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PDBsum entry 2zqs

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Isomerase PDB id
2zqs
Jmol
Contents
Protein chain
153 a.a.
Ligands
SO4
1PG
Waters ×129
HEADER    ISOMERASE                               19-AUG-08   2ZQS
TITLE     CRYSTAL STRUCTURE OF A MUTANT PIN1 PEPTIDYL-PROLYL CIS-TRANS
TITLE    2 ISOMERASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-
COMPND   3 INTERACTING 1;
COMPND   4 CHAIN: A;
COMPND   5 SYNONYM: PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, ROTAMASE
COMPND   6 PIN1, PPIASE PIN1;
COMPND   7 EC: 5.2.1.8;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PIN1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B+
KEYWDS    PIN1 MUTANT, C113A, CELL CYCLE, ISOMERASE, NUCLEUS,
KEYWDS   2 PHOSPHOPROTEIN, ROTAMASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.JOBICHEN,Y.C.LIOU,J.SIVARAMAN
REVDAT   1   25-AUG-09 2ZQS    0
JRNL        AUTH   C.JOBICHEN,Y.C.LIOU,J.SIVARAMAN
JRNL        TITL   STRUCTURAL STUDIES ON PIN1 MUTANTS
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 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-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.84
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4
REMARK   3   NUMBER OF REFLECTIONS             : 13062
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238
REMARK   3   R VALUE            (WORKING SET) : 0.238
REMARK   3   FREE R VALUE                     : 0.284
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 12.380
REMARK   3   FREE R VALUE TEST SET COUNT      : 1617
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 30.8440 -  4.3500    1.00     1121   167  0.2490 0.2870
REMARK   3     2  4.3500 -  3.4540    0.99     1018   157  0.2070 0.2470
REMARK   3     3  3.4540 -  3.0180    0.98     1004   143  0.2530 0.3120
REMARK   3     4  3.0180 -  2.7420    0.98     1001   136  0.2580 0.3050
REMARK   3     5  2.7420 -  2.5460    0.97      970   135  0.2380 0.2990
REMARK   3     6  2.5460 -  2.3960    0.95      943   152  0.2280 0.2750
REMARK   3     7  2.3960 -  2.2760    0.93      912   139  0.2290 0.2580
REMARK   3     8  2.2760 -  2.1770    0.95      944   127  0.2170 0.2990
REMARK   3     9  2.1770 -  2.0930    0.93      928   107  0.2240 0.2730
REMARK   3    10  2.0930 -  2.0210    0.91      891   141  0.2190 0.3020
REMARK   3    11  2.0210 -  1.9580    0.89      893   103  0.2190 0.3090
REMARK   3    12  1.9580 -  1.9020    0.83      820   110  0.2170 0.2940
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              : 0.37
REMARK   3   B_SOL              : 51.47
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.690
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 29.21
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.27
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.57600
REMARK   3    B22 (A**2) : 1.57600
REMARK   3    B33 (A**2) : -3.15100
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.00000
REMARK   3    B23 (A**2) : 0.00000
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      :  0.005           1237
REMARK   3   ANGLE     :  0.848           1657
REMARK   3   CHIRALITY :  0.060            166
REMARK   3   PLANARITY :  0.004            220
REMARK   3   DIHEDRAL  : 17.143            472
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
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 2ZQS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB028308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-06
REMARK 200  TEMPERATURE           (KELVIN) : 298
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) : 1.54178
REMARK 200  MONOCHROMATOR                  : CN1707
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13863
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.902
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07300
REMARK 200   FOR THE DATA SET  : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1PIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 45.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING
REMARK 280  DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.99000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       24.37900
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       24.37900
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      103.48500
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       24.37900
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       24.37900
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       34.49500
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       24.37900
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       24.37900
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      103.48500
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       24.37900
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       24.37900
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       34.49500
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.99000
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 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     ALA A     2
REMARK 465     ASP A     3
REMARK 465     GLU A     4
REMARK 465     GLU A     5
REMARK 465     ASN A    40
REMARK 465     SER A    41
REMARK 465     SER A    42
REMARK 465     SER A    43
REMARK 465     GLY A    44
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   458     O    HOH A   458     8555     1.66
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    LEU A   7      142.97     83.78
REMARK 500    ARG A  69       86.04   -153.48
REMARK 500    PRO A  70       60.14    -64.28
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 400
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PG A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZQT   RELATED DB: PDB
REMARK 900 RELATED ID: 2ZQU   RELATED DB: PDB
REMARK 900 RELATED ID: 2ZQV   RELATED DB: PDB
REMARK 900 RELATED ID: 1PIN   RELATED DB: PDB
REMARK 900 THIS STRUCTURE IS SIMILAR TO 1PIN EXCEPT THE MUTATION OF
REMARK 900 CYSTEINE 113 TO ALANINE.
DBREF  2ZQS A    1   163  UNP    Q13526   PIN1_HUMAN       1    163
SEQADV 2ZQS ALA A  113  UNP  Q13526    CYS   113 ENGINEERED
SEQRES   1 A  163  MET ALA ASP GLU GLU LYS LEU PRO PRO GLY TRP GLU LYS
SEQRES   2 A  163  ARG MET SER ARG SER SER GLY ARG VAL TYR TYR PHE ASN
SEQRES   3 A  163  HIS ILE THR ASN ALA SER GLN TRP GLU ARG PRO SER GLY
SEQRES   4 A  163  ASN SER SER SER GLY GLY LYS ASN GLY GLN GLY GLU PRO
SEQRES   5 A  163  ALA ARG VAL ARG CYS SER HIS LEU LEU VAL LYS HIS SER
SEQRES   6 A  163  GLN SER ARG ARG PRO SER SER TRP ARG GLN GLU LYS ILE
SEQRES   7 A  163  THR ARG THR LYS GLU GLU ALA LEU GLU LEU ILE ASN GLY
SEQRES   8 A  163  TYR ILE GLN LYS ILE LYS SER GLY GLU GLU ASP PHE GLU
SEQRES   9 A  163  SER LEU ALA SER GLN PHE SER ASP ALA SER SER ALA LYS
SEQRES  10 A  163  ALA ARG GLY ASP LEU GLY ALA PHE SER ARG GLY GLN MET
SEQRES  11 A  163  GLN LYS PRO PHE GLU ASP ALA SER PHE ALA LEU ARG THR
SEQRES  12 A  163  GLY GLU MET SER GLY PRO VAL PHE THR ASP SER GLY ILE
SEQRES  13 A  163  HIS ILE ILE LEU ARG THR GLU
HET    SO4  A 400       5
HET    1PG  A 300      17
HETNAM     SO4 SULFATE ION
HETNAM     1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM   2 1PG  ETHANOL
FORMUL   2  SO4    O4 S 2-
FORMUL   3  1PG    C11 H24 O6
FORMUL   4  HOH   *129(H2 O)
HELIX    1   1 THR A   81  GLY A   99  1                                  19
HELIX    2   2 ASP A  102  SER A  111  1                                  10
HELIX    3   3 ALA A  113  ARG A  119  5                                   7
HELIX    4   4 GLN A  131  PHE A  139  1                                   9
SHEET    1   A 3 TRP A  11  MET A  15  0
SHEET    2   A 3 VAL A  22  ASN A  26 -1  O  TYR A  23   N  ARG A  14
SHEET    3   A 3 SER A  32  GLN A  33 -1  O  GLN A  33   N  TYR A  24
SHEET    1   B 4 ASP A 121  PHE A 125  0
SHEET    2   B 4 VAL A  55  VAL A  62 -1  N  VAL A  55   O  PHE A 125
SHEET    3   B 4 ILE A 156  GLU A 163 -1  O  THR A 162   N  ARG A  56
SHEET    4   B 4 VAL A 150  PHE A 151 -1  N  VAL A 150   O  HIS A 157
SITE     1 AC1  6 LYS A  63  ARG A  68  ARG A  69  SER A 154
SITE     2 AC1  6 HOH A 464  HOH A 516
SITE     1 AC2  6 TYR A  23  SER A  32  TRP A  34  GLU A  35
SITE     2 AC2  6 LYS A  97  HOH A 459
CRYST1   48.758   48.758  137.980  90.00  90.00  90.00 P 43 21 2     8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.020509  0.000000  0.000000        0.00000
SCALE2      0.000000  0.020509  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007247        0.00000
      
PROCHECK
Go to PROCHECK summary
 References