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PDBsum entry 1ht8

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1ht8
Jmol
Contents
Protein chains
551 a.a. *
Ligands
NAG ×8
BOG ×3
HEM ×2
34C ×2
Waters ×235
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          29-DEC-00   1HT8
TITLE     THE 2.7 ANGSTROM RESOLUTION MODEL OF OVINE COX-1 COMPLEXED WITH
TITLE    2 ALCLOFENAC
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN H2 SYNTHASE-1;
COMPND   3 CHAIN: A, B;
COMPND   4 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 VESICLE
KEYWDS    MEMBRANE PROTEIN, PEROXIDASE, DIOXYGENASE, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.S.SELINSKY,K.GUPTA,C.T.SHARKEY,P.J.LOLL
REVDAT   4   13-JUL-11 1HT8    1       VERSN
REVDAT   3   24-FEB-09 1HT8    1       VERSN
REVDAT   2   27-JUN-01 1HT8    1       JRNL
REVDAT   1   11-APR-01 1HT8    0
JRNL        AUTH   B.S.SELINSKY,K.GUPTA,C.T.SHARKEY,P.J.LOLL
JRNL        TITL   STRUCTURAL ANALYSIS OF NSAID BINDING BY PROSTAGLANDIN H2
JRNL        TITL 2 SYNTHASE: TIME-DEPENDENT AND TIME-INDEPENDENT INHIBITORS
JRNL        TITL 3 ELICIT IDENTICAL ENZYME CONFORMATIONS.
JRNL        REF    BIOCHEMISTRY                  V.  40  5172 2001
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11318639
JRNL        DOI    10.1021/BI010045S
REMARK   2
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 AND HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 205089.390
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.2
REMARK   3   NUMBER OF REFLECTIONS             : 62943
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 SET) : 0.211
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 4807
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.69
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.86
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9004
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520
REMARK   3   BIN FREE R VALUE                    : 0.3050
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.30
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 707
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8954
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 288
REMARK   3   SOLVENT ATOMS            : 235
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.90
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.92000
REMARK   3    B22 (A**2) : 2.65000
REMARK   3    B33 (A**2) : 0.28000
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30
REMARK   3   ESD FROM SIGMAA              (A) : 0.26
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.36
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.840 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.410 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.440 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.160 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 25.07
REMARK   3
REMARK   3  NCS MODEL : CONSTR
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  PARAMETER FILE  2  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1HT8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-01.
REMARK 100 THE RCSB ID CODE IS RCSB012573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-00
REMARK 200  TEMPERATURE           (KELVIN) : 120
REMARK 200  PH                             : 6.7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X8C
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62943
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.920
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2
REMARK 200  DATA REDUNDANCY                : 6.480
REMARK 200  R MERGE                    (I) : 0.04600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.12500
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: CNS
REMARK 200 STARTING MODEL: 1CQE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 72.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-4000, SODIUM CHLORIDE, BETA-OCTYL
REMARK 280  GLUCOSIDE, POTASSIUM PHOSPHATE (DIBASIC), PH 6.7, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2
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        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
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        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       49.57450
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      104.22500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      111.19950
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       49.57450
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      104.22500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      111.19950
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       49.57450
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      104.22500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      111.19950
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       49.57450
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      104.22500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      111.19950
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
REMARK 350 TOTAL BURIED SURFACE AREA: 12480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    LEU A   294     O    LEU A   408              2.16
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    HIS A  43       49.55     39.19
REMARK 500    ASP A  53       -6.47   -144.38
REMARK 500    THR A 129      -87.18   -102.62
REMARK 500    ASP A 135       44.43    -86.96
REMARK 500    VAL A 145       10.74    -69.56
REMARK 500    ARG A 185      -66.42   -106.49
REMARK 500    PRO A 270       73.55    -60.90
REMARK 500    TRP A 387       45.54    -97.19
REMARK 500    ASN A 439       22.92   -148.24
REMARK 500    PRO A 514      -89.12    -12.26
REMARK 500    ASN A 515       54.90   -116.09
REMARK 500    TRP A 545       67.14    -66.95
REMARK 500    THR B 129      -87.29   -106.60
REMARK 500    ASP B 135       44.25    -96.04
REMARK 500    PRO B 270       77.18    -56.22
REMARK 500    TRP B 387       45.93   -100.73
REMARK 500    SER B 412      -19.01   -140.97
REMARK 500    ARG B 438       55.47     39.60
REMARK 500    ASN B 439       26.25   -145.67
REMARK 500    GLU B 484     -153.39   -133.97
REMARK 500    PHE B 503      -75.65    -41.98
REMARK 500    PRO B 514      -92.28    -16.71
REMARK 500    ASN B 515       53.45   -114.90
REMARK 500    TRP B 545       64.06    -66.45
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    LEU B 408        24.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     NAG A 1661
REMARK 610     NAG A 1671
REMARK 610     NAG A 1672
REMARK 610     NAG A 1681
REMARK 610     NAG B 2661
REMARK 610     NAG B 2671
REMARK 610     NAG B 2672
REMARK 610     NAG B 2681
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 601   NA   95.6
REMARK 620 3 HEM A 601   NB   91.7  90.7
REMARK 620 4 HEM A 601   NC   85.6 178.5  90.1
REMARK 620 5 HEM A 601   ND   90.4  90.7 177.3  88.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 601   NA   94.7
REMARK 620 3 HEM B 601   NB   96.7  90.4
REMARK 620 4 HEM B 601   NC   86.4 179.0  89.5
REMARK 620 5 HEM B 601   ND   85.4  91.1 177.3  89.0
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 1661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 2802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 34C A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 34C B 2701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EQH   RELATED DB: PDB
REMARK 900 THE 2.7 ANGSTROM RESOLUTION MODEL OF OVINE COX-1 COMPLEXED
REMARK 900 WITH FLURBIPROFEN
DBREF  1HT8 A   33   583  UNP    P05979   PGH1_SHEEP      32    582
DBREF  1HT8 B   33   583  UNP    P05979   PGH1_SHEEP      32    582
SEQRES   1 A  551  VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN GLY
SEQRES   2 A  551  ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS ASP
SEQRES   3 A  551  CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR ILE
SEQRES   4 A  551  PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG PRO
SEQRES   5 A  551  SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY ARG
SEQRES   6 A  551  TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG ASP
SEQRES   7 A  551  THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN LEU
SEQRES   8 A  551  ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP TYR
SEQRES   9 A  551  ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR THR
SEQRES  10 A  551  ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR PRO
SEQRES  11 A  551  MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA GLU
SEQRES  12 A  551  PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE ILE
SEQRES  13 A  551  PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE PHE
SEQRES  14 A  551  ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER GLY
SEQRES  15 A  551  LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS GLY
SEQRES  16 A  551  VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU ARG
SEQRES  17 A  551  GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS
SEQRES  18 A  551  TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER VAL
SEQRES  19 A  551  GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY ILE
SEQRES  20 A  551  PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL PHE
SEQRES  21 A  551  GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE TRP
SEQRES  22 A  551  LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS ALA
SEQRES  23 A  551  GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN THR
SEQRES  24 A  551  ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL
SEQRES  25 A  551  ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE LEU
SEQRES  26 A  551  GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA GLN
SEQRES  27 A  551  PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN GLN
SEQRES  28 A  551  LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE ARG
SEQRES  29 A  551  VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU PHE
SEQRES  30 A  551  ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA LEU
SEQRES  31 A  551  VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE GLY
SEQRES  32 A  551  GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL ALA
SEQRES  33 A  551  VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU GLN
SEQRES  34 A  551  PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS PRO
SEQRES  35 A  551  TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU MET
SEQRES  36 A  551  ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP ALA
SEQRES  37 A  551  LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS HIS
SEQRES  38 A  551  PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET GLY
SEQRES  39 A  551  ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO ILE
SEQRES  40 A  551  CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY GLY
SEQRES  41 A  551  GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU LYS
SEQRES  42 A  551  LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR VAL
SEQRES  43 A  551  SER PHE HIS VAL PRO
SEQRES   1 B  551  VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN GLY
SEQRES   2 B  551  ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS ASP
SEQRES   3 B  551  CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR ILE
SEQRES   4 B  551  PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG PRO
SEQRES   5 B  551  SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY ARG
SEQRES   6 B  551  TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG ASP
SEQRES   7 B  551  THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN LEU
SEQRES   8 B  551  ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP TYR
SEQRES   9 B  551  ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR THR
SEQRES  10 B  551  ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR PRO
SEQRES  11 B  551  MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA GLU
SEQRES  12 B  551  PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE ILE
SEQRES  13 B  551  PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE PHE
SEQRES  14 B  551  ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER GLY
SEQRES  15 B  551  LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS GLY
SEQRES  16 B  551  VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU ARG
SEQRES  17 B  551  GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS
SEQRES  18 B  551  TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER VAL
SEQRES  19 B  551  GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY ILE
SEQRES  20 B  551  PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL PHE
SEQRES  21 B  551  GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE TRP
SEQRES  22 B  551  LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS ALA
SEQRES  23 B  551  GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN THR
SEQRES  24 B  551  ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL
SEQRES  25 B  551  ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE LEU
SEQRES  26 B  551  GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA GLN
SEQRES  27 B  551  PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN GLN
SEQRES  28 B  551  LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE ARG
SEQRES  29 B  551  VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU PHE
SEQRES  30 B  551  ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA LEU
SEQRES  31 B  551  VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE GLY
SEQRES  32 B  551  GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL ALA
SEQRES  33 B  551  VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU GLN
SEQRES  34 B  551  PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS PRO
SEQRES  35 B  551  TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU MET
SEQRES  36 B  551  ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP ALA
SEQRES  37 B  551  LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS HIS
SEQRES  38 B  551  PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET GLY
SEQRES  39 B  551  ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO ILE
SEQRES  40 B  551  CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY GLY
SEQRES  41 B  551  GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU LYS
SEQRES  42 B  551  LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR VAL
SEQRES  43 B  551  SER PHE HIS VAL PRO
HET    NAG  A1661      14
HET    NAG  A1671      14
HET    NAG  A1672      14
HET    NAG  A1681      14
HET    BOG  A1802      20
HET    BOG  A1801      20
HET    NAG  B2661      14
HET    NAG  B2671      14
HET    NAG  B2672      14
HET    NAG  B2681      14
HET    BOG  B2802      20
HET    HEM  A 601      43
HET    34C  A1701      15
HET    HEM  B 601      43
HET    34C  B2701      15
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     34C (3-CHLORO-4-PROPOXY-PHENYL)-ACETIC ACID
HETSYN     HEM HEME
FORMUL   3  NAG    8(C8 H15 N O6)
FORMUL   7  BOG    3(C14 H28 O6)
FORMUL  14  HEM    2(C34 H32 FE N4 O4)
FORMUL  15  34C    2(C11 H13 CL O3)
FORMUL  18  HOH   *235(H2 O)
HELIX    1   1 ASN A   34  TYR A   39  5                                   6
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 GLY A   96  ALA A  105  1                                  10
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 LEU A  230  GLY A  235  1                                   6
HELIX   10  10 ASN A  237  ARG A  245  1                                   9
HELIX   11  11 PRO A  280  GLN A  284  5                                   5
HELIX   12  12 VAL A  291  LEU A  294  5                                   4
HELIX   13  13 LEU A  295  HIS A  320  1                                  26
HELIX   14  14 GLY A  324  GLU A  347  1                                  24
HELIX   15  15 GLU A  347  GLY A  354  1                                   8
HELIX   16  16 ASP A  362  PHE A  367  5                                   6
HELIX   17  17 ALA A  378  TYR A  385  1                                   8
HELIX   18  18 TRP A  387  MET A  391  5                                   5
HELIX   19  19 SER A  403  LEU A  408  1                                   6
HELIX   20  20 SER A  412  GLY A  418  1                                   7
HELIX   21  21 TYR A  417  GLN A  429  1                                  13
HELIX   22  22 ASP A  441  HIS A  443  5                                   3
HELIX   23  23 ILE A  444  LEU A  458  1                                  15
HELIX   24  24 PRO A  462  PHE A  470  1                                   9
HELIX   25  25 SER A  477  THR A  482  1                                   6
HELIX   26  26 LYS A  485  GLY A  496  1                                  12
HELIX   27  27 ASP A  497  LEU A  501  5                                   5
HELIX   28  28 GLU A  502  GLU A  510  1                                   9
HELIX   29  29 GLY A  519  GLY A  536  1                                  18
HELIX   30  30 ASN A  537  SER A  541  5                                   5
HELIX   31  31 LYS A  546  GLY A  551  5                                   6
HELIX   32  32 GLY A  552  THR A  561  1                                  10
HELIX   33  33 THR A  563  LEU A  570  1                                   8
HELIX   34  34 ASN B   34  TYR B   39  5                                   6
HELIX   35  35 GLU B   73  ARG B   83  1                                  11
HELIX   36  36 SER B   85  THR B   94  1                                  10
HELIX   37  37 GLY B   96  ASN B  104  1                                   9
HELIX   38  38 THR B  106  ASN B  122  1                                  17
HELIX   39  39 SER B  138  ASN B  144  1                                   7
HELIX   40  40 ASP B  173  LEU B  182  1                                  10
HELIX   41  41 ASN B  195  HIS B  207  1                                  13
HELIX   42  42 LEU B  230  GLY B  235  1                                   6
HELIX   43  43 ASN B  237  ARG B  245  1                                   9
HELIX   44  44 PRO B  280  GLN B  284  5                                   5
HELIX   45  45 VAL B  291  LEU B  294  5                                   4
HELIX   46  46 LEU B  295  HIS B  320  1                                  26
HELIX   47  47 GLY B  324  GLU B  347  1                                  24
HELIX   48  48 GLU B  347  GLY B  354  1                                   8
HELIX   49  49 ASP B  362  PHE B  367  5                                   6
HELIX   50  50 ALA B  378  TYR B  385  1                                   8
HELIX   51  51 TRP B  387  MET B  391  5                                   5
HELIX   52  52 SER B  403  LEU B  408  1                                   6
HELIX   53  53 SER B  412  GLY B  418  1                                   7
HELIX   54  54 TYR B  417  GLN B  429  1                                  13
HELIX   55  55 ILE B  444  ARG B  459  1                                  16
HELIX   56  56 PRO B  462  PHE B  470  1                                   9
HELIX   57  57 SER B  477  THR B  482  1                                   6
HELIX   58  58 LYS B  485  GLY B  496  1                                  12
HELIX   59  59 ASP B  497  LEU B  501  5                                   5
HELIX   60  60 GLU B  502  GLU B  510  1                                   9
HELIX   61  61 GLY B  519  GLY B  536  1                                  18
HELIX   62  62 ASN B  537  SER B  541  5                                   5
HELIX   63  63 ALA B  547  GLY B  551  5                                   5
HELIX   64  64 GLY B  552  THR B  561  1                                  10
HELIX   65  65 THR B  563  LEU B  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 GLN A 255  LEU A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  LEU A 257
SHEET    1   D 2 PHE A 395  VAL A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  GLN A 400   N  VAL A 397
SHEET    1   E 2 ILE B  46  PHE B  50  0
SHEET    2   E 2 ARG B  54  ASP B  58 -1  O  ARG B  54   N  PHE B  50
SHEET    1   F 2 TYR B  64  SER B  65  0
SHEET    2   F 2 ILE B  71  PRO B  72 -1  N  ILE B  71   O  SER B  65
SHEET    1   G 2 TYR B 130  ASN B 131  0
SHEET    2   G 2 THR B 149  ARG B 150 -1  N  ARG B 150   O  TYR B 130
SHEET    1   H 2 GLN B 255  LEU B 257  0
SHEET    2   H 2 GLU B 260  TYR B 262 -1  N  GLU B 260   O  LEU B 257
SHEET    1   I 2 PHE B 395  VAL B 397  0
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  GLN B 400   N  VAL B 397
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.03
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  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.03
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  2.03
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03
LINK        FE   HEM A 601                 NE2 HIS A 388     1555   1555  2.33
LINK        FE   HEM B 601                 NE2 HIS B 388     1555   1555  2.26
CISPEP   1 SER A  126    PRO A  127          0         0.00
CISPEP   2 SER B  126    PRO B  127          0         0.13
SITE     1 AC1  2 TYR A  55  ASN A  68
SITE     1 AC2  7 ASN A 144  TYR A 147  NAG A1672  HOH A1815
SITE     2 AC2  7 HOH A1835  HOH A1872  HOH A1917
SITE     1 AC3  1 NAG A1671
SITE     1 AC4  6 GLN A 406  ASN A 410  HOH A1803  HOH A1807
SITE     2 AC4  6 HOH A1819  GLN B 282
SITE     1 AC5  7 ARG A  83  PRO A  84  PRO A  86  VAL A 116
SITE     2 AC5  7 VAL A 119  ARG A 120  GLU A 524
SITE     1 AC6  6 THR A  70  TRP A  77  TRP B  98  LEU B  99
SITE     2 AC6  6 PHE B 102  VAL B 103
SITE     1 AC7  2 TYR B  55  ASN B  68
SITE     1 AC8  8 GLU B 140  ASN B 144  TYR B 147  NAG B2672
SITE     2 AC8  8 HOH B2809  HOH B2848  HOH B2893  HOH B2911
SITE     1 AC9  3 MET B 216  NAG B2671  HOH B2914
SITE     1 BC1  6 ILE A 279  PRO A 280  GLN B 406  ASN B 410
SITE     2 BC1  6 HOH B2833  HOH B2856
SITE     1 BC2  8 ARG B  83  PRO B  84  PRO B  86  VAL B 116
SITE     2 BC2  8 VAL B 119  ARG B 120  GLU B 524  HOH B2842
SITE     1 BC3 15 ALA A 202  GLN A 203  THR A 206  HIS A 207
SITE     2 BC3 15 PHE A 210  THR A 212  LEU A 295  ASN A 382
SITE     3 BC3 15 TYR A 385  HIS A 386  TRP A 387  HIS A 388
SITE     4 BC3 15 MET A 391  ILE A 444  ASP A 450
SITE     1 BC4  8 VAL A 116  ARG A 120  VAL A 349  TYR A 355
SITE     2 BC4  8 TRP A 387  ILE A 523  ALA A 527  SER A 530
SITE     1 BC5 15 ALA B 202  GLN B 203  THR B 206  HIS B 207
SITE     2 BC5 15 PHE B 210  LYS B 211  THR B 212  ASN B 382
SITE     3 BC5 15 TYR B 385  HIS B 386  HIS B 388  MET B 391
SITE     4 BC5 15 TYR B 404  ILE B 444  ASP B 450
SITE     1 BC6  7 VAL B 116  ARG B 120  TYR B 355  TRP B 387
SITE     2 BC6  7 ILE B 523  ALA B 527  SER B 530
CRYST1   99.149  208.450  222.399  90.00  90.00  90.00 I 2 2 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      0.010086  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004797  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004496        0.00000
      
PROCHECK
Go to PROCHECK summary
 References