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PDBsum entry 1igz

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Oxidoreductase PDB id
1igz
Jmol
Contents
Protein chain
553 a.a. *
Ligands
NAG-NDG
NAG-NAG-BMA-BMA-
MAN
NAG-NAG
BGC
BOG ×2
COH
EIC
Waters ×84
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          18-APR-01   1IGZ
TITLE     CRYSTAL STRUCTURE OF LINOLEIC ACID BOUND IN THE CYCLOOXYGENASE CHANNEL
TITLE    2 OF PROSTAGLANDIN ENDOPEROXIDE H SYNTHASE-1.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN ENDOPEROXIDE H SYNTHASE-1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CYCLOOXYGENASE;
COMPND   5 EC: 1.14.99.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 ORGAN: SEMINAL VESSICLE
KEYWDS    MEMBRANE PROTEIN, FATTY ACID, LINOLEIC ACID, OXIDOREDUCTASE,
KEYWDS   2 PEROXIDASE, DIOXYGENASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.G.MALKOWSKI,E.D.THURESSON,W.L.SMITH,R.M.GARAVITO
REVDAT   5   13-JUL-11 1IGZ    1       VERSN
REVDAT   4   23-MAR-11 1IGZ    1       COMPND
REVDAT   3   21-JUL-09 1IGZ    1       HETATM
REVDAT   2   24-FEB-09 1IGZ    1       VERSN
REVDAT   1   12-DEC-01 1IGZ    0
JRNL        AUTH   M.G.MALKOWSKI,E.D.THURESSON,K.M.LAKKIDES,C.J.RIEKE,
JRNL        AUTH 2 R.MICIELLI,W.L.SMITH,R.M.GARAVITO
JRNL        TITL   STRUCTURE OF EICOSAPENTAENOIC AND LINOLEIC ACIDS IN THE
JRNL        TITL 2 CYCLOOXYGENASE SITE OF PROSTAGLANDIN ENDOPEROXIDE H
JRNL        TITL 3 SYNTHASE-1.
JRNL        REF    J.BIOL.CHEM.                  V. 276 37547 2001
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   11477109
JRNL        DOI    10.1074/JBC.M105982200
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   E.D.THURESSON,M.G.MALKOWSKI,K.M.LAKKIDES,C.J.RIEKE,
REMARK   1  AUTH 2 A.M.MULICHAK,S.L.GINELL,R.M.GARAVITO,W.L.SMITH
REMARK   1  TITL   MUTATIONAL AND X-RAY CRYSTALLOGRAPHIC ANALYSIS OF THE
REMARK   1  TITL 2 INTERACTION OF DIHOMO-GAMMA-LINOLENIC ACID WITH
REMARK   1  TITL 3 PROSTAGLANDIN ENDOPEROXIDE H SYNTHASES.
REMARK   1  REF    J.BIOL.CHEM.                  V. 276 10358 2001
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  DOI    10.1074/JBC.M009378200
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.G.MALKOWSKI,S.L.GINELL,W.L.SMITH,R.M.GARAVITO
REMARK   1  TITL   THE PRODUCTIVE CONFORMATION OF ARACHIDONIC ACID BOUND TO
REMARK   1  TITL 2 PROSTAGLANDIN SYNTHASE.
REMARK   1  REF    SCIENCE                       V. 289  1933 2000
REMARK   1  REFN                   ISSN 0036-8075
REMARK   1  DOI    10.1126/SCIENCE.289.5486.1933
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 0.9
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.7
REMARK   3   NUMBER OF REFLECTIONS             : 21075
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : 4% OF THE TOTAL REFLECTIONS
REMARK   3                                      WERE SELECTED BY CNS USING THE
REMARK   3                                      SCRIPT MAKE_CV.INP
REMARK   3   R VALUE            (WORKING SET) : 0.234
REMARK   3   FREE R VALUE                     : 0.270
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 817
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.00
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3420
REMARK   3   BIN FREE R VALUE                    : 0.3640
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 68
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4389
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 232
REMARK   3   SOLVENT ATOMS            : 84
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.41
REMARK   3   ESD FROM SIGMAA              (A) : 0.55
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.50
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.48
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.54
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.07
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.02
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1IGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-01.
REMARK 100 THE RCSB ID CODE IS RCSB013255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-00
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03320
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22684
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.09100
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 30.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.63900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1DIY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 67.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM CHLORIDE, SODIUM AZIDE, CITRIC
REMARK 280  ACID, N-OCTYL-GLUCOSIDE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293.0K
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       69.10000
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       34.55000
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       51.82500
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       17.27500
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       86.37500
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       69.10000
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       34.55000
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       17.27500
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       51.82500
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       86.37500
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: 17150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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      273.07500
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000     -157.65992
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -34.55000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A    25
REMARK 465     ASP A    26
REMARK 465     PRO A    27
REMARK 465     GLY A    28
REMARK 465     ALA A    29
REMARK 465     PRO A    30
REMARK 465     ALA A    31
REMARK 465     PRO A   585
REMARK 465     ARG A   586
REMARK 465     GLN A   587
REMARK 465     GLU A   588
REMARK 465     ASP A   589
REMARK 465     ARG A   590
REMARK 465     PRO A   591
REMARK 465     GLY A   592
REMARK 465     VAL A   593
REMARK 465     GLU A   594
REMARK 465     ARG A   595
REMARK 465     PRO A   596
REMARK 465     PRO A   597
REMARK 465     THR A   598
REMARK 465     GLU A   599
REMARK 465     LEU A   600
REMARK 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 A  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 168    CG   CD   CE   NZ
REMARK 470     LYS A 169    CG   CD   CE   NZ
REMARK 470     GLN A 170    CG   CD   OE1  NE2
REMARK 470     ASP A 173    CG   OD1  OD2
REMARK 470     GLU A 175    CG   CD   OE1  OE2
REMARK 470     ARG A 185    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     LYS A 215    CG   CD   CE   NZ
REMARK 470     LYS A 248    CG   CD   CE   NZ
REMARK 470     GLU A 267    CG   CD   OE1  OE2
REMARK 470     GLU A 268    CG   CD   OE1  OE2
REMARK 470     GLN A 282    CG   CD   OE1  NE2
REMARK 470     LYS A 317    CG   CD   CE   NZ
REMARK 470     ARG A 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 400    CG   CD   OE1  NE2
REMARK 470     GLU A 405    CG   CD   OE1  OE2
REMARK 470     LYS A 453    CG   CD   CE   NZ
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     GLN A 479    CG   CD   OE1  NE2
REMARK 470     LYS A 485    CG   CD   CE   NZ
REMARK 470     GLU A 486    CG   CD   OE1  OE2
REMARK 470     GLU A 493    CG   CD   OE1  OE2
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   OG1  THR A    70     O    HOH A   867              2.10
REMARK 500   O3   NAG A   672     O2   BMA A   673              2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ARG A 179   CZ    ARG A 179   NH1     0.079
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 179   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASN A  34      103.07    -59.89
REMARK 500    CYS A  36       -0.83    -58.39
REMARK 500    TYR A  39       60.07     61.65
REMARK 500    ARG A  61       29.23     42.70
REMARK 500    CYS A  69       60.46     64.35
REMARK 500    HIS A  95      -42.62   -143.36
REMARK 500    ARG A  97       11.04    -49.21
REMARK 500    TRP A  98      -53.07   -125.23
REMARK 500    ILE A 108      -16.56    -48.79
REMARK 500    LEU A 117      -97.69    -54.17
REMARK 500    THR A 118      -54.09    -16.64
REMARK 500    PRO A 128      157.00    -48.30
REMARK 500    THR A 129      -93.21    -98.12
REMARK 500    ASP A 135       40.55    -96.57
REMARK 500    VAL A 145      -12.51    -46.18
REMARK 500    PRO A 153     -172.38    -63.67
REMARK 500    PRO A 156      129.36    -37.24
REMARK 500    ARG A 157        5.50    -63.35
REMARK 500    PRO A 160      -82.95    -49.27
REMARK 500    LYS A 169        1.11    -57.42
REMARK 500    SER A 178      -74.72    -49.00
REMARK 500    ARG A 185      -83.90   -104.21
REMARK 500    GLN A 192        1.94    -65.43
REMARK 500    HIS A 204      -79.41    -50.70
REMARK 500    VAL A 228       74.43   -104.54
REMARK 500    HIS A 232       10.27   -142.89
REMARK 500    ILE A 233      -57.13   -127.87
REMARK 500    PHE A 247       46.32     14.77
REMARK 500    GLU A 268      -44.01    143.22
REMARK 500    ALA A 269       70.47   -112.39
REMARK 500    PRO A 270       62.52    -61.48
REMARK 500    LEU A 272      157.49    -44.74
REMARK 500    MET A 273     -165.06   -165.86
REMARK 500    HIS A 274       20.39   -146.40
REMARK 500    ARG A 277       95.69    -51.11
REMARK 500    PRO A 280        1.08    -66.67
REMARK 500    PRO A 281      -80.65    -94.48
REMARK 500    GLN A 284       70.90   -105.86
REMARK 500    VAL A 287      -43.19   -137.37
REMARK 500    GLU A 290      -51.73    -26.23
REMARK 500    LEU A 328      -30.23    -37.07
REMARK 500    PHE A 329      -75.45    -77.02
REMARK 500    GLU A 347      -49.93   -143.32
REMARK 500    LEU A 359      150.69    -41.55
REMARK 500    TRP A 387       54.93    -91.04
REMARK 500    PRO A 392     -155.61    -65.86
REMARK 500    ASP A 401       68.22   -157.40
REMARK 500    PHE A 409        7.94     45.27
REMARK 500    THR A 411       14.59   -143.63
REMARK 500    SER A 412      -16.10   -140.49
REMARK 500
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.
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                             COH A 601  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 601   NA  103.5
REMARK 620 3 COH A 601   NB   89.6  84.2
REMARK 620 4 COH A 601   NC   76.7 178.6  94.4
REMARK 620 5 COH A 601   ND   91.8  93.9 177.8  87.5
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 662
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 BMA A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EIC A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 900 1DIY CONTAINS THE SAME PROTEIN COMPLEXED WITH ARACHIDONIC
REMARK 900 ACID (AA) IN THE CYCLOOXYGENASE CHANNEL.
REMARK 900 RELATED ID: 1FE2   RELATED DB: PDB
REMARK 900 1FE2 CONTAINS THE SAME PROTEIN COMPLEXED WITH DIHOMO-GAMMA-
REMARK 900 LINOLENIC ACID (DHLA) IN THE CYCLOOXYGENASE CHANNEL.
REMARK 900 RELATED ID: 1IGX   RELATED DB: PDB
REMARK 900 1IGX CONTAINS THE SAME PROTEIN COMPLEXED WITH
REMARK 900 EICOSAPENTANOIC ACID (EPA) IN THE CYCLOOXYGENASE CHANNEL
DBREF  1IGZ A   25   600  GB     165844   AAA31511        24    599
SEQRES   1 A  576  ALA ASP PRO GLY ALA PRO ALA PRO VAL ASN PRO CYS CYS
SEQRES   2 A  576  TYR TYR PRO CYS GLN HIS GLN GLY ILE CYS VAL ARG PHE
SEQRES   3 A  576  GLY LEU ASP ARG TYR GLN CYS ASP CYS THR ARG THR GLY
SEQRES   4 A  576  TYR SER GLY PRO ASN CYS THR ILE PRO GLU ILE TRP THR
SEQRES   5 A  576  TRP LEU ARG THR THR LEU ARG PRO SER PRO SER PHE ILE
SEQRES   6 A  576  HIS PHE LEU LEU THR HIS GLY ARG TRP LEU TRP ASP PHE
SEQRES   7 A  576  VAL ASN ALA THR PHE ILE ARG ASP THR LEU MET ARG LEU
SEQRES   8 A  576  VAL LEU THR VAL ARG SER ASN LEU ILE PRO SER PRO PRO
SEQRES   9 A  576  THR TYR ASN ILE ALA HIS ASP TYR ILE SER TRP GLU SER
SEQRES  10 A  576  PHE SER ASN VAL SER TYR TYR THR ARG ILE LEU PRO SER
SEQRES  11 A  576  VAL PRO ARG ASP CYS PRO THR PRO MET GLY THR LYS GLY
SEQRES  12 A  576  LYS LYS GLN LEU PRO ASP ALA GLU PHE LEU SER ARG ARG
SEQRES  13 A  576  PHE LEU LEU ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY
SEQRES  14 A  576  THR ASN LEU MET PHE ALA PHE PHE ALA GLN HIS PHE THR
SEQRES  15 A  576  HIS GLN PHE PHE LYS THR SER GLY LYS MET GLY PRO GLY
SEQRES  16 A  576  PHE THR LYS ALA LEU GLY HIS GLY VAL ASP LEU GLY HIS
SEQRES  17 A  576  ILE TYR GLY ASP ASN LEU GLU ARG GLN TYR GLN LEU ARG
SEQRES  18 A  576  LEU PHE LYS ASP GLY LYS LEU LYS TYR GLN MET LEU ASN
SEQRES  19 A  576  GLY GLU VAL TYR PRO PRO SER VAL GLU GLU ALA PRO VAL
SEQRES  20 A  576  LEU MET HIS TYR PRO ARG GLY ILE PRO PRO GLN SER GLN
SEQRES  21 A  576  MET ALA VAL GLY GLN GLU VAL PHE GLY LEU LEU PRO GLY
SEQRES  22 A  576  LEU MET LEU TYR ALA THR ILE TRP LEU ARG GLU HIS ASN
SEQRES  23 A  576  ARG VAL CYS ASP LEU LEU LYS ALA GLU HIS PRO THR TRP
SEQRES  24 A  576  GLY ASP GLU GLN LEU PHE GLN THR ALA ARG LEU ILE LEU
SEQRES  25 A  576  ILE GLY GLU THR ILE LYS ILE VAL ILE GLU GLU TYR VAL
SEQRES  26 A  576  GLN GLN LEU SER GLY TYR PHE LEU GLN LEU LYS PHE ASP
SEQRES  27 A  576  PRO GLU LEU LEU PHE GLY ALA GLN PHE GLN TYR ARG ASN
SEQRES  28 A  576  ARG ILE ALA MET GLU PHE ASN GLN LEU TYR HIS TRP HIS
SEQRES  29 A  576  PRO LEU MET PRO ASP SER PHE ARG VAL GLY PRO GLN ASP
SEQRES  30 A  576  TYR SER TYR GLU GLN PHE LEU PHE ASN THR SER MET LEU
SEQRES  31 A  576  VAL ASP TYR GLY VAL GLU ALA LEU VAL ASP ALA PHE SER
SEQRES  32 A  576  ARG GLN PRO ALA GLY ARG ILE GLY GLY GLY ARG ASN ILE
SEQRES  33 A  576  ASP HIS HIS ILE LEU HIS VAL ALA VAL ASP VAL ILE LYS
SEQRES  34 A  576  GLU SER ARG VAL LEU ARG LEU GLN PRO PHE ASN GLU TYR
SEQRES  35 A  576  ARG LYS ARG PHE GLY MET LYS PRO TYR THR SER PHE GLN
SEQRES  36 A  576  GLU LEU THR GLY GLU LYS GLU MET ALA ALA GLU LEU GLU
SEQRES  37 A  576  GLU LEU TYR GLY ASP ILE ASP ALA LEU GLU PHE TYR PRO
SEQRES  38 A  576  GLY LEU LEU LEU GLU LYS CYS HIS PRO ASN SER ILE PHE
SEQRES  39 A  576  GLY GLU SER MET ILE GLU MET GLY ALA PRO PHE SER LEU
SEQRES  40 A  576  LYS GLY LEU LEU GLY ASN PRO ILE CYS SER PRO GLU TYR
SEQRES  41 A  576  TRP LYS ALA SER THR PHE GLY GLY GLU VAL GLY PHE ASN
SEQRES  42 A  576  LEU VAL LYS THR ALA THR LEU LYS LYS LEU VAL CYS LEU
SEQRES  43 A  576  ASN THR LYS THR CYS PRO TYR VAL SER PHE HIS VAL PRO
SEQRES  44 A  576  ASP PRO ARG GLN GLU ASP ARG PRO GLY VAL GLU ARG PRO
SEQRES  45 A  576  PRO THR GLU LEU
MODRES 1IGZ ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 1IGZ ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 1IGZ ASN A  410  ASN  GLYCOSYLATION SITE
HET    NAG  A 661      14
HET    NDG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    BMA  A 673      11
HET    BMA  A 674      11
HET    MAN  A 675      11
HET    NAG  A 681      14
HET    NAG  A 682      14
HET    BGC  A 750      12
HET    BOG  A 751      20
HET    BOG  A 752      20
HET    COH  A 601      43
HET    EIC  A 700      20
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BGC BETA-D-GLUCOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     EIC LINOLEIC ACID
HETSYN     EIC 9,12-LINOLEIC ACID
FORMUL   2  NAG    5(C8 H15 N O6)
FORMUL   2  NDG    C8 H15 N O6
FORMUL   3  BMA    2(C6 H12 O6)
FORMUL   3  MAN    C6 H12 O6
FORMUL   5  BGC    C6 H12 O6
FORMUL   6  BOG    2(C14 H28 O6)
FORMUL   8  COH    C34 H32 CO N4 O4
FORMUL   9  EIC    C18 H32 O2
FORMUL  10  HOH   *84(H2 O)
HELIX    1   1 ASN A   34  TYR A   38  5                                   5
HELIX    2   2 GLU A   73  ARG A   83  1                                  11
HELIX    3   3 SER A   85  THR A   94  1                                  10
HELIX    4   4 TRP A   98  THR A  106  1                                   9
HELIX    5   5 PHE A  107  ASN A  122  1                                  16
HELIX    6   6 SER A  138  ASN A  144  1                                   7
HELIX    7   7 ASP A  173  LEU A  182  1                                  10
HELIX    8   8 ASN A  195  HIS A  207  1                                  13
HELIX    9   9 ASN A  237  ARG A  245  1                                   9
HELIX   10  10 LEU A  295  HIS A  320  1                                  26
HELIX   11  11 GLY A  324  GLU A  347  1                                  24
HELIX   12  12 GLU A  347  GLY A  354  1                                   8
HELIX   13  13 ASP A  362  PHE A  367  5                                   6
HELIX   14  14 ALA A  378  TYR A  385  1                                   8
HELIX   15  15 HIS A  386  HIS A  386  5                                   1
HELIX   16  16 TRP A  387  MET A  391  5                                   5
HELIX   17  17 SER A  403  LEU A  408  1                                   6
HELIX   18  18 SER A  412  GLY A  418  1                                   7
HELIX   19  19 GLY A  418  SER A  427  1                                  10
HELIX   20  20 ILE A  444  ARG A  459  1                                  16
HELIX   21  21 PRO A  462  PHE A  470  1                                   9
HELIX   22  22 SER A  477  THR A  482  1                                   6
HELIX   23  23 LYS A  485  GLY A  496  1                                  12
HELIX   24  24 ASP A  497  LEU A  501  5                                   5
HELIX   25  25 GLU A  502  GLU A  510  1                                   9
HELIX   26  26 GLY A  519  GLY A  536  1                                  18
HELIX   27  27 ASN A  537  SER A  541  5                                   5
HELIX   28  28 GLY A  552  THR A  561  1                                  10
HELIX   29  29 THR A  563  LEU A  570  1                                   8
SHEET    1   A 2 ILE A  46  PHE A  50  0
SHEET    2   A 2 ARG A  54  ASP A  58 -1  N  ARG A  54   O  PHE A  50
SHEET    1   B 2 TYR A  64  SER A  65  0
SHEET    2   B 2 ILE A  71  PRO A  72 -1  N  ILE A  71   O  SER A  65
SHEET    1   C 2 TYR A 130  ASN A 131  0
SHEET    2   C 2 THR A 149  ARG A 150 -1  N  ARG A 150   O  TYR A 130
SHEET    1   D 2 GLN A 255  LEU A 257  0
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  LEU A 257
SHEET    1   E 2 PHE A 395  VAL A 397  0
SHEET    2   E 2 GLN A 400  TYR A 402 -1  N  GLN A 400   O  VAL A 397
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.06
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.04
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.45
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45
LINK         O4  NAG A 661                 C1  NDG A 662     1555   1555  1.40
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.40
LINK         O4  NAG A 672                 C1  BMA A 673     1555   1555  1.40
LINK         O6  BMA A 673                 C1  BMA A 674     1555   1555  1.41
LINK         O3  BMA A 674                 C1  MAN A 675     1555   1555  1.41
LINK         O4  NAG A 681                 C1  NAG A 682     1555   1555  1.39
LINK        CO   COH A 601                 NE2 HIS A 388     1555   1555  2.21
CISPEP   1 SER A  126    PRO A  127          0         0.12
SITE     1 AC1  4 PRO A  40  TYR A  55  ASN A  68  NDG A 662
SITE     1 AC2  3 TYR A  38  ASP A 584  NAG A 661
SITE     1 AC3  5 GLU A 140  ASN A 144  TYR A 147  LEU A 238
SITE     2 AC3  5 NAG A 672
SITE     1 AC4  7 MET A 216  LEU A 238  GLU A 239  TYR A 242
SITE     2 AC4  7 NAG A 671  BMA A 673  HOH A 814
SITE     1 AC5  3 NAG A 672  BMA A 674  HOH A 824
SITE     1 AC6  4 GLN A 243  BMA A 673  MAN A 675  HOH A 824
SITE     1 AC7  3 GLN A 243  PRO A 270  BMA A 674
SITE     1 AC8  7 GLY A 278  PRO A 281  GLN A 406  ASN A 410
SITE     2 AC8  7 MET A 413  ASP A 416  NAG A 682
SITE     1 AC9  2 GLN A 406  NAG A 681
SITE     1 BC1  3 SER A  87  PHE A  88  PHE A  91
SITE     1 BC2  9 PRO A  86  ILE A  89  LEU A 112  LEU A 115
SITE     2 BC2  9 VAL A 119  ARG A 120  GLU A 524  BOG A 752
SITE     3 BC2  9 HOH A 872
SITE     1 BC3  4 LEU A 115  ASN A 122  LEU A 123  BOG A 751
SITE     1 BC4 16 TYR A 148  GLN A 203  PHE A 210  LYS A 211
SITE     2 BC4 16 THR A 212  LEU A 295  ASN A 382  TYR A 385
SITE     3 BC4 16 HIS A 386  TRP A 387  HIS A 388  MET A 391
SITE     4 BC4 16 ILE A 444  HIS A 446  VAL A 447  ASP A 450
SITE     1 BC5 15 VAL A 116  ARG A 120  PHE A 205  PHE A 209
SITE     2 BC5 15 TYR A 348  VAL A 349  LEU A 352  TYR A 355
SITE     3 BC5 15 PHE A 381  TYR A 385  TRP A 387  ILE A 523
SITE     4 BC5 15 ALA A 527  SER A 530  LEU A 534
CRYST1  182.050  182.050  103.650  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      0.005493  0.003171  0.000000        0.00000
SCALE2      0.000000  0.006343  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009648        0.00000
      
PROCHECK
Go to PROCHECK summary
 References