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PDBsum entry 3ln0

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3ln0
Jmol
Contents
Protein chains
552 a.a.
Ligands
HEM ×4
NAG ×8
NAG-NAG-NAG ×4
52B ×4
BOG ×2
Waters ×1147
HEADER    OXIDOREDUCTASE                          01-FEB-10   3LN0
TITLE     STRUCTURE OF COMPOUND 5C-S BOUND AT THE ACTIVE SITE OF COX-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, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   8 2;
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: COX-2, COX2, PGHS-B, PROSTAGLANDIN H2 SYNTHASE 2, PTGS2,
SOURCE   6 TIS10;
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    COX2, COX-2, PGH2S-2, CYCLOOXYGENASE-2, DIOXYGENASE, DISULFIDE BOND,
KEYWDS   2 ENDOPLASMIC RETICULUM, FATTY ACID BIOSYNTHESIS, GLYCOPROTEIN, HEME,
KEYWDS   3 IRON, LIPID SYNTHESIS, MEMBRANE, METAL-BINDING, MICROSOME,
KEYWDS   4 OXIDOREDUCTASE, PEROXIDASE, PHOSPHOPROTEIN, PROSTAGLANDIN
KEYWDS   5 BIOSYNTHESIS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.R.KIEFER,R.G.KURUMBAIL,W.C.STALLINGS,J.L.PAWLITZ
REVDAT   2   01-DEC-10 3LN0    1       JRNL
REVDAT   1   27-OCT-10 3LN0    0
JRNL        AUTH   J.L.WANG,D.LIMBURG,M.J.GRANETO,J.SPRINGER,J.R.HAMPER,S.LIAO,
JRNL        AUTH 2 J.L.PAWLITZ,R.G.KURUMBAIL,T.MAZIASZ,J.J.TALLEY,J.R.KIEFER,
JRNL        AUTH 3 J.CARTER
JRNL        TITL   THE NOVEL BENZOPYRAN CLASS OF SELECTIVE CYCLOOXYGENASE-2
JRNL        TITL 2 INHIBITORS. PART 2: THE SECOND CLINICAL CANDIDATE HAVING A
JRNL        TITL 3 SHORTER AND FAVORABLE HUMAN HALF-LIFE.
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  7159 2010
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   20709553
JRNL        DOI    10.1016/J.BMCL.2010.07.054
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0067
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.5
REMARK   3   NUMBER OF REFLECTIONS             : 115927
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212
REMARK   3   R VALUE            (WORKING SET) : 0.209
REMARK   3   FREE R VALUE                     : 0.238
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 12935
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7800
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.21
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790
REMARK   3   BIN FREE R VALUE SET COUNT          : 844
REMARK   3   BIN FREE R VALUE                    : 0.3190
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 17896
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 568
REMARK   3   SOLVENT ATOMS            : 1147
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.78
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.27000
REMARK   3    B22 (A**2) : 1.73000
REMARK   3    B33 (A**2) : 0.53000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.366
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.237
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.148
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.916
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19047 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A): 13014 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25931 ; 1.137 ; 2.008
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 31529 ; 0.780 ; 3.003
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2203 ; 5.156 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   896 ;40.284 ;24.107
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3104 ;17.516 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;19.290 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2746 ; 0.071 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20797 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  3835 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 11035 ; 0.428 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4416 ; 0.080 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17933 ; 0.859 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8012 ; 1.381 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7998 ; 2.387 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B C D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A     25       A     550      1
REMARK   3           1     B     25       B     550      1
REMARK   3           1     C     25       C     550      1
REMARK   3           1     D     25       D     550      1
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):   7326 ;  0.02 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):   7326 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    C    (A):   7326 ;  0.02 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    D    (A):   7326 ;  0.02 ;  0.05
REMARK   3   TIGHT THERMAL      1    A (A**2):   7326 ;  0.05 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):   7326 ;  0.05 ;  0.50
REMARK   3   TIGHT THERMAL      1    C (A**2):   7326 ;  0.05 ;  0.50
REMARK   3   TIGHT THERMAL      1    D (A**2):   7326 ;  0.06 ;  0.50
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3LN0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-MAY-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 144570
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08800
REMARK 200   FOR THE DATA SET  : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.36600
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
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       90.50750
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.60050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.50750
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.60050
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: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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   570
REMARK 465     PRO A   571
REMARK 465     GLN A   572
REMARK 465     PRO A   573
REMARK 465     THR A   574
REMARK 465     LYS A   575
REMARK 465     THR A   576
REMARK 465     ALA A   577
REMARK 465     THR A   578
REMARK 465     ILE A   579
REMARK 465     ASN A   580
REMARK 465     ALA A   581
REMARK 465     SER A   582
REMARK 465     ALA A   583
REMARK 465     SER A   584
REMARK 465     HIS A   585
REMARK 465     SER A   586
REMARK 465     ARG A   587
REMARK 465     LEU A   588
REMARK 465     ASP A   589
REMARK 465     ASP A   590
REMARK 465     ILE A   591
REMARK 465     ASN A   592
REMARK 465     PRO A   593
REMARK 465     THR A   594
REMARK 465     VAL A   595
REMARK 465     LEU A   596
REMARK 465     ILE A   597
REMARK 465     LYS A   598
REMARK 465     ARG A   599
REMARK 465     ARG A   600
REMARK 465     SER A   601
REMARK 465     THR A   602
REMARK 465     GLU A   603
REMARK 465     LEU A   604
REMARK 465     ASP B   570
REMARK 465     PRO B   571
REMARK 465     GLN B   572
REMARK 465     PRO B   573
REMARK 465     THR B   574
REMARK 465     LYS B   575
REMARK 465     THR B   576
REMARK 465     ALA B   577
REMARK 465     THR B   578
REMARK 465     ILE B   579
REMARK 465     ASN B   580
REMARK 465     ALA B   581
REMARK 465     SER B   582
REMARK 465     ALA B   583
REMARK 465     SER B   584
REMARK 465     HIS B   585
REMARK 465     SER B   586
REMARK 465     ARG B   587
REMARK 465     LEU B   588
REMARK 465     ASP B   589
REMARK 465     ASP B   590
REMARK 465     ILE B   591
REMARK 465     ASN B   592
REMARK 465     PRO B   593
REMARK 465     THR B   594
REMARK 465     VAL B   595
REMARK 465     LEU B   596
REMARK 465     ILE B   597
REMARK 465     LYS B   598
REMARK 465     ARG B   599
REMARK 465     ARG B   600
REMARK 465     SER B   601
REMARK 465     THR B   602
REMARK 465     GLU B   603
REMARK 465     LEU B   604
REMARK 465     ASP C   570
REMARK 465     PRO C   571
REMARK 465     GLN C   572
REMARK 465     PRO C   573
REMARK 465     THR C   574
REMARK 465     LYS C   575
REMARK 465     THR C   576
REMARK 465     ALA C   577
REMARK 465     THR C   578
REMARK 465     ILE C   579
REMARK 465     ASN C   580
REMARK 465     ALA C   581
REMARK 465     SER C   582
REMARK 465     ALA C   583
REMARK 465     SER C   584
REMARK 465     HIS C   585
REMARK 465     SER C   586
REMARK 465     ARG C   587
REMARK 465     LEU C   588
REMARK 465     ASP C   589
REMARK 465     ASP C   590
REMARK 465     ILE C   591
REMARK 465     ASN C   592
REMARK 465     PRO C   593
REMARK 465     THR C   594
REMARK 465     VAL C   595
REMARK 465     LEU C   596
REMARK 465     ILE C   597
REMARK 465     LYS C   598
REMARK 465     ARG C   599
REMARK 465     ARG C   600
REMARK 465     SER C   601
REMARK 465     THR C   602
REMARK 465     GLU C   603
REMARK 465     LEU C   604
REMARK 465     ASP D   570
REMARK 465     PRO D   571
REMARK 465     GLN D   572
REMARK 465     PRO D   573
REMARK 465     THR D   574
REMARK 465     LYS D   575
REMARK 465     THR D   576
REMARK 465     ALA D   577
REMARK 465     THR D   578
REMARK 465     ILE D   579
REMARK 465     ASN D   580
REMARK 465     ALA D   581
REMARK 465     SER D   582
REMARK 465     ALA D   583
REMARK 465     SER D   584
REMARK 465     HIS D   585
REMARK 465     SER D   586
REMARK 465     ARG D   587
REMARK 465     LEU D   588
REMARK 465     ASP D   589
REMARK 465     ASP D   590
REMARK 465     ILE D   591
REMARK 465     ASN D   592
REMARK 465     PRO D   593
REMARK 465     THR D   594
REMARK 465     VAL D   595
REMARK 465     LEU D   596
REMARK 465     ILE D   597
REMARK 465     LYS D   598
REMARK 465     ARG D   599
REMARK 465     ARG D   600
REMARK 465     SER D   601
REMARK 465     THR D   602
REMARK 465     GLU D   603
REMARK 465     LEU D   604
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    HOH B  4867     O    HOH B  4991              2.17
REMARK 500   O    LEU C   109     NH2  ARG C   455              2.19
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 B  25   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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    PRO A 113      151.44    -49.87
REMARK 500    THR A 115      -89.64   -121.23
REMARK 500    ARG A 171      -69.23    -94.08
REMARK 500    ASP A 235       15.58     59.57
REMARK 500    TRP A 373       44.62    -97.63
REMARK 500    GLU A 384     -120.53     58.27
REMARK 500    TYR A 395       27.36     49.36
REMARK 500    SER A 482      -47.87     71.54
REMARK 500    ARG B  29        8.72     80.38
REMARK 500    ASP B  38       17.67   -140.28
REMARK 500    THR B 115      -91.06   -122.43
REMARK 500    ARG B 171      -72.65    -93.93
REMARK 500    TRP B 373       45.17    -95.57
REMARK 500    GLU B 384     -119.97     57.48
REMARK 500    TYR B 395       27.66     49.65
REMARK 500    SER B 482      -48.31     72.08
REMARK 500    ARG C  46       18.14     59.40
REMARK 500    THR C 115      -90.45   -121.64
REMARK 500    ARG C 171      -72.85    -94.24
REMARK 500    TRP C 373       43.51    -95.78
REMARK 500    GLU C 384     -121.16     56.98
REMARK 500    TYR C 395       28.54     48.77
REMARK 500    SER C 482      -47.63     72.02
REMARK 500    ARG D  29        7.74     80.08
REMARK 500    ASP D  38       17.46   -140.28
REMARK 500    PRO D 113      151.67    -49.87
REMARK 500    THR D 115      -89.62   -122.53
REMARK 500    ARG D 171      -67.93    -94.80
REMARK 500    ASP D 235       14.71     59.72
REMARK 500    TRP D 373       45.88    -96.04
REMARK 500    GLU D 384     -122.06     57.90
REMARK 500    TYR D 395       29.87     48.90
REMARK 500    SER D 482      -48.93     72.10
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 B4751        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH B5225        DISTANCE =  5.21 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 374   NE2
REMARK 620 2 HEM A 605   NA   94.7
REMARK 620 3 HEM A 605   NB   95.6  87.1
REMARK 620 4 HEM A 605   NC   96.1 168.7  88.4
REMARK 620 5 HEM A 605   ND   90.5  91.1 173.7  92.3
REMARK 620 6 HOH A4121   O   176.3  88.8  83.3  80.4  90.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 374   NE2
REMARK 620 2 HEM D 605   NA   93.2
REMARK 620 3 HEM D 605   NB   95.6  83.9
REMARK 620 4 HEM D 605   NC   98.0 168.1  91.2
REMARK 620 5 HEM D 605   ND   90.3  92.2 173.1  91.6
REMARK 620 6 HOH D4018   O   174.2  81.4  81.8  87.2  92.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C4116   O
REMARK 620 2 HEM C 605   NA   87.9
REMARK 620 3 HEM C 605   NB   90.0  87.8
REMARK 620 4 HEM C 605   NC   84.8 172.3  89.4
REMARK 620 5 HEM C 605   ND   86.7  90.7 176.5  91.6
REMARK 620 6 HIS C 374   NE2 177.7  93.7  91.7  93.6  91.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 605  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 374   NE2
REMARK 620 2 HEM B 605   NA   95.9
REMARK 620 3 HEM B 605   NB   93.7  86.9
REMARK 620 4 HEM B 605   NC   94.3 169.5  89.8
REMARK 620 5 HEM B 605   ND   92.4  89.6 173.2  92.6
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 HEM A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 52B A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 52B B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 52B C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 605
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 NAG D 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 52B D 701
DBREF  3LN0 A   18   604  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  3LN0 B   18   604  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  3LN0 C   18   604  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  3LN0 D   18   604  UNP    Q05769   PGH2_MOUSE      18    604
SEQRES   1 A  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 A  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 A  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 A  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 A  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 A  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 A  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 A  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 A  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 A  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 A  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 A  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 A  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 A  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 A  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 A  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 A  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 A  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 A  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 A  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 A  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 A  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 A  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 A  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 A  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 A  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 A  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 A  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 A  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 A  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 A  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 A  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 A  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 A  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 A  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 A  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 A  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 A  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 A  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 A  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 A  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 A  587  GLU LEU
SEQRES   1 B  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 B  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 B  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 B  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 B  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 B  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 B  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 B  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 B  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 B  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 B  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 B  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 B  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 B  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 B  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 B  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 B  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 B  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 B  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 B  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 B  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 B  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 B  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 B  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 B  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 B  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 B  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 B  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 B  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 B  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 B  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 B  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 B  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 B  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 B  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 B  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 B  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 B  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 B  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 B  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 B  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 B  587  GLU LEU
SEQRES   1 C  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 C  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 C  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 C  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 C  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 C  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 C  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 C  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 C  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 C  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 C  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 C  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 C  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 C  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 C  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 C  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 C  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 C  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 C  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 C  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 C  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 C  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 C  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 C  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 C  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 C  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 C  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 C  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 C  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 C  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 C  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 C  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 C  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 C  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 C  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 C  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 C  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 C  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 C  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 C  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 C  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 C  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 C  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 C  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 C  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 C  587  GLU LEU
SEQRES   1 D  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 D  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 D  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 D  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 D  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 D  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 D  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 D  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 D  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 D  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 D  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 D  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 D  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 D  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 D  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 D  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 D  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 D  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 D  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 D  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 D  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 D  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 D  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 D  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 D  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 D  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 D  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 D  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 D  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 D  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 D  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 D  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 D  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 D  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 D  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 D  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 D  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 D  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 D  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 D  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 D  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 D  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 D  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 D  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 D  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 D  587  GLU LEU
MODRES 3LN0 ASN B  396  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN A   53  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN D  396  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN A  396  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN C  396  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN B   53  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN D   53  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN A  130  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN C   53  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN B  130  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN D  130  ASN  GLYCOSYLATION SITE
MODRES 3LN0 ASN C  130  ASN  GLYCOSYLATION SITE
HET    HEM  A 605      43
HET    NAG  A 661      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 673      14
HET    NAG  A 681      14
HET    52B  A 701      19
HET    BOG  A 703      20
HET    HEM  B 605      43
HET    NAG  B 661      14
HET    NAG  B 671      14
HET    NAG  B 672      14
HET    NAG  B 673      14
HET    NAG  B 681      14
HET    52B  B 701      19
HET    HEM  C 605      43
HET    NAG  C 661      14
HET    NAG  C 671      14
HET    NAG  C 672      14
HET    NAG  C 673      14
HET    NAG  C 681      14
HET    52B  C 701      19
HET    HEM  D 605      43
HET    NAG  D 661      14
HET    NAG  D 671      14
HET    NAG  D 672      14
HET    NAG  D 673      14
HET    NAG  D 681      14
HET    BOG  D 703      20
HET    52B  D 701      19
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     52B (2S)-6,8-DICHLORO-2-(TRIFLUOROMETHYL)-2H-CHROMENE-3-
HETNAM   2 52B  CARBOXYLIC ACID
HETNAM     BOG B-OCTYLGLUCOSIDE
HETSYN     HEM HEME
FORMUL   5  HEM    4(C34 H32 FE N4 O4)
FORMUL   6  NAG    20(C8 H15 N O6)
FORMUL   9  52B    4(C11 H5 CL2 F3 O3)
FORMUL  10  BOG    2(C14 H28 O6)
FORMUL  27  HOH   *1147(H2 O)
HELIX    1   1 GLU A   58  LEU A   67  1                                  10
HELIX    2   2 THR A   70  THR A   79  1                                  10
HELIX    3   3 PHE A   81  ASN A   89  1                                   9
HELIX    4   4 ILE A   91  TYR A  108  1                                  18
HELIX    5   5 SER A  124  ASN A  130  1                                   7
HELIX    6   6 ASP A  159  LEU A  168  1                                  10
HELIX    7   7 ASN A  181  HIS A  193  1                                  13
HELIX    8   8 LEU A  216  GLY A  221  1                                   6
HELIX    9   9 THR A  223  ARG A  231  1                                   9
HELIX   10  10 THR A  251  GLN A  256  1                                   6
HELIX   11  11 PRO A  266  GLN A  270  5                                   5
HELIX   12  12 VAL A  277  LEU A  280  5                                   4
HELIX   13  13 VAL A  281  HIS A  306  1                                  26
HELIX   14  14 GLY A  310  ASP A  333  1                                  24
HELIX   15  15 ASP A  333  GLY A  340  1                                   8
HELIX   16  16 ASP A  348  PHE A  353  5                                   6
HELIX   17  17 ALA A  364  TYR A  371  1                                   8
HELIX   18  18 TRP A  373  LEU A  377  5                                   5
HELIX   19  19 SER A  389  LEU A  394  1                                   6
HELIX   20  20 ASN A  397  GLN A  415  1                                  19
HELIX   21  21 PRO A  427  ALA A  429  5                                   3
HELIX   22  22 VAL A  430  MET A  444  1                                  15
HELIX   23  23 SER A  448  PHE A  456  1                                   9
HELIX   24  24 SER A  463  GLY A  469  1                                   7
HELIX   25  25 LYS A  471  SER A  482  1                                  12
HELIX   26  26 ASP A  483  MET A  487  5                                   5
HELIX   27  27 GLU A  488  GLU A  496  1                                   9
HELIX   28  28 GLY A  505  GLY A  522  1                                  18
HELIX   29  29 ASN A  523  SER A  527  5                                   5
HELIX   30  30 LYS A  532  GLY A  537  5                                   6
HELIX   31  31 GLY A  538  THR A  547  1                                  10
HELIX   32  32 SER A  549  VAL A  558  1                                  10
HELIX   33  33 GLU B   58  LEU B   67  1                                  10
HELIX   34  34 THR B   70  THR B   79  1                                  10
HELIX   35  35 PHE B   81  ASN B   89  1                                   9
HELIX   36  36 ILE B   91  TYR B  108  1                                  18
HELIX   37  37 SER B  124  ASN B  130  1                                   7
HELIX   38  38 ASP B  159  LEU B  168  1                                  10
HELIX   39  39 ASN B  181  HIS B  193  1                                  13
HELIX   40  40 LEU B  216  GLY B  221  1                                   6
HELIX   41  41 THR B  223  ARG B  231  1                                   9
HELIX   42  42 THR B  251  GLN B  256  1                                   6
HELIX   43  43 PRO B  266  GLN B  270  5                                   5
HELIX   44  44 VAL B  277  LEU B  280  5                                   4
HELIX   45  45 VAL B  281  HIS B  306  1                                  26
HELIX   46  46 GLY B  310  ASP B  333  1                                  24
HELIX   47  47 ASP B  333  GLY B  340  1                                   8
HELIX   48  48 ASP B  348  PHE B  353  5                                   6
HELIX   49  49 ALA B  364  TYR B  371  1                                   8
HELIX   50  50 TRP B  373  LEU B  377  5                                   5
HELIX   51  51 SER B  389  LEU B  394  1                                   6
HELIX   52  52 ASN B  396  GLN B  415  1                                  20
HELIX   53  53 PRO B  427  ALA B  429  5                                   3
HELIX   54  54 VAL B  430  MET B  444  1                                  15
HELIX   55  55 SER B  448  PHE B  456  1                                   9
HELIX   56  56 SER B  463  GLY B  469  1                                   7
HELIX   57  57 LYS B  471  SER B  482  1                                  12
HELIX   58  58 ASP B  483  MET B  487  5                                   5
HELIX   59  59 GLU B  488  GLU B  496  1                                   9
HELIX   60  60 GLY B  505  GLY B  522  1                                  18
HELIX   61  61 ASN B  523  SER B  527  5                                   5
HELIX   62  62 LYS B  532  GLY B  537  5                                   6
HELIX   63  63 GLY B  538  THR B  547  1                                  10
HELIX   64  64 SER B  549  VAL B  558  1                                  10
HELIX   65  65 GLU C   58  LEU C   67  1                                  10
HELIX   66  66 THR C   70  THR C   79  1                                  10
HELIX   67  67 PHE C   81  ASN C   89  1                                   9
HELIX   68  68 ILE C   91  TYR C  108  1                                  18
HELIX   69  69 SER C  124  ASN C  130  1                                   7
HELIX   70  70 ASP C  159  LEU C  168  1                                  10
HELIX   71  71 ASN C  181  HIS C  193  1                                  13
HELIX   72  72 LEU C  216  GLY C  221  1                                   6
HELIX   73  73 THR C  223  ARG C  231  1                                   9
HELIX   74  74 THR C  251  GLN C  256  1                                   6
HELIX   75  75 PRO C  266  GLN C  270  5                                   5
HELIX   76  76 VAL C  281  HIS C  306  1                                  26
HELIX   77  77 GLY C  310  ASP C  333  1                                  24
HELIX   78  78 ASP C  333  GLY C  340  1                                   8
HELIX   79  79 ASP C  348  PHE C  353  5                                   6
HELIX   80  80 ALA C  364  TYR C  371  1                                   8
HELIX   81  81 TRP C  373  LEU C  377  5                                   5
HELIX   82  82 SER C  389  LEU C  394  1                                   6
HELIX   83  83 ASN C  397  GLN C  415  1                                  19
HELIX   84  84 PRO C  427  ALA C  429  5                                   3
HELIX   85  85 VAL C  430  MET C  444  1                                  15
HELIX   86  86 SER C  448  PHE C  456  1                                   9
HELIX   87  87 SER C  463  GLY C  469  1                                   7
HELIX   88  88 LYS C  471  SER C  482  1                                  12
HELIX   89  89 ASP C  483  MET C  487  5                                   5
HELIX   90  90 GLU C  488  GLU C  496  1                                   9
HELIX   91  91 GLY C  505  GLY C  522  1                                  18
HELIX   92  92 ASN C  523  SER C  527  5                                   5
HELIX   93  93 LYS C  532  GLY C  537  5                                   6
HELIX   94  94 GLY C  538  THR C  547  1                                  10
HELIX   95  95 SER C  549  VAL C  558  1                                  10
HELIX   96  96 GLU D   58  LEU D   67  1                                  10
HELIX   97  97 THR D   70  THR D   79  1                                  10
HELIX   98  98 PHE D   81  ASN D   89  1                                   9
HELIX   99  99 ILE D   91  TYR D  108  1                                  18
HELIX  100 100 SER D  124  ASN D  130  1                                   7
HELIX  101 101 ASP D  159  LEU D  168  1                                  10
HELIX  102 102 ASN D  181  HIS D  193  1                                  13
HELIX  103 103 LEU D  216  GLY D  221  1                                   6
HELIX  104 104 THR D  223  ARG D  231  1                                   9
HELIX  105 105 THR D  251  GLN D  256  1                                   6
HELIX  106 106 PRO D  266  GLN D  270  5                                   5
HELIX  107 107 VAL D  277  LEU D  280  5                                   4
HELIX  108 108 VAL D  281  HIS D  306  1                                  26
HELIX  109 109 GLY D  310  ASP D  333  1                                  24
HELIX  110 110 ASP D  333  GLY D  340  1                                   8
HELIX  111 111 ASP D  348  PHE D  353  5                                   6
HELIX  112 112 ALA D  364  TYR D  371  1                                   8
HELIX  113 113 HIS D  372  LEU D  377  5                                   6
HELIX  114 114 SER D  389  LEU D  394  1                                   6
HELIX  115 115 ASN D  396  GLN D  415  1                                  20
HELIX  116 116 PRO D  427  ALA D  429  5                                   3
HELIX  117 117 VAL D  430  MET D  444  1                                  15
HELIX  118 118 SER D  448  PHE D  456  1                                   9
HELIX  119 119 SER D  463  GLY D  469  1                                   7
HELIX  120 120 LYS D  471  SER D  482  1                                  12
HELIX  121 121 ASP D  483  MET D  487  5                                   5
HELIX  122 122 GLU D  488  GLU D  496  1                                   9
HELIX  123 123 GLY D  505  GLY D  522  1                                  18
HELIX  124 124 ASN D  523  SER D  527  5                                   5
HELIX  125 125 LYS D  532  GLY D  537  5                                   6
HELIX  126 126 GLY D  538  THR D  547  1                                  10
HELIX  127 127 SER D  549  VAL D  558  1                                  10
SHEET    1   A 2 GLU A  31  SER A  34  0
SHEET    2   A 2 TYR A  40  ASP A  43 -1  O  ASP A  43   N  GLU A  31
SHEET    1   B 2 PHE A  49  TYR A  50  0
SHEET    2   B 2 THR A  56  PRO A  57 -1  O  THR A  56   N  TYR A  50
SHEET    1   C 2 TYR A 116  ASN A 117  0
SHEET    2   C 2 THR A 135  ARG A 136 -1  O  ARG A 136   N  TYR A 116
SHEET    1   D 2 GLN A 241  ILE A 243  0
SHEET    2   D 2 GLU A 246  TYR A 248 -1  O  TYR A 248   N  GLN A 241
SHEET    1   E 2 PHE A 381  ILE A 383  0
SHEET    2   E 2 GLN A 386  TYR A 388 -1  O  TYR A 388   N  PHE A 381
SHEET    1   F 2 GLU B  31  SER B  34  0
SHEET    2   F 2 TYR B  40  ASP B  43 -1  O  LYS B  41   N  MET B  33
SHEET    1   G 2 PHE B  49  TYR B  50  0
SHEET    2   G 2 THR B  56  PRO B  57 -1  O  THR B  56   N  TYR B  50
SHEET    1   H 2 GLN B 241  ILE B 243  0
SHEET    2   H 2 GLU B 246  TYR B 248 -1  O  TYR B 248   N  GLN B 241
SHEET    1   I 2 PHE B 381  ILE B 383  0
SHEET    2   I 2 GLN B 386  TYR B 388 -1  O  TYR B 388   N  PHE B 381
SHEET    1   J 2 GLU C  31  SER C  34  0
SHEET    2   J 2 TYR C  40  ASP C  43 -1  O  ASP C  43   N  GLU C  31
SHEET    1   K 2 PHE C  49  TYR C  50  0
SHEET    2   K 2 THR C  56  PRO C  57 -1  O  THR C  56   N  TYR C  50
SHEET    1   L 2 GLN C 241  ILE C 243  0
SHEET    2   L 2 GLU C 246  TYR C 248 -1  O  TYR C 248   N  GLN C 241
SHEET    1   M 2 PHE C 381  ILE C 383  0
SHEET    2   M 2 GLN C 386  TYR C 388 -1  O  TYR C 388   N  PHE C 381
SHEET    1   N 2 GLU D  31  SER D  34  0
SHEET    2   N 2 TYR D  40  ASP D  43 -1  O  ASP D  43   N  GLU D  31
SHEET    1   O 2 PHE D  49  TYR D  50  0
SHEET    2   O 2 THR D  56  PRO D  57 -1  O  THR D  56   N  TYR D  50
SHEET    1   P 2 GLN D 241  ILE D 243  0
SHEET    2   P 2 GLU D 246  TYR D 248 -1  O  TYR D 248   N  GLN D 241
SHEET    1   Q 2 PHE D 381  ILE D 383  0
SHEET    2   Q 2 GLN D 386  TYR D 388 -1  O  TYR D 388   N  PHE D 381
SSBOND   1 CYS A   21    CYS A   32                          1555   1555  2.04
SSBOND   2 CYS A   22    CYS A  145                          1555   1555  2.04
SSBOND   3 CYS A   26    CYS A   42                          1555   1555  2.04
SSBOND   4 CYS A   44    CYS A   54                          1555   1555  2.05
SSBOND   5 CYS A  555    CYS A  561                          1555   1555  2.05
SSBOND   6 CYS B   21    CYS B   32                          1555   1555  2.03
SSBOND   7 CYS B   22    CYS B  145                          1555   1555  2.04
SSBOND   8 CYS B   26    CYS B   42                          1555   1555  2.04
SSBOND   9 CYS B   44    CYS B   54                          1555   1555  2.05
SSBOND  10 CYS B  555    CYS B  561                          1555   1555  2.06
SSBOND  11 CYS C   21    CYS C   32                          1555   1555  2.04
SSBOND  12 CYS C   22    CYS C  145                          1555   1555  2.05
SSBOND  13 CYS C   26    CYS C   42                          1555   1555  2.03
SSBOND  14 CYS C   44    CYS C   54                          1555   1555  2.05
SSBOND  15 CYS C  555    CYS C  561                          1555   1555  2.07
SSBOND  16 CYS D   21    CYS D   32                          1555   1555  2.05
SSBOND  17 CYS D   22    CYS D  145                          1555   1555  2.05
SSBOND  18 CYS D   26    CYS D   42                          1555   1555  2.04
SSBOND  19 CYS D   44    CYS D   54                          1555   1555  2.04
SSBOND  20 CYS D  555    CYS D  561                          1555   1555  2.04
LINK         ND2 ASN B 396                 C1  NAG B 681     1555   1555  1.43
LINK         ND2 ASN A  53                 C1  NAG A 661     1555   1555  1.43
LINK         ND2 ASN D 396                 C1  NAG D 681     1555   1555  1.43
LINK         ND2 ASN A 396                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN C 396                 C1  NAG C 681     1555   1555  1.44
LINK         ND2 ASN B  53                 C1  NAG B 661     1555   1555  1.44
LINK         O4  NAG C 671                 C1  NAG C 672     1555   1555  1.44
LINK         ND2 ASN D  53                 C1  NAG D 661     1555   1555  1.44
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.44
LINK         O4  NAG D 671                 C1  NAG D 672     1555   1555  1.44
LINK         O4  NAG C 672                 C1  NAG C 673     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         ND2 ASN A 130                 C1  NAG A 671     1555   1555  1.45
LINK         O4  NAG D 672                 C1  NAG D 673     1555   1555  1.45
LINK         ND2 ASN C  53                 C1  NAG C 661     1555   1555  1.45
LINK         ND2 ASN B 130                 C1  NAG B 671     1555   1555  1.45
LINK         ND2 ASN D 130                 C1  NAG D 671     1555   1555  1.45
LINK         O4  NAG B 672                 C1  NAG B 673     1555   1555  1.45
LINK         O4  NAG A 672                 C1  NAG A 673     1555   1555  1.46
LINK         ND2 ASN C 130                 C1  NAG C 671     1555   1555  1.46
LINK         NE2 HIS A 374                FE   HEM A 605     1555   1555  2.07
LINK         NE2 HIS D 374                FE   HEM D 605     1555   1555  2.08
LINK        FE   HEM C 605                 O   HOH C4116     1555   1555  2.09
LINK         NE2 HIS B 374                FE   HEM B 605     1555   1555  2.17
LINK         NE2 HIS C 374                FE   HEM C 605     1555   1555  2.20
LINK        FE   HEM A 605                 O   HOH A4121     1555   1555  2.28
LINK        FE   HEM D 605                 O   HOH D4018     1555   1555  2.39
CISPEP   1 SER A  112    PRO A  113          0        -0.82
CISPEP   2 SER B  112    PRO B  113          0        -0.30
CISPEP   3 SER C  112    PRO C  113          0         0.90
CISPEP   4 SER D  112    PRO D  113          0        -0.63
SITE     1 AC1 17 TYR A 134  ALA A 185  PHE A 186  GLN A 189
SITE     2 AC1 17 HIS A 193  PHE A 196  LYS A 197  THR A 198
SITE     3 AC1 17 HIS A 200  VAL A 281  ASN A 368  TYR A 371
SITE     4 AC1 17 HIS A 372  HIS A 374  LEU A 377  VAL A 433
SITE     5 AC1 17 HOH A4121
SITE     1 AC2  4 SER A  23  TYR A  40  GLU A  52  ASN A  53
SITE     1 AC3  8 GLU A 126  ASN A 130  TYR A 133  ARG A 202
SITE     2 AC3  8 NAG A 672  HOH A4017  HOH A4298  HOH A5003
SITE     1 AC4  4 ARG A 202  NAG A 671  NAG A 673  ASP B 225
SITE     1 AC5  1 NAG A 672
SITE     1 AC6  3 GLN A 392  ASN A 396  ILE A 399
SITE     1 AC7 11 VAL A 335  SER A 339  TYR A 341  TYR A 371
SITE     2 AC7 11 TRP A 373  PHE A 504  VAL A 509  GLY A 512
SITE     3 AC7 11 ALA A 513  SER A 516  HOH A4099
SITE     1 AC8  9 GLU A 165  ARG A 171  ILE A 428  GLN A 431
SITE     2 AC8  9 ARG B 170  ARG B 171  ARG B 424  GLU B 472
SITE     3 AC8  9 GLU B 476
SITE     1 AC9 19 TYR B 134  ALA B 185  PHE B 186  ALA B 188
SITE     2 AC9 19 GLN B 189  HIS B 193  PHE B 196  LYS B 197
SITE     3 AC9 19 THR B 198  HIS B 200  VAL B 281  ASN B 368
SITE     4 AC9 19 TYR B 371  HIS B 372  HIS B 374  LEU B 377
SITE     5 AC9 19 VAL B 433  ALA B 436  HOH B4456
SITE     1 BC1  5 SER B  23  TYR B  40  GLU B  52  ASN B  53
SITE     2 BC1  5 HOH B4422
SITE     1 BC2  8 GLU B 126  ASN B 130  TYR B 133  ARG B 202
SITE     2 BC2  8 NAG B 672  HOH B4045  HOH B4370  HOH B4889
SITE     1 BC3  5 ASP A 225  ARG B 202  NAG B 671  NAG B 673
SITE     2 BC3  5 HOH B4882
SITE     1 BC4  1 NAG B 672
SITE     1 BC5  4 TYR B 388  GLN B 392  ASN B 396  ILE B 399
SITE     1 BC6 12 ARG B 106  VAL B 335  SER B 339  TYR B 341
SITE     2 BC6 12 TYR B 371  TRP B 373  PHE B 504  VAL B 509
SITE     3 BC6 12 GLY B 512  ALA B 513  SER B 516  HOH B4699
SITE     1 BC7 19 TYR C 134  ALA C 185  PHE C 186  ALA C 188
SITE     2 BC7 19 GLN C 189  HIS C 193  PHE C 196  LYS C 197
SITE     3 BC7 19 THR C 198  HIS C 200  VAL C 281  ASN C 368
SITE     4 BC7 19 TYR C 371  HIS C 372  HIS C 374  LEU C 377
SITE     5 BC7 19 VAL C 433  ALA C 436  HOH C4116
SITE     1 BC8  4 SER C  23  TYR C  40  GLU C  52  ASN C  53
SITE     1 BC9  8 GLU C 126  ASN C 130  TYR C 133  ARG C 202
SITE     2 BC9  8 NAG C 672  HOH C4085  HOH C4331  HOH C4757
SITE     1 CC1  4 ARG C 202  NAG C 671  NAG C 673  ASP D 225
SITE     1 CC2  1 NAG C 672
SITE     1 CC3  3 GLN C 392  ASN C 396  ILE C 399
SITE     1 CC4 11 VAL C 335  SER C 339  TYR C 341  TYR C 371
SITE     2 CC4 11 TRP C 373  PHE C 504  VAL C 509  GLY C 512
SITE     3 CC4 11 ALA C 513  SER C 516  HOH C4875
SITE     1 CC5 15 ALA D 185  PHE D 186  GLN D 189  HIS D 193
SITE     2 CC5 15 PHE D 196  LYS D 197  THR D 198  HIS D 200
SITE     3 CC5 15 ASN D 368  TYR D 371  HIS D 372  HIS D 374
SITE     4 CC5 15 LEU D 377  VAL D 433  HOH D4018
SITE     1 CC6  3 TYR D  40  GLU D  52  ASN D  53
SITE     1 CC7  7 GLU D 126  ASN D 130  TYR D 133  ARG D 202
SITE     2 CC7  7 NAG D 672  HOH D4013  HOH D4295
SITE     1 CC8  5 ASP C 225  HOH C4575  ARG D 202  NAG D 671
SITE     2 CC8  5 NAG D 673
SITE     1 CC9  1 NAG D 672
SITE     1 DC1  3 GLN D 392  ASN D 396  ILE D 399
SITE     1 DC2 10 ARG C 170  ARG C 171  ARG C 424  GLU C 472
SITE     2 DC2 10 GLU C 476  GLU D 165  ARG D 170  ARG D 171
SITE     3 DC2 10 ILE D 428  GLN D 431
SITE     1 DC3 11 VAL D 335  SER D 339  TYR D 341  TYR D 371
SITE     2 DC3 11 TRP D 373  PHE D 504  VAL D 509  GLY D 512
SITE     3 DC3 11 ALA D 513  SER D 516  HOH D4028
CRYST1  181.015  135.201  124.291  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      0.005524  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007396  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008046        0.00000
      
PROCHECK
Go to PROCHECK summary
 References