spacer
spacer

PDBsum entry 4bm9

Go to PDB code: 
Top Page protein ligands metals links
Ligase PDB id
4bm9
Jmol
Contents
Protein chain
301 a.a.
Ligands
SO4 ×3
GOL
Metals
_ZN ×8
Waters ×87
HEADER    LIGASE                                  07-MAY-13   4BM9
TITLE     STRUCTURE OF THE AUTOINHIBITED PARKIN CATALYTIC DOMAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE PARKIN;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UPD AND RBR DOMAIN, RESIDUES 137-465;
COMPND   5 SYNONYM: PARKINSON JUVENILE DISEASE PROTEIN 2, PARKINSON DISEASE
COMPND   6  PROTEIN 2, PARKIN;
COMPND   7 EC: 6.3.2.-;
COMPND   8 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: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2
KEYWDS    LIGASE, NEURODEGENERATIVE DISEASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.WAUER,D.KOMANDER
REVDAT   2   14-AUG-13 4BM9    1       JRNL
REVDAT   1   12-JUN-13 4BM9    0
JRNL        AUTH   T.WAUER,D.KOMANDER
JRNL        TITL   STRUCTURE OF THE HUMAN PARKIN LIGASE DOMAIN IN AN
JRNL        TITL 2 AUTOINHIBITED STATE.
JRNL        REF    EMBO J.                       V.  32  2099 2013
JRNL        REFN                   ISSN 0261-4189
JRNL        PMID   23727886
JRNL        DOI    10.1038/EMBOJ.2013.125
REMARK   2
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.250
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.619
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.48
REMARK   3   NUMBER OF REFLECTIONS             : 24502
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1918
REMARK   3   R VALUE            (WORKING SET) : 0.1903
REMARK   3   FREE R VALUE                     : 0.2178
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1
REMARK   3   FREE R VALUE TEST SET COUNT      : 1246
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 48.6300 -  4.6791    0.94     2568   136  0.1811 0.2080
REMARK   3     2  4.6791 -  3.7143    0.96     2577   147  0.1542 0.1749
REMARK   3     3  3.7143 -  3.2449    0.97     2560   127  0.1773 0.2063
REMARK   3     4  3.2449 -  2.9483    0.98     2600   126  0.2042 0.2338
REMARK   3     5  2.9483 -  2.7370    0.98     2605   134  0.2224 0.2569
REMARK   3     6  2.7370 -  2.5756    0.98     2586   128  0.2183 0.2778
REMARK   3     7  2.5756 -  2.4466    0.99     2598   150  0.2267 0.2348
REMARK   3     8  2.4466 -  2.3401    0.99     2571   147  0.2385 0.2556
REMARK   3     9  2.3401 -  2.2501    0.99     2591   151  0.2696 0.3016
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.21
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.60
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 42.75
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.006           2361
REMARK   3   ANGLE     :  0.974           3212
REMARK   3   CHIRALITY :  0.066            344
REMARK   3   PLANARITY :  0.005            418
REMARK   3   DIHEDRAL  : 16.629            832
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 5
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: CHAIN A AND (RESID  142  THROUGH  227 )
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6852  37.8283  40.8627
REMARK   3    T TENSOR
REMARK   3      T11:   0.1429 T22:   0.1607
REMARK   3      T33:   0.3154 T12:  -0.0274
REMARK   3      T13:   0.0532 T23:   0.0689
REMARK   3    L TENSOR
REMARK   3      L11:   3.6699 L22:   1.8064
REMARK   3      L33:   3.5802 L12:  -0.2365
REMARK   3      L13:   0.6200 L23:  -1.0270
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1087 S12:   0.0374 S13:   0.4823
REMARK   3      S21:   0.0519 S22:   0.0142 S23:   0.1748
REMARK   3      S31:  -0.1695 S32:  -0.0859 S33:   0.0990
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: CHAIN A AND (RESID  228  THROUGH  327 )
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5073  29.4903  32.7026
REMARK   3    T TENSOR
REMARK   3      T11:   0.1446 T22:   0.2570
REMARK   3      T33:   0.1531 T12:   0.0293
REMARK   3      T13:   0.0220 T23:   0.0067
REMARK   3    L TENSOR
REMARK   3      L11:   5.3074 L22:   3.2795
REMARK   3      L33:   2.7110 L12:   0.5771
REMARK   3      L13:  -0.8566 L23:  -0.0369
REMARK   3    S TENSOR
REMARK   3      S11:   0.0540 S12:   0.6927 S13:  -0.3486
REMARK   3      S21:  -0.1163 S22:  -0.0830 S23:   0.0320
REMARK   3      S31:   0.0795 S32:  -0.0718 S33:  -0.0099
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: CHAIN A AND (RESID  328  THROUGH  382 )
REMARK   3    ORIGIN FOR THE GROUP (A):  37.2630  37.5980  41.5675
REMARK   3    T TENSOR
REMARK   3      T11:   0.8087 T22:   0.4265
REMARK   3      T33:   0.5610 T12:  -0.1976
REMARK   3      T13:  -0.1288 T23:   0.0965
REMARK   3    L TENSOR
REMARK   3      L11:   1.7533 L22:   5.1590
REMARK   3      L33:   1.3574 L12:   0.8209
REMARK   3      L13:  -0.6055 L23:   0.5430
REMARK   3    S TENSOR
REMARK   3      S11:   0.3375 S12:  -0.1642 S13:  -0.1934
REMARK   3      S21:   1.2760 S22:  -0.9036 S23:  -1.7778
REMARK   3      S31:   0.0628 S32:   0.3815 S33:   0.1883
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: CHAIN A AND (RESID  391  THROUGH  404 )
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6201  14.2401  27.2699
REMARK   3    T TENSOR
REMARK   3      T11:   0.4545 T22:   0.4780
REMARK   3      T33:   0.9018 T12:  -0.0458
REMARK   3      T13:  -0.0453 T23:  -0.2219
REMARK   3    L TENSOR
REMARK   3      L11:   0.1097 L22:   5.3914
REMARK   3      L33:   6.5200 L12:   0.0739
REMARK   3      L13:   0.6231 L23:   0.1201
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0301 S12:   0.2973 S13:  -0.2044
REMARK   3      S21:  -0.4234 S22:  -0.0775 S23:   0.2869
REMARK   3      S31:   0.4769 S32:  -0.2901 S33:   0.3001
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: CHAIN A AND (RESID  414  THROUGH  465 )
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2654  22.9616  36.8067
REMARK   3    T TENSOR
REMARK   3      T11:   0.3042 T22:   0.2224
REMARK   3      T33:   0.2854 T12:  -0.0568
REMARK   3      T13:   0.0075 T23:   0.0941
REMARK   3    L TENSOR
REMARK   3      L11:   3.9238 L22:   2.8388
REMARK   3      L33:   1.4560 L12:   2.6615
REMARK   3      L13:   0.1217 L23:  -0.0545
REMARK   3    S TENSOR
REMARK   3      S11:  -0.3499 S12:   0.5719 S13:   0.1755
REMARK   3      S21:  -0.6103 S22:   0.2344 S23:   0.1779
REMARK   3      S31:   0.0441 S32:  -0.0514 S33:   0.1077
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4BM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAY-13.
REMARK 100 THE PDBE ID CODE IS EBI-56782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-13
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I04
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24502
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.25
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.33
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0
REMARK 200  DATA REDUNDANCY                : 5
REMARK 200  R MERGE                    (I) : 0.09
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 5
REMARK 200  R MERGE FOR SHELL          (I) : 0.64
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.8
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M LITHIUM SULPHATE, 10 MM
REMARK 280  MAGNESIUM CHLORIDE, 50 MM MES (PH 5.4)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z
REMARK 290       6555   -X,-X+Y,-Z
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290      18555   -X+1/3,-X+Y+2/3,-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        0.00000
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        0.00000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
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        0.00000
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       84.21000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.61867
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       32.39367
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       84.21000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       48.61867
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       32.39367
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       84.21000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       48.61867
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       32.39367
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       84.21000
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       48.61867
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       32.39367
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       84.21000
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       48.61867
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       32.39367
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       84.21000
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       48.61867
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       32.39367
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       97.23733
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       64.78733
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       97.23733
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       64.78733
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       97.23733
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       64.78733
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       97.23733
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       64.78733
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       97.23733
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       64.78733
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       97.23733
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       64.78733
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -586.4 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        0.00000
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   3  0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       97.18100
REMARK 350   BIOMT1   4 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   4 -0.866025  0.500000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       97.18100
REMARK 350   BIOMT1   5 -0.500000 -0.866025  0.000000        0.00000
REMARK 350   BIOMT2   5  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000       97.18100
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  S   SO4 A1475   LIES ON A SPECIAL POSITION.
REMARK 375      HOH A2039   LIES ON A SPECIAL POSITION.
REMARK 375      HOH A2082   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     PRO A   137
REMARK 465     ALA A   138
REMARK 465     GLY A   139
REMARK 465     ARG A   140
REMARK 465     SER A   141
REMARK 465     GLY A   354
REMARK 465     GLY A   355
REMARK 465     ASN A   356
REMARK 465     GLY A   357
REMARK 465     LEU A   358
REMARK 465     GLY A   359
REMARK 465     CYS A   360
REMARK 465     GLY A   361
REMARK 465     SER A   384
REMARK 465     GLY A   385
REMARK 465     THR A   386
REMARK 465     THR A   387
REMARK 465     THR A   388
REMARK 465     GLN A   389
REMARK 465     ALA A   390
REMARK 465     ALA A   405
REMARK 465     ALA A   406
REMARK 465     SER A   407
REMARK 465     LYS A   408
REMARK 465     GLU A   409
REMARK 465     THR A   410
REMARK 465     ILE A   411
REMARK 465     LYS A   412
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     GLN A 155    CG   CD   OE1  NE2
REMARK 470     GLU A 195    CG   CD   OE1  OE2
REMARK 470     GLN A 197    CG   CD   OE1  NE2
REMARK 470     ARG A 256    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 282    CG   CD   OE1  NE2
REMARK 470     LEU A 283    CG   CD1  CD2
REMARK 470     ASN A 295    CG   OD1  ND2
REMARK 470     GLU A 310    CB   CG   CD   OE1  OE2
REMARK 470     ASN A 313    CG   OD1  ND2
REMARK 470     ARG A 334    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 344    CG   CD   OE1  OE2
REMARK 470     ASP A 346    CG   OD1  OD2
REMARK 470     GLU A 353    CG   CD   OE1  OE2
REMARK 470     GLU A 370    CG   CD   OE1  OE2
REMARK 470     GLU A 374    CG   CD   OE1  OE2
REMARK 470     TYR A 391    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG A 392    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 395    CG   CD   OE1  OE2
REMARK 470     ARG A 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU A 399    CG   CD   OE1  OE2
REMARK 470     ARG A 402    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 413    CG   CD   CE   NZ
REMARK 470     GLU A 426    CG   CD   OE1  OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OH   TYR A   143     OD2  ASP A   464              2.08
REMARK 500
REMARK 500 REMARK: NULL
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    PRO A 199      -73.47    -34.78
REMARK 500    THR A 242       -1.50     61.25
REMARK 500    CYS A 441      -71.84   -110.79
REMARK 500    HIS A 461       55.87   -153.39
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 A1466  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 150   SG
REMARK 620 2 CYS A 154   SG  114.1
REMARK 620 3 CYS A 212   SG  113.3 112.4
REMARK 620 4 HIS A 215   NE2 108.0  99.2 108.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1467  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 253   SG
REMARK 620 2 HIS A 257   ND1  93.0
REMARK 620 3 CYS A 293   SG  116.4 114.8
REMARK 620 4 CYS A 289   SG  113.6  97.9 117.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1468  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 446   SG
REMARK 620 2 CYS A 449   SG  112.9
REMARK 620 3 CYS A 457   SG  113.1 115.1
REMARK 620 4 HIS A 461   NE2 103.2 103.9 107.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1469  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 196   SG
REMARK 620 2 CYS A 201   SG  115.0
REMARK 620 3 CYS A 166   SG  110.7 107.9
REMARK 620 4 CYS A 169   SG  107.6 110.1 105.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1470  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 238   SG
REMARK 620 2 CYS A 241   SG  105.7
REMARK 620 3 CYS A 260   SG  115.6 115.0
REMARK 620 4 CYS A 263   SG  108.3 109.8 102.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1471  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 332   SG
REMARK 620 2 CYS A 337   SG  107.8
REMARK 620 3 CYS A 352   SG   91.9 102.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1472  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 377   SG
REMARK 620 2 HIS A 373   NE2  99.7
REMARK 620 3 CYS A 365   SG  111.7  98.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1473  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 418   SG
REMARK 620 2 CYS A 421   SG  110.7
REMARK 620 3 CYS A 436   SG  114.7 101.5
REMARK 620 4 CYS A 441   SG  104.9 116.5 109.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1466
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1467
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1469
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1470
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1471
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1472
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1473
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1474
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1477
DBREF  4BM9 A  137   465  UNP    O60260   PRKN2_HUMAN    137    465
SEQRES   1 A  329  PRO ALA GLY ARG SER ILE TYR ASN SER PHE TYR VAL TYR
SEQRES   2 A  329  CYS LYS GLY PRO CYS GLN ARG VAL GLN PRO GLY LYS LEU
SEQRES   3 A  329  ARG VAL GLN CYS SER THR CYS ARG GLN ALA THR LEU THR
SEQRES   4 A  329  LEU THR GLN GLY PRO SER CYS TRP ASP ASP VAL LEU ILE
SEQRES   5 A  329  PRO ASN ARG MET SER GLY GLU CYS GLN SER PRO HIS CYS
SEQRES   6 A  329  PRO GLY THR SER ALA GLU PHE PHE PHE LYS CYS GLY ALA
SEQRES   7 A  329  HIS PRO THR SER ASP LYS GLU THR SER VAL ALA LEU HIS
SEQRES   8 A  329  LEU ILE ALA THR ASN SER ARG ASN ILE THR CYS ILE THR
SEQRES   9 A  329  CYS THR ASP VAL ARG SER PRO VAL LEU VAL PHE GLN CYS
SEQRES  10 A  329  ASN SER ARG HIS VAL ILE CYS LEU ASP CYS PHE HIS LEU
SEQRES  11 A  329  TYR CYS VAL THR ARG LEU ASN ASP ARG GLN PHE VAL HIS
SEQRES  12 A  329  ASP PRO GLN LEU GLY TYR SER LEU PRO CYS VAL ALA GLY
SEQRES  13 A  329  CYS PRO ASN SER LEU ILE LYS GLU LEU HIS HIS PHE ARG
SEQRES  14 A  329  ILE LEU GLY GLU GLU GLN TYR ASN ARG TYR GLN GLN TYR
SEQRES  15 A  329  GLY ALA GLU GLU CYS VAL LEU GLN MET GLY GLY VAL LEU
SEQRES  16 A  329  CYS PRO ARG PRO GLY CYS GLY ALA GLY LEU LEU PRO GLU
SEQRES  17 A  329  PRO ASP GLN ARG LYS VAL THR CYS GLU GLY GLY ASN GLY
SEQRES  18 A  329  LEU GLY CYS GLY PHE ALA PHE CYS ARG GLU CYS LYS GLU
SEQRES  19 A  329  ALA TYR HIS GLU GLY GLU CYS SER ALA VAL PHE GLU ALA
SEQRES  20 A  329  SER GLY THR THR THR GLN ALA TYR ARG VAL ASP GLU ARG
SEQRES  21 A  329  ALA ALA GLU GLN ALA ARG TRP GLU ALA ALA SER LYS GLU
SEQRES  22 A  329  THR ILE LYS LYS THR THR LYS PRO CYS PRO ARG CYS HIS
SEQRES  23 A  329  VAL PRO VAL GLU LYS ASN GLY GLY CYS MET HIS MET LYS
SEQRES  24 A  329  CYS PRO GLN PRO GLN CYS ARG LEU GLU TRP CYS TRP ASN
SEQRES  25 A  329  CYS GLY CYS GLU TRP ASN ARG VAL CYS MET GLY ASP HIS
SEQRES  26 A  329  TRP PHE ASP VAL
HET     ZN  A1466       1
HET     ZN  A1467       1
HET     ZN  A1468       1
HET     ZN  A1469       1
HET     ZN  A1470       1
HET     ZN  A1471       1
HET     ZN  A1472       1
HET     ZN  A1473       1
HET    SO4  A1474       5
HET    SO4  A1475       5
HET    SO4  A1476       5
HET    GOL  A1477       6
HETNAM     SO4 SULFATE ION
HETNAM     GOL GLYCEROL
HETNAM      ZN ZINC ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  SO4    3(O4 S 2-)
FORMUL   3  GOL    C3 H8 O3
FORMUL   4   ZN    8(ZN 2+)
FORMUL   5  HOH   *87(H2 O)
HELIX    1   1 CYS A  182  ILE A  188  1                                   7
HELIX    2   2 LEU A  261  ASP A  274  1                                  14
HELIX    3   3 GLU A  300  LEU A  307  5                                   8
HELIX    4   4 GLY A  308  GLN A  317  1                                  10
HELIX    5   5 GLN A  317  MET A  327  1                                  11
HELIX    6   6 SER A  378  GLU A  382  5                                   5
HELIX    7   7 ASP A  394  ALA A  401  1                                   8
HELIX    8   8 ASN A  454  TRP A  462  1                                   9
SHEET    1  AA 4 ALA A 206  CYS A 212  0
SHEET    2  AA 4 ARG A 156  CYS A 166 -1  O  LYS A 161   N  LYS A 211
SHEET    3  AA 4 TYR A 147  CYS A 150 -1  O  VAL A 148   N  GLN A 158
SHEET    4  AA 4 VAL A 224  ALA A 225 -1  O  VAL A 224   N  TYR A 149
SHEET    1  AB 2 LEU A 174  LEU A 176  0
SHEET    2  AB 2 GLY A 194  CYS A 196 -1  O  GLU A 195   N  THR A 175
SHEET    1  AC 3 ILE A 229  ALA A 230  0
SHEET    2  AC 3 VAL A 248  VAL A 250 -1  O  VAL A 248   N  ALA A 230
SHEET    3  AC 3 VAL A 258  CYS A 260 -1  O  ILE A 259   N  LEU A 249
SHEET    1  AD 2 VAL A 278  ASP A 280  0
SHEET    2  AD 2 GLY A 284  SER A 286 -1  O  GLY A 284   N  ASP A 280
SHEET    1  AE 2 VAL A 330  LEU A 331  0
SHEET    2  AE 2 GLY A 340  LEU A 341 -1  O  LEU A 341   N  VAL A 330
SHEET    1  AF 2 LYS A 349  THR A 351  0
SHEET    2  AF 2 ALA A 363  CYS A 365 -1  O  PHE A 364   N  VAL A 350
SHEET    1  AG 2 THR A 415  PRO A 417  0
SHEET    2  AG 2 PRO A 424  GLU A 426 -1  O  VAL A 425   N  LYS A 416
SHEET    1  AH 2 HIS A 433  LYS A 435  0
SHEET    2  AH 2 GLU A 444  CYS A 446 -1  O  TRP A 445   N  MET A 434
LINK        ZN    ZN A1466                 SG  CYS A 150     1555   1555  2.30
LINK        ZN    ZN A1466                 SG  CYS A 154     1555   1555  2.39
LINK        ZN    ZN A1466                 SG  CYS A 212     1555   1555  2.34
LINK        ZN    ZN A1466                 NE2 HIS A 215     1555   1555  2.05
LINK        ZN    ZN A1467                 SG  CYS A 253     1555   1555  2.35
LINK        ZN    ZN A1467                 ND1 HIS A 257     1555   1555  1.83
LINK        ZN    ZN A1467                 SG  CYS A 293     1555   1555  2.46
LINK        ZN    ZN A1467                 SG  CYS A 289     1555   1555  2.44
LINK        ZN    ZN A1468                 SG  CYS A 446     1555   1555  2.26
LINK        ZN    ZN A1468                 SG  CYS A 449     1555   1555  2.36
LINK        ZN    ZN A1468                 SG  CYS A 457     1555   1555  2.24
LINK        ZN    ZN A1468                 NE2 HIS A 461     1555   1555  2.09
LINK        ZN    ZN A1469                 SG  CYS A 196     1555   1555  2.26
LINK        ZN    ZN A1469                 SG  CYS A 201     1555   1555  2.29
LINK        ZN    ZN A1469                 SG  CYS A 166     1555   1555  2.42
LINK        ZN    ZN A1469                 SG  CYS A 169     1555   1555  2.21
LINK        ZN    ZN A1470                 SG  CYS A 241     1555   1555  2.35
LINK        ZN    ZN A1470                 SG  CYS A 260     1555   1555  2.32
LINK        ZN    ZN A1470                 SG  CYS A 263     1555   1555  2.33
LINK        ZN    ZN A1470                 SG  CYS A 238     1555   1555  2.34
LINK        ZN    ZN A1471                 SG  CYS A 337     1555   1555  2.15
LINK        ZN    ZN A1471                 SG  CYS A 352     1555   1555  2.11
LINK        ZN    ZN A1471                 SG  CYS A 332     1555   1555  2.56
LINK        ZN    ZN A1472                 NE2 HIS A 373     1555   1555  1.93
LINK        ZN    ZN A1472                 SG  CYS A 365     1555   1555  2.39
LINK        ZN    ZN A1472                 SG  CYS A 377     1555   1555  2.30
LINK        ZN    ZN A1473                 SG  CYS A 421     1555   1555  2.31
LINK        ZN    ZN A1473                 SG  CYS A 436     1555   1555  2.33
LINK        ZN    ZN A1473                 SG  CYS A 441     1555   1555  2.28
LINK        ZN    ZN A1473                 SG  CYS A 418     1555   1555  2.32
CISPEP   1 GLY A  152    PRO A  153          0         1.67
CISPEP   2 SER A  246    PRO A  247          0        -1.11
SITE     1 AC1  4 CYS A 150  CYS A 154  CYS A 212  HIS A 215
SITE     1 AC2  4 CYS A 253  HIS A 257  CYS A 289  CYS A 293
SITE     1 AC3  4 CYS A 446  CYS A 449  CYS A 457  HIS A 461
SITE     1 AC4  4 CYS A 166  CYS A 169  CYS A 196  CYS A 201
SITE     1 AC5  4 CYS A 238  CYS A 241  CYS A 260  CYS A 263
SITE     1 AC6  3 CYS A 332  CYS A 337  CYS A 352
SITE     1 AC7  4 CYS A 365  CYS A 368  HIS A 373  CYS A 377
SITE     1 AC8  4 CYS A 418  CYS A 421  CYS A 436  CYS A 441
SITE     1 AC9  4 ARG A 163  LYS A 211  ARG A 420  HOH A2045
SITE     1 BC1  2 ASN A 454  ARG A 455
SITE     1 BC2  5 LYS A 151  HIS A 302  ARG A 305  TYR A 312
SITE     2 BC2  5 HOH A2087
SITE     1 BC3  3 LYS A 416  TRP A 447  ASN A 448
CRYST1  168.420  168.420   97.181  90.00  90.00 120.00 H 3 2        18
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      0.005938  0.003428  0.000000        0.00000
SCALE2      0.000000  0.006856  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010290        0.00000
      
PROCHECK
Go to PROCHECK summary
 References