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PDBsum entry 3lpy

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
3lpy
Jmol
Contents
Protein chains
79 a.a.
Ligands
SO4 ×4
EPE ×2
Waters ×100
HEADER    ISOMERASE                               07-FEB-10   3LPY
TITLE     CRYSTAL STRUCTURE OF THE RRM DOMAIN OF CYP33
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: N-TERMINAL RRM DOMAIN;
COMPND   5 SYNONYM: PPIASE E, ROTAMASE E, CYCLOPHILIN E, CYCLOPHILIN-33;
COMPND   6 EC: 5.2.1.8;
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 GENE: PPIE, CYP33;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1
KEYWDS    RRM, CYP33, MLL1 BINDING, ISOMERASE, MRNA PROCESSING, MRNA SPLICING,
KEYWDS   2 NUCLEUS, RNA-BINDING, ROTAMASE, SPLICEOSOME
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Z.WANG,D.J.PATEL
REVDAT   2   21-JUL-10 3LPY    1       JRNL
REVDAT   1   07-JUL-10 3LPY    0
JRNL        AUTH   Z.WANG,J.SONG,T.A.MILNE,G.G.WANG,H.LI,C.D.ALLIS,D.J.PATEL
JRNL        TITL   PRO ISOMERIZATION IN MLL1 PHD3-BROMO CASSETTE CONNECTS
JRNL        TITL 2 H3K4ME READOUT TO CYP33 AND HDAC-MEDIATED REPRESSION.
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 141  1183 2010
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   20541251
JRNL        DOI    10.1016/J.CELL.2010.05.016
REMARK   2
REMARK   2 RESOLUTION.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
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)   (%) : 96.3
REMARK   3   NUMBER OF REFLECTIONS             : 13240
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) : 0.216
REMARK   3   FREE R VALUE                     : 0.246
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1153
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.08
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340
REMARK   3   BIN FREE R VALUE                    : 0.3310
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 95
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            : 1246
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 50
REMARK   3   SOLVENT ATOMS            : 100
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 33.20
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) : 0.26
REMARK   3   ESD FROM SIGMAA              (A) : 0.18
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) : 0.31
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.82
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.36
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 3LPY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB057583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-08
REMARK 200  TEMPERATURE           (KELVIN) : 197
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13240
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3
REMARK 200  DATA REDUNDANCY                : 8.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06700
REMARK 200   FOR THE DATA SET  : 58.1000
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) : 2.08
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.41800
REMARK 200   FOR SHELL         : 7.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES-NA, 2.4 M AMMONIUM
REMARK 280  SULFATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
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       16.96967
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       33.93933
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  18     -167.36   -129.05
REMARK 500    ASP B  18     -167.29   -126.53
REMARK 500    TYR B  41      -14.69    -49.58
REMARK 500    GLU B  42      -69.14   -103.12
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 SO4 A 83
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 83
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 84
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 86
DBREF  3LPY A    5    82  UNP    Q9UNP9   PPIE_HUMAN       5     82
DBREF  3LPY B    5    82  UNP    Q9UNP9   PPIE_HUMAN       5     82
SEQADV 3LPY SER A    4  UNP  Q9UNP9              EXPRESSION TAG
SEQADV 3LPY SER B    4  UNP  Q9UNP9              EXPRESSION TAG
SEQRES   1 A   79  SER LYS ARG VAL LEU TYR VAL GLY GLY LEU ALA GLU GLU
SEQRES   2 A   79  VAL ASP ASP LYS VAL LEU HIS ALA ALA PHE ILE PRO PHE
SEQRES   3 A   79  GLY ASP ILE THR ASP ILE GLN ILE PRO LEU ASP TYR GLU
SEQRES   4 A   79  THR GLU LYS HIS ARG GLY PHE ALA PHE VAL GLU PHE GLU
SEQRES   5 A   79  LEU ALA GLU ASP ALA ALA ALA ALA ILE ASP ASN MET ASN
SEQRES   6 A   79  GLU SER GLU LEU PHE GLY ARG THR ILE ARG VAL ASN LEU
SEQRES   7 A   79  ALA
SEQRES   1 B   79  SER LYS ARG VAL LEU TYR VAL GLY GLY LEU ALA GLU GLU
SEQRES   2 B   79  VAL ASP ASP LYS VAL LEU HIS ALA ALA PHE ILE PRO PHE
SEQRES   3 B   79  GLY ASP ILE THR ASP ILE GLN ILE PRO LEU ASP TYR GLU
SEQRES   4 B   79  THR GLU LYS HIS ARG GLY PHE ALA PHE VAL GLU PHE GLU
SEQRES   5 B   79  LEU ALA GLU ASP ALA ALA ALA ALA ILE ASP ASN MET ASN
SEQRES   6 B   79  GLU SER GLU LEU PHE GLY ARG THR ILE ARG VAL ASN LEU
SEQRES   7 B   79  ALA
HET    SO4  A  83       5
HET    SO4  A  84       5
HET    SO4  B  83       5
HET    SO4  B  84       5
HET    EPE  B  85      15
HET    EPE  B  86      15
HETNAM     SO4 SULFATE ION
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN     EPE HEPES
FORMUL   3  SO4    4(O4 S 2-)
FORMUL   7  EPE    2(C8 H18 N2 O4 S)
FORMUL   9  HOH   *100(H2 O)
HELIX    1   1 ASP A   18  ILE A   27  1                                  10
HELIX    2   2 PRO A   28  GLY A   30  5                                   3
HELIX    3   3 LEU A   56  ASN A   68  1                                  13
HELIX    4   4 ASP B   18  ILE B   27  1                                  10
HELIX    5   5 PRO B   28  GLY B   30  5                                   3
HELIX    6   6 LEU B   56  ASN B   68  1                                  13
SHEET    1   A 4 ILE A  32  GLN A  36  0
SHEET    2   A 4 PHE A  49  PHE A  54 -1  O  GLU A  53   N  ASP A  34
SHEET    3   A 4 VAL A   7  GLY A  11 -1  N  VAL A  10   O  ALA A  50
SHEET    4   A 4 ARG A  78  LEU A  81 -1  O  ASN A  80   N  TYR A   9
SHEET    1   B 2 GLU A  71  LEU A  72  0
SHEET    2   B 2 ARG A  75  THR A  76 -1  O  ARG A  75   N  LEU A  72
SHEET    1   C 4 ILE B  32  GLN B  36  0
SHEET    2   C 4 PHE B  49  PHE B  54 -1  O  GLU B  53   N  ASP B  34
SHEET    3   C 4 VAL B   7  GLY B  11 -1  N  LEU B   8   O  VAL B  52
SHEET    4   C 4 ARG B  78  LEU B  81 -1  O  ASN B  80   N  TYR B   9
SHEET    1   D 2 GLU B  71  LEU B  72  0
SHEET    2   D 2 ARG B  75  THR B  76 -1  O  ARG B  75   N  LEU B  72
SITE     1 AC1  3 GLU A  15  LYS A  20  ARG A  75
SITE     1 AC2  4 ARG A  75  THR A  76  HOH A 119  HOH A 125
SITE     1 AC3  4 ALA B  14  GLU B  15  LYS B  20  ARG B  75
SITE     1 AC4  4 ARG B  75  THR B  76  HOH B  96  HOH B 129
SITE     1 AC5  6 ARG A  47  PHE A  49  GLN B  36  PRO B  38
SITE     2 AC5  6 ALA B  82  HOH B 135
SITE     1 AC6  9 GLN A  36  PHE A  51  ALA A  82  TYR B   9
SITE     2 AC6  9 GLY B  11  GLY B  12  ARG B  47  GLY B  48
SITE     3 AC6  9 PHE B  49
CRYST1   59.833   59.833   50.909  90.00  90.00 120.00 P 31          6
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      0.016713  0.009649  0.000000        0.00000
SCALE2      0.000000  0.019299  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019643        0.00000
      
PROCHECK
Go to PROCHECK summary
 References