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PDBsum entry 1ag8

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Top Page protein Protein-protein interface(s) links
Oxidoreductase PDB id
1ag8
Jmol
Contents
Protein chains
493 a.a. *
Waters ×140
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          03-APR-97   1AG8
TITLE     ALDEHYDE DEHYDROGENASE FROM BOVINE MITOCHONDRIA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALDEHYDE DEHYDROGENASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 1.2.1.3;
COMPND   5 OTHER_DETAILS: MITOCHONDRIAL ALDEHYDE DEHYDROGENASE
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 ORGAN: LIVER;
SOURCE   6 ORGANELLE: MITOCHONDRIA;
SOURCE   7 CELLULAR_LOCATION: MITOCHONDRIA
KEYWDS    OXIDOREDUCTASE, ALCOHOL METABOLISM, ALDEHYDE OXIDATION,
KEYWDS   2 ALPHA/BETA DOMAIN, DEHYDROGENASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.G.STEINMETZ,T.D.HURLEY
REVDAT   2   24-FEB-09 1AG8    1       VERSN
REVDAT   1   08-OCT-97 1AG8    0
JRNL        AUTH   C.G.STEINMETZ,P.XIE,H.WEINER,T.D.HURLEY
JRNL        TITL   STRUCTURE OF MITOCHONDRIAL ALDEHYDE DEHYDROGENASE:
JRNL        TITL 2 THE GENETIC COMPONENT OF ETHANOL AVERSION.
JRNL        REF    STRUCTURE                     V.   5   701 1997
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9195888
JRNL        DOI    10.1016/S0969-2126(97)00224-4
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 83.1
REMARK   3   NUMBER OF REFLECTIONS             : 52458
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) : 0.217
REMARK   3   FREE R VALUE                     : 0.282
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3743
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4403
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060
REMARK   3   BIN FREE R VALUE                    : 0.3210
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 300
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            : 15336
REMARK   3   NUCLEIC ACID ATOMS       : NULL
REMARK   3   HETEROGEN ATOMS          : NULL
REMARK   3   SOLVENT ATOMS            : 140
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.70
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) : 0.27
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 8.00
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.34
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.23
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) : 2.600 ; 1.000
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.990 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.600 ; 1.500
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.990 ; 2.500
REMARK   3
REMARK   3  NCS MODEL : RESTRAINTS
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.06  ; 100
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.06  ; 100
REMARK   3   GROUP  2  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3   GROUP  3  POSITIONAL            (A) : 0.06  ; 100
REMARK   3   GROUP  3  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3   GROUP  4  POSITIONAL            (A) : 0.06  ; 100
REMARK   3   GROUP  4  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1AG8 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        : AUG-96
REMARK 200  TEMPERATURE           (KELVIN) : 113
REMARK 200  PH                             : 6.5
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 RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BIOTEX
REMARK 200  DATA SCALING SOFTWARE          : BIOTEX
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55485
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.640
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.0
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.07700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.73
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : 0.14900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200  REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES, X-PLOR 3.1, XTALVIEW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 8000, 100 MM MES, PH 6.5,
REMARK 280  0.2 MM MGCL2, 1MM NAD; THEN SOAKED IN SAME SOLUTION WITHOUT
REMARK 280  NAD OR MGCL2 FOR 1 WEEK.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       61.30000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.80000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       99.20000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.80000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       61.30000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       99.20000
REMARK 290   SMTRY3   4  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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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     ALA A     3
REMARK 465     ALA A     4
REMARK 465     THR A     5
REMARK 465     GLN A     6
REMARK 465     ALA A     7
REMARK 465     SER B     2
REMARK 465     ALA B     3
REMARK 465     ALA B     4
REMARK 465     THR B     5
REMARK 465     GLN B     6
REMARK 465     ALA B     7
REMARK 465     SER C     2
REMARK 465     ALA C     3
REMARK 465     ALA C     4
REMARK 465     THR C     5
REMARK 465     GLN C     6
REMARK 465     ALA C     7
REMARK 465     SER D     2
REMARK 465     ALA D     3
REMARK 465     ALA D     4
REMARK 465     THR D     5
REMARK 465     GLN D     6
REMARK 465     ALA D     7
DBREF  1AG8 A    2   500  UNP    P20000   ALDH2_BOVIN     22    520
DBREF  1AG8 B    2   500  UNP    P20000   ALDH2_BOVIN     22    520
DBREF  1AG8 C    2   500  UNP    P20000   ALDH2_BOVIN     22    520
DBREF  1AG8 D    2   500  UNP    P20000   ALDH2_BOVIN     22    520
SEQRES   1 A  499  SER ALA ALA THR GLN ALA VAL PRO THR PRO ASN GLN GLN
SEQRES   2 A  499  PRO GLU VAL LEU TYR ASN GLN ILE PHE ILE ASN ASN GLU
SEQRES   3 A  499  TRP HIS ASP ALA VAL SER LYS LYS THR PHE PRO THR VAL
SEQRES   4 A  499  ASN PRO SER THR GLY ASP VAL ILE CYS HIS VAL ALA GLU
SEQRES   5 A  499  GLY ASP LYS ALA ASP VAL ASP ARG ALA VAL LYS ALA ALA
SEQRES   6 A  499  ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG MET
SEQRES   7 A  499  ASP ALA SER GLU ARG GLY ARG LEU LEU ASN ARG LEU ALA
SEQRES   8 A  499  ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA LEU
SEQRES   9 A  499  GLU THR LEU ASP ASN GLY LYS PRO TYR ILE ILE SER TYR
SEQRES  10 A  499  LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG TYR
SEQRES  11 A  499  TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR ILE
SEQRES  12 A  499  PRO ILE ASP GLY ASP TYR PHE SER TYR THR ARG HIS GLU
SEQRES  13 A  499  PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN PHE
SEQRES  14 A  499  PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA LEU
SEQRES  15 A  499  ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU GLN
SEQRES  16 A  499  THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE LYS
SEQRES  17 A  499  GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN VAL ILE PRO
SEQRES  18 A  499  GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER HIS
SEQRES  19 A  499  GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR GLU
SEQRES  20 A  499  VAL GLY HIS LEU ILE GLN VAL ALA ALA GLY LYS SER ASN
SEQRES  21 A  499  LEU LYS ARG VAL THR LEU GLU ILE GLY GLY LYS SER PRO
SEQRES  22 A  499  ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA VAL
SEQRES  23 A  499  GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY GLN
SEQRES  24 A  499  CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU ASP
SEQRES  25 A  499  ILE TYR ALA GLU PHE VAL GLU ARG SER VAL ALA ARG ALA
SEQRES  26 A  499  LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER ARG THR
SEQRES  27 A  499  GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS LYS
SEQRES  28 A  499  VAL LEU GLY TYR ILE LYS SER GLY LYS GLU GLU GLY LEU
SEQRES  29 A  499  LYS LEU LEU CYS GLY GLY GLY ALA ALA ALA ASP ARG GLY
SEQRES  30 A  499  TYR PHE ILE GLN PRO THR VAL PHE GLY ASP LEU GLN ASP
SEQRES  31 A  499  GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES  32 A  499  MET GLN ILE LEU LYS PHE LYS SER MET GLU GLU VAL VAL
SEQRES  33 A  499  GLY ARG ALA ASN ASN SER LYS TYR GLY LEU ALA ALA ALA
SEQRES  34 A  499  VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU SER
SEQRES  35 A  499  GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS TYR
SEQRES  36 A  499  ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR LYS
SEQRES  37 A  499  LEU SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY LEU
SEQRES  38 A  499  GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL ARG VAL
SEQRES  39 A  499  PRO GLN LYS ASN SER
SEQRES   1 B  499  SER ALA ALA THR GLN ALA VAL PRO THR PRO ASN GLN GLN
SEQRES   2 B  499  PRO GLU VAL LEU TYR ASN GLN ILE PHE ILE ASN ASN GLU
SEQRES   3 B  499  TRP HIS ASP ALA VAL SER LYS LYS THR PHE PRO THR VAL
SEQRES   4 B  499  ASN PRO SER THR GLY ASP VAL ILE CYS HIS VAL ALA GLU
SEQRES   5 B  499  GLY ASP LYS ALA ASP VAL ASP ARG ALA VAL LYS ALA ALA
SEQRES   6 B  499  ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG MET
SEQRES   7 B  499  ASP ALA SER GLU ARG GLY ARG LEU LEU ASN ARG LEU ALA
SEQRES   8 B  499  ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA LEU
SEQRES   9 B  499  GLU THR LEU ASP ASN GLY LYS PRO TYR ILE ILE SER TYR
SEQRES  10 B  499  LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG TYR
SEQRES  11 B  499  TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR ILE
SEQRES  12 B  499  PRO ILE ASP GLY ASP TYR PHE SER TYR THR ARG HIS GLU
SEQRES  13 B  499  PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN PHE
SEQRES  14 B  499  PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA LEU
SEQRES  15 B  499  ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU GLN
SEQRES  16 B  499  THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE LYS
SEQRES  17 B  499  GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN VAL ILE PRO
SEQRES  18 B  499  GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER HIS
SEQRES  19 B  499  GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR GLU
SEQRES  20 B  499  VAL GLY HIS LEU ILE GLN VAL ALA ALA GLY LYS SER ASN
SEQRES  21 B  499  LEU LYS ARG VAL THR LEU GLU ILE GLY GLY LYS SER PRO
SEQRES  22 B  499  ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA VAL
SEQRES  23 B  499  GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY GLN
SEQRES  24 B  499  CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU ASP
SEQRES  25 B  499  ILE TYR ALA GLU PHE VAL GLU ARG SER VAL ALA ARG ALA
SEQRES  26 B  499  LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER ARG THR
SEQRES  27 B  499  GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS LYS
SEQRES  28 B  499  VAL LEU GLY TYR ILE LYS SER GLY LYS GLU GLU GLY LEU
SEQRES  29 B  499  LYS LEU LEU CYS GLY GLY GLY ALA ALA ALA ASP ARG GLY
SEQRES  30 B  499  TYR PHE ILE GLN PRO THR VAL PHE GLY ASP LEU GLN ASP
SEQRES  31 B  499  GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES  32 B  499  MET GLN ILE LEU LYS PHE LYS SER MET GLU GLU VAL VAL
SEQRES  33 B  499  GLY ARG ALA ASN ASN SER LYS TYR GLY LEU ALA ALA ALA
SEQRES  34 B  499  VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU SER
SEQRES  35 B  499  GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS TYR
SEQRES  36 B  499  ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR LYS
SEQRES  37 B  499  LEU SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY LEU
SEQRES  38 B  499  GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL ARG VAL
SEQRES  39 B  499  PRO GLN LYS ASN SER
SEQRES   1 C  499  SER ALA ALA THR GLN ALA VAL PRO THR PRO ASN GLN GLN
SEQRES   2 C  499  PRO GLU VAL LEU TYR ASN GLN ILE PHE ILE ASN ASN GLU
SEQRES   3 C  499  TRP HIS ASP ALA VAL SER LYS LYS THR PHE PRO THR VAL
SEQRES   4 C  499  ASN PRO SER THR GLY ASP VAL ILE CYS HIS VAL ALA GLU
SEQRES   5 C  499  GLY ASP LYS ALA ASP VAL ASP ARG ALA VAL LYS ALA ALA
SEQRES   6 C  499  ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG MET
SEQRES   7 C  499  ASP ALA SER GLU ARG GLY ARG LEU LEU ASN ARG LEU ALA
SEQRES   8 C  499  ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA LEU
SEQRES   9 C  499  GLU THR LEU ASP ASN GLY LYS PRO TYR ILE ILE SER TYR
SEQRES  10 C  499  LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG TYR
SEQRES  11 C  499  TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR ILE
SEQRES  12 C  499  PRO ILE ASP GLY ASP TYR PHE SER TYR THR ARG HIS GLU
SEQRES  13 C  499  PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN PHE
SEQRES  14 C  499  PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA LEU
SEQRES  15 C  499  ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU GLN
SEQRES  16 C  499  THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE LYS
SEQRES  17 C  499  GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN VAL ILE PRO
SEQRES  18 C  499  GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER HIS
SEQRES  19 C  499  GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR GLU
SEQRES  20 C  499  VAL GLY HIS LEU ILE GLN VAL ALA ALA GLY LYS SER ASN
SEQRES  21 C  499  LEU LYS ARG VAL THR LEU GLU ILE GLY GLY LYS SER PRO
SEQRES  22 C  499  ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA VAL
SEQRES  23 C  499  GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY GLN
SEQRES  24 C  499  CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU ASP
SEQRES  25 C  499  ILE TYR ALA GLU PHE VAL GLU ARG SER VAL ALA ARG ALA
SEQRES  26 C  499  LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER ARG THR
SEQRES  27 C  499  GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS LYS
SEQRES  28 C  499  VAL LEU GLY TYR ILE LYS SER GLY LYS GLU GLU GLY LEU
SEQRES  29 C  499  LYS LEU LEU CYS GLY GLY GLY ALA ALA ALA ASP ARG GLY
SEQRES  30 C  499  TYR PHE ILE GLN PRO THR VAL PHE GLY ASP LEU GLN ASP
SEQRES  31 C  499  GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES  32 C  499  MET GLN ILE LEU LYS PHE LYS SER MET GLU GLU VAL VAL
SEQRES  33 C  499  GLY ARG ALA ASN ASN SER LYS TYR GLY LEU ALA ALA ALA
SEQRES  34 C  499  VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU SER
SEQRES  35 C  499  GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS TYR
SEQRES  36 C  499  ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR LYS
SEQRES  37 C  499  LEU SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY LEU
SEQRES  38 C  499  GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL ARG VAL
SEQRES  39 C  499  PRO GLN LYS ASN SER
SEQRES   1 D  499  SER ALA ALA THR GLN ALA VAL PRO THR PRO ASN GLN GLN
SEQRES   2 D  499  PRO GLU VAL LEU TYR ASN GLN ILE PHE ILE ASN ASN GLU
SEQRES   3 D  499  TRP HIS ASP ALA VAL SER LYS LYS THR PHE PRO THR VAL
SEQRES   4 D  499  ASN PRO SER THR GLY ASP VAL ILE CYS HIS VAL ALA GLU
SEQRES   5 D  499  GLY ASP LYS ALA ASP VAL ASP ARG ALA VAL LYS ALA ALA
SEQRES   6 D  499  ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG MET
SEQRES   7 D  499  ASP ALA SER GLU ARG GLY ARG LEU LEU ASN ARG LEU ALA
SEQRES   8 D  499  ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA LEU
SEQRES   9 D  499  GLU THR LEU ASP ASN GLY LYS PRO TYR ILE ILE SER TYR
SEQRES  10 D  499  LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG TYR
SEQRES  11 D  499  TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR ILE
SEQRES  12 D  499  PRO ILE ASP GLY ASP TYR PHE SER TYR THR ARG HIS GLU
SEQRES  13 D  499  PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN PHE
SEQRES  14 D  499  PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA LEU
SEQRES  15 D  499  ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU GLN
SEQRES  16 D  499  THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE LYS
SEQRES  17 D  499  GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN VAL ILE PRO
SEQRES  18 D  499  GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER HIS
SEQRES  19 D  499  GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR GLU
SEQRES  20 D  499  VAL GLY HIS LEU ILE GLN VAL ALA ALA GLY LYS SER ASN
SEQRES  21 D  499  LEU LYS ARG VAL THR LEU GLU ILE GLY GLY LYS SER PRO
SEQRES  22 D  499  ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA VAL
SEQRES  23 D  499  GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY GLN
SEQRES  24 D  499  CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU ASP
SEQRES  25 D  499  ILE TYR ALA GLU PHE VAL GLU ARG SER VAL ALA ARG ALA
SEQRES  26 D  499  LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER ARG THR
SEQRES  27 D  499  GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS LYS
SEQRES  28 D  499  VAL LEU GLY TYR ILE LYS SER GLY LYS GLU GLU GLY LEU
SEQRES  29 D  499  LYS LEU LEU CYS GLY GLY GLY ALA ALA ALA ASP ARG GLY
SEQRES  30 D  499  TYR PHE ILE GLN PRO THR VAL PHE GLY ASP LEU GLN ASP
SEQRES  31 D  499  GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO VAL
SEQRES  32 D  499  MET GLN ILE LEU LYS PHE LYS SER MET GLU GLU VAL VAL
SEQRES  33 D  499  GLY ARG ALA ASN ASN SER LYS TYR GLY LEU ALA ALA ALA
SEQRES  34 D  499  VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU SER
SEQRES  35 D  499  GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS TYR
SEQRES  36 D  499  ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR LYS
SEQRES  37 D  499  LEU SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY LEU
SEQRES  38 D  499  GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL ARG VAL
SEQRES  39 D  499  PRO GLN LYS ASN SER
FORMUL   5  HOH   *140(H2 O)
HELIX    1   1 LYS A   56  ALA A   69  1                                  14
HELIX    2   2 PRO A   75  ARG A   78  1                                   4
HELIX    3   3 ALA A   81  ARG A   97  1                                  17
HELIX    4   4 ARG A   99  ASN A  110  1                                  12
HELIX    5   5 TYR A  114  LEU A  119  1                                   6
HELIX    6   6 ASP A  121  GLY A  134  1                                  14
HELIX    7   7 PRO A  171  THR A  185  1                                  15
HELIX    8   8 LEU A  199  ALA A  211  1                                  13
HELIX    9   9 GLY A  225  ALA A  233  1                                   9
HELIX   10  10 THR A  247  LYS A  259  1                                  13
HELIX   11  11 MET A  283  GLY A  299  1                                  17
HELIX   12  12 GLU A  312  SER A  328  1                                  17
HELIX   13  13 GLU A  347  GLU A  363  1                                  17
HELIX   14  14 THR A  394  LYS A  397  1                                   4
HELIX   15  15 MET A  413  ASN A  421  1                                   9
HELIX   16  16 LEU A  436  ALA A  445  1                                  10
HELIX   17  17 TYR A  480  TYR A  485  1                                   6
HELIX   18  18 LYS B   56  PHE B   70  1                                  15
HELIX   19  19 PRO B   75  ARG B   78  1                                   4
HELIX   20  20 ALA B   81  ARG B   97  1                                  17
HELIX   21  21 ARG B   99  ASN B  110  1                                  12
HELIX   22  22 TYR B  114  LEU B  119  1                                   6
HELIX   23  23 ASP B  121  GLY B  134  1                                  14
HELIX   24  24 PRO B  171  THR B  185  1                                  15
HELIX   25  25 LEU B  199  ALA B  211  1                                  13
HELIX   26  26 GLY B  225  ALA B  233  1                                   9
HELIX   27  27 THR B  247  LYS B  259  1                                  13
HELIX   28  28 MET B  283  GLY B  299  1                                  17
HELIX   29  29 GLU B  312  SER B  328  1                                  17
HELIX   30  30 GLU B  347  GLU B  363  1                                  17
HELIX   31  31 THR B  394  LYS B  397  1                                   4
HELIX   32  32 MET B  413  ASN B  421  1                                   9
HELIX   33  33 LEU B  436  ALA B  445  1                                  10
HELIX   34  34 TYR B  480  TYR B  485  1                                   6
HELIX   35  35 LYS C   56  PHE C   70  1                                  15
HELIX   36  36 PRO C   75  ARG C   78  1                                   4
HELIX   37  37 ALA C   81  ARG C   97  1                                  17
HELIX   38  38 ARG C   99  ASN C  110  1                                  12
HELIX   39  39 TYR C  114  LEU C  119  1                                   6
HELIX   40  40 ASP C  121  GLY C  134  1                                  14
HELIX   41  41 PRO C  171  ALA C  184  1                                  14
HELIX   42  42 LEU C  199  ALA C  211  1                                  13
HELIX   43  43 GLY C  225  ALA C  233  1                                   9
HELIX   44  44 THR C  247  LYS C  259  1                                  13
HELIX   45  45 MET C  283  GLY C  299  1                                  17
HELIX   46  46 GLU C  312  SER C  328  1                                  17
HELIX   47  47 GLU C  347  GLU C  363  1                                  17
HELIX   48  48 THR C  394  ALA C  396  5                                   3
HELIX   49  49 MET C  413  ASN C  421  1                                   9
HELIX   50  50 LEU C  436  ALA C  445  1                                  10
HELIX   51  51 GLU C  479  TYR C  485  5                                   7
HELIX   52  52 LYS D   56  PHE D   70  1                                  15
HELIX   53  53 PRO D   75  ARG D   78  1                                   4
HELIX   54  54 ALA D   81  ARG D   97  1                                  17
HELIX   55  55 ARG D   99  ASN D  110  1                                  12
HELIX   56  56 TYR D  114  LEU D  119  1                                   6
HELIX   57  57 ASP D  121  GLY D  134  1                                  14
HELIX   58  58 PRO D  171  THR D  185  1                                  15
HELIX   59  59 LEU D  199  ALA D  211  1                                  13
HELIX   60  60 ALA D  228  ALA D  233  1                                   6
HELIX   61  61 THR D  247  LYS D  259  1                                  13
HELIX   62  62 MET D  283  GLY D  299  1                                  17
HELIX   63  63 GLU D  312  SER D  328  1                                  17
HELIX   64  64 GLU D  347  GLU D  363  1                                  17
HELIX   65  65 THR D  394  ALA D  396  5                                   3
HELIX   66  66 MET D  413  ASN D  421  1                                   9
HELIX   67  67 LEU D  436  ALA D  445  1                                  10
HELIX   68  68 GLU D  479  TYR D  485  5                                   7
SHEET    1   A 2 GLY A 141  THR A 143  0
SHEET    2   A 2 GLY D 141  THR D 143 -1  N  THR D 143   O  GLY A 141
SHEET    1   B 7 TYR A 150  PRO A 158  0
SHEET    2   B 7 THR A 486  ARG A 494 -1  N  VAL A 493   O  PHE A 151
SHEET    3   B 7 THR B 450  VAL B 453  1  N  VAL B 451   O  THR A 490
SHEET    4   B 7 ALA B 428  PHE B 432  1  N  ALA B 429   O  THR B 450
SHEET    5   B 7 PRO B 274  ILE B 277  1  N  PRO B 274   O  ALA B 430
SHEET    6   B 7 ARG B 307  GLN B 311  1  N  ARG B 307   O  ASN B 275
SHEET    7   B 7 ILE B 407  PHE B 410  1  N  LEU B 408   O  THR B 308
SHEET    1   C 5 ARG A 264  GLU A 268  0
SHEET    2   C 5 LYS A 240  THR A 244  1  N  VAL A 241   O  ARG A 264
SHEET    3   C 5 VAL A 161  ILE A 165  1  N  GLY A 163   O  LYS A 240
SHEET    4   C 5 VAL A 188  VAL A 193  1  N  VAL A 188   O  CYS A 162
SHEET    5   C 5 VAL A 218  PRO A 222  1  N  ASN A 219   O  VAL A 189
SHEET    1   D 7 TYR B 150  PRO B 158  0
SHEET    2   D 7 THR B 486  ARG B 494 -1  N  VAL B 493   O  PHE B 151
SHEET    3   D 7 THR A 450  VAL A 453  1  N  VAL A 451   O  THR B 490
SHEET    4   D 7 ALA A 428  PHE A 432  1  N  ALA A 429   O  THR A 450
SHEET    5   D 7 PRO A 274  ILE A 277  1  N  PRO A 274   O  ALA A 430
SHEET    6   D 7 ARG A 307  GLN A 311  1  N  ARG A 307   O  ASN A 275
SHEET    7   D 7 ILE A 407  PHE A 410  1  N  LEU A 408   O  THR A 308
SHEET    1   E 3 VAL A 404  GLN A 406  0
SHEET    2   E 3 THR A 384  GLY A 387  1  N  THR A 384   O  MET A 405
SHEET    3   E 3 LYS A 366  CYS A 369 -1  N  CYS A 369   O  VAL A 385
SHEET    1   F 2 GLY B 141  THR B 143  0
SHEET    2   F 2 GLY C 141  THR C 143 -1  N  THR C 143   O  GLY B 141
SHEET    1   G 5 ARG B 264  GLU B 268  0
SHEET    2   G 5 LYS B 240  THR B 244  1  N  VAL B 241   O  ARG B 264
SHEET    3   G 5 VAL B 161  ILE B 165  1  N  GLY B 163   O  LYS B 240
SHEET    4   G 5 VAL B 188  VAL B 193  1  N  VAL B 188   O  CYS B 162
SHEET    5   G 5 VAL B 218  PRO B 222  1  N  ASN B 219   O  VAL B 189
SHEET    1   H 3 VAL B 404  GLN B 406  0
SHEET    2   H 3 THR B 384  GLY B 387  1  N  THR B 384   O  MET B 405
SHEET    3   H 3 LYS B 366  CYS B 369 -1  N  CYS B 369   O  VAL B 385
SHEET    1   I 7 TYR C 150  PRO C 158  0
SHEET    2   I 7 THR C 486  ARG C 494 -1  N  VAL C 493   O  PHE C 151
SHEET    3   I 7 THR D 450  VAL D 453  1  N  VAL D 451   O  THR C 490
SHEET    4   I 7 ALA D 428  PHE D 432  1  N  ALA D 429   O  THR D 450
SHEET    5   I 7 PRO D 274  ILE D 277  1  N  PRO D 274   O  ALA D 430
SHEET    6   I 7 ARG D 307  GLN D 311  1  N  ARG D 307   O  ASN D 275
SHEET    7   I 7 ILE D 407  PHE D 410  1  N  LEU D 408   O  THR D 308
SHEET    1   J 5 ARG C 264  GLU C 268  0
SHEET    2   J 5 LYS C 240  THR C 244  1  N  VAL C 241   O  ARG C 264
SHEET    3   J 5 VAL C 161  ILE C 165  1  N  GLY C 163   O  LYS C 240
SHEET    4   J 5 VAL C 188  VAL C 193  1  N  VAL C 188   O  CYS C 162
SHEET    5   J 5 VAL C 218  PRO C 222  1  N  ASN C 219   O  VAL C 189
SHEET    1   K 7 TYR D 150  PRO D 158  0
SHEET    2   K 7 THR D 486  ARG D 494 -1  N  VAL D 493   O  PHE D 151
SHEET    3   K 7 THR C 450  VAL C 453  1  N  VAL C 451   O  THR D 490
SHEET    4   K 7 ALA C 428  PHE C 432  1  N  ALA C 429   O  THR C 450
SHEET    5   K 7 PRO C 274  ILE C 277  1  N  PRO C 274   O  ALA C 430
SHEET    6   K 7 ARG C 307  GLN C 311  1  N  ARG C 307   O  ASN C 275
SHEET    7   K 7 ILE C 407  PHE C 410  1  N  LEU C 408   O  THR C 308
SHEET    1   L 3 VAL C 404  GLN C 406  0
SHEET    2   L 3 THR C 384  GLY C 387  1  N  THR C 384   O  MET C 405
SHEET    3   L 3 LYS C 366  CYS C 369 -1  N  CYS C 369   O  VAL C 385
SHEET    1   M 5 ARG D 264  GLU D 268  0
SHEET    2   M 5 LYS D 240  THR D 244  1  N  VAL D 241   O  ARG D 264
SHEET    3   M 5 VAL D 161  ILE D 165  1  N  GLY D 163   O  LYS D 240
SHEET    4   M 5 VAL D 188  VAL D 193  1  N  VAL D 188   O  CYS D 162
SHEET    5   M 5 VAL D 218  PRO D 222  1  N  ASN D 219   O  VAL D 189
SHEET    1   N 3 VAL D 404  GLN D 406  0
SHEET    2   N 3 THR D 384  GLY D 387  1  N  THR D 384   O  MET D 405
SHEET    3   N 3 LYS D 366  CYS D 369 -1  N  CYS D 369   O  VAL D 385
SHEET    1   O 2 THR A  36  ASN A  41  0
SHEET    2   O 2 ASP A  46  ALA A  52 -1  N  VAL A  51   O  PHE A  37
SHEET    1   P 2 THR B  36  ASN B  41  0
SHEET    2   P 2 ASP B  46  ALA B  52 -1  N  VAL B  51   O  PHE B  37
SHEET    1   Q 2 THR C  36  VAL C  40  0
SHEET    2   Q 2 VAL C  47  ALA C  52 -1  N  VAL C  51   O  PHE C  37
SHEET    1   R 2 THR D  36  ASN D  41  0
SHEET    2   R 2 ASP D  46  ALA D  52 -1  N  VAL D  51   O  PHE D  37
SSBOND   1 CYS A  301    CYS A  303                          1555   1555  2.98
SSBOND   2 CYS D  301    CYS D  303                          1555   1555  2.87
CRYST1  122.600  198.400   91.600  90.00  90.00  90.00 P 21 21 21   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      0.008157  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005040  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010917        0.00000
MTRIX1   1  0.255423  0.966826  0.002632      -73.52570    1
MTRIX2   1  0.966829 -0.255421 -0.001078       95.53410    1
MTRIX3   1 -0.000370  0.002820 -0.999996       43.58090    1
MTRIX1   2 -0.504331 -0.633817 -0.586452      190.59280    1
MTRIX2   2 -0.640469 -0.180961  0.746360      174.12260    1
MTRIX3   2 -0.579180  0.752017 -0.314676      -28.23390    1
MTRIX1   3 -0.747123 -0.336176  0.573405      143.36501    1
MTRIX2   3 -0.321781 -0.571912 -0.754568      235.73950    1
MTRIX3   3  0.581605 -0.748266  0.319114       71.46620    1
      
PROCHECK
Go to PROCHECK summary
 References