spacer
spacer

PDBsum entry 9rub

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Lyase(carbon-carbon) PDB id
9rub
Jmol
Contents
Protein chains
459 a.a. *
Ligands
RUB ×2
FMT ×2
Metals
_MG ×2
* Residue conservation analysis
HEADER    LYASE(CARBON-CARBON)                    28-NOV-90   9RUB
TITLE     CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE
TITLE    2 CARBOXYLASE COMPLEXED WITH ITS SUBSTRATE, RIBULOSE-1,5-
TITLE    3 BISPHOSPHATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.1.1.39;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOSPIRILLUM RUBRUM;
SOURCE   3 ORGANISM_TAXID: 1085
KEYWDS    LYASE(CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.LUNDQVIST,G.SCHNEIDER
REVDAT   3   24-FEB-09 9RUB    1       VERSN
REVDAT   2   15-JAN-95 9RUB    1       COMPND
REVDAT   1   15-JAN-93 9RUB    0
JRNL        AUTH   T.LUNDQVIST,G.SCHNEIDER
JRNL        TITL   CRYSTAL STRUCTURE OF ACTIVATED
JRNL        TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE COMPLEXED
JRNL        TITL 3 WITH ITS SUBSTRATE, RIBULOSE-1,5-BISPHOSPHATE.
JRNL        REF    J.BIOL.CHEM.                  V. 266 12604 1991
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   1905726
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.SCHNEIDER,S.KNIGHT,I.ANDERSSON,Y.LINDQVIST,
REMARK   1  AUTH 2 T.LUNDQVIST,C.-I.BRANDEN
REMARK   1  TITL   COMPARISON OF THE CRYSTAL STRUCTURES OF L2 AND
REMARK   1  TITL 2 L8S8 RUBISCO SUGGESTS A FUNCTIONAL ROLE FOR THE
REMARK   1  TITL 3 SMALL SUBUNIT
REMARK   1  REF    EMBO J.                       V.   9  2045 1990
REMARK   1  REFN                   ISSN 0261-4189
REMARK   1 REFERENCE 2
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,T.LUNDQVIST
REMARK   1  TITL   CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE FROM
REMARK   1  TITL 3 RHODOSPIRILLUM RUBRUM AT 1.7 ANGSTROMS RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 211   989 1990
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 3
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE COMPLEX OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND A
REMARK   1  TITL 3 TRANSITION STATE ANALOGUE, 2-CARBOXY-D-ARABINITOL
REMARK   1  TITL 4 1,5-BISPHOSPHATE
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  7078 1989
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 4
REMARK   1  AUTH   T.LUNDQVIST,G.SCHNEIDER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS
REMARK   1  TITL 3 PRODUCT, 3-PHOSPHO-D-GLYCERATE
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  3643 1989
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1 REFERENCE 5
REMARK   1  AUTH   G.SCHNEIDER,Y.LINDQVIST,C.-I.BRANDEN,G.LORIMER
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)
REMARK   1  TITL 3 OXYGENASE FROM RHODOSPIRILLUM RUBRUM AT 2.9
REMARK   1  TITL 4 ANGSTROMS RESOLUTION
REMARK   1  REF    EMBO J.                       V.   5  3409 1986
REMARK   1  REFN                   ISSN 0261-4189
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROLSQ
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
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) : 0.199
REMARK   3   R VALUE            (WORKING SET) : NULL
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7000
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 44
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.017 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
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) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
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) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS:  RESIDUES A 191 AND B 191 ARE
REMARK   3  MODIFIED LYSINES WHICH ARE CARBAMYLATED AT THE EPSILON-AMINO
REMARK   3  GROUP. THE CARBAMYL GROUPS ARE PRESENTED AS HET GROUPS *CBX*
REMARK   3  AT THE END OF CHAINS *A* AND *B*.
REMARK   4
REMARK   4 9RUB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
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 : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       35.30000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
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 300 REMARK:
REMARK 300 THE TRANSFORMATION GIVEN ON THE *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO
REMARK 300 COORDINATES OF CHAIN *B*.  RESIDUES 422 - 450 WERE OMITTED
REMARK 300 WHEN GENERATING THIS TRANSFORMATION MATRIX.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 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     ARG A   461
REMARK 465     SER A   462
REMARK 465     ALA A   463
REMARK 465     LEU A   464
REMARK 465     PRO A   465
REMARK 465     ALA A   466
REMARK 465     MET B     1
REMARK 465     THR B   460
REMARK 465     ARG B   461
REMARK 465     SER B   462
REMARK 465     ALA B   463
REMARK 465     LEU B   464
REMARK 465     PRO B   465
REMARK 465     ALA B   466
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     THR A 460    CB   OG1  CG2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     GLU A  458   CD    OE1   OE2
REMARK 480     ASP A  459   CG    OD1
REMARK 480     THR A  460   CA    C     O
REMARK 480     VAL B  457   O
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    SER A   356     N    GLY A   358              2.12
REMARK 500   OH   TYR B     7     OG1  THR B    51              2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 458   CG    GLU A 458   CD      0.324
REMARK 500    ASP A 459   CG    ASP A 459   OD2     0.311
REMARK 500    THR A 460   N     THR A 460   CA     -0.205
REMARK 500    VAL B 457   C     VAL B 457   O      -0.175
REMARK 500
REMARK 500 REMARK: NULL
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    SER A   4   N   -  CA  -  CB  ANGL. DEV. =   9.4 DEGREES
REMARK 500    SER A   4   C   -  N   -  CA  ANGL. DEV. =  21.0 DEGREES
REMARK 500    ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    LEU A  10   N   -  CA  -  C   ANGL. DEV. = -18.5 DEGREES
REMARK 500    GLU A  22   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES
REMARK 500    GLU A  22   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    LEU A  25   O   -  C   -  N   ANGL. DEV. =  10.7 DEGREES
REMARK 500    TYR A  38   C   -  N   -  CA  ANGL. DEV. =  17.2 DEGREES
REMARK 500    ASN A  54   CA  -  CB  -  CG  ANGL. DEV. =  20.6 DEGREES
REMARK 500    VAL A  55   CA  -  CB  -  CG2 ANGL. DEV. =   9.7 DEGREES
REMARK 500    GLU A  56   CA  -  C   -  O   ANGL. DEV. =  18.2 DEGREES
REMARK 500    GLU A  56   O   -  C   -  N   ANGL. DEV. = -12.9 DEGREES
REMARK 500    VAL A  57   C   -  N   -  CA  ANGL. DEV. =  36.0 DEGREES
REMARK 500    CYS A  58   N   -  CA  -  CB  ANGL. DEV. =   9.3 DEGREES
REMARK 500    CYS A  58   CA  -  CB  -  SG  ANGL. DEV. =   8.6 DEGREES
REMARK 500    THR A  59   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES
REMARK 500    THR A  59   C   -  N   -  CA  ANGL. DEV. =  19.9 DEGREES
REMARK 500    THR A  60   C   -  N   -  CA  ANGL. DEV. =  18.3 DEGREES
REMARK 500    ASP A  61   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP A  62   CB  -  CG  -  OD2 ANGL. DEV. =  -9.9 DEGREES
REMARK 500    ASP A  62   C   -  N   -  CA  ANGL. DEV. =  18.2 DEGREES
REMARK 500    THR A  64   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES
REMARK 500    THR A  64   CA  -  C   -  O   ANGL. DEV. =  17.5 DEGREES
REMARK 500    ARG A  65   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    THR A  64   CA  -  C   -  N   ANGL. DEV. = -13.8 DEGREES
REMARK 500    ARG A  65   C   -  N   -  CA  ANGL. DEV. =  22.1 DEGREES
REMARK 500    VAL A  67   C   -  N   -  CA  ANGL. DEV. =  21.6 DEGREES
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =   7.3 DEGREES
REMARK 500    VAL A  71   N   -  CA  -  CB  ANGL. DEV. =  20.6 DEGREES
REMARK 500    TYR A  72   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ASP A  75   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES
REMARK 500    ASP A  75   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES
REMARK 500    ARG A  78   CD  -  NE  -  CZ  ANGL. DEV. =  32.4 DEGREES
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    PHE A  90   CB  -  CG  -  CD2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ASP A  91   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A  92   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    THR A  95   CA  -  CB  -  CG2 ANGL. DEV. =   9.0 DEGREES
REMARK 500    ASP A  96   CB  -  CG  -  OD1 ANGL. DEV. =  18.7 DEGREES
REMARK 500    ASP A  96   CB  -  CG  -  OD2 ANGL. DEV. = -12.0 DEGREES
REMARK 500    LYS A  98   O   -  C   -  N   ANGL. DEV. =  10.7 DEGREES
REMARK 500    PHE A 104   CB  -  CG  -  CD1 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    LEU A 105   CA  -  C   -  O   ANGL. DEV. = -15.6 DEGREES
REMARK 500    THR A 106   N   -  CA  -  CB  ANGL. DEV. =  21.2 DEGREES
REMARK 500    LEU A 105   CA  -  C   -  N   ANGL. DEV. =  16.8 DEGREES
REMARK 500    ASN A 112   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES
REMARK 500    MET A 115   CB  -  CA  -  C   ANGL. DEV. =  13.1 DEGREES
REMARK 500    MET A 115   CA  -  CB  -  CG  ANGL. DEV. =  10.5 DEGREES
REMARK 500    ASP A 117   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     398 ANGLE DEVIATIONS.
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    GLN A   3     -155.03     65.79
REMARK 500    SER A   4      -91.70   -149.47
REMARK 500    SER A   5      145.60    -29.90
REMARK 500    ARG A   6      -35.05     79.52
REMARK 500    ASN A   9       61.69   -171.07
REMARK 500    ALA A  11       -8.52    146.95
REMARK 500    TYR A  38      -80.36     21.15
REMARK 500    SER A  50      -97.10   -139.34
REMARK 500    THR A  53       67.31     31.27
REMARK 500    VAL A  55     -119.67     61.27
REMARK 500    ASP A  62      132.14     80.95
REMARK 500    PHE A  63       91.47     78.02
REMARK 500    THR A  64       77.56   -151.31
REMARK 500    VAL A  67       20.12   -151.24
REMARK 500    PRO A  86      159.09    -49.85
REMARK 500    ASP A  96      -16.59   -140.77
REMARK 500    MET A 115      135.99    -37.56
REMARK 500    PRO A 129      169.77    -25.81
REMARK 500    PHE A 136      139.73    156.16
REMARK 500    ASP A 137      -70.86    -50.38
REMARK 500    SER A 144       15.55    -52.39
REMARK 500    LYS A 148       -7.32    -59.15
REMARK 500    ASP A 156       19.41     24.52
REMARK 500    LEU A 169      143.85   -170.75
REMARK 500    LEU A 171      100.04      8.50
REMARK 500    ARG A 172     -179.07    -54.05
REMARK 500    TRP A 184       16.40    -65.05
REMARK 500    PRO A 195       42.33    -84.01
REMARK 500    ALA A 202       75.91   -151.52
REMARK 500    LEU A 204      -60.53    -13.99
REMARK 500    ASP A 220      -77.71   -106.74
REMARK 500    GLU A 221       -2.55    -51.15
REMARK 500    ASP A 263       14.86    -67.10
REMARK 500    TYR A 265      -63.17    -97.65
REMARK 500    VAL A 266       40.11    -60.43
REMARK 500    ALA A 267        4.58    176.80
REMARK 500    ARG A 288       40.43    -57.43
REMARK 500    ALA A 289      151.06    -44.70
REMARK 500    VAL A 294      -72.29   -105.67
REMARK 500    PRO A 297        8.55    -58.32
REMARK 500    HIS A 321       78.92    -69.72
REMARK 500    THR A 324      148.16    176.41
REMARK 500    PHE A 327     -143.85   -130.60
REMARK 500    LYS A 329     -108.01     62.56
REMARK 500    GLU A 333       54.66      2.21
REMARK 500    SER A 334       72.69     75.12
REMARK 500    ALA A 338      -56.20    -28.63
REMARK 500    GLU A 347       60.70   -174.20
REMARK 500    PRO A 351        2.20    -56.60
REMARK 500    PHE A 352      -48.37   -157.36
REMARK 500    SER A 356       47.49   -102.74
REMARK 500    TRP A 357       12.37    -19.45
REMARK 500    MET A 360     -123.97    -60.26
REMARK 500    LYS A 361     -156.87   -164.38
REMARK 500    ASN A 372     -177.56    -49.59
REMARK 500    ALA A 373      -62.01    -18.64
REMARK 500    PHE A 380      -17.74    -48.35
REMARK 500    LEU A 383      -89.68    -83.65
REMARK 500    ASN A 385     -168.92   -170.92
REMARK 500    ALA A 386       19.10   -149.75
REMARK 500    PRO A 403       11.93    -56.21
REMARK 500    ARG A 418      -76.83    -44.45
REMARK 500    PRO A 422      125.89     40.46
REMARK 500    PHE A 440       66.60   -118.65
REMARK 500    ASP A 443      -57.44   -123.57
REMARK 500    ALA A 444       74.19    -65.90
REMARK 500    ASP A 445      -84.89    171.48
REMARK 500    PRO A 449      -80.38     16.51
REMARK 500    TRP A 451      -33.92    -17.87
REMARK 500    ARG A 452      -70.44    -48.73
REMARK 500    VAL A 457     -157.64    118.72
REMARK 500    ASP A 459      155.46    127.79
REMARK 500    GLN B   3      -25.44     53.19
REMARK 500    SER B   4      170.94    131.96
REMARK 500    SER B   5       17.17   -155.76
REMARK 500    ASN B   9       83.68   -168.05
REMARK 500    SER B  50      -89.98   -108.21
REMARK 500    THR B  53       72.51     63.12
REMARK 500    ASN B  54      -87.80    -17.64
REMARK 500    GLU B  56     -103.39     87.92
REMARK 500    CYS B  58      -34.01    -28.13
REMARK 500    THR B  59     -157.69     51.28
REMARK 500    ASP B  61      168.05     66.14
REMARK 500    ASP B  62       87.42     84.24
REMARK 500    PHE B  63      -22.69    110.00
REMARK 500    GLU B  73      141.88   -170.94
REMARK 500    GLU B  79       65.16     70.23
REMARK 500    PRO B  86      147.72    -37.49
REMARK 500    ASP B  91      110.93     71.83
REMARK 500    ALA B  99      176.81    -54.76
REMARK 500    LEU B 107      -73.22    -72.23
REMARK 500    MET B 109       59.81   -158.04
REMARK 500    ASN B 111       23.91    -74.94
REMARK 500    MET B 115      123.24   -170.59
REMARK 500    TYR B 120      131.24     65.43
REMARK 500    ASP B 125      138.70    150.32
REMARK 500    ASP B 137      -75.70    -66.70
REMARK 500    GLU B 154        0.37    -56.71
REMARK 500    LYS B 191      -88.71    -88.23
REMARK 500    ASN B 192      121.29    124.03
REMARK 500    GLU B 194      -56.77    -28.29
REMARK 500    ALA B 202       62.10    167.84
REMARK 500    ASP B 213      -70.84    -66.98
REMARK 500    ALA B 214        9.18    -52.84
REMARK 500    ASP B 235      -60.36   -103.38
REMARK 500    ARG B 243      -76.04    -86.98
REMARK 500    TYR B 246      -79.64    -63.16
REMARK 500    ALA B 267      -17.09   -140.92
REMARK 500    ALA B 269      -10.35    -39.29
REMARK 500    ARG B 276     -130.04    -72.30
REMARK 500    ARG B 277      -49.33     11.55
REMARK 500    PHE B 279       77.74   -115.67
REMARK 500    ARG B 288      -87.47    -73.53
REMARK 500    ALA B 289     -122.24    106.05
REMARK 500    THR B 322     -145.66   -153.73
REMARK 500    PHE B 327      175.86    143.99
REMARK 500    MET B 330       14.72    160.70
REMARK 500    GLU B 333     -168.81   -106.62
REMARK 500    SER B 335       18.85      7.93
REMARK 500    ALA B 338        2.00    -65.33
REMARK 500    PHE B 352      -33.18   -137.50
REMARK 500    ALA B 373       -4.29    -50.54
REMARK 500    ASN B 385     -169.56   -127.60
REMARK 500    PRO B 403      -84.64    -37.14
REMARK 500    PRO B 422       52.80    -63.94
REMARK 500    VAL B 423      -55.76     44.05
REMARK 500    ARG B 428       94.43    -68.75
REMARK 500    GLU B 429      -46.83    143.48
REMARK 500    LEU B 433      -70.24    -59.45
REMARK 500    PHE B 440       78.61   -112.57
REMARK 500    ALA B 444      -76.13    -68.31
REMARK 500    ASP B 445       26.39    -46.91
REMARK 500    GLN B 446      -18.87   -159.53
REMARK 500    GLU B 458      158.97      8.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    VAL B 457         16.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 RUB A 600   O2
REMARK 620 2 RUB A 600   O3   73.1
REMARK 620 3 ASP A 193   OD1 102.9 154.1
REMARK 620 4 FMT A 601   O1  144.2  74.4  99.8
REMARK 620 5 FMT A 601   O2  124.5 105.9  54.5  52.8
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 500  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT B 701   O1
REMARK 620 2 ASP B 193   OD1  66.6
REMARK 620 3 RUB B 700   O3   74.4 137.9
REMARK 620 4 RUB B 700   O2  145.0 147.0  74.8
REMARK 620 N                    1     2     3
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEETS *ACT* AND *BCT* PRESENTED BELOW ARE ACTUALLY
REMARK 700 EIGHT-STRANDED BETA/ALPHA BARRELS.  THESE ARE REPRESENTED
REMARK 700 AS NINE-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CHAIN A
REMARK 800 SITE_IDENTIFIER: BCT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE CHAIN B
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB A 600
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RUB B 700
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 601
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 701
DBREF  9RUB A    1   466  UNP    P04718   RBL2_RHORU       1    466
DBREF  9RUB B    1   466  UNP    P04718   RBL2_RHORU       1    466
SEQADV 9RUB ASP A   91  UNP  P04718    HIS    91 CONFLICT
SEQADV 9RUB ASP B   91  UNP  P04718    HIS    91 CONFLICT
SEQRES   1 A  466  MET ASP GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS
SEQRES   2 A  466  GLU GLU ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS
SEQRES   3 A  466  ALA TYR ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL
SEQRES   4 A  466  ALA THR ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY
SEQRES   5 A  466  THR ASN VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG
SEQRES   6 A  466  GLY VAL ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG
SEQRES   7 A  466  GLU LEU THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP
SEQRES   8 A  466  ARG ASN ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE
SEQRES   9 A  466  LEU THR LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP
SEQRES  10 A  466  VAL GLU TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU
SEQRES  11 A  466  ALA TYR ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE
SEQRES  12 A  466  SER ALA LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP
SEQRES  13 A  466  GLY GLY LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU
SEQRES  14 A  466  GLY LEU ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA
SEQRES  15 A  466  PHE TRP LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO
SEQRES  16 A  466  GLN GLY ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE
SEQRES  17 A  466  ALA LEU VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU
SEQRES  18 A  466  THR GLY GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA
SEQRES  19 A  466  ASP ASP PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL
SEQRES  20 A  466  LEU GLU THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU
SEQRES  21 A  466  LEU VAL ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR
SEQRES  22 A  466  THR ALA ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR
SEQRES  23 A  466  HIS ARG ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER
SEQRES  24 A  466  LYS ARG GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA
SEQRES  25 A  466  ARG LEU GLN GLY ALA SER GLY ILE HIS THR GLY THR MET
SEQRES  26 A  466  GLY PHE GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA
SEQRES  27 A  466  ILE ALA TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO
SEQRES  28 A  466  PHE TYR ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR
SEQRES  29 A  466  PRO ILE ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO
SEQRES  30 A  466  GLY PHE PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU
SEQRES  31 A  466  THR ALA GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO
SEQRES  32 A  466  VAL ALA GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA
SEQRES  33 A  466  TRP ARG ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU
SEQRES  34 A  466  HIS LYS GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY
SEQRES  35 A  466  ASP ALA ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU
SEQRES  36 A  466  GLY VAL GLU ASP THR ARG SER ALA LEU PRO ALA
SEQRES   1 B  466  MET ASP GLN SER SER ARG TYR VAL ASN LEU ALA LEU LYS
SEQRES   2 B  466  GLU GLU ASP LEU ILE ALA GLY GLY GLU HIS VAL LEU CYS
SEQRES   3 B  466  ALA TYR ILE MET LYS PRO LYS ALA GLY TYR GLY TYR VAL
SEQRES   4 B  466  ALA THR ALA ALA HIS PHE ALA ALA GLU SER SER THR GLY
SEQRES   5 B  466  THR ASN VAL GLU VAL CYS THR THR ASP ASP PHE THR ARG
SEQRES   6 B  466  GLY VAL ASP ALA LEU VAL TYR GLU VAL ASP GLU ALA ARG
SEQRES   7 B  466  GLU LEU THR LYS ILE ALA TYR PRO VAL ALA LEU PHE ASP
SEQRES   8 B  466  ARG ASN ILE THR ASP GLY LYS ALA MET ILE ALA SER PHE
SEQRES   9 B  466  LEU THR LEU THR MET GLY ASN ASN GLN GLY MET GLY ASP
SEQRES  10 B  466  VAL GLU TYR ALA LYS MET HIS ASP PHE TYR VAL PRO GLU
SEQRES  11 B  466  ALA TYR ARG ALA LEU PHE ASP GLY PRO SER VAL ASN ILE
SEQRES  12 B  466  SER ALA LEU TRP LYS VAL LEU GLY ARG PRO GLU VAL ASP
SEQRES  13 B  466  GLY GLY LEU VAL VAL GLY THR ILE ILE LYS PRO LYS LEU
SEQRES  14 B  466  GLY LEU ARG PRO LYS PRO PHE ALA GLU ALA CYS HIS ALA
SEQRES  15 B  466  PHE TRP LEU GLY GLY ASP PHE ILE LYS ASN ASP GLU PRO
SEQRES  16 B  466  GLN GLY ASN GLN PRO PHE ALA PRO LEU ARG ASP THR ILE
SEQRES  17 B  466  ALA LEU VAL ALA ASP ALA MET ARG ARG ALA GLN ASP GLU
SEQRES  18 B  466  THR GLY GLU ALA LYS LEU PHE SER ALA ASN ILE THR ALA
SEQRES  19 B  466  ASP ASP PRO PHE GLU ILE ILE ALA ARG GLY GLU TYR VAL
SEQRES  20 B  466  LEU GLU THR PHE GLY GLU ASN ALA SER HIS VAL ALA LEU
SEQRES  21 B  466  LEU VAL ASP GLY TYR VAL ALA GLY ALA ALA ALA ILE THR
SEQRES  22 B  466  THR ALA ARG ARG ARG PHE PRO ASP ASN PHE LEU HIS TYR
SEQRES  23 B  466  HIS ARG ALA GLY HIS GLY ALA VAL THR SER PRO GLN SER
SEQRES  24 B  466  LYS ARG GLY TYR THR ALA PHE VAL HIS CYS LYS MET ALA
SEQRES  25 B  466  ARG LEU GLN GLY ALA SER GLY ILE HIS THR GLY THR MET
SEQRES  26 B  466  GLY PHE GLY LYS MET GLU GLY GLU SER SER ASP ARG ALA
SEQRES  27 B  466  ILE ALA TYR MET LEU THR GLN ASP GLU ALA GLN GLY PRO
SEQRES  28 B  466  PHE TYR ARG GLN SER TRP GLY GLY MET LYS ALA CYS THR
SEQRES  29 B  466  PRO ILE ILE SER GLY GLY MET ASN ALA LEU ARG MET PRO
SEQRES  30 B  466  GLY PHE PHE GLU ASN LEU GLY ASN ALA ASN VAL ILE LEU
SEQRES  31 B  466  THR ALA GLY GLY GLY ALA PHE GLY HIS ILE ASP GLY PRO
SEQRES  32 B  466  VAL ALA GLY ALA ARG SER LEU ARG GLN ALA TRP GLN ALA
SEQRES  33 B  466  TRP ARG ASP GLY VAL PRO VAL LEU ASP TYR ALA ARG GLU
SEQRES  34 B  466  HIS LYS GLU LEU ALA ARG ALA PHE GLU SER PHE PRO GLY
SEQRES  35 B  466  ASP ALA ASP GLN ILE TYR PRO GLY TRP ARG LYS ALA LEU
SEQRES  36 B  466  GLY VAL GLU ASP THR ARG SER ALA LEU PRO ALA
HET    RUB  A 600      18
HET    RUB  B 700      18
HET     MG  A 500       1
HET     MG  B 500       1
HET    FMT  A 601       3
HET    FMT  B 701       3
HETNAM     RUB RIBULOSE-1,5-DIPHOSPHATE
HETNAM      MG MAGNESIUM ION
HETNAM     FMT FORMIC ACID
FORMUL   3  RUB    2(C5 H12 O11 P2)
FORMUL   5   MG    2(MG 2+)
FORMUL   7  FMT    2(C H2 O2)
HELIX    1  AA GLU A   14  GLY A   20  1                                   7
HELIX    2  AB TYR A   38  SER A   49  1                                  12
HELIX    3  AC ILE A  101  MET A  109  1                                   9
HELIX    4  AD GLU A  130  ARG A  133  1                                   4
HELIX    5  AE SER A  144  LEU A  150  1                                   7
HELIX    6  A1 PRO A  173  TRP A  184  1                                  12
HELIX    7  A2 LEU A  204  THR A  222  1                                  19
HELIX    8  A3 ASP A  235  PHE A  251  1                                  17
HELIX    9  A4 ALA A  269  ARG A  278  1                                  10
HELIX   10  AF GLY A  292  THR A  295  1                                   4
HELIX   11  A5 ALA A  305  GLN A  315  1                                  11
HELIX   12  A6 ARG A  337  THR A  344  1                                   8
HELIX   13  A7 ARG A  375  GLY A  378  5                                   4
HELIX   14  A8 PRO A  403  ASP A  419  1                                  17
HELIX   15  AG VAL A  423  GLU A  429  1                                   7
HELIX   16  AH LYS A  431  PHE A  440  1                                  10
HELIX   17  AI GLY A  442  TYR A  448  1                                   7
HELIX   18  AJ TRP A  451  LEU A  455  1                                   5
HELIX   19  BA GLU B   14  GLY B   20  1                                   7
HELIX   20  BB TYR B   38  SER B   49  1                                  12
HELIX   21  BC ILE B  101  MET B  109  1                                   9
HELIX   22  BD GLU B  130  ARG B  133  1                                   4
HELIX   23  BE SER B  144  LEU B  150  1                                   7
HELIX   24  B1 PRO B  173  TRP B  184  1                                  12
HELIX   25  B2 LEU B  204  THR B  222  1                                  19
HELIX   26  B3 ASP B  235  PHE B  251  1                                  17
HELIX   27  B4 ALA B  269  ARG B  278  1                                  10
HELIX   28  BF GLY B  292  THR B  295  1                                   4
HELIX   29  B5 ALA B  305  GLN B  315  1                                  11
HELIX   30  B6 ARG B  337  THR B  344  1                                   8
HELIX   31  B6 ARG B  375  LEU B  383  1                                   9
HELIX   32  B8 PRO B  403  ASP B  419  1                                  17
HELIX   33  BG VAL B  423  GLU B  429  1                                   7
HELIX   34  BH LYS B  431  PHE B  440  1                                  10
HELIX   35  BI GLY B  442  TYR B  448  1                                   7
HELIX   36  BJ TRP B  451  LEU B  455  1                                   5
SHEET    1 ANT 5 VAL A   8  LEU A  10  0
SHEET    2 ANT 5 ALA A  69  ASP A  75  1
SHEET    3 ANT 5 GLU A  79  PRO A  86 -1
SHEET    4 ANT 5 HIS A  23  PRO A  32 -1
SHEET    5 ANT 5 ASP A 117  TYR A 127 -1
SHEET    1 CTA 9 VAL A 160  ILE A 164  0
SHEET    2 CTA 9 PHE A 189  LYS A 191  1
SHEET    3 CTA 9 LEU A 227  ASN A 231  1
SHEET    4 CTA 9 VAL A 258  ASP A 263  1
SHEET    5 CTA 9 LEU A 284  HIS A 287  1
SHEET    6 CTA 9 GLY A 319  HIS A 321  1
SHEET    7 CTA 9 THR A 364  GLY A 369  1
SHEET    8 CTA 9 ILE A 389  ALA A 392  1
SHEET    9 CTA 9 VAL A 160  ILE A 164  1
SHEET    1 BNT 5 VAL B   8  LEU B  10  0
SHEET    2 BNT 5 ALA B  69  ASP B  75  1
SHEET    3 BNT 5 GLU B  79  PRO B  86 -1
SHEET    4 BNT 5 HIS B  23  PRO B  32 -1
SHEET    5 BNT 5 ASP B 117  TYR B 127 -1
SHEET    1 CTB 9 VAL B 160  ILE B 164  0
SHEET    2 CTB 9 PHE B 189  LYS B 191  1
SHEET    3 CTB 9 LEU B 227  ASN B 231  1
SHEET    4 CTB 9 VAL B 258  ASP B 263  1
SHEET    5 CTB 9 LEU B 284  HIS B 287  1
SHEET    6 CTB 9 GLY B 319  HIS B 321  1
SHEET    7 CTB 9 THR B 364  GLY B 369  1
SHEET    8 CTB 9 ILE A 389  ALA A 392  1
SHEET    9 CTB 9 VAL B 160  ILE B 164  1
LINK         NZ  LYS A 191                 C   FMT A 601     1555   1555  1.45
LINK         NZ  LYS B 191                 C   FMT B 701     1555   1555  1.51
LINK        MG    MG A 500                 O2  RUB A 600     1555   1555  2.47
LINK        MG    MG A 500                 O3  RUB A 600     1555   1555  2.62
LINK        MG    MG A 500                 OD1 ASP A 193     1555   1555  2.55
LINK        MG    MG A 500                 O1  FMT A 601     1555   1555  2.39
LINK        MG    MG A 500                 O2  FMT A 601     1555   1555  2.45
LINK        MG    MG B 500                 O1  FMT B 701     1555   1555  2.46
LINK        MG    MG B 500                 OD1 ASP B 193     1555   1555  2.53
LINK        MG    MG B 500                 O3  RUB B 700     1555   1555  2.17
LINK        MG    MG B 500                 O2  RUB B 700     1555   1555  2.42
LINK         O3  RUB B 700                 O2  FMT B 701     1555   1555  2.03
CISPEP   1 LYS A  166    PRO A  167          0         5.20
CISPEP   2 LYS B  166    PRO B  167          0         3.51
SITE     1 ACT  5 FMT A 601  LYS A 191  ASP A 193  GLU A 194
SITE     2 ACT  5  MG A 500
SITE     1 BCT  5 FMT B 701  LYS B 191  ASP B 193  GLU B 194
SITE     2 BCT  5  MG B 500
SITE     1 AC1 10 ILE A 164  ASP A 193  HIS A 321  ILE A 366
SITE     2 AC1 10 SER A 368  ALA A 392  GLY A 393   MG A 500
SITE     3 AC1 10 FMT A 601  ASN B 111
SITE     1 AC2 11 ILE B 164  HIS B 287  HIS B 321  THR B 322
SITE     2 AC2 11 SER B 368  GLY B 369  THR B 391  ALA B 392
SITE     3 AC2 11 GLY B 393   MG B 500  FMT B 701
SITE     1 AC3  3 ASP A 193  RUB A 600  FMT A 601
SITE     1 AC4  4 ASP B 193  GLU B 194  RUB B 700  FMT B 701
SITE     1 AC5  6 ILE A 164  LYS A 191  ASN A 192  ASP A 193
SITE     2 AC5  6  MG A 500  RUB A 600
SITE     1 AC6  7 LYS B 191  ASP B 193  GLU B 194  HIS B 287
SITE     2 AC6  7 HIS B 321   MG B 500  RUB B 700
CRYST1   65.500   70.600  104.100  90.00  92.10  90.00 P 1 21 1      4
ORIGX1      1.000000  0.000000  0.036668        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000672        0.00000
SCALE1      0.015267  0.000000  0.000560        0.00000
SCALE2      0.000000  0.014164  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009613        0.00000
MTRIX1   1  0.373740 -0.056007  0.940855        6.14161    1
MTRIX2   1 -0.073400 -0.996800 -0.033512       17.87800    1
MTRIX3   1  0.909789 -0.054363 -0.376740       -7.57091    1
      
PROCHECK
Go to PROCHECK summary
 References