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PDBsum entry 1h4n

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Lyase PDB id
1h4n
Jmol
Contents
Protein chain
257 a.a.
Ligands
TRS
Metals
_ZN
Waters ×137
HEADER    LYASE                                   29-MAY-97   1H4N
TITLE     H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE II;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CAII, CARBONIC DEHYDRATASE;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 CELL_LINE: BL21;
SOURCE   6 GENE: CAII;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PCAM;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BL21;
SOURCE  11 EXPRESSION_SYSTEM_GENE: CAII;
SOURCE  12 OTHER_DETAILS: THIS CAII VARIANT WAS PRODUCED USING
SOURCE  13 OLIGONUCLEOTIDE-DIRECTED MUTAGENESIS OF THE CLONED HUMAN
SOURCE  14 CAII GENE IN BL21 (DE3) PCAM
KEYWDS    LYASE, OXO-ACID, ACETYLATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.A.LESBURG,D.W.CHRISTIANSON
REVDAT   2   24-FEB-09 1H4N    1       VERSN
REVDAT   1   17-SEP-97 1H4N    0
JRNL        AUTH   C.A.LESBURG,C.HUANG,D.W.CHRISTIANSON,C.A.FIERKE
JRNL        TITL   HISTIDINE --> CARBOXAMIDE LIGAND SUBSTITUTIONS IN
JRNL        TITL 2 THE ZINC BINDING SITE OF CARBONIC ANHYDRASE II
JRNL        TITL 3 ALTER METAL COORDINATION GEOMETRY BUT RETAIN
JRNL        TITL 4 CATALYTIC ACTIVITY.
JRNL        REF    BIOCHEMISTRY                  V.  36 15780 1997
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   9398308
JRNL        DOI    10.1021/BI971296X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2
REMARK   3   NUMBER OF REFLECTIONS             : 16036
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) : 0.154
REMARK   3   FREE R VALUE                     : 0.207
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800
REMARK   3   FREE R VALUE TEST SET COUNT      : 777
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.09
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1452
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190
REMARK   3   BIN FREE R VALUE                    : 0.1990
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 60
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2045
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 9
REMARK   3   SOLVENT ATOMS            : 137
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 15.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.10
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) : 0.35
REMARK   3   ESD FROM SIGMAA              (A) : 0.29
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) : 0.39
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.31
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.30
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) : 2.000 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.500 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 1.500
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 2.000
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  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : NULL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1H4N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : JAN-97
REMARK 200  TEMPERATURE           (KELVIN) : 287
REMARK 200  PH                             : 8.0
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16217
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 2.800
REMARK 200  R MERGE                    (I) : 0.06700
REMARK 200  R SYM                      (I) : 0.06700
REMARK 200   FOR THE DATA SET  : 10.0000
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) : 2.05
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.22300
REMARK 200  R SYM FOR SHELL            (I) : 0.22300
REMARK 200   FOR SHELL         : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 2CBA LESS MUTANT SIDE CHAIN AND
REMARK 200  SOLVENT MOLECULES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4; 100 MM TRIS PH 8.0; 5
REMARK 280  MM N-HEXYL BETA-D-GLUCOPYRANOSIDE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       20.85000
REMARK 290   SMTRY3   2  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 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     SER A     2
REMARK 465     HIS A     3
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  11       18.37   -142.55
REMARK 500    ALA A  65     -175.26   -177.69
REMARK 500    LYS A 111       -6.07     74.83
REMARK 500    PHE A 176       73.18   -151.74
REMARK 500    ASN A 244       49.75    -92.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A  94   OD1
REMARK 620 2 HIS A  96   NE2 102.9
REMARK 620 3 HIS A 119   ND1 123.0  93.2
REMARK 620 4 TRS A 263   N   116.4  96.5 115.4
REMARK 620 5 TRS A 263   O2   82.3 168.1  92.9  71.7
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 262
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 263
DBREF  1H4N A    2   261  UNP    P00918   CAH2_HUMAN       1    259
SEQADV 1H4N ASN A   94  UNP  P00918    HIS    93 ENGINEERED
SEQRES   1 A  259  SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU
SEQRES   2 A  259  HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG
SEQRES   3 A  259  GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR
SEQRES   4 A  259  ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN
SEQRES   5 A  259  ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE
SEQRES   6 A  259  ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU
SEQRES   7 A  259  LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN
SEQRES   8 A  259  PHE ASN PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER
SEQRES   9 A  259  GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU
SEQRES  10 A  259  HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY
SEQRES  11 A  259  LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY
SEQRES  12 A  259  ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN
SEQRES  13 A  259  LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY
SEQRES  14 A  259  LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU
SEQRES  15 A  259  LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER
SEQRES  16 A  259  LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE
SEQRES  17 A  259  VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL
SEQRES  18 A  259  LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU
SEQRES  19 A  259  PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN
SEQRES  20 A  259  PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET    TRS  A 263       8
HETNAM      ZN ZINC ION
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN     TRS TRIS BUFFER
FORMUL   2   ZN    ZN 2+
FORMUL   3  TRS    C4 H12 N O3 1+
FORMUL   4  HOH   *137(H2 O)
HELIX    1   1 TRP A   16  LYS A   18  5                                   3
HELIX    2   2 PRO A   21  LYS A   24  5                                   4
HELIX    3   3 THR A  125  TYR A  128  5                                   3
HELIX    4   4 PHE A  131  GLN A  136  1                                   6
HELIX    5   5 PRO A  155  ILE A  167  5                                  13
HELIX    6   6 PRO A  181  LEU A  184  5                                   4
HELIX    7   7 SER A  220  LYS A  228  1                                   9
SHEET    1   A 2 LEU A  47  SER A  50  0
SHEET    2   A 2 VAL A  78  GLY A  81 -1  N  LYS A  80   O  SER A  48
SHEET    1   B 8 SER A 173  ASP A 175  0
SHEET    2   B 8 SER A  56  ASN A  61 -1  N  ILE A  59   O  ALA A 174
SHEET    3   B 8 PHE A  66  PHE A  70 -1  N  GLU A  69   O  LEU A  57
SHEET    4   B 8 TYR A  88  TRP A  97 -1  N  PHE A  93   O  VAL A  68
SHEET    5   B 8 ALA A 116  ASN A 124 -1  N  TRP A 123   O  ARG A  89
SHEET    6   B 8 LEU A 141  LEU A 148 -1  N  LEU A 148   O  ALA A 116
SHEET    7   B 8 VAL A 207  LEU A 212  1  N  THR A 208   O  LEU A 141
SHEET    8   B 8 TYR A 191  GLY A 196 -1  N  GLY A 196   O  VAL A 207
SHEET    1   C 2 LEU A 148  VAL A 150  0
SHEET    2   C 2 ILE A 216  VAL A 218  1  N  ILE A 216   O  LYS A 149
LINK        ZN    ZN A 262                 OD1 ASN A  94     1555   1555  2.04
LINK        ZN    ZN A 262                 NE2 HIS A  96     1555   1555  2.10
LINK        ZN    ZN A 262                 ND1 HIS A 119     1555   1555  2.00
LINK        ZN    ZN A 262                 N   TRS A 263     1555   1555  2.28
LINK        ZN    ZN A 262                 O2  TRS A 263     1555   1555  2.38
CISPEP   1 SER A   29    PRO A   30          0        -0.23
CISPEP   2 PRO A  201    PRO A  202          0         0.37
SITE     1  ZN  4 ASN A  94  HIS A  96  HIS A 119  TRS A 263
SITE     1 AC1  4 ASN A  94  HIS A  96  HIS A 119  TRS A 263
SITE     1 AC2  9 ASN A  94  HIS A  96  HIS A 119  VAL A 121
SITE     2 AC2  9 LEU A 198  THR A 199  THR A 200  TRP A 209
SITE     3 AC2  9  ZN A 262
CRYST1   42.700   41.700   73.000  90.00 104.60  90.00 P 1 21 1      2
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      0.023419  0.000000  0.006100        0.00000
SCALE2      0.000000  0.023981  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014156        0.00000
      
PROCHECK
Go to PROCHECK summary
 References