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PDBsum entry 2oyu

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Oxidoreductase PDB id
2oyu
Jmol
Contents
Protein chain
553 a.a.
Ligands
NAG-NAG ×2
NAG-NAG-BMA
BOG ×2
IMS
HEM
Waters ×52
HEADER    OXIDOREDUCTASE                          23-FEB-07   2OYU
TITLE     INDOMETHACIN-(S)-ALPHA-ETHYL-ETHANOLAMIDE BOUND TO CYCLOOXYGENASE-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1;
COMPND   3 CHAIN: P;
COMPND   4 SYNONYM: CYCLOOXYGENASE-1, COX-1, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 1, PROSTAGLANDIN H2 SYNTHASE 1, PGH SYNTHASE 1, PGHS-1, PHS 1;
COMPND   6 EC: 1.14.99.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 OTHER_DETAILS: SHEEP VESICULAR GLAND
KEYWDS    COX, PGHS, INDOMETHACIN, NSAID, HEME, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.A.HARMAN,R.M.GARAVITO
REVDAT   4   13-JUL-11 2OYU    1       VERSN
REVDAT   3   24-FEB-09 2OYU    1       VERSN
REVDAT   2   09-OCT-07 2OYU    1       JRNL
REVDAT   1   24-JUL-07 2OYU    0
JRNL        AUTH   C.A.HARMAN,M.V.TURMAN,K.R.KOZAK,L.J.MARNETT,W.L.SMITH,
JRNL        AUTH 2 R.M.GARAVITO
JRNL        TITL   STRUCTURAL BASIS OF ENANTIOSELECTIVE INHIBITION OF
JRNL        TITL 2 CYCLOOXYGENASE-1 BY S-ALPHA-SUBSTITUTED INDOMETHACIN
JRNL        TITL 3 ETHANOLAMIDES.
JRNL        REF    J.BIOL.CHEM.                  V. 282 28096 2007
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   17656360
JRNL        DOI    10.1074/JBC.M701335200
REMARK   2
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 27878
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) : 0.241
REMARK   3   R VALUE            (WORKING SET) : 0.241
REMARK   3   FREE R VALUE                     : 0.292
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1400
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) : 2.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1912
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.55
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3740
REMARK   3   BIN FREE R VALUE SET COUNT          : 88
REMARK   3   BIN FREE R VALUE                    : 0.4150
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4408
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 192
REMARK   3   SOLVENT ATOMS            : 52
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : UNVERIFIED
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.26
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.94000
REMARK   3    B22 (A**2) : 0.94000
REMARK   3    B33 (A**2) : -1.41000
REMARK   3    B12 (A**2) : 0.47000
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): 0.510
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.336
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.352
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.204
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4761 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6509 ; 1.520 ; 2.018
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   552 ; 6.412 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   209 ;38.495 ;22.967
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   703 ;20.021 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.336 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   701 ; 0.094 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3639 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2534 ; 0.243 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3301 ; 0.324 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   183 ; 0.147 ; 0.200
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):    64 ; 0.230 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.213 ; 0.200
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):  2828 ; 0.371 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4472 ; 0.656 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2209 ; 1.005 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2035 ; 1.665 ; 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  : 1
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 :   P    35        P   582
REMARK   3    ORIGIN FOR THE GROUP (A): 245.9604  99.6051 -36.3582
REMARK   3    T TENSOR
REMARK   3      T11:   0.2570 T22:  -0.3506
REMARK   3      T33:  -0.2234 T12:  -0.4447
REMARK   3      T13:  -0.0243 T23:  -0.0164
REMARK   3    L TENSOR
REMARK   3      L11:   1.1297 L22:   0.7273
REMARK   3      L33:   1.6470 L12:  -0.5156
REMARK   3      L13:  -0.0687 L23:   0.1519
REMARK   3    S TENSOR
REMARK   3      S11:   0.0243 S12:   0.2693 S13:  -0.0627
REMARK   3      S21:  -0.0758 S22:  -0.0737 S23:   0.0003
REMARK   3      S31:   0.6082 S32:  -0.3265 S33:   0.0494
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: NULL
REMARK   4
REMARK   4 2OYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-07.
REMARK 100 THE RCSB ID CODE IS RCSB041754.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 32-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 : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28010
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 19.000
REMARK 200  R MERGE                    (I) : 0.09700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1DIY (PROTEIN ONLY)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 67.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM CHLORIDE,
REMARK 280  SODIUM AZIDE, AND BETA-OCTYLGLUCOSIDE, PH 6.5, VAPOR DIFFUSION,
REMARK 280  SITTING DROP, TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
REMARK 290       7555   Y,X,-Z+2/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+1/3
REMARK 290      10555   -Y,-X,-Z+1/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.93200
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.46600
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.69900
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.23300
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.16500
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.93200
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       34.46600
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       17.23300
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       51.69900
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       86.16500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 14490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P
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   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       68.93200
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET P     1
REMARK 465     SER P     2
REMARK 465     ARG P     3
REMARK 465     GLN P     4
REMARK 465     SER P     5
REMARK 465     ILE P     6
REMARK 465     SER P     7
REMARK 465     LEU P     8
REMARK 465     ARG P     9
REMARK 465     PHE P    10
REMARK 465     PRO P    11
REMARK 465     LEU P    12
REMARK 465     LEU P    13
REMARK 465     LEU P    14
REMARK 465     LEU P    15
REMARK 465     LEU P    16
REMARK 465     LEU P    17
REMARK 465     SER P    18
REMARK 465     PRO P    19
REMARK 465     SER P    20
REMARK 465     PRO P    21
REMARK 465     VAL P    22
REMARK 465     PHE P    23
REMARK 465     SER P    24
REMARK 465     ALA P    25
REMARK 465     ASP P    26
REMARK 465     PRO P    27
REMARK 465     GLY P    28
REMARK 465     ALA P    29
REMARK 465     PRO P    30
REMARK 465     ALA P    31
REMARK 465     PRO P   585
REMARK 465     ARG P   586
REMARK 465     GLN P   587
REMARK 465     GLU P   588
REMARK 465     ASP P   589
REMARK 465     ARG P   590
REMARK 465     PRO P   591
REMARK 465     GLY P   592
REMARK 465     VAL P   593
REMARK 465     GLU P   594
REMARK 465     ARG P   595
REMARK 465     PRO P   596
REMARK 465     PRO P   597
REMARK 465     THR P   598
REMARK 465     GLU P   599
REMARK 465     LEU P   600
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG P  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG P  83    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS P 169    CG   CD   CE   NZ
REMARK 470     GLN P 170    CG   CD   OE1  NE2
REMARK 470     ASP P 173    CG   OD1  OD2
REMARK 470     GLU P 175    CG   CD   OE1  OE2
REMARK 470     LYS P 186    CG   CD   CE   NZ
REMARK 470     LYS P 215    CG   CD   CE   NZ
REMARK 470     LYS P 248    CG   CD   CE   NZ
REMARK 470     GLU P 267    CG   CD   OE1  OE2
REMARK 470     GLU P 290    CG   CD   OE1  OE2
REMARK 470     LYS P 317    CG   CD   CE   NZ
REMARK 470     ARG P 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN P 400    CG   CD   OE1  NE2
REMARK 470     GLU P 405    CG   CD   OE1  OE2
REMARK 470     ASP P 416    CG   OD1  OD2
REMARK 470     LYS P 473    CG   CD   CE   NZ
REMARK 470     GLN P 479    CG   CD   OE1  NE2
REMARK 470     LYS P 485    CG   CD   CE   NZ
REMARK 470     GLU P 486    CG   CD   OE1  OE2
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    ASP P  53       22.31   -164.17
REMARK 500    CYS P  69       64.22     69.67
REMARK 500    THR P 129      -80.15   -113.47
REMARK 500    VAL P 145        8.11    -67.77
REMARK 500    PRO P 160      -72.88    -60.13
REMARK 500    PRO P 172      126.01    -39.86
REMARK 500    ASP P 173       99.72    -59.06
REMARK 500    ALA P 174      -63.12    -13.97
REMARK 500    ARG P 185      -90.86    -80.74
REMARK 500    HIS P 204      -72.31    -39.70
REMARK 500    ASP P 249       25.34     48.73
REMARK 500    VAL P 271      137.03   -179.74
REMARK 500    LEU P 272      108.81    -52.38
REMARK 500    ILE P 279       72.29   -119.53
REMARK 500    PRO P 281     -100.82   -103.35
REMARK 500    SER P 283      -42.57     79.12
REMARK 500    GLU P 290       15.44    -66.63
REMARK 500    LEU P 294      -88.28    -62.07
REMARK 500    TYR P 348      -71.07    -55.05
REMARK 500    ASN P 410       98.09    -59.35
REMARK 500    PRO P 430     -150.64    -55.80
REMARK 500    ALA P 431      151.53    178.86
REMARK 500    ASN P 439        7.29   -150.21
REMARK 500    PRO P 583      172.63    -56.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ASP P 584        22.3      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH P 802        DISTANCE =  5.96 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     BOG P  750
REMARK 610     BOG P  751
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 P 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 388   NE2
REMARK 620 2 HEM P 601   NA   77.7
REMARK 620 3 HEM P 601   NB  106.2  91.2
REMARK 620 4 HEM P 601   NC  117.5 163.7  89.9
REMARK 620 5 HEM P 601   ND   83.8  82.3 166.7  93.2
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA P 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG P 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG P 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG P 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMS P 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PGG   RELATED DB: PDB
REMARK 900 INDOMETHACIN BOUND TO COX-1 (TRANS MODEL)
REMARK 900 RELATED ID: 1PGF   RELATED DB: PDB
REMARK 900 INDOMETHACIN BOUND TO COX-1
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB
REMARK 900 FLURIBPROFEN BOUND TO COX-1
REMARK 900 RELATED ID: 1EQE   RELATED DB: PDB
REMARK 900 FLURBIPROFEN BOUND TO COX-1 (HIGHER RESOLUTION)
REMARK 900 RELATED ID: 2OYE   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999
REMARK 999 THERE IS A SEQUENCE CONFLICT IN UNP DATABASE AT RESIDUE 92
REMARK 999 (MET -> LEU).
DBREF  2OYU P    1   600  UNP    P05979   PGH1_SHEEP       1    600
SEQADV 2OYU LEU P   92  UNP  P05979    MET    92 SEE REMARK 999
SEQRES   1 P  600  MET SER ARG GLN SER ILE SER LEU ARG PHE PRO LEU LEU
SEQRES   2 P  600  LEU LEU LEU LEU SER PRO SER PRO VAL PHE SER ALA ASP
SEQRES   3 P  600  PRO GLY ALA PRO ALA PRO VAL ASN PRO CYS CYS TYR TYR
SEQRES   4 P  600  PRO CYS GLN HIS GLN GLY ILE CYS VAL ARG PHE GLY LEU
SEQRES   5 P  600  ASP ARG TYR GLN CYS ASP CYS THR ARG THR GLY TYR SER
SEQRES   6 P  600  GLY PRO ASN CYS THR ILE PRO GLU ILE TRP THR TRP LEU
SEQRES   7 P  600  ARG THR THR LEU ARG PRO SER PRO SER PHE ILE HIS PHE
SEQRES   8 P  600  LEU LEU THR HIS GLY ARG TRP LEU TRP ASP PHE VAL ASN
SEQRES   9 P  600  ALA THR PHE ILE ARG ASP THR LEU MET ARG LEU VAL LEU
SEQRES  10 P  600  THR VAL ARG SER ASN LEU ILE PRO SER PRO PRO THR TYR
SEQRES  11 P  600  ASN ILE ALA HIS ASP TYR ILE SER TRP GLU SER PHE SER
SEQRES  12 P  600  ASN VAL SER TYR TYR THR ARG ILE LEU PRO SER VAL PRO
SEQRES  13 P  600  ARG ASP CYS PRO THR PRO MET GLY THR LYS GLY LYS LYS
SEQRES  14 P  600  GLN LEU PRO ASP ALA GLU PHE LEU SER ARG ARG PHE LEU
SEQRES  15 P  600  LEU ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY THR ASN
SEQRES  16 P  600  LEU MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES  17 P  600  PHE PHE LYS THR SER GLY LYS MET GLY PRO GLY PHE THR
SEQRES  18 P  600  LYS ALA LEU GLY HIS GLY VAL ASP LEU GLY HIS ILE TYR
SEQRES  19 P  600  GLY ASP ASN LEU GLU ARG GLN TYR GLN LEU ARG LEU PHE
SEQRES  20 P  600  LYS ASP GLY LYS LEU LYS TYR GLN MET LEU ASN GLY GLU
SEQRES  21 P  600  VAL TYR PRO PRO SER VAL GLU GLU ALA PRO VAL LEU MET
SEQRES  22 P  600  HIS TYR PRO ARG GLY ILE PRO PRO GLN SER GLN MET ALA
SEQRES  23 P  600  VAL GLY GLN GLU VAL PHE GLY LEU LEU PRO GLY LEU MET
SEQRES  24 P  600  LEU TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES  25 P  600  CYS ASP LEU LEU LYS ALA GLU HIS PRO THR TRP GLY ASP
SEQRES  26 P  600  GLU GLN LEU PHE GLN THR ALA ARG LEU ILE LEU ILE GLY
SEQRES  27 P  600  GLU THR ILE LYS ILE VAL ILE GLU GLU TYR VAL GLN GLN
SEQRES  28 P  600  LEU SER GLY TYR PHE LEU GLN LEU LYS PHE ASP PRO GLU
SEQRES  29 P  600  LEU LEU PHE GLY ALA GLN PHE GLN TYR ARG ASN ARG ILE
SEQRES  30 P  600  ALA MET GLU PHE ASN GLN LEU TYR HIS TRP HIS PRO LEU
SEQRES  31 P  600  MET PRO ASP SER PHE ARG VAL GLY PRO GLN ASP TYR SER
SEQRES  32 P  600  TYR GLU GLN PHE LEU PHE ASN THR SER MET LEU VAL ASP
SEQRES  33 P  600  TYR GLY VAL GLU ALA LEU VAL ASP ALA PHE SER ARG GLN
SEQRES  34 P  600  PRO ALA GLY ARG ILE GLY GLY GLY ARG ASN ILE ASP HIS
SEQRES  35 P  600  HIS ILE LEU HIS VAL ALA VAL ASP VAL ILE LYS GLU SER
SEQRES  36 P  600  ARG VAL LEU ARG LEU GLN PRO PHE ASN GLU TYR ARG LYS
SEQRES  37 P  600  ARG PHE GLY MET LYS PRO TYR THR SER PHE GLN GLU LEU
SEQRES  38 P  600  THR GLY GLU LYS GLU MET ALA ALA GLU LEU GLU GLU LEU
SEQRES  39 P  600  TYR GLY ASP ILE ASP ALA LEU GLU PHE TYR PRO GLY LEU
SEQRES  40 P  600  LEU LEU GLU LYS CYS HIS PRO ASN SER ILE PHE GLY GLU
SEQRES  41 P  600  SER MET ILE GLU MET GLY ALA PRO PHE SER LEU LYS GLY
SEQRES  42 P  600  LEU LEU GLY ASN PRO ILE CYS SER PRO GLU TYR TRP LYS
SEQRES  43 P  600  ALA SER THR PHE GLY GLY GLU VAL GLY PHE ASN LEU VAL
SEQRES  44 P  600  LYS THR ALA THR LEU LYS LYS LEU VAL CYS LEU ASN THR
SEQRES  45 P  600  LYS THR CYS PRO TYR VAL SER PHE HIS VAL PRO ASP PRO
SEQRES  46 P  600  ARG GLN GLU ASP ARG PRO GLY VAL GLU ARG PRO PRO THR
SEQRES  47 P  600  GLU LEU
MODRES 2OYU ASN P   68  ASN  GLYCOSYLATION SITE
MODRES 2OYU ASN P  144  ASN  GLYCOSYLATION SITE
MODRES 2OYU ASN P  410  ASN  GLYCOSYLATION SITE
HET    NAG  P 661      14
HET    NAG  P 662      14
HET    NAG  P 671      14
HET    NAG  P 672      14
HET    BMA  P 673      11
HET    NAG  P 681      14
HET    NAG  P 682      14
HET    BOG  P 750      12
HET    BOG  P 751      12
HET    IMS  P 700      30
HET    HEM  P 601      43
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     IMS 2-[1-(4-CHLOROBENZOYL)-5-METHOXY-2-METHYL-1H-INDOL-3-
HETNAM   2 IMS  YL]-N-[(1S)-1-(HYDROXYMETHYL)PROPYL]ACETAMIDE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN     HEM HEME
FORMUL   2  NAG    6(C8 H15 N O6)
FORMUL   3  BMA    C6 H12 O6
FORMUL   5  BOG    2(C14 H28 O6)
FORMUL   7  IMS    C23 H25 CL N2 O4
FORMUL   8  HEM    C34 H32 FE N4 O4
FORMUL   9  HOH   *52(H2 O)
HELIX    1   1 ASN P   34  TYR P   39  5                                   6
HELIX    2   2 GLU P   73  ARG P   83  1                                  11
HELIX    3   3 SER P   85  THR P   94  1                                  10
HELIX    4   4 GLY P   96  THR P  106  1                                  11
HELIX    5   5 PHE P  107  ASN P  122  1                                  16
HELIX    6   6 SER P  138  ASN P  144  1                                   7
HELIX    7   7 ASP P  173  LEU P  182  1                                  10
HELIX    8   8 ASN P  195  HIS P  207  1                                  13
HELIX    9   9 ASN P  237  ARG P  245  1                                   9
HELIX   10  10 LEU P  295  HIS P  320  1                                  26
HELIX   11  11 GLY P  324  GLU P  347  1                                  24
HELIX   12  12 GLU P  347  GLY P  354  1                                   8
HELIX   13  13 ASP P  362  LEU P  366  5                                   5
HELIX   14  14 ALA P  378  TYR P  385  1                                   8
HELIX   15  15 HIS P  386  MET P  391  5                                   6
HELIX   16  16 SER P  403  LEU P  408  1                                   6
HELIX   17  17 SER P  412  GLY P  418  1                                   7
HELIX   18  18 GLY P  418  GLN P  429  1                                  12
HELIX   19  19 ILE P  444  LEU P  458  1                                  15
HELIX   20  20 PRO P  462  PHE P  470  1                                   9
HELIX   21  21 SER P  477  THR P  482  1                                   6
HELIX   22  22 GLU P  484  GLY P  496  1                                  13
HELIX   23  23 ASP P  497  LEU P  501  5                                   5
HELIX   24  24 GLU P  502  GLU P  510  1                                   9
HELIX   25  25 GLY P  519  GLY P  536  1                                  18
HELIX   26  26 ASN P  537  SER P  541  5                                   5
HELIX   27  27 ALA P  547  GLY P  551  5                                   5
HELIX   28  28 GLY P  552  THR P  561  1                                  10
HELIX   29  29 THR P  563  LEU P  570  1                                   8
SHEET    1   A 2 ILE P  46  PHE P  50  0
SHEET    2   A 2 ARG P  54  ASP P  58 -1  O  ARG P  54   N  PHE P  50
SHEET    1   B 2 TYR P  64  SER P  65  0
SHEET    2   B 2 ILE P  71  PRO P  72 -1  O  ILE P  71   N  SER P  65
SHEET    1   C 2 GLN P 255  LEU P 257  0
SHEET    2   C 2 GLU P 260  TYR P 262 -1  O  TYR P 262   N  GLN P 255
SHEET    1   D 2 PHE P 395  VAL P 397  0
SHEET    2   D 2 GLN P 400  TYR P 402 -1  O  TYR P 402   N  PHE P 395
SSBOND   1 CYS P   36    CYS P   47                          1555   1555  2.10
SSBOND   2 CYS P   37    CYS P  159                          1555   1555  2.05
SSBOND   3 CYS P   41    CYS P   57                          1555   1555  2.03
SSBOND   4 CYS P   59    CYS P   69                          1555   1555  2.05
SSBOND   5 CYS P  569    CYS P  575                          1555   1555  2.06
LINK         ND2 ASN P  68                 C1  NAG P 661     1555   1555  1.45
LINK         ND2 ASN P 144                 C1  NAG P 671     1555   1555  1.46
LINK         ND2 ASN P 410                 C1  NAG P 681     1555   1555  1.45
LINK         O4  NAG P 661                 C1  NAG P 662     1555   1555  1.45
LINK         O4  NAG P 671                 C1  NAG P 672     1555   1555  1.46
LINK         O4  NAG P 672                 C1  BMA P 673     1555   1555  1.48
LINK         O4  NAG P 681                 C1  NAG P 682     1555   1555  1.46
LINK         NE2 HIS P 388                FE   HEM P 601     1555   1555  2.47
CISPEP   1 SER P  126    PRO P  127          0        -2.74
SITE     1 AC1  3 TYR P  55  ASN P  68  NAG P 662
SITE     1 AC2  2 TYR P  38  NAG P 661
SITE     1 AC3  6 GLU P 140  ASN P 144  TYR P 147  LEU P 238
SITE     2 AC3  6 NAG P 672  HOH P 759
SITE     1 AC4  5 MET P 216  GLU P 239  NAG P 671  BMA P 673
SITE     2 AC4  5 HOH P 789
SITE     1 AC5  1 NAG P 672
SITE     1 AC6  6 GLY P 278  PRO P 280  TYR P 402  GLN P 406
SITE     2 AC6  6 ASN P 410  NAG P 682
SITE     1 AC7  3 TYR P 402  GLN P 406  NAG P 681
SITE     1 AC8  2 SER P  87  PHE P  88
SITE     1 AC9  6 PRO P  86  ILE P  89  VAL P 119  ARG P 120
SITE     2 AC9  6 LEU P 123  GLU P 524
SITE     1 BC1 18 HIS P  90  MET P 113  VAL P 116  ARG P 120
SITE     2 BC1 18 GLN P 192  VAL P 349  LEU P 352  SER P 353
SITE     3 BC1 18 TYR P 355  LEU P 359  TRP P 387  SER P 516
SITE     4 BC1 18 PHE P 518  ILE P 523  GLY P 526  ALA P 527
SITE     5 BC1 18 SER P 530  LEU P 531
SITE     1 BC2 17 ALA P 199  ALA P 202  GLN P 203  THR P 206
SITE     2 BC2 17 HIS P 207  PHE P 210  LYS P 211  THR P 212
SITE     3 BC2 17 LEU P 295  ASN P 382  HIS P 386  TRP P 387
SITE     4 BC2 17 HIS P 388  MET P 391  VAL P 447  ASP P 450
SITE     5 BC2 17 HOH P 763
CRYST1  181.410  181.410  103.398  90.00  90.00 120.00 P 65 2 2     12
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      0.005512  0.003183  0.000000        0.00000
SCALE2      0.000000  0.006365  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009671        0.00000
      
PROCHECK
Go to PROCHECK summary
 References