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PDBsum entry 2esb

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Hydrolase PDB id
2esb
Jmol
Contents
Protein chain
162 a.a.
Ligands
ACT
EPE
Waters ×169
HEADER    HYDROLASE                               25-OCT-05   2ESB
TITLE     CRYSTAL STRUCTURE OF HUMAN DUSP18
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DUAL SPECIFICITY PROTEIN PHOSPHATASE 18;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: DUAL SPECIFIC PHOSPHATASE 18, LOW MOLECULAR
COMPND   5 WEIGHT DUAL SPECIFICITY PHOSPHATASE 20;
COMPND   6 EC: 3.1.3.48, 3.1.3.16;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ALPHA/BETA STRUCTURE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.J.KIM,S.E.RYU,D.G.JEONG,Y.H.CHO,T.S.YOON,J.H.KIM
REVDAT   2   24-FEB-09 2ESB    1       VERSN
REVDAT   1   06-JUN-06 2ESB    0
JRNL        AUTH   D.G.JEONG,Y.H.CHO,T.S.YOON,J.H.KIM,J.H.SON,S.E.RYU,
JRNL        AUTH 2 S.J.KIM
JRNL        TITL   STRUCTURE OF HUMAN DSP18, A MEMBER OF THE
JRNL        TITL 2 DUAL-SPECIFICITY PROTEIN TYROSINE PHOSPHATASE
JRNL        TITL 3 FAMILY.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62   582 2006
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   16699184
JRNL        DOI    10.1107/S0907444906010109
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 13478
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.189
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 685
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) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 1269
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 19
REMARK   3   SOLVENT ATOMS            : 169
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
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) : 22.70
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80
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 2ESB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-05.
REMARK 100 THE RCSB ID CODE IS RCSB035031.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PAL/PLS
REMARK 200  BEAMLINE                       : 4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13478
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.10700
REMARK 200  R SYM                      (I) : 0.10700
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.6
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.19600
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: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES-NAOH, 10% ISOPROPANOL,
REMARK 280  20% PEG 4000, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
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
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       58.32700
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       58.32700
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       17.87000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.04150
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       17.87000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.04150
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.32700
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       17.87000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.04150
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.32700
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       17.87000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.04150
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
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: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A1160  LIES ON A SPECIAL POSITION.
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     THR A     2
REMARK 465     ALA A     3
REMARK 465     PRO A     4
REMARK 465     SER A     5
REMARK 465     CYS A     6
REMARK 465     ALA A     7
REMARK 465     PHE A     8
REMARK 465     PRO A     9
REMARK 465     VAL A    10
REMARK 465     GLN A    11
REMARK 465     PHE A    12
REMARK 465     ARG A    13
REMARK 465     GLN A    14
REMARK 465     PRO A    15
REMARK 465     SER A    16
REMARK 465     VAL A    17
REMARK 465     LYS A   180
REMARK 465     GLU A   181
REMARK 465     VAL A   182
REMARK 465     ARG A   183
REMARK 465     LEU A   184
REMARK 465     MET A   185
REMARK 465     ILE A   186
REMARK 465     PRO A   187
REMARK 465     LEU A   188
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    CYS A 104     -143.28   -138.24
REMARK 500    SER A 109      -64.76   -106.53
REMARK 500    ARG A 142       84.77   -161.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1002
DBREF  2ESB A    1   188  UNP    Q8NEJ0   DUS18_HUMAN      1    188
SEQRES   1 A  188  MET THR ALA PRO SER CYS ALA PHE PRO VAL GLN PHE ARG
SEQRES   2 A  188  GLN PRO SER VAL SER GLY LEU SER GLN ILE THR LYS SER
SEQRES   3 A  188  LEU TYR ILE SER ASN GLY VAL ALA ALA ASN ASN LYS LEU
SEQRES   4 A  188  MET LEU SER SER ASN GLN ILE THR MET VAL ILE ASN VAL
SEQRES   5 A  188  SER VAL GLU VAL VAL ASN THR LEU TYR GLU ASP ILE GLN
SEQRES   6 A  188  TYR MET GLN VAL PRO VAL ALA ASP SER PRO ASN SER ARG
SEQRES   7 A  188  LEU CYS ASP PHE PHE ASP PRO ILE ALA ASP HIS ILE HIS
SEQRES   8 A  188  SER VAL GLU MET LYS GLN GLY ARG THR LEU LEU HIS CYS
SEQRES   9 A  188  ALA ALA GLY VAL SER ARG SER ALA ALA LEU CYS LEU ALA
SEQRES  10 A  188  TYR LEU MET LYS TYR HIS ALA MET SER LEU LEU ASP ALA
SEQRES  11 A  188  HIS THR TRP THR LYS SER CYS ARG PRO ILE ILE ARG PRO
SEQRES  12 A  188  ASN SER GLY PHE TRP GLU GLN LEU ILE HIS TYR GLU PHE
SEQRES  13 A  188  GLN LEU PHE GLY LYS ASN THR VAL HIS MET VAL SER SER
SEQRES  14 A  188  PRO VAL GLY MET ILE PRO ASP ILE TYR GLU LYS GLU VAL
SEQRES  15 A  188  ARG LEU MET ILE PRO LEU
HET    ACT  A1001       4
HET    EPE  A1002      15
HETNAM     ACT ACETATE ION
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN     EPE HEPES
FORMUL   2  ACT    C2 H3 O2 1-
FORMUL   3  EPE    C8 H18 N2 O4 S
FORMUL   4  HOH   *169(H2 O)
HELIX    1   1 VAL A   33  ASN A   36  5                                   4
HELIX    2   2 ASN A   37  ASN A   44  1                                   8
HELIX    3   3 ARG A   78  ASP A   81  5                                   4
HELIX    4   4 PHE A   82  LYS A   96  1                                  15
HELIX    5   5 SER A  109  HIS A  123  1                                  15
HELIX    6   6 SER A  126  ARG A  138  1                                  13
HELIX    7   7 ASN A  144  GLY A  160  1                                  17
HELIX    8   8 ILE A  177  GLU A  179  5                                   3
SHEET    1   A 5 SER A  21  THR A  24  0
SHEET    2   A 5 LEU A  27  SER A  30 -1  O  ILE A  29   N  SER A  21
SHEET    3   A 5 THR A 100  HIS A 103  1  O  LEU A 102   N  TYR A  28
SHEET    4   A 5 MET A  48  ASN A  51  1  N  ILE A  50   O  LEU A 101
SHEET    5   A 5 GLN A  65  GLN A  68  1  O  GLN A  65   N  VAL A  49
SHEET    1   B 2 MET A 166  VAL A 167  0
SHEET    2   B 2 ILE A 174  PRO A 175 -1  O  ILE A 174   N  VAL A 167
SITE     1 AC1  3 THR A  24  LYS A  25  HIS A 123
SITE     1 AC2 10 ASP A  73  CYS A 104  ALA A 105  ALA A 106
SITE     2 AC2 10 GLY A 107  VAL A 108  SER A 109  ARG A 110
SITE     3 AC2 10 HOH A1063  HOH A1152
CRYST1   35.740   96.083  116.654  90.00  90.00  90.00 C 2 2 21      8
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      0.027980  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010408  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008572        0.00000
      
PROCHECK
Go to PROCHECK summary
 References