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PDBsum entry 3ntb

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
3ntb
Jmol
Contents
Protein chains
552 a.a.
Ligands
HEM ×4
NAG ×8
NAG-NAG-NAG ×4
BOG ×6
T1N ×4
Waters ×1109
HEADER    OXIDOREDUCTASE                          03-JUL-10   3NTB
TITLE     STRUCTURE OF 6-METHYLTHIO NAPROXEN ANALOG BOUND TO MCOX-2.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE 2;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: UNP RESIDUES 18-604, CATALYTIC DOMAIN;
COMPND   5 EC: 1.14.99.1;
COMPND   6 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 PGHS-B, MCG_5001, PTGS2;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS    PROSTAGLANDIN H2 SYNTHASE, CYCLOOXYGEANSE-2, NAPROXEN ANALOG,
KEYWDS   2 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.C.DUGGAN,J.MUSEE,M.J.WALTERS,J.M.HARP,J.R.KIEFER,J.A.OATES,
AUTHOR   2 L.J.MARNETT
REVDAT   2   17-NOV-10 3NTB    1       JRNL
REVDAT   1   01-SEP-10 3NTB    0
JRNL        AUTH   K.C.DUGGAN,M.J.WALTERS,J.MUSEE,J.M.HARP,J.R.KIEFER,
JRNL        AUTH 2 J.A.OATES,L.J.MARNETT
JRNL        TITL   MOLECULAR BASIS FOR CYCLOOXYGENASE INHIBITION BY THE
JRNL        TITL 2 NON-STEROIDAL ANTI-INFLAMMATORY DRUG NAPROXEN.
JRNL        REF    J.BIOL.CHEM.                  V. 285 34950 2010
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   20810665
JRNL        DOI    10.1074/JBC.M110.162982
REMARK   2
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 2.27
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.48
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0
REMARK   3   NUMBER OF REFLECTIONS             : 121009
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) : 0.235
REMARK   3   R VALUE            (WORKING SET) : 0.231
REMARK   3   FREE R VALUE                     : 0.266
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 13517
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) : 2.27
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8277
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.35
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880
REMARK   3   BIN FREE R VALUE SET COUNT          : 903
REMARK   3   BIN FREE R VALUE                    : 0.3300
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 17887
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 640
REMARK   3   SOLVENT ATOMS            : 1109
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.13
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -7.04000
REMARK   3    B22 (A**2) : 3.93000
REMARK   3    B33 (A**2) : 3.11000
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): 0.372
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.253
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.186
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.946
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19109 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25994 ; 0.923 ; 2.011
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2203 ; 4.350 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   895 ;35.776 ;24.101
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3102 ;12.967 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;12.904 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2765 ; 0.062 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14532 ; 0.003 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
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): 11029 ; 0.127 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17924 ; 0.251 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8080 ; 0.476 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8070 ; 0.903 ; 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 4
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    33        A   583
REMARK   3    ORIGIN FOR THE GROUP (A): -56.0870  38.1550  -8.9610
REMARK   3    T TENSOR
REMARK   3      T11:   0.3264 T22:   0.0387
REMARK   3      T33:   0.0198 T12:  -0.0074
REMARK   3      T13:  -0.0163 T23:  -0.0014
REMARK   3    L TENSOR
REMARK   3      L11:   1.4879 L22:   0.9510
REMARK   3      L33:   1.1061 L12:   0.1895
REMARK   3      L13:   0.3877 L23:   0.6038
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0242 S12:   0.0091 S13:   0.2332
REMARK   3      S21:  -0.0238 S22:  -0.0921 S23:   0.1439
REMARK   3      S31:  -0.0117 S32:  -0.1470 S33:   0.1163
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    33        B   583
REMARK   3    ORIGIN FOR THE GROUP (A): -17.6540  45.8870  -2.4240
REMARK   3    T TENSOR
REMARK   3      T11:   0.3175 T22:   0.1414
REMARK   3      T33:   0.0372 T12:  -0.0237
REMARK   3      T13:  -0.0057 T23:   0.0229
REMARK   3    L TENSOR
REMARK   3      L11:   1.4821 L22:   0.7908
REMARK   3      L33:   1.2981 L12:   0.1648
REMARK   3      L13:   0.0893 L23:   0.5717
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0416 S12:   0.2356 S13:   0.0606
REMARK   3      S21:  -0.0744 S22:   0.1062 S23:  -0.1175
REMARK   3      S31:  -0.0574 S32:   0.3778 S33:  -0.0647
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C    33        C   583
REMARK   3    ORIGIN FOR THE GROUP (A): -67.3610  21.8430 -63.3420
REMARK   3    T TENSOR
REMARK   3      T11:   0.3343 T22:   0.0595
REMARK   3      T33:  -0.0034 T12:  -0.0059
REMARK   3      T13:   0.0065 T23:  -0.0155
REMARK   3    L TENSOR
REMARK   3      L11:   1.2574 L22:   0.6018
REMARK   3      L33:   1.0506 L12:   0.0152
REMARK   3      L13:   0.0754 L23:  -0.4650
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0154 S12:   0.1523 S13:  -0.0183
REMARK   3      S21:  -0.0366 S22:   0.0468 S23:   0.0667
REMARK   3      S31:   0.0111 S32:  -0.2437 S33:  -0.0314
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D    33        D   583
REMARK   3    ORIGIN FOR THE GROUP (A): -28.8050  28.5340 -70.3040
REMARK   3    T TENSOR
REMARK   3      T11:   0.3330 T22:   0.0180
REMARK   3      T33:  -0.0064 T12:  -0.0064
REMARK   3      T13:   0.0067 T23:  -0.0042
REMARK   3    L TENSOR
REMARK   3      L11:   1.3254 L22:   0.8668
REMARK   3      L33:   0.8917 L12:   0.0627
REMARK   3      L13:  -0.1776 L23:  -0.4364
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0027 S12:   0.0535 S13:  -0.1311
REMARK   3      S21:  -0.0124 S22:  -0.0588 S23:  -0.1049
REMARK   3      S31:   0.0051 S32:   0.1291 S33:   0.0615
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3NTB COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060253.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : CRYSTAL
REMARK 200  OPTICS                         : CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136496
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.480
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8
REMARK 200  DATA REDUNDANCY                : 4.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.12400
REMARK 200   FOR THE DATA SET  : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.50900
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MMP550, MGCL2, PH 8, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 291.15K
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       90.59850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.11250
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.59850
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.11250
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: 12500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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: 12360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     THR A   592
REMARK 465     ILE A   593
REMARK 465     ASN A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     ARG A   614
REMARK 465     SER A   615
REMARK 465     THR A   616
REMARK 465     GLU A   617
REMARK 465     LEU A   618
REMARK 465     GLN B   583
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     THR B   592
REMARK 465     ILE B   593
REMARK 465     ASN B   594
REMARK 465     ALA B   595
REMARK 465     SER B   596
REMARK 465     ALA B   597
REMARK 465     SER B   598
REMARK 465     HIS B   599
REMARK 465     SER B   600
REMARK 465     ARG B   601
REMARK 465     LEU B   602
REMARK 465     ASP B   603
REMARK 465     ASP B   604
REMARK 465     ILE B   605
REMARK 465     ASN B   606
REMARK 465     PRO B   607
REMARK 465     THR B   608
REMARK 465     VAL B   609
REMARK 465     LEU B   610
REMARK 465     ILE B   611
REMARK 465     LYS B   612
REMARK 465     ARG B   613
REMARK 465     ARG B   614
REMARK 465     SER B   615
REMARK 465     THR B   616
REMARK 465     GLU B   617
REMARK 465     LEU B   618
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     THR C   592
REMARK 465     ILE C   593
REMARK 465     ASN C   594
REMARK 465     ALA C   595
REMARK 465     SER C   596
REMARK 465     ALA C   597
REMARK 465     SER C   598
REMARK 465     HIS C   599
REMARK 465     SER C   600
REMARK 465     ARG C   601
REMARK 465     LEU C   602
REMARK 465     ASP C   603
REMARK 465     ASP C   604
REMARK 465     ILE C   605
REMARK 465     ASN C   606
REMARK 465     PRO C   607
REMARK 465     THR C   608
REMARK 465     VAL C   609
REMARK 465     LEU C   610
REMARK 465     ILE C   611
REMARK 465     LYS C   612
REMARK 465     ARG C   613
REMARK 465     ARG C   614
REMARK 465     SER C   615
REMARK 465     THR C   616
REMARK 465     GLU C   617
REMARK 465     LEU C   618
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 465     THR D   592
REMARK 465     ILE D   593
REMARK 465     ASN D   594
REMARK 465     ALA D   595
REMARK 465     SER D   596
REMARK 465     ALA D   597
REMARK 465     SER D   598
REMARK 465     HIS D   599
REMARK 465     SER D   600
REMARK 465     ARG D   601
REMARK 465     LEU D   602
REMARK 465     ASP D   603
REMARK 465     ASP D   604
REMARK 465     ILE D   605
REMARK 465     ASN D   606
REMARK 465     PRO D   607
REMARK 465     THR D   608
REMARK 465     VAL D   609
REMARK 465     LEU D   610
REMARK 465     ILE D   611
REMARK 465     LYS D   612
REMARK 465     ARG D   613
REMARK 465     ARG D   614
REMARK 465     SER D   615
REMARK 465     THR D   616
REMARK 465     GLU D   617
REMARK 465     LEU D   618
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   ND2  ASN B   410     C2   NAG B   681              2.17
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    ARG A  61       18.28     58.96
REMARK 500    THR A 129      -89.69   -116.21
REMARK 500    ARG A 185      -70.09    -88.27
REMARK 500    ASP A 249       19.20     59.44
REMARK 500    TRP A 387       52.97    -98.81
REMARK 500    GLU A 398     -119.80     58.58
REMARK 500    SER A 496      -46.75     73.56
REMARK 500    CYS A 575       64.92     38.19
REMARK 500    THR B 129      -87.88   -120.31
REMARK 500    TRP B 387       54.34    -93.03
REMARK 500    GLU B 398     -113.16     59.63
REMARK 500    TYR B 409        6.84     50.27
REMARK 500    ASN B 439       10.04   -142.30
REMARK 500    SER B 496      -50.22     70.97
REMARK 500    THR C 129      -93.90   -117.26
REMARK 500    ARG C 185      -71.23    -97.62
REMARK 500    HIS C 386       71.25    -69.71
REMARK 500    TRP C 387       51.70    -91.06
REMARK 500    GLU C 398     -117.83     56.03
REMARK 500    TYR C 409        9.24     56.12
REMARK 500    ASN C 410       77.02   -105.38
REMARK 500    ASN C 439       11.43   -140.53
REMARK 500    SER C 496      -50.53     71.00
REMARK 500    THR D 129      -88.05   -117.56
REMARK 500    ARG D 185      -76.64    -92.59
REMARK 500    ASP D 347      -51.89   -127.62
REMARK 500    TRP D 387       50.58    -96.93
REMARK 500    GLU D 398     -117.17     57.12
REMARK 500    ASN D 410       77.51   -119.67
REMARK 500    SER D 496      -56.65     72.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 619  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 388   NE2
REMARK 620 2 HEM C 619   NA   90.7
REMARK 620 3 HEM C 619   NB   88.7  89.0
REMARK 620 4 HEM C 619   NC   92.4 176.7  89.9
REMARK 620 5 HEM C 619   ND   90.9  90.5 179.3  90.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 619  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 619   NA   90.7
REMARK 620 3 HEM A 619   NB   92.7  89.0
REMARK 620 4 HEM A 619   NC   91.8 177.3  89.9
REMARK 620 5 HEM A 619   ND   86.8  90.7 179.4  90.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 619  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 388   NE2
REMARK 620 2 HEM D 619   NA   92.0
REMARK 620 3 HEM D 619   NB   94.4  89.3
REMARK 620 4 HEM D 619   NC   90.6 177.4  90.1
REMARK 620 5 HEM D 619   ND   85.4  90.2 179.5  90.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 619  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 619   NA   91.4
REMARK 620 3 HEM B 619   NB   94.9  89.8
REMARK 620 4 HEM B 619   NC   90.8 177.6  89.2
REMARK 620 5 HEM B 619   ND   84.8  89.5 179.2  91.5
REMARK 620 6 HOH B  19   O   167.6  77.6  90.8 100.3  89.4
REMARK 620 N                    1     2     3     4     5
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 619
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 BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N C 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T1N D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PGH   RELATED DB: PDB
REMARK 900 COX-2:FLURBIPROFEN
REMARK 900 RELATED ID: 1PXX   RELATED DB: PDB
REMARK 900 COX-2:DICLOFENAC
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB
REMARK 900 COX-1:FLURBIPROFEN
REMARK 900 RELATED ID: 3NT1   RELATED DB: PDB
REMARK 900 COX-2:NAPROXEN
DBREF  3NTB A   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604
DBREF  3NTB B   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604
DBREF  3NTB C   33   618  UNP    Q543K3   Q543K3_MOUSE    18    604
DBREF  3NTB D   33   618  UNP    Q543K3   Q543K3_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 3NTB ASN C  410  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN D  410  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN D   68  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN D  144  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN C   68  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 3NTB ASN C  144  ASN  GLYCOSYLATION SITE
HET    HEM  A 619      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    BOG  A 703      20
HET    T1N  A   3      17
HET    BOG  A   7      20
HET    HEM  B 619      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    T1N  B   1      17
HET    BOG  B   6      20
HET    HEM  C 619      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    T1N  C   2      17
HET    BOG  C   5      20
HET    HEM  D 619      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    T1N  D   4      17
HET    BOG  D   8      20
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     T1N (2S)-2-[6-(METHYLSULFANYL)NAPHTHALEN-2-YL]PROPANOIC
HETNAM   2 T1N  ACID
HETSYN     HEM HEME
FORMUL   5  HEM    4(C34 H32 FE N4 O4)
FORMUL   6  NAG    20(C8 H15 N O6)
FORMUL   9  BOG    6(C14 H28 O6)
FORMUL  10  T1N    4(C14 H14 O2 S)
FORMUL  31  HOH   *1109(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  295  HIS A  320  1                                  26
HELIX   13  13 GLY A  324  ASP A  347  1                                  24
HELIX   14  14 ASP A  347  GLY A  354  1                                   8
HELIX   15  15 ASP A  362  PHE A  367  5                                   6
HELIX   16  16 ALA A  378  TYR A  385  1                                   8
HELIX   17  17 TRP A  387  LEU A  391  5                                   5
HELIX   18  18 SER A  403  LEU A  408  1                                   6
HELIX   19  19 ASN A  411  GLN A  429  1                                  19
HELIX   20  20 PRO A  441  ALA A  443  5                                   3
HELIX   21  21 VAL A  444  MET A  458  1                                  15
HELIX   22  22 SER A  462  PHE A  470  1                                   9
HELIX   23  23 SER A  477  GLY A  483  1                                   7
HELIX   24  24 LYS A  485  SER A  496  1                                  12
HELIX   25  25 ASP A  497  MET A  501  5                                   5
HELIX   26  26 GLU A  502  GLU A  510  1                                   9
HELIX   27  27 GLY A  519  GLY A  536  1                                  18
HELIX   28  28 ASN A  537  SER A  541  5                                   5
HELIX   29  29 LYS A  546  GLY A  551  5                                   6
HELIX   30  30 GLY A  552  THR A  561  1                                  10
HELIX   31  31 SER A  563  VAL A  572  1                                  10
HELIX   32  32 GLU B   73  LYS B   83  1                                  11
HELIX   33  33 THR B   85  THR B   94  1                                  10
HELIX   34  34 PHE B   96  ASN B  104  1                                   9
HELIX   35  35 ILE B  105A TYR B  122  1                                  18
HELIX   36  36 SER B  138  ASN B  144  1                                   7
HELIX   37  37 ASP B  173  LEU B  182  1                                  10
HELIX   38  38 ASN B  195  HIS B  207  1                                  13
HELIX   39  39 LEU B  230  GLY B  235  1                                   6
HELIX   40  40 THR B  237  ARG B  245  1                                   9
HELIX   41  41 THR B  265  GLN B  270  1                                   6
HELIX   42  42 PRO B  280  GLN B  284  5                                   5
HELIX   43  43 VAL B  295  HIS B  320  1                                  26
HELIX   44  44 GLY B  324  ASP B  347  1                                  24
HELIX   45  45 ASP B  347  GLY B  354  1                                   8
HELIX   46  46 ASP B  362  PHE B  367  5                                   6
HELIX   47  47 ALA B  378  TYR B  385  1                                   8
HELIX   48  48 HIS B  386  LEU B  391  5                                   6
HELIX   49  49 SER B  403  LEU B  408  1                                   6
HELIX   50  50 ASN B  411  GLY B  418  1                                   8
HELIX   51  51 GLY B  418  GLN B  429  1                                  12
HELIX   52  52 PRO B  441  ALA B  443  5                                   3
HELIX   53  53 VAL B  444  MET B  458  1                                  15
HELIX   54  54 SER B  462  PHE B  470  1                                   9
HELIX   55  55 SER B  477  GLY B  483  1                                   7
HELIX   56  56 LYS B  485  SER B  496  1                                  12
HELIX   57  57 ASP B  497  MET B  501  5                                   5
HELIX   58  58 GLU B  502  GLU B  510  1                                   9
HELIX   59  59 GLY B  519  GLY B  536  1                                  18
HELIX   60  60 ASN B  537  SER B  541  5                                   5
HELIX   61  61 LYS B  546  GLY B  551  5                                   6
HELIX   62  62 GLY B  552  THR B  561  1                                  10
HELIX   63  63 SER B  563  VAL B  572  1                                  10
HELIX   64  64 GLU C   73  LYS C   83  1                                  11
HELIX   65  65 THR C   85  THR C   94  1                                  10
HELIX   66  66 PHE C   96  ASN C  105  1                                  10
HELIX   67  67 ILE C  105A TYR C  122  1                                  18
HELIX   68  68 SER C  138  ASN C  144  1                                   7
HELIX   69  69 ASP C  173  LEU C  182  1                                  10
HELIX   70  70 ASN C  195  HIS C  207  1                                  13
HELIX   71  71 LEU C  230  GLY C  235  1                                   6
HELIX   72  72 THR C  237  ARG C  245  1                                   9
HELIX   73  73 THR C  265  GLN C  270  1                                   6
HELIX   74  74 PRO C  280  GLN C  284  5                                   5
HELIX   75  75 VAL C  291  LEU C  294  5                                   4
HELIX   76  76 VAL C  295  HIS C  320  1                                  26
HELIX   77  77 GLY C  324  ASP C  347  1                                  24
HELIX   78  78 ASP C  347  GLY C  354  1                                   8
HELIX   79  79 ASP C  362  PHE C  367  5                                   6
HELIX   80  80 ALA C  378  TYR C  385  1                                   8
HELIX   81  81 HIS C  386  LEU C  391  5                                   6
HELIX   82  82 SER C  403  LEU C  408  1                                   6
HELIX   83  83 ASN C  411  GLY C  418  1                                   8
HELIX   84  84 GLY C  418  GLN C  429  1                                  12
HELIX   85  85 PRO C  441  ALA C  443  5                                   3
HELIX   86  86 VAL C  444  MET C  458  1                                  15
HELIX   87  87 SER C  462  PHE C  470  1                                   9
HELIX   88  88 SER C  477  GLY C  483  1                                   7
HELIX   89  89 LYS C  485  SER C  496  1                                  12
HELIX   90  90 ASP C  497  MET C  501  5                                   5
HELIX   91  91 GLU C  502  GLU C  510  1                                   9
HELIX   92  92 GLY C  519  GLY C  536  1                                  18
HELIX   93  93 ASN C  537  SER C  541  5                                   5
HELIX   94  94 LYS C  546  GLY C  551  5                                   6
HELIX   95  95 GLY C  552  THR C  561  1                                  10
HELIX   96  96 SER C  563  VAL C  572  1                                  10
HELIX   97  97 ASN D   34  ASN D   39  5                                   6
HELIX   98  98 GLU D   73  LYS D   83  1                                  11
HELIX   99  99 THR D   85  HIS D   95  1                                  11
HELIX  100 100 PHE D   96  ASN D  105  1                                  10
HELIX  101 101 ILE D  105A TYR D  122  1                                  18
HELIX  102 102 SER D  138  ASN D  144  1                                   7
HELIX  103 103 ASP D  173  LEU D  182  1                                  10
HELIX  104 104 ASN D  195  HIS D  207  1                                  13
HELIX  105 105 LEU D  230  GLY D  235  1                                   6
HELIX  106 106 THR D  237  ARG D  245  1                                   9
HELIX  107 107 THR D  265  GLN D  270  1                                   6
HELIX  108 108 PRO D  280  GLN D  284  5                                   5
HELIX  109 109 VAL D  295  HIS D  320  1                                  26
HELIX  110 110 GLY D  324  ASP D  347  1                                  24
HELIX  111 111 ASP D  347  GLY D  354  1                                   8
HELIX  112 112 ASP D  362  PHE D  367  5                                   6
HELIX  113 113 ALA D  378  TYR D  385  1                                   8
HELIX  114 114 TRP D  387  LEU D  391  5                                   5
HELIX  115 115 SER D  403  LEU D  408  1                                   6
HELIX  116 116 ASN D  411  GLY D  418  1                                   8
HELIX  117 117 GLY D  418  GLN D  429  1                                  12
HELIX  118 118 PRO D  441  ALA D  443  5                                   3
HELIX  119 119 VAL D  444  MET D  458  1                                  15
HELIX  120 120 SER D  462  PHE D  470  1                                   9
HELIX  121 121 SER D  477  GLY D  483  1                                   7
HELIX  122 122 LYS D  485  SER D  496  1                                  12
HELIX  123 123 ASP D  497  MET D  501  5                                   5
HELIX  124 124 GLU D  502  GLU D  510  1                                   9
HELIX  125 125 GLY D  519  GLY D  536  1                                  18
HELIX  126 126 ASN D  537  SER D  541  5                                   5
HELIX  127 127 LYS D  546  GLY D  551  5                                   6
HELIX  128 128 GLY D  552  THR D  561  1                                  10
HELIX  129 129 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 TYR A 130  ASN A 131  0
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130
SHEET    1   D 2 GLN A 255  VAL A 256  0
SHEET    2   D 2 VAL A 261  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   E 2 PHE A 395  ILE A 397  0
SHEET    2   E 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395
SHEET    1   F 2 GLU B  46  SER B  49  0
SHEET    2   F 2 TYR B  55  ASP B  58 -1  O  LYS B  56   N  MET B  48
SHEET    1   G 2 PHE B  64  TYR B  65  0
SHEET    2   G 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65
SHEET    1   H 2 TYR B 130  ASN B 131  0
SHEET    2   H 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130
SHEET    1   I 2 GLN B 255  ILE B 257  0
SHEET    2   I 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255
SHEET    1   J 2 PHE B 395  ILE B 397  0
SHEET    2   J 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395
SHEET    1   K 2 GLU C  46  SER C  49  0
SHEET    2   K 2 TYR C  55  ASP C  58 -1  O  ASP C  58   N  GLU C  46
SHEET    1   L 2 PHE C  64  TYR C  65  0
SHEET    2   L 2 THR C  71  PRO C  72 -1  O  THR C  71   N  TYR C  65
SHEET    1   M 2 TYR C 130  ASN C 131  0
SHEET    2   M 2 THR C 149  ARG C 150 -1  O  ARG C 150   N  TYR C 130
SHEET    1   N 2 GLN C 255  ILE C 257  0
SHEET    2   N 2 GLU C 260  TYR C 262 -1  O  TYR C 262   N  GLN C 255
SHEET    1   O 2 PHE C 395  ILE C 397  0
SHEET    2   O 2 GLN C 400  TYR C 402 -1  O  TYR C 402   N  PHE C 395
SHEET    1   P 2 GLU D  46  SER D  49  0
SHEET    2   P 2 TYR D  55  ASP D  58 -1  O  LYS D  56   N  MET D  48
SHEET    1   Q 2 PHE D  64  TYR D  65  0
SHEET    2   Q 2 THR D  71  PRO D  72 -1  O  THR D  71   N  TYR D  65
SHEET    1   R 2 GLN D 255  ILE D 257  0
SHEET    2   R 2 GLU D 260  TYR D 262 -1  O  TYR D 262   N  GLN D 255
SHEET    1   S 2 PHE D 395  ILE D 397  0
SHEET    2   S 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  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.04
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
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  2.04
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03
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  2.03
SSBOND  14 CYS C   59    CYS C   69                          1555   1555  2.04
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.04
SSBOND  16 CYS D   36    CYS D   47                          1555   1555  2.04
SSBOND  17 CYS D   37    CYS D  159                          1555   1555  2.04
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  2.04
LINK         ND2 ASN C 410                 C1  NAG C 681     1555   1555  1.44
LINK         ND2 ASN D 410                 C1  NAG D 681     1555   1555  1.44
LINK         ND2 ASN B 410                 C1  NAG B 681     1555   1555  1.44
LINK         ND2 ASN D  68                 C1  NAG D 661     1555   1555  1.44
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         ND2 ASN B 144                 C1  NAG B 671     1555   1555  1.44
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         ND2 ASN B  68                 C1  NAG B 661     1555   1555  1.45
LINK         ND2 ASN D 144                 C1  NAG D 671     1555   1555  1.45
LINK         ND2 ASN C  68                 C1  NAG C 661     1555   1555  1.45
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.45
LINK         ND2 ASN C 144                 C1  NAG C 671     1555   1555  1.45
LINK         O4  NAG C 671                 C1  NAG C 672     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.45
LINK         O4  NAG D 671                 C1  NAG D 672     1555   1555  1.45
LINK         O4  NAG B 671                 C1  NAG B 672     1555   1555  1.45
LINK         O4  NAG B 672                 C1  NAG B 673     1555   1555  1.45
LINK         O4  NAG C 672                 C1  NAG C 673     1555   1555  1.45
LINK         O4  NAG D 672                 C1  NAG D 673     1555   1555  1.45
LINK         O4  NAG A 672                 C1  NAG A 673     1555   1555  1.46
LINK         NE2 HIS C 388                FE   HEM C 619     1555   1555  2.18
LINK         NE2 HIS A 388                FE   HEM A 619     1555   1555  2.25
LINK         NE2 HIS D 388                FE   HEM D 619     1555   1555  2.30
LINK         NE2 HIS B 388                FE   HEM B 619     1555   1555  2.33
LINK        FE   HEM B 619                 O   HOH B  19     1555   1555  2.35
CISPEP   1 SER A  126    PRO A  127          0        -0.70
CISPEP   2 SER B  126    PRO B  127          0        -0.12
CISPEP   3 SER C  126    PRO C  127          0         0.25
CISPEP   4 SER D  126    PRO D  127          0        -0.72
SITE     1 AC1 17 HOH A  10  ALA A 199  PHE A 200  ALA A 202
SITE     2 AC1 17 GLN A 203  HIS A 207  PHE A 210  LYS A 211
SITE     3 AC1 17 THR A 212  HIS A 214  VAL A 295  ASN A 382
SITE     4 AC1 17 TYR A 385  HIS A 386  HIS A 388  LEU A 391
SITE     5 AC1 17 VAL A 447
SITE     1 AC2  5 TYR A  55  GLU A  67  ASN A  68  HOH A4050
SITE     2 AC2  5 HOH A4063
SITE     1 AC3  8 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC3  8 NAG A 672  HOH A4017  HOH A4298  HOH A4799
SITE     1 AC4  3 ARG A 216  NAG A 671  NAG A 673
SITE     1 AC5  2 NAG A 672  HOH A4059
SITE     1 AC6  4 GLN A 406  ASN A 410  SER A 412  ILE A 413
SITE     1 AC7 10 GLU A 179  ARG A 184  ARG A 185  ILE A 442
SITE     2 AC7 10 GLN A 445  ARG B 184  ARG B 185  ARG B 438
SITE     3 AC7 10 GLU B 486  GLU B 490
SITE     1 AC8  9 ARG A 120  VAL A 349  LEU A 352  TYR A 355
SITE     2 AC8  9 TYR A 385  TRP A 387  VAL A 523  ALA A 527
SITE     3 AC8  9 LEU A 531
SITE     1 AC9  5 LYS A  83  PRO A  84  VAL A  89  SER A 119
SITE     2 AC9  5 ARG A 120
SITE     1 BC1 16 HOH B  19  ALA B 199  ALA B 202  GLN B 203
SITE     2 BC1 16 HIS B 207  PHE B 210  THR B 212  HIS B 214
SITE     3 BC1 16 VAL B 295  ASN B 382  TYR B 385  HIS B 386
SITE     4 BC1 16 HIS B 388  LEU B 391  LEU B 408  VAL B 447
SITE     1 BC2  5 TYR B  55  GLU B  67  ASN B  68  HOH B4018
SITE     2 BC2  5 HOH B4422
SITE     1 BC3  7 GLU B 140  ASN B 144  TYR B 147  ARG B 216
SITE     2 BC3  7 NAG B 672  HOH B4045  HOH B4370
SITE     1 BC4  4 ASP A 239  ARG B 216  NAG B 671  NAG B 673
SITE     1 BC5  1 NAG B 672
SITE     1 BC6  6 TYR B 402  GLN B 406  TYR B 409  ASN B 410
SITE     2 BC6  6 ILE B 413  HOH B4700
SITE     1 BC7  9 ARG B 120  VAL B 349  TYR B 355  TYR B 385
SITE     2 BC7  9 TRP B 387  VAL B 523  GLY B 526  ALA B 527
SITE     3 BC7  9 LEU B 531
SITE     1 BC8  7 LYS B  83  PRO B  84  PRO B  86  TYR B 115
SITE     2 BC8  7 SER B 119  ARG B 120  LEU B 123
SITE     1 BC9 17 ALA C 199  PHE C 200  ALA C 202  GLN C 203
SITE     2 BC9 17 HIS C 207  PHE C 210  THR C 212  HIS C 214
SITE     3 BC9 17 VAL C 295  ASN C 382  TYR C 385  HIS C 386
SITE     4 BC9 17 HIS C 388  LEU C 391  LEU C 408  ALA C 450
SITE     5 BC9 17 HOH C4061
SITE     1 CC1  4 TYR C  55  GLU C  67  ASN C  68  HOH C4349
SITE     1 CC2  7 ASN C 144  TYR C 147  ARG C 216  NAG C 672
SITE     2 CC2  7 HOH C4085  HOH C4331  HOH C4974
SITE     1 CC3  3 ARG C 216  NAG C 671  NAG C 673
SITE     1 CC4  1 NAG C 672
SITE     1 CC5  6 TYR C 402  GLN C 406  ASN C 410  SER C 412
SITE     2 CC5  6 ILE C 413  HOH C4055
SITE     1 CC6  8 VAL C 116  ARG C 120  VAL C 349  TYR C 355
SITE     2 CC6  8 TYR C 385  TRP C 387  VAL C 523  ALA C 527
SITE     1 CC7  4 LYS C  83  PRO C  84  SER C 119  ARG C 120
SITE     1 CC8 16 ALA D 199  PHE D 200  ALA D 202  GLN D 203
SITE     2 CC8 16 HIS D 207  PHE D 210  LYS D 211  THR D 212
SITE     3 CC8 16 HIS D 214  VAL D 295  ASN D 382  TYR D 385
SITE     4 CC8 16 HIS D 386  HIS D 388  LEU D 391  LEU D 408
SITE     1 CC9  5 TYR D  55  GLU D  67  ASN D  68  HOH D 654
SITE     2 CC9  5 HOH D 689
SITE     1 DC1  9 LEU C 238  GLU D 140  ASN D 144  TYR D 147
SITE     2 DC1  9 ARG D 216  HOH D 640  NAG D 672  HOH D4013
SITE     3 DC1  9 HOH D4295
SITE     1 DC2  3 ARG D 216  NAG D 671  NAG D 673
SITE     1 DC3  1 NAG D 672
SITE     1 DC4  8 GLN D 406  ASN D 410  SER D 412  ILE D 413
SITE     2 DC4  8 GLU D 416  HOH D 670  HOH D 688  HOH D4821
SITE     1 DC5 11 GLU C 179  LYS C 180  ARG C 184  ARG C 185
SITE     2 DC5 11 ARG C 438  GLU C 486  GLU C 490  GLU D 179
SITE     3 DC5 11 ARG D 185  ILE D 442  GLN D 445
SITE     1 DC6  7 ARG D 120  VAL D 349  TYR D 355  TYR D 385
SITE     2 DC6  7 TRP D 387  ALA D 527  LEU D 531
SITE     1 DC7  7 LYS D  83  PRO D  84  PRO D  86  SER D 119
SITE     2 DC7  7 ARG D 120  LEU D 123  GLU D 524
CRYST1  181.197  134.225  121.990  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      0.005519  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007450  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008197        0.00000
      
PROCHECK
Go to PROCHECK summary
 References