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PDBsum entry 1oy6

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Membrane protein PDB id
1oy6
Jmol
Contents
Protein chain
1006 a.a. *
* Residue conservation analysis
HEADER    MEMBRANE PROTEIN                        03-APR-03   1OY6
TITLE     STRUCTURAL BASIS OF THE MULTIPLE BINDING CAPACITY OF THE ACRB
TITLE    2 MULTIDRUG EFFLUX PUMP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ACRIFLAVINE RESISTANCE PROTEIN B;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: ACRB OR ACRE OR B0462;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    MEMBRANE PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.W.YU,G.MCDERMOTT,H.I.ZGURSKAYA,H.NIKAIDO,D.E.KOSHLAND JR.
REVDAT   3   13-JUL-11 1OY6    1       VERSN
REVDAT   2   24-FEB-09 1OY6    1       VERSN
REVDAT   1   13-MAY-03 1OY6    0
JRNL        AUTH   E.W.YU,G.MCDERMOTT,H.I.ZGURSKAYA,H.NIKAIDO,D.E.KOSHLAND
JRNL        TITL   STRUCTURAL BASIS OF MULTIPLE DRUG-BINDING CAPACITY OF THE
JRNL        TITL 2 ACRB MULTIDRUG EFFLUX PUMP.
JRNL        REF    SCIENCE                       V. 300   976 2003
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   12738864
JRNL        DOI    10.1126/SCIENCE.1083137
REMARK   2
REMARK   2 RESOLUTION.    3.68 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.68
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 34832
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.275
REMARK   3   R VALUE            (WORKING SET) : 0.272
REMARK   3   FREE R VALUE                     : 0.330
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1741
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7639
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1OY6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-03.
REMARK 100 THE RCSB ID CODE IS RCSB018793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 8.2.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34832
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 74.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       71.77850
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       41.44134
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      173.21233
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       71.77850
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       41.44134
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      173.21233
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       71.77850
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       41.44134
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      173.21233
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       71.77850
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       41.44134
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      173.21233
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       71.77850
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       41.44134
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      173.21233
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       71.77850
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       41.44134
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      173.21233
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       82.88267
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      346.42467
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       82.88267
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      346.42467
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       82.88267
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      346.42467
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       82.88267
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      346.42467
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       82.88267
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      346.42467
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       82.88267
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      346.42467
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 19040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 112260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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      143.55700
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       71.77850
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      124.32401
REMARK 350   BIOMT3   3  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     PRO A     2
REMARK 465     ASN A     3
REMARK 465     PHE A     4
REMARK 465     PHE A     5
REMARK 465     ILE A     6
REMARK 465     PRO A   499
REMARK 465     ILE A   500
REMARK 465     ALA A   501
REMARK 465     LYS A   502
REMARK 465     GLY A   503
REMARK 465     ASP A   504
REMARK 465     HIS A   505
REMARK 465     GLY A   506
REMARK 465     GLU A   507
REMARK 465     GLY A   508
REMARK 465     LYS A   509
REMARK 465     LYS A   510
REMARK 465     GLY A   511
REMARK 465     PHE A   512
REMARK 465     ASP A   711
REMARK 465     THR A   860
REMARK 465     GLY A   861
REMARK 465     MET A   862
REMARK 465     SER A   863
REMARK 465     TYR A   864
REMARK 465     GLN A   865
REMARK 465     GLU A   866
REMARK 465     ARG A   867
REMARK 465     LEU A   868
REMARK 465     ASN A  1037
REMARK 465     GLU A  1038
REMARK 465     ASP A  1039
REMARK 465     ILE A  1040
REMARK 465     GLU A  1041
REMARK 465     HIS A  1042
REMARK 465     SER A  1043
REMARK 465     HIS A  1044
REMARK 465     THR A  1045
REMARK 465     VAL A  1046
REMARK 465     ASP A  1047
REMARK 465     HIS A  1048
REMARK 465     HIS A  1049
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 407   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 795   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 858   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A1032   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
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   9     -110.67    -64.73
REMARK 500    ILE A  10      -82.91     13.95
REMARK 500    LEU A  21      -70.07    -80.55
REMARK 500    LYS A  29       48.84   -160.23
REMARK 500    ALA A  33      175.81    -57.08
REMARK 500    GLN A  34     -163.14    -72.95
REMARK 500    TYR A  35      149.46    -28.04
REMARK 500    ALA A  47      134.97   -170.63
REMARK 500    TYR A  49       86.77   -156.84
REMARK 500    ALA A  52      125.89    -38.47
REMARK 500    ASN A  68       30.23    -92.43
REMARK 500    ASN A  74      120.90     62.67
REMARK 500    LEU A  75      115.34   -177.54
REMARK 500    ASN A 109       48.36   -109.03
REMARK 500    LYS A 110      -42.18   -164.55
REMARK 500    LEU A 117       40.88   -101.70
REMARK 500    SER A 133        3.79   -152.70
REMARK 500    SER A 134       42.87     26.79
REMARK 500    SER A 135      124.94   -172.31
REMARK 500    LEU A 137      -74.62   -138.94
REMARK 500    THR A 145      -55.97   -122.76
REMARK 500    ASP A 146      -81.36    -81.84
REMARK 500    GLU A 152      -40.96    178.98
REMARK 500    ASN A 161      -51.32   -168.11
REMARK 500    SER A 167        3.80    -69.56
REMARK 500    ARG A 168      -52.89   -125.67
REMARK 500    SER A 170       70.71     37.21
REMARK 500    ASP A 174      105.00   -163.05
REMARK 500    MET A 184       96.37    -58.40
REMARK 500    GLN A 197       83.06     66.44
REMARK 500    LYS A 208       57.15    -93.63
REMARK 500    ALA A 209      -54.90   -176.39
REMARK 500    GLN A 218      145.97   -171.37
REMARK 500    LYS A 226      107.90    -54.45
REMARK 500    ALA A 236     -146.87   -115.02
REMARK 500    LYS A 248       43.22   -102.38
REMARK 500    GLN A 255      -51.86     -9.43
REMARK 500    ASP A 256       35.46    -87.67
REMARK 500    THR A 295      101.61    -11.32
REMARK 500    ALA A 299      -94.74     60.98
REMARK 500    TYR A 327       89.22      7.90
REMARK 500    THR A 365       48.04    -90.24
REMARK 500    LEU A 366      -41.15   -138.57
REMARK 500    SER A 389     -168.76   -114.29
REMARK 500    MET A 420       36.43    -92.07
REMARK 500    ALA A 421      -50.42   -166.97
REMARK 500    PRO A 427      174.84    -40.73
REMARK 500    PHE A 459      158.93    -22.34
REMARK 500    THR A 463       37.19    -89.15
REMARK 500    ILE A 466      -71.19    -49.61
REMARK 500
REMARK 500 THIS ENTRY HAS     105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ILE A  10        24.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IWG   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
DBREF  1OY6 A    1  1049  UNP    P31224   ACRB_ECOLI       1   1049
SEQRES   1 A 1049  MET PRO ASN PHE PHE ILE ASP ARG PRO ILE PHE ALA TRP
SEQRES   2 A 1049  VAL ILE ALA ILE ILE ILE MET LEU ALA GLY GLY LEU ALA
SEQRES   3 A 1049  ILE LEU LYS LEU PRO VAL ALA GLN TYR PRO THR ILE ALA
SEQRES   4 A 1049  PRO PRO ALA VAL THR ILE SER ALA SER TYR PRO GLY ALA
SEQRES   5 A 1049  ASP ALA LYS THR VAL GLN ASP THR VAL THR GLN VAL ILE
SEQRES   6 A 1049  GLU GLN ASN MET ASN GLY ILE ASP ASN LEU MET TYR MET
SEQRES   7 A 1049  SER SER ASN SER ASP SER THR GLY THR VAL GLN ILE THR
SEQRES   8 A 1049  LEU THR PHE GLU SER GLY THR ASP ALA ASP ILE ALA GLN
SEQRES   9 A 1049  VAL GLN VAL GLN ASN LYS LEU GLN LEU ALA MET PRO LEU
SEQRES  10 A 1049  LEU PRO GLN GLU VAL GLN GLN GLN GLY VAL SER VAL GLU
SEQRES  11 A 1049  LYS SER SER SER SER PHE LEU MET VAL VAL GLY VAL ILE
SEQRES  12 A 1049  ASN THR ASP GLY THR MET THR GLN GLU ASP ILE SER ASP
SEQRES  13 A 1049  TYR VAL ALA ALA ASN MET LYS ASP ALA ILE SER ARG THR
SEQRES  14 A 1049  SER GLY VAL GLY ASP VAL GLN LEU PHE GLY SER GLN TYR
SEQRES  15 A 1049  ALA MET ARG ILE TRP MET ASN PRO ASN GLU LEU ASN LYS
SEQRES  16 A 1049  PHE GLN LEU THR PRO VAL ASP VAL ILE THR ALA ILE LYS
SEQRES  17 A 1049  ALA GLN ASN ALA GLN VAL ALA ALA GLY GLN LEU GLY GLY
SEQRES  18 A 1049  THR PRO PRO VAL LYS GLY GLN GLN LEU ASN ALA SER ILE
SEQRES  19 A 1049  ILE ALA GLN THR ARG LEU THR SER THR GLU GLU PHE GLY
SEQRES  20 A 1049  LYS ILE LEU LEU LYS VAL ASN GLN ASP GLY SER ARG VAL
SEQRES  21 A 1049  LEU LEU ARG ASP VAL ALA LYS ILE GLU LEU GLY GLY GLU
SEQRES  22 A 1049  ASN TYR ASP ILE ILE ALA GLU PHE ASN GLY GLN PRO ALA
SEQRES  23 A 1049  SER GLY LEU GLY ILE LYS LEU ALA THR GLY ALA ASN ALA
SEQRES  24 A 1049  LEU ASP THR ALA ALA ALA ILE ARG ALA GLU LEU ALA LYS
SEQRES  25 A 1049  MET GLU PRO PHE PHE PRO SER GLY LEU LYS ILE VAL TYR
SEQRES  26 A 1049  PRO TYR ASP THR THR PRO PHE VAL LYS ILE SER ILE HIS
SEQRES  27 A 1049  GLU VAL VAL LYS THR LEU VAL GLU ALA ILE ILE LEU VAL
SEQRES  28 A 1049  PHE LEU VAL MET TYR LEU PHE LEU GLN ASN PHE ARG ALA
SEQRES  29 A 1049  THR LEU ILE PRO THR ILE ALA VAL PRO VAL VAL LEU LEU
SEQRES  30 A 1049  GLY THR PHE ALA VAL LEU ALA ALA PHE GLY PHE SER ILE
SEQRES  31 A 1049  ASN THR LEU THR MET PHE GLY MET VAL LEU ALA ILE GLY
SEQRES  32 A 1049  LEU LEU VAL ASP ASP ALA ILE VAL VAL VAL GLU ASN VAL
SEQRES  33 A 1049  GLU ARG VAL MET ALA GLU GLU GLY LEU PRO PRO LYS GLU
SEQRES  34 A 1049  ALA THR ARG LYS SER MET GLY GLN ILE GLN GLY ALA LEU
SEQRES  35 A 1049  VAL GLY ILE ALA MET VAL LEU SER ALA VAL PHE VAL PRO
SEQRES  36 A 1049  MET ALA PHE PHE GLY GLY SER THR GLY ALA ILE TYR ARG
SEQRES  37 A 1049  GLN PHE SER ILE THR ILE VAL SER ALA MET ALA LEU SER
SEQRES  38 A 1049  VAL LEU VAL ALA LEU ILE LEU THR PRO ALA LEU CYS ALA
SEQRES  39 A 1049  THR MET LEU LYS PRO ILE ALA LYS GLY ASP HIS GLY GLU
SEQRES  40 A 1049  GLY LYS LYS GLY PHE PHE GLY TRP PHE ASN ARG MET PHE
SEQRES  41 A 1049  GLU LYS SER THR HIS HIS TYR THR ASP SER VAL GLY GLY
SEQRES  42 A 1049  ILE LEU ARG SER THR GLY ARG TYR LEU VAL LEU TYR LEU
SEQRES  43 A 1049  ILE ILE VAL VAL GLY MET ALA TYR LEU PHE VAL ARG LEU
SEQRES  44 A 1049  PRO SER SER PHE LEU PRO ASP GLU ASP GLN GLY VAL PHE
SEQRES  45 A 1049  MET THR MET VAL GLN LEU PRO ALA GLY ALA THR GLN GLU
SEQRES  46 A 1049  ARG THR GLN LYS VAL LEU ASN GLU VAL THR HIS TYR TYR
SEQRES  47 A 1049  LEU THR LYS GLU LYS ASN ASN VAL GLU SER VAL PHE ALA
SEQRES  48 A 1049  VAL ASN GLY PHE GLY PHE ALA GLY ARG GLY GLN ASN THR
SEQRES  49 A 1049  GLY ILE ALA PHE VAL SER LEU LYS ASP TRP ALA ASP ARG
SEQRES  50 A 1049  PRO GLY GLU GLU ASN LYS VAL GLU ALA ILE THR MET ARG
SEQRES  51 A 1049  ALA THR ARG ALA PHE SER GLN ILE LYS ASP ALA MET VAL
SEQRES  52 A 1049  PHE ALA PHE ASN LEU PRO ALA ILE VAL GLU LEU GLY THR
SEQRES  53 A 1049  ALA THR GLY PHE ASP PHE GLU LEU ILE ASP GLN ALA GLY
SEQRES  54 A 1049  LEU GLY HIS GLU LYS LEU THR GLN ALA ARG ASN GLN LEU
SEQRES  55 A 1049  LEU ALA GLU ALA ALA LYS HIS PRO ASP MET LEU THR SER
SEQRES  56 A 1049  VAL ARG PRO ASN GLY LEU GLU ASP THR PRO GLN PHE LYS
SEQRES  57 A 1049  ILE ASP ILE ASP GLN GLU LYS ALA GLN ALA LEU GLY VAL
SEQRES  58 A 1049  SER ILE ASN ASP ILE ASN THR THR LEU GLY ALA ALA TRP
SEQRES  59 A 1049  GLY GLY SER TYR VAL ASN ASP PHE ILE ASP ARG GLY ARG
SEQRES  60 A 1049  VAL LYS LYS VAL TYR VAL MET SER GLU ALA LYS TYR ARG
SEQRES  61 A 1049  MET LEU PRO ASP ASP ILE GLY ASP TRP TYR VAL ARG ALA
SEQRES  62 A 1049  ALA ASP GLY GLN MET VAL PRO PHE SER ALA PHE SER SER
SEQRES  63 A 1049  SER ARG TRP GLU TYR GLY SER PRO ARG LEU GLU ARG TYR
SEQRES  64 A 1049  ASN GLY LEU PRO SER MET GLU ILE LEU GLY GLN ALA ALA
SEQRES  65 A 1049  PRO GLY LYS SER THR GLY GLU ALA MET GLU LEU MET GLU
SEQRES  66 A 1049  GLN LEU ALA SER LYS LEU PRO THR GLY VAL GLY TYR ASP
SEQRES  67 A 1049  TRP THR GLY MET SER TYR GLN GLU ARG LEU SER GLY ASN
SEQRES  68 A 1049  GLN ALA PRO SER LEU TYR ALA ILE SER LEU ILE VAL VAL
SEQRES  69 A 1049  PHE LEU CYS LEU ALA ALA LEU TYR GLU SER TRP SER ILE
SEQRES  70 A 1049  PRO PHE SER VAL MET LEU VAL VAL PRO LEU GLY VAL ILE
SEQRES  71 A 1049  GLY ALA LEU LEU ALA ALA THR PHE ARG GLY LEU THR ASN
SEQRES  72 A 1049  ASP VAL TYR PHE GLN VAL GLY LEU LEU THR THR ILE GLY
SEQRES  73 A 1049  LEU SER ALA LYS ASN ALA ILE LEU ILE VAL GLU PHE ALA
SEQRES  74 A 1049  LYS ASP LEU MET ASP LYS GLU GLY LYS GLY LEU ILE GLU
SEQRES  75 A 1049  ALA THR LEU ASP ALA VAL ARG MET ARG LEU ARG PRO ILE
SEQRES  76 A 1049  LEU MET THR SER LEU ALA PHE ILE LEU GLY VAL MET PRO
SEQRES  77 A 1049  LEU VAL ILE SER THR GLY ALA GLY SER GLY ALA GLN ASN
SEQRES  78 A 1049  ALA VAL GLY THR GLY VAL MET GLY GLY MET VAL THR ALA
SEQRES  79 A 1049  THR VAL LEU ALA ILE PHE PHE VAL PRO VAL PHE PHE VAL
SEQRES  80 A 1049  VAL VAL ARG ARG ARG PHE SER ARG LYS ASN GLU ASP ILE
SEQRES  81 A 1049  GLU HIS SER HIS THR VAL ASP HIS HIS
HELIX    1   1 PRO A    9  ILE A   27  1                                  19
HELIX    2   2 ASP A   53  VAL A   61  1                                   9
HELIX    3   3 VAL A   61  ASN A   68  1                                   8
HELIX    4   4 ASP A   99  GLN A  112  1                                  14
HELIX    5   5 ALA A  114  LEU A  118  5                                   5
HELIX    6   6 PRO A  119  GLN A  124  1                                   6
HELIX    7   7 GLU A  152  ALA A  160  1                                   9
HELIX    8   8 MET A  162  SER A  167  1                                   6
HELIX    9   9 ASN A  189  PHE A  196  1                                   8
HELIX   10  10 THR A  199  ASN A  211  1                                  13
HELIX   11  11 SER A  242  LYS A  248  1                                   7
HELIX   12  12 LEU A  262  VAL A  265  1                                   4
HELIX   13  13 ALA A  299  LYS A  312  1                                  14
HELIX   14  14 MET A  313  PHE A  317  5                                   5
HELIX   15  15 THR A  329  LEU A  359  1                                  31
HELIX   16  16 ALA A  371  ALA A  385  1                                  15
HELIX   17  17 ASN A  391  GLU A  423  1                                  33
HELIX   18  18 PRO A  427  VAL A  454  1                                  28
HELIX   19  19 GLY A  460  SER A  462  5                                   3
HELIX   20  20 THR A  463  ALA A  485  1                                  23
HELIX   21  21 ILE A  487  MET A  496  1                                  10
HELIX   22  22 PHE A  513  HIS A  525  1                                  13
HELIX   23  23 HIS A  525  SER A  537  1                                  13
HELIX   24  24 THR A  538  ARG A  558  1                                  21
HELIX   25  25 THR A  583  LYS A  601  1                                  19
HELIX   26  26 LYS A  643  ILE A  658  1                                  16
HELIX   27  27 GLY A  691  HIS A  709  1                                  19
HELIX   28  28 ASP A  732  GLY A  740  1                                   9
HELIX   29  29 SER A  742  GLY A  755  1                                  14
HELIX   30  30 GLU A  776  ARG A  780  5                                   5
HELIX   31  31 LEU A  782  GLY A  787  5                                   6
HELIX   32  32 PHE A  801  SER A  805  1                                   5
HELIX   33  33 TYR A  819  LEU A  822  5                                   4
HELIX   34  34 SER A  836  SER A  849  1                                  14
HELIX   35  35 ASN A  871  LEU A  888  1                                  18
HELIX   36  36 SER A  896  VAL A  901  1                                   6
HELIX   37  37 LEU A  903  ARG A  919  1                                  17
HELIX   38  38 ASP A  924  LEU A  952  1                                  29
HELIX   39  39 ILE A  961  MET A  970  1                                  10
HELIX   40  40 ARG A  971  VAL A  986  1                                  16
HELIX   41  41 VAL A  986  ILE A  991  1                                   6
HELIX   42  42 GLY A  998  ILE A 1019  1                                  22
HELIX   43  43 PHE A 1025  PHE A 1033  1                                   9
SHEET    1   A 4 TYR A  77  SER A  79  0
SHEET    2   A 4 THR A  87  THR A  93 -1  O  THR A  91   N  SER A  79
SHEET    3   A 4 ALA A  42  SER A  48 -1  N  ILE A  45   O  ILE A  90
SHEET    4   A 4 SER A 128  LYS A 131 -1  O  GLU A 130   N  THR A  44
SHEET    1   B 2 ASN A  81  ASP A  83  0
SHEET    2   B 2 ARG A 815  GLU A 817 -1  O  LEU A 816   N  SER A  82
SHEET    1   C 4 VAL A 172  ASP A 174  0
SHEET    2   C 4 LEU A 289  LEU A 293 -1  O  LYS A 292   N  ASP A 174
SHEET    3   C 4 PHE A 136  ASN A 144 -1  N  VAL A 140   O  LEU A 289
SHEET    4   C 4 LEU A 321  VAL A 324 -1  O  VAL A 324   N  GLY A 141
SHEET    1   D 4 ALA A 266  GLY A 272  0
SHEET    2   D 4 TYR A 182  MET A 188 -1  N  TRP A 187   O  LYS A 267
SHEET    3   D 4 ARG A 767  VAL A 773  1  O  LYS A 770   N  MET A 184
SHEET    4   D 4 TYR A 758  ASP A 764 -1  N  PHE A 762   O  LYS A 769
SHEET    1   E 2 GLN A 218  LEU A 219  0
SHEET    2   E 2 ALA A 232  SER A 233 -1  O  ALA A 232   N  LEU A 219
SHEET    1   F 2 LEU A 250  ASN A 254  0
SHEET    2   F 2 SER A 258  LEU A 261 -1  O  VAL A 260   N  LYS A 252
SHEET    1   G 6 GLN A 284  ALA A 286  0
SHEET    2   G 6 ILE A 278  PHE A 281 -1  N  ALA A 279   O  ALA A 286
SHEET    3   G 6 ALA A 611  ASN A 613 -1  O  ASN A 613   N  ILE A 278
SHEET    4   G 6 THR A 624  PHE A 628 -1  O  ILE A 626   N  VAL A 612
SHEET    5   G 6 PHE A 572  GLN A 577 -1  N  VAL A 576   O  GLY A 625
SHEET    6   G 6 MET A 662  VAL A 663 -1  O  MET A 662   N  GLN A 577
SHEET    1   H 6 GLN A 284  ALA A 286  0
SHEET    2   H 6 ILE A 278  PHE A 281 -1  N  ALA A 279   O  ALA A 286
SHEET    3   H 6 ALA A 611  ASN A 613 -1  O  ASN A 613   N  ILE A 278
SHEET    4   H 6 THR A 624  PHE A 628 -1  O  ILE A 626   N  VAL A 612
SHEET    5   H 6 PHE A 572  GLN A 577 -1  N  VAL A 576   O  GLY A 625
SHEET    6   H 6 PHE A 666  ASN A 667 -1  O  PHE A 666   N  MET A 573
SHEET    1   I 2 VAL A 606  SER A 608  0
SHEET    2   I 2 SER A 630  LEU A 631 -1  O  SER A 630   N  SER A 608
SHEET    1   J 3 PHE A 682  ILE A 685  0
SHEET    2   J 3 SER A 824  GLN A 830 -1  O  ILE A 827   N  PHE A 682
SHEET    3   J 3 SER A 715  PRO A 718 -1  N  SER A 715   O  GLN A 830
SHEET    1   K 2 PRO A 725  ILE A 729  0
SHEET    2   K 2 SER A 807  TYR A 811 -1  O  ARG A 808   N  LYS A 728
SHEET    1   L 2 TYR A 790  ALA A 793  0
SHEET    2   L 2 GLN A 797  PRO A 800 -1  O  VAL A 799   N  VAL A 791
CRYST1  143.557  143.557  519.637  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      0.006966  0.004022  0.000000        0.00000
SCALE2      0.000000  0.008043  0.000000        0.00000
SCALE3      0.000000  0.000000  0.001924        0.00000
      
PROCHECK
Go to PROCHECK summary
 References