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PDBsum entry 1jqo

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Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
1jqo
Jmol
Contents
Protein chains
904 a.a. *
Ligands
SO4 ×2
* Residue conservation analysis
HEADER    LYASE                                   07-AUG-01   1JQO
TITLE     CRYSTAL STRUCTURE OF C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE FROM
TITLE    2 MAIZE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYLASE;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PHOSPHOENOLPYRUVATE CARBOXYLASE 1, PEPCASE;
COMPND   5 EC: 4.1.1.31
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE   3 ORGANISM_TAXID: 4577;
SOURCE   4 STRAIN: B37;
SOURCE   5 TISSUE: LEAVES
KEYWDS    BETA BARREL, CARBON DIOXIDE FIXATION, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.MATSUMURA,Y.KAI
REVDAT   3   13-JUL-11 1JQO    1       VERSN
REVDAT   2   24-FEB-09 1JQO    1       VERSN
REVDAT   1   14-JAN-03 1JQO    0
JRNL        AUTH   H.MATSUMURA,Y.XIE,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,Y.UENO,
JRNL        AUTH 2 K.IZUI,Y.KAI
JRNL        TITL   CRYSTAL STRUCTURES OF C4 FORM MAIZE AND QUATERNARY COMPLEX
JRNL        TITL 2 OF E. COLI PHOSPHOENOLPYRUVATE CARBOXYLASES.
JRNL        REF    STRUCTURE                     V.  10  1721 2002
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   12467579
JRNL        DOI    10.1016/S0969-2126(02)00913-9
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   H.MATSUMURA,M.TERADA,S.SHIRAKATA,T.INOUE,T.YOSHINAGA,K.IZUI,
REMARK   1  AUTH 2 Y.KAI
REMARK   1  TITL   PLAUSIBLE PHOSPHOENOLPYRUVATE BINDING SITE REVEALED BY 2.6 A
REMARK   1  TITL 2 STRUCTURE OF MN2+-BOUND PHOSPHOENOLPYRUVATE CARBOXYLASE FROM
REMARK   1  TITL 3 ESCHERICHIA COLI.
REMARK   1  REF    FEBS LETT.                    V. 458    93 1999
REMARK   1  REFN                   ISSN 0014-5793
REMARK   1 REFERENCE 2
REMARK   1  AUTH   Y.KAI,H.MATSUMURA,T.INOUE,K.TERADA,Y.NAGARA,T.YOSHINAGA,
REMARK   1  AUTH 2 A.KIHARA,K.TSUMURA,K.IZUI
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF PHOSPHOENOLPYRUVATE
REMARK   1  TITL 2 CARBOXYLASE: A PROPOSED MECHANISM FOR ALLOSTERIC INHIBITION
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  96   823 1999
REMARK   1  REFN                   ISSN 0027-8424
REMARK   1 REFERENCE 3
REMARK   1  AUTH   H.MATSUMURA,T.NAGATA,M.TERADA,S.SHIRAKATA,T.INOUE,
REMARK   1  AUTH 2 T.YOSHINAGA,Y.UENO,H.SAZE,K.IZUI,Y.KAI
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES OF
REMARK   1  TITL 2 C4-FORM PHOSPHOENOLPYRUVATE CARBOXYLASE FROM MAIZE
REMARK   1  TITL 3 DIFFRACTION STUDIES OF C4-FORM PHOSPHOENOLPYRUVATE
REMARK   1  TITL 4 CARBOXYLASE FROM MAIZE.
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55  1937 1999
REMARK   1  REFN                   ISSN 0907-4449
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 86.20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 57271
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 SET) : 0.236
REMARK   3   FREE R VALUE                     : 0.272
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2893
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.14
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4130
REMARK   3   BIN FREE R VALUE                    : 0.4150
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 14424
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
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 COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.43
REMARK   3   ESD FROM SIGMAA              (A) : 1.06
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1JQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-AUG-01.
REMARK 100 THE RCSB ID CODE IS RCSB014076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 25-MAR-99
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL41XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.708
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58078
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 7.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.09100
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) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 57.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 69.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, TRIS-HCL, LISO4, PH 7.5,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
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
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      127.14000
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      127.14000
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       79.22000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       87.30500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       79.22000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       87.30500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      127.14000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       79.22000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       87.30500
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      127.14000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       79.22000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       87.30500
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER GENERATED FROM DIMER
REMARK 300 IN THE ASSYMMETRIC UNIT BY TWO FOLE AXIS.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      174.61000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      254.28000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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     SER A     3
REMARK 465     THR A     4
REMARK 465     LYS A     5
REMARK 465     ALA A     6
REMARK 465     PRO A     7
REMARK 465     GLY A     8
REMARK 465     PRO A     9
REMARK 465     GLY A    10
REMARK 465     GLU A    11
REMARK 465     LYS A    12
REMARK 465     HIS A    13
REMARK 465     HIS A    14
REMARK 465     SER A    15
REMARK 465     ILE A    16
REMARK 465     ASP A    17
REMARK 465     ALA A    18
REMARK 465     GLN A    19
REMARK 465     LEU A    20
REMARK 465     ARG A    21
REMARK 465     GLN A    22
REMARK 465     LEU A    23
REMARK 465     VAL A    24
REMARK 465     PRO A    25
REMARK 465     GLY A    26
REMARK 465     LYS A    27
REMARK 465     VAL A    28
REMARK 465     SER A    29
REMARK 465     GLU A    30
REMARK 465     ASP A    31
REMARK 465     ASP A    32
REMARK 465     LYS A    33
REMARK 465     LEU A    34
REMARK 465     SER A   124
REMARK 465     LYS A   125
REMARK 465     LEU A   126
REMARK 465     LYS A   127
REMARK 465     LYS A   128
REMARK 465     GLY A   129
REMARK 465     GLY A   130
REMARK 465     PHE A   131
REMARK 465     ALA A   132
REMARK 465     ASP A   133
REMARK 465     GLU A   134
REMARK 465     GLY A   135
REMARK 465     SER A   136
REMARK 465     ALA A   137
REMARK 465     THR A   138
REMARK 465     THR A   139
REMARK 465     GLU A   140
REMARK 465     ALA A   761
REMARK 465     LYS A   762
REMARK 465     ARG A   763
REMARK 465     ARG A   764
REMARK 465     PRO A   765
REMARK 465     GLY A   766
REMARK 465     GLY A   767
REMARK 465     GLY A   768
REMARK 465     PHE A   929
REMARK 465     ALA A   930
REMARK 465     ASP A   931
REMARK 465     GLU A   932
REMARK 465     ASN A   933
REMARK 465     LYS A   934
REMARK 465     PRO A   935
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     SER B     3
REMARK 465     THR B     4
REMARK 465     LYS B     5
REMARK 465     ALA B     6
REMARK 465     PRO B     7
REMARK 465     GLY B     8
REMARK 465     PRO B     9
REMARK 465     GLY B    10
REMARK 465     GLU B    11
REMARK 465     LYS B    12
REMARK 465     HIS B    13
REMARK 465     HIS B    14
REMARK 465     SER B    15
REMARK 465     ILE B    16
REMARK 465     ASP B    17
REMARK 465     ALA B    18
REMARK 465     GLN B    19
REMARK 465     LEU B    20
REMARK 465     ARG B    21
REMARK 465     GLN B    22
REMARK 465     LEU B    23
REMARK 465     VAL B    24
REMARK 465     PRO B    25
REMARK 465     GLY B    26
REMARK 465     LYS B    27
REMARK 465     VAL B    28
REMARK 465     SER B    29
REMARK 465     GLU B    30
REMARK 465     ASP B    31
REMARK 465     ASP B    32
REMARK 465     LYS B    33
REMARK 465     LEU B    34
REMARK 465     SER B   124
REMARK 465     LYS B   125
REMARK 465     LEU B   126
REMARK 465     LYS B   127
REMARK 465     LYS B   128
REMARK 465     GLY B   129
REMARK 465     GLY B   130
REMARK 465     PHE B   131
REMARK 465     ALA B   132
REMARK 465     ASP B   133
REMARK 465     GLU B   134
REMARK 465     GLY B   135
REMARK 465     SER B   136
REMARK 465     ALA B   137
REMARK 465     THR B   138
REMARK 465     THR B   139
REMARK 465     GLU B   140
REMARK 465     ALA B   761
REMARK 465     LYS B   762
REMARK 465     ARG B   763
REMARK 465     ARG B   764
REMARK 465     PRO B   765
REMARK 465     GLY B   766
REMARK 465     GLY B   767
REMARK 465     GLY B   768
REMARK 465     PHE B   929
REMARK 465     ALA B   930
REMARK 465     ASP B   931
REMARK 465     GLU B   932
REMARK 465     ASN B   933
REMARK 465     LYS B   934
REMARK 465     PRO B   935
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    PRO A  55   C   -  N   -  CA  ANGL. DEV. =   9.5 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    ARG A 120      -76.09    -45.16
REMARK 500    SER A 152      -82.40    -77.64
REMARK 500    GLU A 153      -71.71    -50.55
REMARK 500    ALA A 176       52.81    -97.74
REMARK 500    PRO A 178       62.13    -59.28
REMARK 500    THR A 206     -172.01    -61.82
REMARK 500    HIS A 249       35.38    -91.14
REMARK 500    GLU A 250      -24.05   -146.99
REMARK 500    THR A 251      -37.90   -143.50
REMARK 500    ILE A 272       96.05    -50.85
REMARK 500    ASN A 273       47.28    -84.41
REMARK 500    MET A 289       95.04    -67.17
REMARK 500    SER A 331       32.31    -87.72
REMARK 500    ARG A 334       98.49    -68.54
REMARK 500    SER A 350      -70.56    -68.51
REMARK 500    LYS A 353       -3.99   -144.77
REMARK 500    VAL A 354       10.50    -64.33
REMARK 500    PRO A 367        4.00    -69.37
REMARK 500    GLU A 369       74.56   -119.24
REMARK 500    ALA A 394      -72.72    -59.48
REMARK 500    SER A 395     -149.53    -92.58
REMARK 500    CYS A 426       24.52    -75.06
REMARK 500    ASP A 428       69.43    -45.47
REMARK 500    ASP A 433        9.76    -68.53
REMARK 500    LEU A 450      -50.21    -21.92
REMARK 500    GLN A 457      126.26   -173.41
REMARK 500    ILE A 475       43.36   -150.60
REMARK 500    GLU A 480       10.66    -65.68
REMARK 500    LYS A 497      -16.81   -149.28
REMARK 500    SER A 528        9.04    -64.15
REMARK 500    MET A 536       42.61     35.38
REMARK 500    THR A 538      -90.46   -102.66
REMARK 500    LEU A 548      -71.15    -72.19
REMARK 500    ARG A 556      -81.24    -43.00
REMARK 500    GLU A 566      -53.93   -132.65
REMARK 500    SER A 573       31.31    -73.89
REMARK 500    ALA A 576      -71.46    -67.69
REMARK 500    PRO A 660      139.33    -39.68
REMARK 500    ILE A 664      -61.07   -122.90
REMARK 500    GLU A 684      -79.89    -65.24
REMARK 500    HIS A 704       65.04   -154.14
REMARK 500    PRO A 705      159.76    -49.91
REMARK 500    TYR A 728      -74.83    -62.48
REMARK 500    VAL A 733      -64.38   -107.95
REMARK 500    ARG A 737        8.64    -65.11
REMARK 500    PRO A 747       36.47    -90.53
REMARK 500    ARG A 773      144.68      1.24
REMARK 500    VAL A 794      -36.65    -25.21
REMARK 500    ASP A 837      100.11   -166.33
REMARK 500    ASN A 895      -53.92    -27.55
REMARK 500
REMARK 500 THIS ENTRY HAS     118 RAMACHANDRAN OUTLIERS.
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 971
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1071
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FIY   RELATED DB: PDB
REMARK 900 1FIY CONTAINS THE NATIVE STRUCTURE OF E.COLI PEPC.
REMARK 900 RELATED ID: 1JQN   RELATED DB: PDB
REMARK 900 1JQN CONTAINS STRUCTURE OF E.COLI PHOSPHOENOLPYRUVATE
REMARK 900 CARBOXYLASE IN COMPLEX WITH MN2+ AND DCDP
DBREF  1JQO A    1   970  UNP    P04711   CAPP1_MAIZE      1    970
DBREF  1JQO B    1   970  UNP    P04711   CAPP1_MAIZE      1    970
SEQRES   1 A  970  MET ALA SER THR LYS ALA PRO GLY PRO GLY GLU LYS HIS
SEQRES   2 A  970  HIS SER ILE ASP ALA GLN LEU ARG GLN LEU VAL PRO GLY
SEQRES   3 A  970  LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR ASP ALA
SEQRES   4 A  970  LEU LEU VAL ASP ARG PHE LEU ASN ILE LEU GLN ASP LEU
SEQRES   5 A  970  HIS GLY PRO SER LEU ARG GLU PHE VAL GLN GLU CYS TYR
SEQRES   6 A  970  GLU VAL SER ALA ASP TYR GLU GLY LYS GLY ASP THR THR
SEQRES   7 A  970  LYS LEU GLY GLU LEU GLY ALA LYS LEU THR GLY LEU ALA
SEQRES   8 A  970  PRO ALA ASP ALA ILE LEU VAL ALA SER SER ILE LEU HIS
SEQRES   9 A  970  MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL GLN ILE
SEQRES  10 A  970  ALA HIS ARG ARG ARG ASN SER LYS LEU LYS LYS GLY GLY
SEQRES  11 A  970  PHE ALA ASP GLU GLY SER ALA THR THR GLU SER ASP ILE
SEQRES  12 A  970  GLU GLU THR LEU LYS ARG LEU VAL SER GLU VAL GLY LYS
SEQRES  13 A  970  SER PRO GLU GLU VAL PHE GLU ALA LEU LYS ASN GLN THR
SEQRES  14 A  970  VAL ASP LEU VAL PHE THR ALA HIS PRO THR GLN SER ALA
SEQRES  15 A  970  ARG ARG SER LEU LEU GLN LYS ASN ALA ARG ILE ARG ASN
SEQRES  16 A  970  CYS LEU THR GLN LEU ASN ALA LYS ASP ILE THR ASP ASP
SEQRES  17 A  970  ASP LYS GLN GLU LEU ASP GLU ALA LEU GLN ARG GLU ILE
SEQRES  18 A  970  GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG ALA GLN
SEQRES  19 A  970  PRO THR PRO GLN ALA GLU MET ARG TYR GLY MET SER TYR
SEQRES  20 A  970  ILE HIS GLU THR VAL TRP LYS GLY VAL PRO LYS PHE LEU
SEQRES  21 A  970  ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE ASN
SEQRES  22 A  970  GLU ARG LEU PRO TYR ASN VAL SER LEU ILE ARG PHE SER
SEQRES  23 A  970  SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG VAL
SEQRES  24 A  970  THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA ARG
SEQRES  25 A  970  MET MET ALA ALA ASN LEU TYR ILE ASP GLN ILE GLU GLU
SEQRES  26 A  970  LEU MET PHE GLU LEU SER MET TRP ARG CYS ASN ASP GLU
SEQRES  27 A  970  LEU ARG VAL ARG ALA GLU GLU LEU HIS SER SER SER GLY
SEQRES  28 A  970  SER LYS VAL THR LYS TYR TYR ILE GLU PHE TRP LYS GLN
SEQRES  29 A  970  ILE PRO PRO ASN GLU PRO TYR ARG VAL ILE LEU GLY HIS
SEQRES  30 A  970  VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG ALA ARG
SEQRES  31 A  970  HIS LEU LEU ALA SER GLY VAL SER GLU ILE SER ALA GLU
SEQRES  32 A  970  SER SER PHE THR SER ILE GLU GLU PHE LEU GLU PRO LEU
SEQRES  33 A  970  GLU LEU CYS TYR LYS SER LEU CYS ASP CYS GLY ASP LYS
SEQRES  34 A  970  ALA ILE ALA ASP GLY SER LEU LEU ASP LEU LEU ARG GLN
SEQRES  35 A  970  VAL PHE THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE
SEQRES  36 A  970  ARG GLN GLU SER GLU ARG HIS THR ASP VAL ILE ASP ALA
SEQRES  37 A  970  ILE THR THR HIS LEU GLY ILE GLY SER TYR ARG GLU TRP
SEQRES  38 A  970  PRO GLU ASP LYS ARG GLN GLU TRP LEU LEU SER GLU LEU
SEQRES  39 A  970  ARG GLY LYS ARG PRO LEU LEU PRO PRO ASP LEU PRO GLN
SEQRES  40 A  970  THR ASP GLU ILE ALA ASP VAL ILE GLY ALA PHE HIS VAL
SEQRES  41 A  970  LEU ALA GLU LEU PRO PRO ASP SER PHE GLY PRO TYR ILE
SEQRES  42 A  970  ILE SER MET ALA THR ALA PRO SER ASP VAL LEU ALA VAL
SEQRES  43 A  970  GLU LEU LEU GLN ARG GLU CYS GLY VAL ARG GLN PRO LEU
SEQRES  44 A  970  PRO VAL VAL PRO LEU PHE GLU ARG LEU ALA ASP LEU GLN
SEQRES  45 A  970  SER ALA PRO ALA SER VAL GLU ARG LEU PHE SER VAL ASP
SEQRES  46 A  970  TRP TYR MET ASP ARG ILE LYS GLY LYS GLN GLN VAL MET
SEQRES  47 A  970  VAL GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG LEU
SEQRES  48 A  970  SER ALA ALA TRP GLN LEU TYR ARG ALA GLN GLU GLU MET
SEQRES  49 A  970  ALA GLN VAL ALA LYS ARG TYR GLY VAL LYS LEU THR LEU
SEQRES  50 A  970  PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY
SEQRES  51 A  970  PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR
SEQRES  52 A  970  ILE ASN GLY SER ILE ARG VAL THR VAL GLN GLY GLU VAL
SEQRES  53 A  970  ILE GLU PHE CYS PHE GLY GLU GLU HIS LEU CYS PHE GLN
SEQRES  54 A  970  THR LEU GLN ARG PHE THR ALA ALA THR LEU GLU HIS GLY
SEQRES  55 A  970  MET HIS PRO PRO VAL SER PRO LYS PRO GLU TRP ARG LYS
SEQRES  56 A  970  LEU MET ASP GLU MET ALA VAL VAL ALA THR GLU GLU TYR
SEQRES  57 A  970  ARG SER VAL VAL VAL LYS GLU ALA ARG PHE VAL GLU TYR
SEQRES  58 A  970  PHE ARG SER ALA THR PRO GLU THR GLU TYR GLY ARG MET
SEQRES  59 A  970  ASN ILE GLY SER ARG PRO ALA LYS ARG ARG PRO GLY GLY
SEQRES  60 A  970  GLY ILE THR THR LEU ARG ALA ILE PRO TRP ILE PHE SER
SEQRES  61 A  970  TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY
SEQRES  62 A  970  VAL GLY ALA ALA PHE LYS PHE ALA ILE ASP LYS ASP VAL
SEQRES  63 A  970  ARG ASN PHE GLN VAL LEU LYS GLU MET TYR ASN GLU TRP
SEQRES  64 A  970  PRO PHE PHE ARG VAL THR LEU ASP LEU LEU GLU MET VAL
SEQRES  65 A  970  PHE ALA LYS GLY ASP PRO GLY ILE ALA GLY LEU TYR ASP
SEQRES  66 A  970  GLU LEU LEU VAL ALA GLU GLU LEU LYS PRO PHE GLY LYS
SEQRES  67 A  970  GLN LEU ARG ASP LYS TYR VAL GLU THR GLN GLN LEU LEU
SEQRES  68 A  970  LEU GLN ILE ALA GLY HIS LYS ASP ILE LEU GLU GLY ASP
SEQRES  69 A  970  PRO PHE LEU LYS GLN GLY LEU VAL LEU ARG ASN PRO TYR
SEQRES  70 A  970  ILE THR THR LEU ASN VAL PHE GLN ALA TYR THR LEU LYS
SEQRES  71 A  970  ARG ILE ARG ASP PRO ASN PHE LYS VAL THR PRO GLN PRO
SEQRES  72 A  970  PRO LEU SER LYS GLU PHE ALA ASP GLU ASN LYS PRO ALA
SEQRES  73 A  970  GLY LEU VAL LYS LEU ASN PRO ALA SER GLU TYR PRO PRO
SEQRES  74 A  970  GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS GLY ILE
SEQRES  75 A  970  ALA ALA GLY MET GLN ASN THR GLY
SEQRES   1 B  970  MET ALA SER THR LYS ALA PRO GLY PRO GLY GLU LYS HIS
SEQRES   2 B  970  HIS SER ILE ASP ALA GLN LEU ARG GLN LEU VAL PRO GLY
SEQRES   3 B  970  LYS VAL SER GLU ASP ASP LYS LEU ILE GLU TYR ASP ALA
SEQRES   4 B  970  LEU LEU VAL ASP ARG PHE LEU ASN ILE LEU GLN ASP LEU
SEQRES   5 B  970  HIS GLY PRO SER LEU ARG GLU PHE VAL GLN GLU CYS TYR
SEQRES   6 B  970  GLU VAL SER ALA ASP TYR GLU GLY LYS GLY ASP THR THR
SEQRES   7 B  970  LYS LEU GLY GLU LEU GLY ALA LYS LEU THR GLY LEU ALA
SEQRES   8 B  970  PRO ALA ASP ALA ILE LEU VAL ALA SER SER ILE LEU HIS
SEQRES   9 B  970  MET LEU ASN LEU ALA ASN LEU ALA GLU GLU VAL GLN ILE
SEQRES  10 B  970  ALA HIS ARG ARG ARG ASN SER LYS LEU LYS LYS GLY GLY
SEQRES  11 B  970  PHE ALA ASP GLU GLY SER ALA THR THR GLU SER ASP ILE
SEQRES  12 B  970  GLU GLU THR LEU LYS ARG LEU VAL SER GLU VAL GLY LYS
SEQRES  13 B  970  SER PRO GLU GLU VAL PHE GLU ALA LEU LYS ASN GLN THR
SEQRES  14 B  970  VAL ASP LEU VAL PHE THR ALA HIS PRO THR GLN SER ALA
SEQRES  15 B  970  ARG ARG SER LEU LEU GLN LYS ASN ALA ARG ILE ARG ASN
SEQRES  16 B  970  CYS LEU THR GLN LEU ASN ALA LYS ASP ILE THR ASP ASP
SEQRES  17 B  970  ASP LYS GLN GLU LEU ASP GLU ALA LEU GLN ARG GLU ILE
SEQRES  18 B  970  GLN ALA ALA PHE ARG THR ASP GLU ILE ARG ARG ALA GLN
SEQRES  19 B  970  PRO THR PRO GLN ALA GLU MET ARG TYR GLY MET SER TYR
SEQRES  20 B  970  ILE HIS GLU THR VAL TRP LYS GLY VAL PRO LYS PHE LEU
SEQRES  21 B  970  ARG ARG VAL ASP THR ALA LEU LYS ASN ILE GLY ILE ASN
SEQRES  22 B  970  GLU ARG LEU PRO TYR ASN VAL SER LEU ILE ARG PHE SER
SEQRES  23 B  970  SER TRP MET GLY GLY ASP ARG ASP GLY ASN PRO ARG VAL
SEQRES  24 B  970  THR PRO GLU VAL THR ARG ASP VAL CYS LEU LEU ALA ARG
SEQRES  25 B  970  MET MET ALA ALA ASN LEU TYR ILE ASP GLN ILE GLU GLU
SEQRES  26 B  970  LEU MET PHE GLU LEU SER MET TRP ARG CYS ASN ASP GLU
SEQRES  27 B  970  LEU ARG VAL ARG ALA GLU GLU LEU HIS SER SER SER GLY
SEQRES  28 B  970  SER LYS VAL THR LYS TYR TYR ILE GLU PHE TRP LYS GLN
SEQRES  29 B  970  ILE PRO PRO ASN GLU PRO TYR ARG VAL ILE LEU GLY HIS
SEQRES  30 B  970  VAL ARG ASP LYS LEU TYR ASN THR ARG GLU ARG ALA ARG
SEQRES  31 B  970  HIS LEU LEU ALA SER GLY VAL SER GLU ILE SER ALA GLU
SEQRES  32 B  970  SER SER PHE THR SER ILE GLU GLU PHE LEU GLU PRO LEU
SEQRES  33 B  970  GLU LEU CYS TYR LYS SER LEU CYS ASP CYS GLY ASP LYS
SEQRES  34 B  970  ALA ILE ALA ASP GLY SER LEU LEU ASP LEU LEU ARG GLN
SEQRES  35 B  970  VAL PHE THR PHE GLY LEU SER LEU VAL LYS LEU ASP ILE
SEQRES  36 B  970  ARG GLN GLU SER GLU ARG HIS THR ASP VAL ILE ASP ALA
SEQRES  37 B  970  ILE THR THR HIS LEU GLY ILE GLY SER TYR ARG GLU TRP
SEQRES  38 B  970  PRO GLU ASP LYS ARG GLN GLU TRP LEU LEU SER GLU LEU
SEQRES  39 B  970  ARG GLY LYS ARG PRO LEU LEU PRO PRO ASP LEU PRO GLN
SEQRES  40 B  970  THR ASP GLU ILE ALA ASP VAL ILE GLY ALA PHE HIS VAL
SEQRES  41 B  970  LEU ALA GLU LEU PRO PRO ASP SER PHE GLY PRO TYR ILE
SEQRES  42 B  970  ILE SER MET ALA THR ALA PRO SER ASP VAL LEU ALA VAL
SEQRES  43 B  970  GLU LEU LEU GLN ARG GLU CYS GLY VAL ARG GLN PRO LEU
SEQRES  44 B  970  PRO VAL VAL PRO LEU PHE GLU ARG LEU ALA ASP LEU GLN
SEQRES  45 B  970  SER ALA PRO ALA SER VAL GLU ARG LEU PHE SER VAL ASP
SEQRES  46 B  970  TRP TYR MET ASP ARG ILE LYS GLY LYS GLN GLN VAL MET
SEQRES  47 B  970  VAL GLY TYR SER ASP SER GLY LYS ASP ALA GLY ARG LEU
SEQRES  48 B  970  SER ALA ALA TRP GLN LEU TYR ARG ALA GLN GLU GLU MET
SEQRES  49 B  970  ALA GLN VAL ALA LYS ARG TYR GLY VAL LYS LEU THR LEU
SEQRES  50 B  970  PHE HIS GLY ARG GLY GLY THR VAL GLY ARG GLY GLY GLY
SEQRES  51 B  970  PRO THR HIS LEU ALA ILE LEU SER GLN PRO PRO ASP THR
SEQRES  52 B  970  ILE ASN GLY SER ILE ARG VAL THR VAL GLN GLY GLU VAL
SEQRES  53 B  970  ILE GLU PHE CYS PHE GLY GLU GLU HIS LEU CYS PHE GLN
SEQRES  54 B  970  THR LEU GLN ARG PHE THR ALA ALA THR LEU GLU HIS GLY
SEQRES  55 B  970  MET HIS PRO PRO VAL SER PRO LYS PRO GLU TRP ARG LYS
SEQRES  56 B  970  LEU MET ASP GLU MET ALA VAL VAL ALA THR GLU GLU TYR
SEQRES  57 B  970  ARG SER VAL VAL VAL LYS GLU ALA ARG PHE VAL GLU TYR
SEQRES  58 B  970  PHE ARG SER ALA THR PRO GLU THR GLU TYR GLY ARG MET
SEQRES  59 B  970  ASN ILE GLY SER ARG PRO ALA LYS ARG ARG PRO GLY GLY
SEQRES  60 B  970  GLY ILE THR THR LEU ARG ALA ILE PRO TRP ILE PHE SER
SEQRES  61 B  970  TRP THR GLN THR ARG PHE HIS LEU PRO VAL TRP LEU GLY
SEQRES  62 B  970  VAL GLY ALA ALA PHE LYS PHE ALA ILE ASP LYS ASP VAL
SEQRES  63 B  970  ARG ASN PHE GLN VAL LEU LYS GLU MET TYR ASN GLU TRP
SEQRES  64 B  970  PRO PHE PHE ARG VAL THR LEU ASP LEU LEU GLU MET VAL
SEQRES  65 B  970  PHE ALA LYS GLY ASP PRO GLY ILE ALA GLY LEU TYR ASP
SEQRES  66 B  970  GLU LEU LEU VAL ALA GLU GLU LEU LYS PRO PHE GLY LYS
SEQRES  67 B  970  GLN LEU ARG ASP LYS TYR VAL GLU THR GLN GLN LEU LEU
SEQRES  68 B  970  LEU GLN ILE ALA GLY HIS LYS ASP ILE LEU GLU GLY ASP
SEQRES  69 B  970  PRO PHE LEU LYS GLN GLY LEU VAL LEU ARG ASN PRO TYR
SEQRES  70 B  970  ILE THR THR LEU ASN VAL PHE GLN ALA TYR THR LEU LYS
SEQRES  71 B  970  ARG ILE ARG ASP PRO ASN PHE LYS VAL THR PRO GLN PRO
SEQRES  72 B  970  PRO LEU SER LYS GLU PHE ALA ASP GLU ASN LYS PRO ALA
SEQRES  73 B  970  GLY LEU VAL LYS LEU ASN PRO ALA SER GLU TYR PRO PRO
SEQRES  74 B  970  GLY LEU GLU ASP THR LEU ILE LEU THR MET LYS GLY ILE
SEQRES  75 B  970  ALA ALA GLY MET GLN ASN THR GLY
HET    SO4  A 971       5
HET    SO4  B1071       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    2(O4 S 2-)
HELIX    1   1 ILE A   35  GLY A   54  1                                  20
HELIX    2   2 GLY A   54  GLY A   73  1                                  20
HELIX    3   3 THR A   77  LEU A   90  1                                  14
HELIX    4   4 ALA A   91  ASN A  123  1                                  33
HELIX    5   5 ASP A  142  SER A  152  1                                  11
HELIX    6   6 SER A  157  ASN A  167  1                                  11
HELIX    7   7 ARG A  183  LEU A  200  1                                  18
HELIX    8   8 THR A  206  THR A  227  1                                  22
HELIX    9   9 THR A  236  HIS A  249  1                                  14
HELIX   10  10 GLY A  255  ASN A  269  1                                  15
HELIX   11  11 THR A  300  LEU A  330  1                                  31
HELIX   12  12 ASN A  336  GLY A  351  1                                  16
HELIX   13  13 GLU A  369  SER A  395  1                                  27
HELIX   14  14 SER A  408  CYS A  426  1                                  19
HELIX   15  15 GLY A  434  GLY A  447  1                                  14
HELIX   16  16 GLU A  458  GLY A  474  1                                  17
HELIX   17  17 PRO A  482  GLY A  496  1                                  15
HELIX   18  18 THR A  508  LEU A  524  1                                  17
HELIX   19  19 PRO A  540  CYS A  553  1                                  14
HELIX   20  20 ARG A  567  SER A  573  1                                   7
HELIX   21  21 SER A  573  SER A  583  1                                  11
HELIX   22  22 VAL A  584  LYS A  592  1                                   9
HELIX   23  23 ASP A  603  ALA A  608  1                                   6
HELIX   24  24 GLY A  609  ARG A  630  1                                  22
HELIX   25  25 THR A  644  GLY A  648  5                                   5
HELIX   26  26 PRO A  651  SER A  658  1                                   8
HELIX   27  27 GLY A  674  GLY A  682  1                                   9
HELIX   28  28 GLU A  683  HIS A  704  1                                  22
HELIX   29  29 LYS A  710  VAL A  733  1                                  24
HELIX   30  30 ARG A  737  THR A  746  1                                  10
HELIX   31  31 GLU A  748  ASN A  755  5                                   8
HELIX   32  32 ALA A  774  THR A  784  1                                  11
HELIX   33  33 HIS A  787  LEU A  792  1                                   6
HELIX   34  34 GLY A  793  ASP A  805  1                                  13
HELIX   35  35 ARG A  807  TRP A  819  1                                  13
HELIX   36  36 TRP A  819  ALA A  834  1                                  16
HELIX   37  37 ASP A  837  LEU A  848  1                                  12
HELIX   38  38 LEU A  853  GLY A  876  1                                  24
HELIX   39  39 ASP A  884  ASP A  914  1                                  31
HELIX   40  40 GLY A  950  GLN A  967  1                                  18
HELIX   41  41 GLU B   36  GLY B   54  1                                  19
HELIX   42  42 GLY B   54  GLY B   73  1                                  20
HELIX   43  43 ASP B   76  GLY B   89  1                                  14
HELIX   44  44 ALA B   91  ARG B  122  1                                  32
HELIX   45  45 ASP B  142  SER B  152  1                                  11
HELIX   46  46 SER B  157  ASN B  167  1                                  11
HELIX   47  47 ARG B  183  LEU B  200  1                                  18
HELIX   48  48 THR B  206  ARG B  226  1                                  21
HELIX   49  49 THR B  236  THR B  251  1                                  16
HELIX   50  50 THR B  251  ASN B  269  1                                  19
HELIX   51  51 THR B  300  LEU B  330  1                                  31
HELIX   52  52 ASN B  336  SER B  349  1                                  14
HELIX   53  53 GLU B  369  SER B  395  1                                  27
HELIX   54  54 SER B  408  CYS B  426  1                                  19
HELIX   55  55 ASP B  428  ASP B  433  1                                   6
HELIX   56  56 GLY B  434  GLY B  447  1                                  14
HELIX   57  57 SER B  459  HIS B  472  1                                  14
HELIX   58  58 PRO B  482  GLY B  496  1                                  15
HELIX   59  59 THR B  508  LEU B  524  1                                  17
HELIX   60  60 PRO B  525  ASP B  527  5                                   3
HELIX   61  61 ALA B  539  GLU B  552  1                                  14
HELIX   62  62 ARG B  567  PHE B  582  1                                  16
HELIX   63  63 VAL B  584  LYS B  592  1                                   9
HELIX   64  64 ASP B  603  ALA B  608  1                                   6
HELIX   65  65 GLY B  609  TYR B  631  1                                  23
HELIX   66  66 THR B  644  GLY B  648  5                                   5
HELIX   67  67 PRO B  651  SER B  658  1                                   8
HELIX   68  68 GLY B  674  GLY B  682  1                                   9
HELIX   69  69 GLU B  683  HIS B  704  1                                  22
HELIX   70  70 LYS B  710  VAL B  733  1                                  24
HELIX   71  71 GLU B  735  THR B  746  1                                  12
HELIX   72  72 PRO B  747  ASN B  755  5                                   9
HELIX   73  73 ARG B  773  THR B  784  1                                  12
HELIX   74  74 HIS B  787  LEU B  792  1                                   6
HELIX   75  75 GLY B  793  LYS B  804  1                                  12
HELIX   76  76 VAL B  806  TRP B  819  1                                  14
HELIX   77  77 TRP B  819  ALA B  834  1                                  16
HELIX   78  78 ASP B  837  TYR B  844  1                                   8
HELIX   79  79 TYR B  844  VAL B  849  1                                   6
HELIX   80  80 LEU B  853  GLY B  876  1                                  24
HELIX   81  81 ASP B  884  ASP B  914  1                                  31
HELIX   82  82 LEU B  938  ASN B  942  5                                   5
HELIX   83  83 GLY B  950  GLN B  967  1                                  18
SHEET    1   A 9 THR A 169  THR A 175  0
SHEET    2   A 9 ILE A 283  SER A 287  1  O  ARG A 284   N  LEU A 172
SHEET    3   A 9 LYS A 452  ARG A 456  1  O  ASP A 454   N  SER A 287
SHEET    4   A 9 PHE A 529  ILE A 534  1  O  ILE A 533   N  ILE A 455
SHEET    5   A 9 VAL A 561  PHE A 565  1  O  VAL A 562   N  ILE A 534
SHEET    6   A 9 LYS A 594  GLY A 600  1  O  GLY A 600   N  PHE A 565
SHEET    7   A 9 LYS A 634  GLY A 640  1  O  PHE A 638   N  VAL A 599
SHEET    8   A 9 SER A 667  GLN A 673  1  O  ARG A 669   N  HIS A 639
SHEET    9   A 9 THR A 169  THR A 175  1  N  VAL A 173   O  VAL A 672
SHEET    1   B 9 THR B 169  THR B 175  0
SHEET    2   B 9 ILE B 283  SER B 287  1  O  SER B 286   N  PHE B 174
SHEET    3   B 9 LYS B 452  GLU B 458  1  O  LYS B 452   N  SER B 287
SHEET    4   B 9 PHE B 529  SER B 535  1  O  GLY B 530   N  LEU B 453
SHEET    5   B 9 VAL B 561  PHE B 565  1  O  VAL B 562   N  TYR B 532
SHEET    6   B 9 LYS B 594  GLY B 600  1  O  MET B 598   N  PHE B 565
SHEET    7   B 9 LYS B 634  GLY B 640  1  O  PHE B 638   N  VAL B 599
SHEET    8   B 9 SER B 667  GLN B 673  1  O  ARG B 669   N  HIS B 639
SHEET    9   B 9 THR B 169  THR B 175  1  N  VAL B 173   O  VAL B 670
SITE     1 AC1  4 ARG A 183  ARG A 184  SER A 185  ARG A 231
SITE     1 AC2  4 ARG B 183  ARG B 184  SER B 185  ARG B 231
CRYST1  158.440  174.610  254.280  90.00  90.00  90.00 C 2 2 21     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.006312  0.000000  0.000000        0.00000
SCALE2      0.000000  0.005727  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003933        0.00000
      
PROCHECK
Go to PROCHECK summary
 References