 H15 N O6)
FORMUL   8  HEM    4(C34 H32 FE N4 O4)
FORMUL   9  FLR    4(C15 H13 F O2)
FORMUL  10  BOG    6(C14 H28 O6)
FORMUL  35  HOH   *241(H2 O)
HELIX    1   1 GLU A   73  LYS A   83  1                                  11
HELIX    2   2 THR A   85  HIS A   95  1                                  11
HELIX    3   3 PHE A   96  ASN A  104  1                                   9
HELIX    4   4 ILE A  105A TYR A  122  1                                  18
HELIX    5   5 SER A  138  ASN A  144  1                                   7
HELIX    6   6 ASP A  173  LEU A  182  1                                  10
HELIX    7   7 ASN A  195  HIS A  207  1                                  13
HELIX    8   8 LEU A  230  GLY A  235  1                                   6
HELIX    9   9 THR A  237  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  291  LEU A  294  5                                   4
HELIX   13  13 VAL A  295  HIS A  320  1                                  26
HELIX   14  14 GLY A  324  ASP A  347  1                                  24
HELIX   15  15 ASP A  347  GLY A  354  1                                   8
HELIX   16  16 ASP A  362  PHE A  367  5                                   6
HELIX   17  17 ALA A  378  TYR A  385  1                                   8
HELIX   18  18 HIS A  386  LEU A  391  5                                   6
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 ASN A  411  GLY A  418  1                                   8
HELIX   21  21 LEU A  419  GLN A  429  1                                  11
HELIX   22  22 PRO A  441  ALA A  443  5                                   3
HELIX   23  23 VAL A  444  MET A  458  1                                  15
HELIX   24  24 SER A  462  PHE A  470  1                                   9
HELIX   25  25 SER A  477  GLY A  483  1                                   7
HELIX   26  26 LYS A  485  TYR A  495  1                                  11
HELIX   27  27 ASP A  497  MET A  501  5                                   5
HELIX   28  28 GLU A  502  GLU A  510  1                                   9
HELIX   29  29 GLY A  519  GLY A  536  1                                  18
HELIX   30  30 ASN A  537  SER A  541  5                                   5
HELIX   31  31 LYS A  546  GLY A  551  5                                   6
HELIX   32  32 GLY A  552  THR A  561  1                                  10
HELIX   33  33 SER A  563  VAL A  572  1                                  10
HELIX   34  34 GLU B   73  LYS B   83  1                                  11
HELIX   35  35 THR B   85  HIS B   95  1                                  11
HELIX   36  36 PHE B   96  ASN B  104  1                                   9
HELIX   37  37 ILE B  105A TYR B  122  1                                  18
HELIX   38  38 SER B  138  ASN B  144  1                                   7
HELIX   39  39 ASP B  173  LEU B  182  1                                  10
HELIX   40  40 ASN B  195  HIS B  207  1                                  13
HELIX   41  41 LEU B  230  GLY B  235  1                                   6
HELIX   42  42 THR B  237  ARG B  245  1                                   9
HELIX   43  43 THR B  265  GLN B  270  1                                   6
HELIX   44  44 PRO B  280  GLN B  284  5                                   5
HELIX   45  45 VAL B  291  LEU B  294  5                                   4
HELIX   46  46 VAL B  295  HIS B  320  1                                  26
HELIX   47  47 GLY B  324  ASP B  347  1                                  24
HELIX   48  48 ASP B  347  GLY B  354  1                                   8
HELIX   49  49 ASP B  362  PHE B  367  5                                   6
HELIX   50  50 ALA B  378  TYR B  385  1                                   8
HELIX   51  51 HIS B  386  LEU B  391  5                                   6
HELIX   52  52 SER B  403  LEU B  408  1                                   6
HELIX   53  53 ASN B  411  GLY B  418  1                                   8
HELIX   54  54 LEU B  419  GLN B  429  1                                  11
HELIX   55  55 PRO B  441  ALA B  443  5                                   3
HELIX   56  56 VAL B  444  MET B  458  1                                  15
HELIX   57  57 SER B  462  PHE B  470  1                                   9
HELIX   58  58 SER B  477  GLY B  483  1                                   7
HELIX   59  59 LYS B  485  TYR B  495  1                                  11
HELIX   60  60 ASP B  497  MET B  501  5                                   5
HELIX   61  61 GLU B  502  GLU B  510  1                                   9
HELIX   62  62 GLY B  519  GLY B  536  1                                  18
HELIX   63  63 ASN B  537  SER B  541  5                                   5
HELIX   64  64 LYS B  546  GLY B  551  5                                   6
HELIX   65  65 GLY B  552  THR B  561  1                                  10
HELIX   66  66 SER B  563  VAL B  572  1                                  10
HELIX   67  67 GLU C   73  LYS C   83  1                                  11
HELIX   68  68 THR C   85  HIS C   95  1                                  11
HELIX   69  69 PHE C   96  ASN C  104  1                                   9
HELIX   70  70 ILE C  105A TYR C  122  1                                  18
HELIX   71  71 SER C  138  ASN C  144  1                                   7
HELIX   72  72 ASP C  173  LEU C  182  1                                  10
HELIX   73  73 ASN C  195  HIS C  207  1                                  13
HELIX   74  74 LEU C  230  GLY C  235  1                                   6
HELIX   75  75 THR C  237  ARG C  245  1                                   9
HELIX   76  76 THR C  265  GLN C  270  1                                   6
HELIX   77  77 PRO C  280  GLN C  284  5                                   5
HELIX   78  78 VAL C  291  LEU C  294  5                                   4
HELIX   79  79 VAL C  295  HIS C  320  1                                  26
HELIX   80  80 GLY C  324  ASP C  347  1                                  24
HELIX   81  81 ASP C  347  GLY C  354  1                                   8
HELIX   82  82 ASP C  362  PHE C  367  5                                   6
HELIX   83  83 ALA C  378  TYR C  385  1                                   8
HELIX   84  84 HIS C  386  LEU C  391  5                                   6
HELIX   85  85 SER C  403  LEU C  408  1                                   6
HELIX   86  86 ASN C  410  GLY C  418  1                                   9
HELIX   87  87 LEU C  419  GLN C  429  1                                  11
HELIX   88  88 PRO C  441  ALA C  443  5                                   3
HELIX   89  89 VAL C  444  MET C  458  1                                  15
HELIX   90  90 SER C  462  PHE C  470  1                                   9
HELIX   91  91 SER C  477  GLY C  483  1                                   7
HELIX   92  92 LYS C  485  TYR C  495  1                                  11
HELIX   93  93 ASP C  497  MET C  501  5                                   5
HELIX   94  94 GLU C  502  GLU C  510  1                                   9
HELIX   95  95 GLY C  519  GLY C  536  1                                  18
HELIX   96  96 ASN C  537  SER C  541  5                                   5
HELIX   97  97 LYS C  546  GLY C  551  5                                   6
HELIX   98  98 GLY C  552  THR C  561  1                                  10
HELIX   99  99 SER C  563  VAL C  572  1                                  10
HELIX  100 100 GLU D   73  LYS D   83  1                                  11
HELIX  101 101 THR D   85  HIS D   95  1                                  11
HELIX  102 102 PHE D   96  ASN D  104  1                                   9
HELIX  103 103 ILE D  105A TYR D  122  1                                  18
HELIX  104 104 SER D  138  ASN D  144  1                                   7
HELIX  105 105 ASP D  173  LEU D  182  1                                  10
HELIX  106 106 ASN D  195  HIS D  207  1                                  13
HELIX  107 107 LEU D  230  GLY D  235  1                                   6
HELIX  108 108 THR D  237  ARG D  245  1                                   9
HELIX  109 109 THR D  265  GLN D  270  1                                   6
HELIX  110 110 PRO D  280  GLN D  284  5                                   5
HELIX  111 111 VAL D  291  LEU D  294  5                                   4
HELIX  112 112 VAL D  295  HIS D  320  1                                  26
HELIX  113 113 GLY D  324  ASP D  347  1                                  24
HELIX  114 114 ASP D  347  GLY D  354  1                                   8
HELIX  115 115 ASP D  362  PHE D  367  5                                   6
HELIX  116 116 ALA D  378  TYR D  385  1                                   8
HELIX  117 117 HIS D  386  LEU D  391  5                                   6
HELIX  118 118 SER D  403  LEU D  408  1                                   6
HELIX  119 119 ASN D  410  GLY D  418  1                                   9
HELIX  120 120 LEU D  419  GLN D  429  1                                  11
HELIX  121 121 PRO D  441  ALA D  443  5                                   3
HELIX  122 122 VAL D  444  MET D  458  1                                  15
HELIX  123 123 SER D  462  PHE D  470  1                                   9
HELIX  124 124 SER D  477  GLY D  483  1                                   7
HELIX  125 125 LYS D  485  TYR D  495  1                                  11
HELIX  126 126 ASP D  497  MET D  501  5                                   5
HELIX  127 127 GLU D  502  GLU D  510  1                                   9
HELIX  128 128 GLY D  519  GLY D  536  1                                  18
HELIX  129 129 ASN D  537  SER D  541  5                                   5
HELIX  130 130 LYS D  546  GLY D  551  5                                   6
HELIX  131 131 GLY D  552  THR D  561  1                                  10
HELIX  132 132 SER D  563  VAL D  572  1                                  10
SHEET    1   A 2 GLU A  46  SER A  49  0
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46
SHEET    1   B 2 PHE A  64  TYR A  65  0
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65
SHEET    1   C 2 GLN A 255  ILE A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   D 2 PHE A 395  ILE A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   E 2 GLU B  46  SER B  49  0
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46
SHEET    1   F 2 PHE B  64  TYR B  65  0
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   G 2 GLN B 255  ILE B 257  0
SHEET    2   G 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   H 2 PHE B 395  ILE B 397  0
SHEET    2   H 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SHEET    1   I 2 GLU C  46  SER C  49  0
SHEET    2   I 2 TYR C  55  ASP C  58 -1  O  ASP C  58   N  GLU C  46
SHEET    1   J 2 PHE C  64  TYR C  65  0
SHEET    2   J 2 THR C  71  PRO C  72 -1  O  THR C  71   N  TYR C  65
SHEET    1   K 2 GLN C 255  ILE C 257  0
SHEET    2   K 2 GLU C 260  TYR C 262 -1  O  TYR C 262   N  GLN C 255
SHEET    1   L 2 PHE C 395  ILE C 397  0
SHEET    2   L 2 GLN C 400  TYR C 402 -1  O  TYR C 402   N  PHE C 395
SHEET    1   M 2 GLU D  46  SER D  49  0
SHEET    2   M 2 TYR D  55  ASP D  58 -1  O  ASP D  58   N  GLU D  46
SHEET    1   N 2 PHE D  64  TYR D  65  0
SHEET    2   N 2 THR D  71  PRO D  72 -1  O  THR D  71   N  TYR D  65
SHEET    1   O 2 GLN D 255  ILE D 257  0
SHEET    2   O 2 GLU D 260  TYR D 262 -1  O  TYR D 262   N  GLN D 255
SHEET    1   P 2 PHE D 395  ILE D 397  0
SHEET    2   P 2 GLN D 400  TYR D 402 -1  O  TYR D 402   N  PHE D 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.04
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.06
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.05
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.06
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05
SSBOND  11 CYS C   36    CYS C   47                          1555   1555  2.04
SSBOND  12 CYS C   37    CYS C  159                          1555   1555  2.03
SSBOND  13 CYS C   41    CYS C   57                          1555   1555  2.04
SSBOND  14 CYS C   59    CYS C   69                          1555   1555  2.05
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.05
SSBOND  16 CYS D   36    CYS D   47                          1555   1555  2.04
SSBOND  17 CYS D   37    CYS D  159                          1555   1555  2.03
SSBOND  18 CYS D   41    CYS D   57                          1555   1555  2.03
SSBOND  19 CYS D   59    CYS D   69                          1555   1555  2.04
SSBOND  20 CYS D  569    CYS D  575                          1555   1555  2.02
LINK         NE2 HIS A 388                FE   HEM A 682     1555   1555  2.41
LINK         NE2 HIS C 388                FE   HEM C 682     1555   1555  2.50
LINK         NE2 HIS D 388                FE   HEM D 682     1555   1555  2.53
LINK         NE2 HIS B 388                FE   HEM B 682     1555   1555  2.58
CISPEP   1 SER A  126    PRO A  127          0         5.82
CISPEP   2 SER B  126    PRO B  127          0         7.00
CISPEP   3 SER C  126    PRO C  127          0         7.02
CISPEP   4 SER D  126    PRO D  127          0         6.37
SITE     1 AC1  5 HOH A   4  TYR A  55  GLU A  67  ASN A  68
SITE     2 AC1  5 HOH A 592
SITE     1 AC2  5 NAG A   9  GLU A 140  ASN A 144  TYR A 147
SITE     2 AC2  5 ARG A 216
SITE     1 AC3  3 GLN A 406  ASN A 410  SER A 412
SITE     1 AC4 14 TYR A 148  ALA A 199  GLN A 203  HIS A 207
SITE     2 AC4 14 PHE A 210  LYS A 211  THR A 212  HIS A 214
SITE     3 AC4 14 VAL A 295  ASN A 382  TYR A 385  HIS A 386
SITE     4 AC4 14 HIS A 388  LEU A 391
SITE     1 AC5 11 ARG A 120  VAL A 349  LEU A 352  TYR A 355
SITE     2 AC5 11 LEU A 359  TYR A 385  TRP A 387  VAL A 523
SITE     3 AC5 11 GLY A 526  ALA A 527  SER A 530
SITE     1 AC6 12 GLU A 179  ARG A 184  ARG A 185  ARG A 438
SITE     2 AC6 12 GLU A 486  GLU A 490  GLU B 179  LEU B 183
SITE     3 AC6 12 ARG B 184  ARG B 185  ILE B 442  GLN B 445
SITE     1 AC7  6 PRO A  84  TYR A 115  SER A 119  ARG A 120
SITE     2 AC7  6 HOH A 619  HOH A 620
SITE     1 AC8  2 ARG A 216  NAG A 671
SITE     1 AC9  4 TYR B  55  GLU B  67  ASN B  68  HOH B 599
SITE     1 BC1  6 NAG B   9  GLU B 140  ASN B 144  TYR B 147
SITE     2 BC1  6 ARG B 216  HOH B 593
SITE     1 BC2  3 ASN B 410  SER B 412  HOH B 634
SITE     1 BC3 12 ALA B 199  GLN B 203  HIS B 207  PHE B 210
SITE     2 BC3 12 THR B 212  HIS B 214  ASN B 382  TYR B 385
SITE     3 BC3 12 HIS B 386  HIS B 388  LEU B 391  VAL B 447
SITE     1 BC4 11 ARG B 120  VAL B 349  LEU B 352  TYR B 355
SITE     2 BC4 11 LEU B 359  TYR B 385  TRP B 387  VAL B 523
SITE     3 BC4 11 GLY B 526  ALA B 527  SER B 530
SITE     1 BC5  6 LYS B  83  PRO B  84  TYR B 115  SER B 119
SITE     2 BC5  6 ARG B 120  GLU B 524
SITE     1 BC6  3 ARG B 216  HOH B 649  NAG B 671
SITE     1 BC7  8 SER C  38  PRO C  40  TYR C  55  GLU C  67
SITE     2 BC7  8 ASN C  68  HOH C 593  HOH C 594  HOH C 595
SITE     1 BC8  5 NAG C   9  GLU C 140  ASN C 144  TYR C 147
SITE     2 BC8  5 ARG C 216
SITE     1 BC9  4 GLN C 406  ASN C 410  SER C 412  HOH C 633
SITE     1 CC1 11 ARG C 120  VAL C 349  LEU C 352  TYR C 355
SITE     2 CC1 11 LEU C 359  TYR C 385  TRP C 387  VAL C 523
SITE     3 CC1 11 GLY C 526  ALA C 527  SER C 530
SITE     1 CC2 11 ALA C 199  ALA C 202  GLN C 203  HIS C 207
SITE     2 CC2 11 THR C 212  HIS C 214  VAL C 295  ASN C 382
SITE     3 CC2 11 HIS C 386  HIS C 388  LEU C 391
SITE     1 CC3 12 LYS C 180  LEU C 183  ARG C 184  ARG C 185
SITE     2 CC3 12 ARG C 438  ILE C 442  GLU C 486  GLU C 490
SITE     3 CC3 12 GLU D 179  ARG D 184  ARG D 185  ILE D 442
SITE     1 CC4  4 PRO C  84  TYR C 115  SER C 119  GLU C 524
SITE     1 CC5  3 ARG C 216  HOH C 637  NAG C 671
SITE     1 CC6  6 SER D  38  TYR D  55  GLU D  67  ASN D  68
SITE     2 CC6  6 HOH D 603  HOH D 640
SITE     1 CC7  5 NAG D   9  GLU D 140  ASN D 144  TYR D 147
SITE     2 CC7  5 ARG D 216
SITE     1 CC8 11 VAL D 116  ARG D 120  VAL D 349  LEU D 352
SITE     2 CC8 11 TYR D 355  TYR D 385  TRP D 387  VAL D 523
SITE     3 CC8 11 GLY D 526  ALA D 527  SER D 530
SITE     1 CC9  3 ASN D 410  SER D 412  ILE D 413
SITE     1 DC1 13 ALA D 199  GLN D 203  HIS D 207  THR D 212
SITE     2 DC1 13 HIS D 214  ASN D 382  TYR D 385  HIS D 386
SITE     3 DC1 13 TRP D 387  HIS D 388  LEU D 391  VAL D 447
SITE     4 DC1 13 HOH D 642
SITE     1 DC2  7 LYS D  83  PRO D  84  TYR D 115  SER D 119
SITE     2 DC2  7 ARG D 120  LEU D 123  GLU D 524
SITE     1 DC3  2 ARG D 216  NAG D 671
CRYST1  180.615  134.549  122.775  90.00  90.00  90.00 P 21 21 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      0.005537  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007432  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008145        0.00000
      
PROCHECK
Go to PROCHECK summary
 References