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PDBsum entry 1fiy

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Complex (lyase/inhibitor) PDB id
1fiy
Jmol
Contents
Protein chain
873 a.a.
Ligands
ASP
Waters ×39
HEADER    COMPLEX (LYASE/INHIBITOR)               02-MAY-98   1FIY
TITLE     THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE CARBOXYLASE FROM
TITLE    2 ESCHERICHIA COLI AT 2.8 A RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PEPC;
COMPND   5 EC: 4.1.1.31
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 83333;
SOURCE   4 STRAIN: K12
KEYWDS    PHOSPHOENOLPYRUVATE, CARBOXYLASE, COMPLEX (LYASE-INHIBITOR), COMPLEX
KEYWDS   2 (LYASE-INHIBITOR) COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.KAI,H.MATSUMURA,T.INOUE,K.TERADA,Y.NAGARA,T.YOSHINAGA,A.KIHARA,
AUTHOR   2 K.IZUI
REVDAT   4   13-JUL-11 1FIY    1       VERSN
REVDAT   3   24-FEB-09 1FIY    1       VERSN
REVDAT   2   23-MAR-99 1FIY    1       COMPND REMARK TITLE  SEQADV
REVDAT   2 2                   1       HEADER SOURCE JRNL   KEYWDS
REVDAT   1   09-FEB-99 1FIY    0
JRNL        AUTH   Y.KAI,H.MATSUMURA,T.INOUE,K.TERADA,Y.NAGARA,T.YOSHINAGA,
JRNL        AUTH 2 A.KIHARA,K.TSUMURA,K.IZUI
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE
JRNL        TITL 2 CARBOXYLASE: A PROPOSED MECHANISM FOR ALLOSTERIC INHIBITION.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  96   823 1999
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   9927652
JRNL        DOI    10.1073/PNAS.96.3.823
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.INOUE,M.HAYASHI,M.SUGIMOTO,S.HARADA,Y.KAI,N.KASAI,
REMARK   1  AUTH 2 K.TERADA,K.IZUI
REMARK   1  TITL   FIRST CRYSTALLIZATION OF A PHOSPHOENOLPYRUVATE CARBOXYLASE
REMARK   1  TITL 2 FROM ESCHERICHIA COLI
REMARK   1  REF    J.MOL.BIOL.                   V. 208   509 1989
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 26242
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : 0.259
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1409
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6888
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 9
REMARK   3   SOLVENT ATOMS            : 39
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 59.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.80
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  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.011 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.026 ; 0.030
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.035 ; 0.050
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.144 ; 0.140
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.194 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.273 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.177 ; 0.300
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : 6.200 ; 2.000
REMARK   3    STAGGERED                 (DEGREES) : 26.000; 15.000
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.303 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.290 ; 3.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.473 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.499 ; 3.000
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1FIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
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        : 15-DEC-96
REMARK 200  TEMPERATURE           (KELVIN) : 298
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 4
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : SYNCHROTRON RADIATION
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28509
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3
REMARK 200  DATA REDUNDANCY                : 3.600
REMARK 200  R MERGE                    (I) : 0.06900
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) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.25100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200  REPLACEMENT
REMARK 200 SOFTWARE USED: DM, MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       58.80000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      124.20000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       41.35000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       58.80000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      124.20000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       41.35000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       58.80000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      124.20000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       41.35000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       58.80000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      124.20000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       41.35000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 132010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 -1.000000  0.000000  0.000000      117.60000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      117.60000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 -1.000000  0.000000  0.000000      117.60000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     ASN A     2
REMARK 465     GLU A     3
REMARK 465     LYS A   702
REMARK 465     ARG A   703
REMARK 465     ARG A   704
REMARK 465     PRO A   705
REMARK 465     THR A   706
REMARK 465     GLY A   707
REMARK 465     GLY A   708
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    ARG A  46   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ARG A 320   CD  -  NE  -  CZ  ANGL. DEV. =  13.9 DEGREES
REMARK 500    ARG A 320   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A 382   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG A 382   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 392   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP A 394   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 394   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 438   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES
REMARK 500    ARG A 438   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG A 581   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES
REMARK 500    ARG A 618   CD  -  NE  -  CZ  ANGL. DEV. =  18.7 DEGREES
REMARK 500    ARG A 618   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG A 699   CD  -  NE  -  CZ  ANGL. DEV. =  15.4 DEGREES
REMARK 500    ARG A 713   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 725   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG A 863   CD  -  NE  -  CZ  ANGL. DEV. =  12.0 DEGREES
REMARK 500    ARG A 863   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 880   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 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    ALA A  26      -83.40    -25.41
REMARK 500    LEU A  27       -5.27   -142.07
REMARK 500    ALA A  47       24.55    -77.61
REMARK 500    ASN A  49       95.04    -56.90
REMARK 500    LYS A  94       64.10   -107.61
REMARK 500    PRO A 101       -7.19    -51.33
REMARK 500    ASN A 113       61.88   -106.39
REMARK 500    ARG A 195      131.71    -39.25
REMARK 500    SER A 212      -45.50   -151.34
REMARK 500    ASP A 254      107.11    -46.56
REMARK 500    ASN A 258      -11.78    -49.28
REMARK 500    GLU A 305      167.04     70.77
REMARK 500    GLU A 306      -65.53     73.21
REMARK 500    GLU A 310       60.32   -175.89
REMARK 500    PRO A 340      143.88    -37.81
REMARK 500    LEU A 390      -61.76     75.68
REMARK 500    GLU A 419       28.18    -78.80
REMARK 500    SER A 598       32.68    -91.60
REMARK 500    SER A 603      -27.30    -31.32
REMARK 500    ARG A 673      -63.22    -94.25
REMARK 500    PRO A 687       32.20    -91.07
REMARK 500    ARG A 725       -5.46     79.64
REMARK 500    TRP A 731      -35.10   -139.78
REMARK 500    LEU A 732      -85.59     -3.65
REMARK 500    GLU A 743        5.24    -66.30
REMARK 500    LEU A 818      116.97    121.33
REMARK 500    GLU A 856       27.48    -79.57
REMARK 500    ARG A 880     -140.07     43.99
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    LEU A 732        20.2      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 RESIDUE ASP 884 IS AN ALLOSTERIC INHIBITOR.
REMARK 600 THIS GROUP IS ASSIGNED AS A SEPARATE STANDARD-ALONE
REMARK 600 RESIDUE WITH THE CHAIN ID "L".
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASP A 884
DBREF  1FIY A    1   883  UNP    P00864   CAPP_ECOLI       1    883
SEQRES   1 A  883  MET ASN GLU GLN TYR SER ALA LEU ARG SER ASN VAL SER
SEQRES   2 A  883  MET LEU GLY LYS VAL LEU GLY GLU THR ILE LYS ASP ALA
SEQRES   3 A  883  LEU GLY GLU HIS ILE LEU GLU ARG VAL GLU THR ILE ARG
SEQRES   4 A  883  LYS LEU SER LYS SER SER ARG ALA GLY ASN ASP ALA ASN
SEQRES   5 A  883  ARG GLN GLU LEU LEU THR THR LEU GLN ASN LEU SER ASN
SEQRES   6 A  883  ASP GLU LEU LEU PRO VAL ALA ARG ALA PHE SER GLN PHE
SEQRES   7 A  883  LEU ASN LEU ALA ASN THR ALA GLU GLN TYR HIS SER ILE
SEQRES   8 A  883  SER PRO LYS GLY GLU ALA ALA SER ASN PRO GLU VAL ILE
SEQRES   9 A  883  ALA ARG THR LEU ARG LYS LEU LYS ASN GLN PRO GLU LEU
SEQRES  10 A  883  SER GLU ASP THR ILE LYS LYS ALA VAL GLU SER LEU SER
SEQRES  11 A  883  LEU GLU LEU VAL LEU THR ALA HIS PRO THR GLU ILE THR
SEQRES  12 A  883  ARG ARG THR LEU ILE HIS LYS MET VAL GLU VAL ASN ALA
SEQRES  13 A  883  CYS LEU LYS GLN LEU ASP ASN LYS ASP ILE ALA ASP TYR
SEQRES  14 A  883  GLU HIS ASN GLN LEU MET ARG ARG LEU ARG GLN LEU ILE
SEQRES  15 A  883  ALA GLN SER TRP HIS THR ASP GLU ILE ARG LYS LEU ARG
SEQRES  16 A  883  PRO SER PRO VAL ASP GLU ALA LYS TRP GLY PHE ALA VAL
SEQRES  17 A  883  VAL GLU ASN SER LEU TRP GLN GLY VAL PRO ASN TYR LEU
SEQRES  18 A  883  ARG GLU LEU ASN GLU GLN LEU GLU GLU ASN LEU GLY TYR
SEQRES  19 A  883  LYS LEU PRO VAL GLU PHE VAL PRO VAL ARG PHE THR SER
SEQRES  20 A  883  TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ASN VAL THR
SEQRES  21 A  883  ALA ASP ILE THR ARG HIS VAL LEU LEU LEU SER ARG TRP
SEQRES  22 A  883  LYS ALA THR ASP LEU PHE LEU LYS ASP ILE GLN VAL LEU
SEQRES  23 A  883  VAL SER GLU LEU SER MET VAL GLU ALA THR PRO GLU LEU
SEQRES  24 A  883  LEU ALA LEU VAL GLY GLU GLU GLY ALA ALA GLU PRO TYR
SEQRES  25 A  883  ARG TYR LEU MET LYS ASN LEU ARG SER ARG LEU MET ALA
SEQRES  26 A  883  THR GLN ALA TRP LEU GLU ALA ARG LEU LYS GLY GLU GLU
SEQRES  27 A  883  LEU PRO LYS PRO GLU GLY LEU LEU THR GLN ASN GLU GLU
SEQRES  28 A  883  LEU TRP GLU PRO LEU TYR ALA CYS TYR GLN SER LEU GLN
SEQRES  29 A  883  ALA CYS GLY MET GLY ILE ILE ALA ASN GLY ASP LEU LEU
SEQRES  30 A  883  ASP THR LEU ARG ARG VAL LYS CYS PHE GLY VAL PRO LEU
SEQRES  31 A  883  VAL ARG ILE ASP ILE ARG GLN GLU SER THR ARG HIS THR
SEQRES  32 A  883  GLU ALA LEU GLY GLU LEU THR ARG TYR LEU GLY ILE GLY
SEQRES  33 A  883  ASP TYR GLU SER TRP SER GLU ALA ASP LYS GLN ALA PHE
SEQRES  34 A  883  LEU ILE ARG GLU LEU ASN SER LYS ARG PRO LEU LEU PRO
SEQRES  35 A  883  ARG ASN TRP GLN PRO SER ALA GLU THR ARG GLU VAL LEU
SEQRES  36 A  883  ASP THR CYS GLN VAL ILE ALA GLU ALA PRO GLN GLY SER
SEQRES  37 A  883  ILE ALA ALA TYR VAL ILE SER MET ALA LYS THR PRO SER
SEQRES  38 A  883  ASP VAL LEU ALA VAL HIS LEU LEU LEU LYS GLU ALA GLY
SEQRES  39 A  883  ILE GLY PHE ALA MET PRO VAL ALA PRO LEU PHE GLU THR
SEQRES  40 A  883  LEU ASP ASP LEU ASN ASN ALA ASN ASP VAL MET THR GLN
SEQRES  41 A  883  LEU LEU ASN ILE ASP TRP TYR ARG GLY LEU ILE GLN GLY
SEQRES  42 A  883  LYS GLN MET VAL MET ILE GLY TYR SER ASP SER ALA LYS
SEQRES  43 A  883  ASP ALA GLY VAL MET ALA ALA SER TRP ALA GLN TYR GLN
SEQRES  44 A  883  ALA GLN ASP ALA LEU ILE LYS THR CYS GLU LYS ALA GLY
SEQRES  45 A  883  ILE GLU LEU THR LEU PHE HIS GLY ARG GLY GLY SER ILE
SEQRES  46 A  883  GLY ARG GLY GLY ALA PRO ALA HIS ALA ALA LEU LEU SER
SEQRES  47 A  883  GLN PRO PRO GLY SER LEU LYS GLY GLY LEU ARG VAL THR
SEQRES  48 A  883  GLU GLN GLY GLU MET ILE ARG PHE LYS TYR GLY LEU PRO
SEQRES  49 A  883  GLU ILE THR VAL SER SER LEU SER LEU TYR THR GLY ALA
SEQRES  50 A  883  ILE LEU GLU ALA ASN LEU LEU PRO PRO PRO GLU PRO LYS
SEQRES  51 A  883  GLU SER TRP ARG ARG ILE MET ASP GLU LEU SER VAL ILE
SEQRES  52 A  883  SER CYS ASP VAL TYR ARG GLY TYR VAL ARG GLU ASN LYS
SEQRES  53 A  883  ASP PHE VAL PRO TYR PHE ARG SER ALA THR PRO GLU GLN
SEQRES  54 A  883  GLU LEU GLY LYS LEU PRO LEU GLY SER ARG PRO ALA LYS
SEQRES  55 A  883  ARG ARG PRO THR GLY GLY VAL GLU SER LEU ARG ALA ILE
SEQRES  56 A  883  PRO TRP ILE PHE ALA TRP THR GLN ASN ARG LEU MET LEU
SEQRES  57 A  883  PRO ALA TRP LEU GLY ALA GLY THR ALA LEU GLN LYS VAL
SEQRES  58 A  883  VAL GLU ASP GLY LYS GLN SER GLU LEU GLU ALA MET CYS
SEQRES  59 A  883  ARG ASP TRP PRO PHE PHE SER THR ARG LEU GLY MET LEU
SEQRES  60 A  883  GLU MET VAL PHE ALA LYS ALA ASP LEU TRP LEU ALA GLU
SEQRES  61 A  883  TYR TYR ASP GLN ARG LEU VAL ASP LYS ALA LEU TRP PRO
SEQRES  62 A  883  LEU GLY LYS GLU LEU ARG ASN LEU GLN GLU GLU ASP ILE
SEQRES  63 A  883  LYS VAL VAL LEU ALA ILE ALA ASN ASP SER HIS LEU MET
SEQRES  64 A  883  ALA ASP LEU PRO TRP ILE ALA GLU SER ILE GLN LEU ARG
SEQRES  65 A  883  ASN ILE TYR THR ASP PRO LEU ASN VAL LEU GLN ALA GLU
SEQRES  66 A  883  LEU LEU HIS ARG SER ARG GLN ALA GLU LYS GLU GLY GLN
SEQRES  67 A  883  GLU PRO ASP PRO ARG VAL GLU GLN ALA LEU MET VAL THR
SEQRES  68 A  883  ILE ALA GLY ILE ALA ALA GLY MET ARG ASN THR GLY
HET    ASP  A 884       9
HETNAM     ASP ASPARTIC ACID
FORMUL   2  ASP    C4 H7 N O4
FORMUL   3  HOH   *39(H2 O)
HELIX    1   1 SER A    6  ALA A   26  1                                  21
HELIX    2   2 HIS A   30  ALA A   47  1                                  18
HELIX    3   3 ASN A   52  GLN A   61  1                                  10
HELIX    4   4 ASN A   65  ILE A   91  1                                  27
HELIX    5   5 GLU A  102  LYS A  112  1                                  11
HELIX    6   6 GLU A  119  GLU A  127  1                                   9
HELIX    7   7 ILE A  148  ASP A  162  1                                  15
HELIX    8   8 ASP A  168  HIS A  187  1                                  20
HELIX    9   9 PRO A  198  ASN A  211  1                                  14
HELIX   10  10 LEU A  213  LEU A  232  1                                  20
HELIX   11  11 ALA A  261  GLU A  289  1                                  29
HELIX   12  12 PRO A  297  ALA A  301  1                                   5
HELIX   13  13 PRO A  311  LYS A  335  1                                  25
HELIX   14  14 ASN A  349  ALA A  365  1                                  17
HELIX   15  15 GLY A  369  ALA A  372  1                                   4
HELIX   16  16 ASP A  375  CYS A  385  1                                  11
HELIX   17  17 SER A  399  LEU A  413  1                                  15
HELIX   18  18 TYR A  418  SER A  420  5                                   3
HELIX   19  19 GLU A  423  ASN A  435  1                                  13
HELIX   20  20 ALA A  449  GLU A  463  1                                  15
HELIX   21  21 PRO A  480  GLU A  492  1                                  13
HELIX   22  22 LEU A  508  ASN A  523  1                                  16
HELIX   23  23 ASP A  525  ILE A  531  1                                   7
HELIX   24  24 TYR A  541  ALA A  548  1                                   8
HELIX   25  25 VAL A  550  ALA A  571  1                                  22
HELIX   26  26 GLY A  589  LEU A  597  1                                   9
HELIX   27  27 GLY A  614  TYR A  621  5                                   8
HELIX   28  28 PRO A  624  LEU A  643  1                                  20
HELIX   29  29 GLU A  651  VAL A  672  1                                  22
HELIX   30  30 PHE A  678  ALA A  685  1                                   8
HELIX   31  31 GLU A  688  LYS A  693  1                                   6
HELIX   32  32 ALA A  714  ASN A  724  1                                  11
HELIX   33  33 LEU A  728  ALA A  730  5                                   3
HELIX   34  34 LEU A  732  ASP A  744  1                                  13
HELIX   35  35 LYS A  746  ASP A  756  5                                  11
HELIX   36  36 PRO A  758  LYS A  773  1                                  16
HELIX   37  37 LEU A  776  LEU A  786  1                                  11
HELIX   38  38 LYS A  789  ALA A  813  5                                  25
HELIX   39  39 PRO A  823  LYS A  855  1                                  33
HELIX   40  40 PRO A  862  MET A  879  1                                  18
SHEET    1   A 3 VAL A 243  SER A 247  0
SHEET    2   A 3 LEU A 131  LEU A 135  1  N  LEU A 131   O  ARG A 244
SHEET    3   A 3 LEU A 608  GLU A 612  1  N  LEU A 608   O  GLU A 132
SHEET    1   B 3 VAL A 501  LEU A 504  0
SHEET    2   B 3 ILE A 469  SER A 475  1  N  TYR A 472   O  ALA A 502
SHEET    3   B 3 ILE A 393  GLU A 398  1  N  ILE A 393   O  ALA A 470
SHEET    1   C 2 LYS A 534  ILE A 539  0
SHEET    2   C 2 GLU A 574  HIS A 579  1  N  GLU A 574   O  GLN A 535
SITE     1 AC1 10 ARG A 587  MET A 769  LYS A 773  MET A 819
SITE     2 AC1 10 ILE A 825  ARG A 832  ARG A 880  ASN A 881
SITE     3 AC1 10 HOH A 893  HOH A 905
CRYST1  117.600  248.400   82.700  90.00  90.00  90.00 I 2 2 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      0.008503  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004026  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012092        0.00000
      
PROCHECK
Go to PROCHECK summary
 References