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PDBsum entry 1u67

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Oxidoreductase PDB id
1u67
Jmol
Contents
Protein chain
553 a.a. *
Ligands
NAG-NDG ×2
NAG-NAG-BMA-BMA
BOG ×4
COH
ACD
Waters ×24
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          29-JUL-04   1U67
TITLE     CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO A MUTANT OF
TITLE    2 PROSTAGLADIN H SYNTHASE-1 THAT FORMS PREDOMINANTLY 11-HPETE.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 1 PRECURSOR;
COMPND   3 CHAIN: A;
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;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 GENE: PTGS1, COX1;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC-HTOCOX-1
KEYWDS    CYCLOOXGENASE, ARACHIDONIC ACID, HEME, EICOSANOID, 11-HETE, COX-1,
KEYWDS   2 COX-2, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.A.HARMAN,C.J.RIEKE,R.M.GARAVITO,W.L.SMITH
REVDAT   4   13-JUL-11 1U67    1       VERSN
REVDAT   3   24-FEB-09 1U67    1       VERSN
REVDAT   2   07-DEC-04 1U67    1       JRNL
REVDAT   1   07-SEP-04 1U67    0
JRNL        AUTH   C.A.HARMAN,C.J.RIEKE,R.M.GARAVITO,W.L.SMITH
JRNL        TITL   CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO A MUTANT OF
JRNL        TITL 2 PROSTAGLANDIN ENDOPEROXIDE H SYNTHASE-1 THAT FORMS
JRNL        TITL 3 PREDOMINANTLY 11-HYDROPEROXYEICOSATETRAENOIC ACID.
JRNL        REF    J.BIOL.CHEM.                  V. 279 42929 2004
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   15292194
JRNL        DOI    10.1074/JBC.M403013200
REMARK   2
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
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) : 3.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.8
REMARK   3   NUMBER OF REFLECTIONS             : 17717
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) : 0.238
REMARK   3   FREE R VALUE                     : 0.311
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 705
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) : 3.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3477
REMARK   3   BIN FREE R VALUE                    : 0.4350
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 50
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            : 4307
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 244
REMARK   3   SOLVENT ATOMS            : 24
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.10
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) : 0.43
REMARK   3   ESD FROM SIGMAA              (A) : 0.60
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) : 0.58
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.79
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.60
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1U67 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB023295.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
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) : 0.999872
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18564
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1
REMARK 200  DATA REDUNDANCY                : 13.900
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07600
REMARK 200   FOR THE DATA SET  : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000
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: PDB ENTRY 1DIY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, LITHIUM CHLORIDE,
REMARK 280  SODIUM AZIDE, N-OCTYL GLUCOSIDE, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280  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       68.91200
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       34.45600
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       51.68400
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       17.22800
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       86.14000
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       68.91200
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       34.45600
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       17.22800
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       51.68400
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       86.14000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATORS: X, Y, Z; -Y, X-Y,
REMARK 300 Z+2/3; Y-X, -X, Z+1/3; -X, -Y, Z+1/2; Y, Y-X, Z+1/6; X-Y, X, Z+5/6;
REMARK 300 Y, X, 2/3-Z; -X, Y-X, 1/3-Z; X-Y, -Y, -Z; -Y, -X, 1/6-Z; X, X-Y, 5/
REMARK 300 6-Z; Y-X, Y, 1/2-Z;
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: 16840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 20.0 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      272.81850
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000     -157.51183
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -34.45600
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 A     1
REMARK 465     SER A     2
REMARK 465     ARG A     3
REMARK 465     GLN A     4
REMARK 465     SER A     5
REMARK 465     ILE A     6
REMARK 465     SER A     7
REMARK 465     LEU A     8
REMARK 465     ARG A     9
REMARK 465     PHE A    10
REMARK 465     PRO A    11
REMARK 465     LEU A    12
REMARK 465     LEU A    13
REMARK 465     LEU A    14
REMARK 465     LEU A    15
REMARK 465     LEU A    16
REMARK 465     LEU A    17
REMARK 465     SER A    18
REMARK 465     PRO A    19
REMARK 465     SER A    20
REMARK 465     PRO A    21
REMARK 465     VAL A    22
REMARK 465     PHE A    23
REMARK 465     SER A    24
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     THR A  62    OG1  CG2
REMARK 470     SER A  65    OG
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER A  85    OG
REMARK 470     ILE A  89    CG1  CG2  CD1
REMARK 470     ARG A  97    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LEU A  99    CG   CD1  CD2
REMARK 470     ASP A 101    CG   OD1  OD2
REMARK 470     VAL A 103    CG1  CG2
REMARK 470     ILE A 108    CG1  CG2  CD1
REMARK 470     ILE A 132    CG1  CG2  CD1
REMARK 470     SER A 146    OG
REMARK 470     ARG A 157    CG   CD   NE   CZ   NH1  NH2
REMARK 470     THR A 161    OG1  CG2
REMARK 470     THR A 165    OG1  CG2
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 179    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     ILE A 188    CG1  CG2  CD1
REMARK 470     LYS A 215    CG   CD   CE   NZ
REMARK 470     GLU A 239    CG   CD   OE1  OE2
REMARK 470     GLN A 243    CG   CD   OE1  NE2
REMARK 470     LYS A 248    CG   CD   CE   NZ
REMARK 470     VAL A 266    CG1  CG2
REMARK 470     GLU A 267    CG   CD   OE1  OE2
REMARK 470     GLU A 268    CG   CD   OE1  OE2
REMARK 470     VAL A 271    CG1  CG2
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ILE A 279    CG1  CG2  CD1
REMARK 470     GLN A 282    CG   CD   OE1  NE2
REMARK 470     SER A 283    OG
REMARK 470     VAL A 287    CG1  CG2
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     SER A 412    OG
REMARK 470     ASP A 416    CG   OD1  OD2
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 470     ILE A 498    CG1  CG2  CD1
REMARK 470     SER A 516    OG
REMARK 470     LYS A 573    CG   CD   CE   NZ
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      105.96    -55.25
REMARK 500    ARG A  61       11.02     52.06
REMARK 500    LEU A  93      -15.82    -46.30
REMARK 500    HIS A  95      -34.96   -138.71
REMARK 500    ILE A 108       -9.16    -51.64
REMARK 500    LEU A 117      -83.02    -61.87
REMARK 500    SER A 121        2.97    -66.83
REMARK 500    THR A 129      -60.33   -108.87
REMARK 500    PRO A 153     -166.51    -67.61
REMARK 500    PRO A 156      123.37    -34.76
REMARK 500    PRO A 160      -81.05    -47.96
REMARK 500    THR A 165      -31.10   -133.95
REMARK 500    LYS A 169       13.44    -61.66
REMARK 500    ASP A 173       99.73    -52.14
REMARK 500    PHE A 176      -71.18    -59.92
REMARK 500    ARG A 185      -88.11   -125.89
REMARK 500    HIS A 204      -74.40    -42.41
REMARK 500    LYS A 215      -71.95    -54.95
REMARK 500    ALA A 223       77.09    -63.33
REMARK 500    HIS A 226      108.97     41.90
REMARK 500    ILE A 233      -72.05   -136.72
REMARK 500    PHE A 247       36.47     25.65
REMARK 500    ASP A 249       29.66     43.29
REMARK 500    TYR A 254     -176.60   -177.32
REMARK 500    ASN A 258       13.71     80.12
REMARK 500    PRO A 270       19.45    -64.58
REMARK 500    MET A 273     -169.04   -101.60
REMARK 500    ARG A 277       73.37    -47.43
REMARK 500    ILE A 279       55.73   -111.82
REMARK 500    PRO A 280      -34.74    -32.36
REMARK 500    PRO A 281      -95.04    -60.62
REMARK 500    SER A 283      -15.61     63.23
REMARK 500    PHE A 292        7.87    -54.06
REMARK 500    LYS A 317      -19.55    -43.88
REMARK 500    LEU A 328       11.10    -63.84
REMARK 500    PHE A 329      -55.29   -121.11
REMARK 500    ARG A 333      -70.48    -51.85
REMARK 500    GLU A 339      -36.11    -37.54
REMARK 500    GLU A 347      -51.47   -133.26
REMARK 500    GLN A 350      -73.57    -47.10
REMARK 500    ASN A 382      -74.89    -44.95
REMARK 500    PHE A 387       32.01    -91.80
REMARK 500    PRO A 392     -161.57    -60.71
REMARK 500    GLN A 400     -172.62    -62.50
REMARK 500    ASP A 401       69.15   -178.00
REMARK 500    PHE A 409       -0.82     48.04
REMARK 500    THR A 411      -60.31   -138.80
REMARK 500    VAL A 419      -74.09    -45.82
REMARK 500    GLU A 420      -77.98    -27.61
REMARK 500    ASP A 424      -16.65    -47.94
REMARK 500
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.
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     ACD A  700
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  106.1
REMARK 620 3 COH A 601   NB   88.6  86.0
REMARK 620 4 COH A 601   NC   75.0 178.9  93.7
REMARK 620 5 COH A 601   ND   92.7  95.2 177.9  85.1
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 NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 753
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 ACD A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DIY   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE THERE IS AN INDICATION OF SEQUENCE CONFLICT AT RESIDUE 92
REMARK 999 IN SWS DATABASE. THERE HAS NOT BEEN A VERIFICATION OF THIS RESIDUE
REMARK 999 BEING A METHIONINE, AND SEVERAL CRYSTAL STRUCTURE COORDINATES
REMARK 999 REFERENCED ON SWISS PROT HAVE LISTED THIS RESIDUE AS A LEU.
DBREF  1U67 A    1   600  UNP    P05979   PGH1_SHEEP       1    600
SEQADV 1U67 LEU A   92  UNP  P05979    MET    92 SEE REMARK 999
SEQADV 1U67 ALA A  349  UNP  P05979    VAL   349 ENGINEERED
SEQADV 1U67 PHE A  387  UNP  P05979    TRP   387 ENGINEERED
SEQRES   1 A  600  MET SER ARG GLN SER ILE SER LEU ARG PHE PRO LEU LEU
SEQRES   2 A  600  LEU LEU LEU LEU SER PRO SER PRO VAL PHE SER ALA ASP
SEQRES   3 A  600  PRO GLY ALA PRO ALA PRO VAL ASN PRO CYS CYS TYR TYR
SEQRES   4 A  600  PRO CYS GLN HIS GLN GLY ILE CYS VAL ARG PHE GLY LEU
SEQRES   5 A  600  ASP ARG TYR GLN CYS ASP CYS THR ARG THR GLY TYR SER
SEQRES   6 A  600  GLY PRO ASN CYS THR ILE PRO GLU ILE TRP THR TRP LEU
SEQRES   7 A  600  ARG THR THR LEU ARG PRO SER PRO SER PHE ILE HIS PHE
SEQRES   8 A  600  LEU LEU THR HIS GLY ARG TRP LEU TRP ASP PHE VAL ASN
SEQRES   9 A  600  ALA THR PHE ILE ARG ASP THR LEU MET ARG LEU VAL LEU
SEQRES  10 A  600  THR VAL ARG SER ASN LEU ILE PRO SER PRO PRO THR TYR
SEQRES  11 A  600  ASN ILE ALA HIS ASP TYR ILE SER TRP GLU SER PHE SER
SEQRES  12 A  600  ASN VAL SER TYR TYR THR ARG ILE LEU PRO SER VAL PRO
SEQRES  13 A  600  ARG ASP CYS PRO THR PRO MET GLY THR LYS GLY LYS LYS
SEQRES  14 A  600  GLN LEU PRO ASP ALA GLU PHE LEU SER ARG ARG PHE LEU
SEQRES  15 A  600  LEU ARG ARG LYS PHE ILE PRO ASP PRO GLN GLY THR ASN
SEQRES  16 A  600  LEU MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN
SEQRES  17 A  600  PHE PHE LYS THR SER GLY LYS MET GLY PRO GLY PHE THR
SEQRES  18 A  600  LYS ALA LEU GLY HIS GLY VAL ASP LEU GLY HIS ILE TYR
SEQRES  19 A  600  GLY ASP ASN LEU GLU ARG GLN TYR GLN LEU ARG LEU PHE
SEQRES  20 A  600  LYS ASP GLY LYS LEU LYS TYR GLN MET LEU ASN GLY GLU
SEQRES  21 A  600  VAL TYR PRO PRO SER VAL GLU GLU ALA PRO VAL LEU MET
SEQRES  22 A  600  HIS TYR PRO ARG GLY ILE PRO PRO GLN SER GLN MET ALA
SEQRES  23 A  600  VAL GLY GLN GLU VAL PHE GLY LEU LEU PRO GLY LEU MET
SEQRES  24 A  600  LEU TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL
SEQRES  25 A  600  CYS ASP LEU LEU LYS ALA GLU HIS PRO THR TRP GLY ASP
SEQRES  26 A  600  GLU GLN LEU PHE GLN THR ALA ARG LEU ILE LEU ILE GLY
SEQRES  27 A  600  GLU THR ILE LYS ILE VAL ILE GLU GLU TYR ALA GLN GLN
SEQRES  28 A  600  LEU SER GLY TYR PHE LEU GLN LEU LYS PHE ASP PRO GLU
SEQRES  29 A  600  LEU LEU PHE GLY ALA GLN PHE GLN TYR ARG ASN ARG ILE
SEQRES  30 A  600  ALA MET GLU PHE ASN GLN LEU TYR HIS PHE HIS PRO LEU
SEQRES  31 A  600  MET PRO ASP SER PHE ARG VAL GLY PRO GLN ASP TYR SER
SEQRES  32 A  600  TYR GLU GLN PHE LEU PHE ASN THR SER MET LEU VAL ASP
SEQRES  33 A  600  TYR GLY VAL GLU ALA LEU VAL ASP ALA PHE SER ARG GLN
SEQRES  34 A  600  PRO ALA GLY ARG ILE GLY GLY GLY ARG ASN ILE ASP HIS
SEQRES  35 A  600  HIS ILE LEU HIS VAL ALA VAL ASP VAL ILE LYS GLU SER
SEQRES  36 A  600  ARG VAL LEU ARG LEU GLN PRO PHE ASN GLU TYR ARG LYS
SEQRES  37 A  600  ARG PHE GLY MET LYS PRO TYR THR SER PHE GLN GLU LEU
SEQRES  38 A  600  THR GLY GLU LYS GLU MET ALA ALA GLU LEU GLU GLU LEU
SEQRES  39 A  600  TYR GLY ASP ILE ASP ALA LEU GLU PHE TYR PRO GLY LEU
SEQRES  40 A  600  LEU LEU GLU LYS CYS HIS PRO ASN SER ILE PHE GLY GLU
SEQRES  41 A  600  SER MET ILE GLU MET GLY ALA PRO PHE SER LEU LYS GLY
SEQRES  42 A  600  LEU LEU GLY ASN PRO ILE CYS SER PRO GLU TYR TRP LYS
SEQRES  43 A  600  ALA SER THR PHE GLY GLY GLU VAL GLY PHE ASN LEU VAL
SEQRES  44 A  600  LYS THR ALA THR LEU LYS LYS LEU VAL CYS LEU ASN THR
SEQRES  45 A  600  LYS THR CYS PRO TYR VAL SER PHE HIS VAL PRO ASP PRO
SEQRES  46 A  600  ARG GLN GLU ASP ARG PRO GLY VAL GLU ARG PRO PRO THR
SEQRES  47 A  600  GLU LEU
MODRES 1U67 ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 1U67 ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 1U67 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    NAG  A 681      14
HET    NDG  A 682      14
HET    BOG  A 750      20
HET    BOG  A 751      20
HET    BOG  A 752      20
HET    BOG  A 753      20
HET    COH  A 601      43
HET    ACD  A 700      15
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     ACD ARACHIDONIC ACID
FORMUL   2  NAG    4(C8 H15 N O6)
FORMUL   2  NDG    2(C8 H15 N O6)
FORMUL   3  BMA    2(C6 H12 O6)
FORMUL   5  BOG    4(C14 H28 O6)
FORMUL   9  COH    C34 H32 CO N4 O4
FORMUL  10  ACD    C20 H32 O2
FORMUL  11  HOH   *24(H2 O)
HELIX    1   1 ASN A   34  TYR A   38  5                                   5
HELIX    2   2 GLU A   73  LEU A   82  1                                  10
HELIX    3   3 SER A   85  THR A   94  1                                  10
HELIX    4   4 GLY A   96  ASN A  104  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  PHE A  181  1                                   9
HELIX    8   8 ASN A  195  HIS A  207  1                                  13
HELIX    9   9 ASN A  237  GLN A  243  1                                   7
HELIX   10  10 LEU A  295  HIS A  320  1                                  26
HELIX   11  11 GLU A  326  GLU A  347  1                                  22
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  MET A  391  5                                   6
HELIX   16  16 SER A  403  LEU A  408  1                                   6
HELIX   17  17 THR A  411  GLY A  418  1                                   8
HELIX   18  18 GLY A  418  SER A  427  1                                  10
HELIX   19  19 ILE A  444  ARG A  459  1                                  16
HELIX   20  20 PRO A  462  PHE A  470  1                                   9
HELIX   21  21 SER A  477  THR A  482  1                                   6
HELIX   22  22 LYS A  485  GLY A  496  1                                  12
HELIX   23  23 ASP A  497  LEU A  501  5                                   5
HELIX   24  24 GLU A  502  GLU A  510  1                                   9
HELIX   25  25 GLY A  519  LEU A  535  1                                  17
HELIX   26  26 ASN A  537  SER A  541  5                                   5
HELIX   27  27 ALA A  547  PHE A  550  5                                   4
HELIX   28  28 GLY A  551  ALA A  562  1                                  12
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  O  ARG A  54   N  PHE A  50
SHEET    1   B 2 GLN A 255  LEU A 257  0
SHEET    2   B 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  LEU A 257
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04
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  2.03
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.46
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.45
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.44
LINK         O4  NAG A 661                 C1  NDG A 662     1555   1555  1.40
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.39
LINK         O4  NAG A 672                 C1  BMA A 673     1555   1555  1.40
LINK         O6  BMA A 673                 C1  BMA A 674     1555   1555  1.40
LINK         O4  NAG A 681                 C1  NDG A 682     1555   1555  1.39
LINK        CO   COH A 601                 NE2 HIS A 388     1555   1555  2.18
CISPEP   1 SER A  126    PRO A  127          0         0.04
SITE     1 AC1  4 TYR A  38  TYR A  55  ASN A  68  NDG A 662
SITE     1 AC2  3 TYR A  55  ASP A 584  NAG A 661
SITE     1 AC3  5 ASN A 144  TYR A 147  LEU A 238  NAG A 672
SITE     2 AC3  5 BOG A 752
SITE     1 AC4  4 MET A 216  TYR A 242  NAG A 671  BMA A 673
SITE     1 AC5  2 NAG A 672  BMA A 674
SITE     1 AC6  1 BMA A 673
SITE     1 AC7  7 GLY A 278  TYR A 402  GLN A 406  ASN A 410
SITE     2 AC7  7 MET A 413  ASP A 416  NDG A 682
SITE     1 AC8  1 NAG A 681
SITE     1 AC9  3 SER A  87  PHE A  88  PHE A  91
SITE     1 BC1  8 PRO A  86  LEU A 112  VAL A 116  VAL A 119
SITE     2 BC1  8 ARG A 120  LEU A 123  GLU A 524  HOH A 800
SITE     1 BC2  7 ILE A 132  ALA A 133  TYR A 147  PHE A 220
SITE     2 BC2  7 TYR A 242  PHE A 247  NAG A 671
SITE     1 BC3  2 ARG A  97  TRP A  98
SITE     1 BC4 18 TYR A 148  GLN A 203  THR A 206  HIS A 207
SITE     2 BC4 18 PHE A 210  LYS A 211  THR A 212  LEU A 295
SITE     3 BC4 18 ASN A 382  TYR A 385  HIS A 386  PHE A 387
SITE     4 BC4 18 HIS A 388  MET A 391  ILE A 444  HIS A 446
SITE     5 BC4 18 VAL A 447  ASP A 450
SITE     1 BC5  9 VAL A 116  ARG A 120  ALA A 349  TYR A 355
SITE     2 BC5  9 TYR A 385  PHE A 387  ILE A 523  ALA A 527
SITE     3 BC5  9 SER A 530
CRYST1  181.879  181.879  103.368  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      0.005498  0.003174  0.000000        0.00000
SCALE2      0.000000  0.006349  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009674        0.00000
      
PROCHECK
Go to PROCHECK summary
 References