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PDBsum entry 4rub

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase(carbon-carbon) PDB id
4rub
Jmol
Contents
Protein chains
465 a.a. *
123 a.a. *
Ligands
CAP ×4
FMT ×4
Metals
_MG ×4
* Residue conservation analysis
HEADER    LYASE(CARBON-CARBON)                    25-MAY-90   4RUB
TITLE     A CRYSTAL FORM OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)
TITLE    2 OXYGENASE FROM NICOTIANA TABACUM IN THE ACTIVATED STATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (FORM IV);
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 4.1.1.39;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (FORM IV);
COMPND   8 CHAIN: S, T, U, V;
COMPND   9 EC: 4.1.1.39;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: NICOTIANA TABACUM;
SOURCE   3 ORGANISM_COMMON: COMMON TOBACCO;
SOURCE   4 ORGANISM_TAXID: 4097;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: NICOTIANA TABACUM;
SOURCE   7 ORGANISM_COMMON: COMMON TOBACCO;
SOURCE   8 ORGANISM_TAXID: 4097
KEYWDS    LYASE(CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.SCHREUDER,D.CASCIO,P.M.G.CURMI,D.EISENBERG
REVDAT   6   13-JUL-11 4RUB    1       VERSN
REVDAT   5   24-FEB-09 4RUB    1       VERSN
REVDAT   4   01-APR-03 4RUB    1       JRNL
REVDAT   3   30-APR-94 4RUB    1       SOURCE
REVDAT   2   15-JAN-93 4RUB    1       REMARK
REVDAT   1   15-OCT-92 4RUB    0
JRNL        AUTH   S.W.SUH,D.CASCIO,M.S.CHAPMAN,D.EISENBERG
JRNL        TITL   A CRYSTAL FORM OF RIBULOSE-1,5-BISPHOSPHATE
JRNL        TITL 2 CARBOXYLASE/OXYGENASE FROM NICOTIANA TABACUM IN THE
JRNL        TITL 3 ACTIVATED STATE.
JRNL        REF    J.MOL.BIOL.                   V. 197   363 1987
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   3681999
JRNL        DOI    10.1016/0022-2836(87)90129-X
REMARK   2
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PROFFT
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
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) : 0.202
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            : 18608
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 100
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) : 0.019 ; 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: NULL
REMARK   4
REMARK   4 4RUB 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        : 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   (%): 53.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.13333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       78.26667
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       78.26667
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       39.13333
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: THE FOLLOWING TRANSFORMATION GENERATES APPROXIMATE
REMARK 300 COORDINATES OF LARGE CHAIN *B* WHEN APPLIED TO CHAIN *A*
REMARK 300 AND THE SMALL CHAIN *T* WHEN APPLIED TO CHAIN *S*:
REMARK 300
REMARK 300   1.0     0.0       0.0            0.0
REMARK 300   0.0     0.0       1.0      +   -39.13
REMARK 300   0.0    -1.0       0.0           39.13
REMARK 300
REMARK 300 THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS EIGHT LARGE
REMARK 300 AND EIGHT SMALL SUBUNITS.  COORDINATES ARE PRESENTED IN
REMARK 300 THIS ENTRY FOR FOUR LARGE SUBUNITS WITH CHAIN IDENTIFIERS
REMARK 300 *A*-*D* AND FOUR SMALL SUBUNITS WITH CHAIN IDENTIFIERS
REMARK 300 *S*-*V*.  THE FOLLOWING TRANSFORMATION GENERATES THE
REMARK 300 COORDINATES OF THE REMAINING HALF-MOLECULE FROM THE
REMARK 300 COORDINATES OF THE HALF-MOLECULE PRESENTED IN THIS ENTRY.
REMARK 300
REMARK 300   1.0     0.0       0.0            0.0
REMARK 300   0.0    -1.0       0.0      +     0.0
REMARK 300   0.0     0.0      -1.0           78.27
REMARK 300
REMARK 300 THE TRANSFORMATION PRESENTED IN MTRIX 1 RECORDS GENERATES
REMARK 300 THE LARGE SUBUNIT *C* WHEN APPLIED TO CHAIN *A* AND
REMARK 300 GENERATES THE SMALL SUBUNIT *U* WHEN APPLIED TO CHAIN *S*.
REMARK 300 THE TRANSFORMATION PRESENTED IN MTRIX 2 RECORDS GENERATES
REMARK 300 THE LARGE SUBUNIT *D* WHEN APPLIED TO CHAIN *A* AND
REMARK 300 GENERATES THE SMALL SUBUNIT *V* WHEN APPLIED TO CHAIN *S*.
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 110320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 117040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -528.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S, B, T, C, U, D, V
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        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       78.26667
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THE FOLLOWING SALT BRIDGES EXIST BETWEEN ATOMS WITH
REMARK 400 COORDINATES IN THE ATOM RECORDS PRESENTED IN THIS ENTRY
REMARK 400 AND ATOMS IN THE SYMMETRY RELATED MOLECULES, WHERE THE
REMARK 400 SYMMETRY TRANSFORMATION IS GIVEN IN REMARK 7 ABOVE.
REMARK 400 THE SYMMETRY RELATED CHAIN INDICATOR IS INDICATED WITH '*'.
REMARK 400
REMARK 400   OE2 GLU A 110      NZ  LYS C* 146
REMARK 400   OE2 GLU C 110      NZ  LYS A* 146
REMARK 400   NZ  LYS A 161      OD1 ASP B* 216
REMARK 400   NZ  LYS C 161      OD1 ASP D* 216
REMARK 400   NZ  LYS B 252      OD1 ASP A* 286
REMARK 400   NZ  LYS D 252      OD1 ASP C* 286
REMARK 400   NH1 ARG A 258      OE2 GLU B* 259
REMARK 400   NH1 ARG C 258      OE2 GLU D* 259
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     SER A     2
REMARK 465     PRO A     3
REMARK 465     GLN A     4
REMARK 465     THR A     5
REMARK 465     GLU A     6
REMARK 465     THR A     7
REMARK 465     LYS A     8
REMARK 465     VAL A   474
REMARK 465     LEU A   475
REMARK 465     ASP A   476
REMARK 465     LYS A   477
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     PRO B     3
REMARK 465     GLN B     4
REMARK 465     THR B     5
REMARK 465     GLU B     6
REMARK 465     THR B     7
REMARK 465     LYS B     8
REMARK 465     VAL B   474
REMARK 465     LEU B   475
REMARK 465     ASP B   476
REMARK 465     LYS B   477
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     PRO C     3
REMARK 465     GLN C     4
REMARK 465     THR C     5
REMARK 465     GLU C     6
REMARK 465     THR C     7
REMARK 465     LYS C     8
REMARK 465     VAL C   474
REMARK 465     LEU C   475
REMARK 465     ASP C   476
REMARK 465     LYS C   477
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     PRO D     3
REMARK 465     GLN D     4
REMARK 465     THR D     5
REMARK 465     GLU D     6
REMARK 465     THR D     7
REMARK 465     LYS D     8
REMARK 465     VAL D   474
REMARK 465     LEU D   475
REMARK 465     ASP D   476
REMARK 465     LYS D   477
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     ASP A 473    CA   C    O    CB   CG   OD1  OD2
REMARK 470     ASP B 473    CA   C    O    CB   CG   OD1  OD2
REMARK 470     ASP C 473    CA   C    O    CB   CG   OD1  OD2
REMARK 470     ASP D 473    CA   C    O    CB   CG   OD1  OD2
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   OH   TYR B    29     NZ   LYS B    32              2.01
REMARK 500   NZ   LYS D   201     O1   FMT D   492              2.09
REMARK 500   O    GLY T    60     NH2  ARG T    65              2.09
REMARK 500   NZ   LYS A   201     O1   FMT A   492              2.11
REMARK 500   NZ   LYS C   201     O1   FMT C   492              2.11
REMARK 500   OH   TYR D    29     NZ   LYS D    32              2.13
REMARK 500   OH   TYR D    29     OD2  ASP D    35              2.14
REMARK 500   NZ   LYS B   201     O1   FMT B   492              2.15
REMARK 500   NZ   LYS B   201     O2   FMT B   492              2.15
REMARK 500   O    GLY D   171     N    PHE D   402              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NH2  ARG B   446     NE2  GLN C    30     3654     2.00
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    SER A  61   CA    SER A  61   CB      0.091
REMARK 500    ASP A  72   C     ASP A  72   O       0.122
REMARK 500    ARG A 134   CZ    ARG A 134   NH1     0.104
REMARK 500    LYS A 201   CA    LYS A 201   CB      0.152
REMARK 500    LYS A 201   CE    LYS A 201   NZ     -0.150
REMARK 500    GLU A 234   CD    GLU A 234   OE2    -0.087
REMARK 500    HIS A 238   CE1   HIS A 238   NE2    -0.103
REMARK 500    SER A 279   CA    SER A 279   CB     -0.097
REMARK 500    ARG A 319   CD    ARG A 319   NE     -0.115
REMARK 500    ARG A 319   NE    ARG A 319   CZ     -0.091
REMARK 500    CYS A 427   CB    CYS A 427   SG     -0.109
REMARK 500    CYS A 449   CB    CYS A 449   SG     -0.099
REMARK 500    CYS A 459   CB    CYS A 459   SG     -0.138
REMARK 500    ILE S   7   C     ILE S   7   O       0.124
REMARK 500    SER S  58   CB    SER S  58   OG     -0.119
REMARK 500    GLU B  52   CD    GLU B  52   OE1    -0.071
REMARK 500    GLU B 110   CD    GLU B 110   OE2    -0.072
REMARK 500    LYS B 201   CA    LYS B 201   CB      0.147
REMARK 500    GLU B 223   CD    GLU B 223   OE1    -0.076
REMARK 500    CYS B 247   CA    CYS B 247   CB     -0.085
REMARK 500    HIS B 282   CE1   HIS B 282   NE2    -0.075
REMARK 500    HIS B 292   NE2   HIS B 292   CD2    -0.068
REMARK 500    GLU B 425   CD    GLU B 425   OE1    -0.068
REMARK 500    CYS B 459   CB    CYS B 459   SG     -0.113
REMARK 500    TYR T  62   CZ    TYR T  62   CE2    -0.084
REMARK 500    GLU C 110   CB    GLU C 110   CG     -0.148
REMARK 500    PHE C 127   C     PHE C 127   O       0.115
REMARK 500    HIS C 153   C     HIS C 153   O       0.117
REMARK 500    GLN C 156   CD    GLN C 156   NE2     0.165
REMARK 500    SER C 181   CB    SER C 181   OG      0.117
REMARK 500    LYS C 201   CA    LYS C 201   CB      0.171
REMARK 500    HIS C 238   CE1   HIS C 238   NE2    -0.098
REMARK 500    THR C 243   CB    THR C 243   OG1     0.147
REMARK 500    ARG C 253   CZ    ARG C 253   NH1     0.086
REMARK 500    GLU C 259   CD    GLU C 259   OE2     0.074
REMARK 500    MET C 266   C     MET C 266   O       0.146
REMARK 500    HIS C 267   CE1   HIS C 267   NE2    -0.070
REMARK 500    SER C 279   CB    SER C 279   OG      0.093
REMARK 500    ARG C 285   CZ    ARG C 285   NH1     0.094
REMARK 500    HIS C 310   C     HIS C 310   O       0.124
REMARK 500    ARG C 319   CD    ARG C 319   NE     -0.131
REMARK 500    GLY C 323   N     GLY C 323   CA      0.133
REMARK 500    GLY C 405   C     GLY C 405   O       0.124
REMARK 500    GLU C 454   CD    GLU C 454   OE2     0.078
REMARK 500    ILE U   7   C     ILE U   7   O       0.141
REMARK 500    ARG U  65   NE    ARG U  65   CZ      0.084
REMARK 500    GLU D  60   CD    GLU D  60   OE2    -0.066
REMARK 500    GLU D 158   CD    GLU D 158   OE1     0.080
REMARK 500    CYS D 172   CB    CYS D 172   SG     -0.101
REMARK 500    LYS D 201   CA    LYS D 201   CB      0.163
REMARK 500
REMARK 500 THIS ENTRY HAS      61 BOND DEVIATIONS.
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  10   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES
REMARK 500    GLU A  19   N   -  CA  -  CB  ANGL. DEV. =  12.7 DEGREES
REMARK 500    TYR A  24   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES
REMARK 500    TYR A  24   N   -  CA  -  CB  ANGL. DEV. = -11.4 DEGREES
REMARK 500    TYR A  25   CB  -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TYR A  25   CB  -  CG  -  CD1 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    GLU A  28   OE1 -  CD  -  OE2 ANGL. DEV. =   8.7 DEGREES
REMARK 500    ASP A  33   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ASP A  33   CB  -  CG  -  OD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500    ASP A  35   CB  -  CG  -  OD1 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    PRO A  46   N   -  CA  -  CB  ANGL. DEV. = -10.3 DEGREES
REMARK 500    GLU A  60   CG  -  CD  -  OE2 ANGL. DEV. =  14.5 DEGREES
REMARK 500    SER A  61   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES
REMARK 500    ASP A  72   CA  -  CB  -  CG  ANGL. DEV. =  23.0 DEGREES
REMARK 500    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG A  83   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES
REMARK 500    ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    ARG A  83   NE  -  CZ  -  NH2 ANGL. DEV. =   5.0 DEGREES
REMARK 500    CYS A  84   CA  -  CB  -  SG  ANGL. DEV. = -12.3 DEGREES
REMARK 500    TYR A  85   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A  86   N   -  CA  -  CB  ANGL. DEV. =  11.9 DEGREES
REMARK 500    GLU A  88   CG  -  CD  -  OE1 ANGL. DEV. = -12.4 DEGREES
REMARK 500    ARG A  89   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES
REMARK 500    ARG A  89   CD  -  NE  -  CZ  ANGL. DEV. =  22.3 DEGREES
REMARK 500    GLU A  93   CA  -  C   -  N   ANGL. DEV. = -13.7 DEGREES
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A  95   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    GLN A  96   CA  -  CB  -  CG  ANGL. DEV. =  16.6 DEGREES
REMARK 500    TYR A  97   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES
REMARK 500    VAL A 101   CG1 -  CB  -  CG2 ANGL. DEV. =  10.8 DEGREES
REMARK 500    ASP A 106   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    GLU A 110   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    GLU A 110   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.2 DEGREES
REMARK 500    GLU A 110   CG  -  CD  -  OE2 ANGL. DEV. =  12.9 DEGREES
REMARK 500    VAL A 121   N   -  CA  -  CB  ANGL. DEV. = -18.3 DEGREES
REMARK 500    PHE A 125   CA  -  C   -  N   ANGL. DEV. =  13.5 DEGREES
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 134   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ARG A 134   NE  -  CZ  -  NH1 ANGL. DEV. =  -9.4 DEGREES
REMARK 500    LEU A 135   CB  -  CA  -  C   ANGL. DEV. =  11.7 DEGREES
REMARK 500    ASP A 137   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ARG A 139   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    ARG A 139   NE  -  CZ  -  NH2 ANGL. DEV. =  11.6 DEGREES
REMARK 500    TYR A 144   CB  -  CG  -  CD1 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    GLN A 149   O   -  C   -  N   ANGL. DEV. =  12.9 DEGREES
REMARK 500    GLN A 156   CB  -  CG  -  CD  ANGL. DEV. =  21.3 DEGREES
REMARK 500    GLN A 156   CG  -  CD  -  OE1 ANGL. DEV. =  17.7 DEGREES
REMARK 500    ARG A 159   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ASP A 160   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    GLY A 166   C   -  N   -  CA  ANGL. DEV. =  14.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     699 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    SER A  10      144.97     90.60
REMARK 500    VAL A  11      109.66     73.20
REMARK 500    PRO A  46      -62.01     -1.95
REMARK 500    SER A  62      -70.04   -150.13
REMARK 500    THR A  65     -168.16   -121.43
REMARK 500    THR A  75     -159.29   -113.99
REMARK 500    ARG A  86      146.00    168.92
REMARK 500    LYS A  94      109.21    -45.05
REMARK 500    ASP A  95       59.08      8.97
REMARK 500    ASP A 106      -23.06    -38.25
REMARK 500    SER A 119      -71.35    -74.36
REMARK 500    HIS A 153      -45.11   -134.01
REMARK 500    ARG A 167      153.60    155.95
REMARK 500    ASN A 207      -92.10   -121.29
REMARK 500    MET A 297      -21.06     86.12
REMARK 500    VAL A 331      -65.39     73.70
REMARK 500    ASP A 357       83.39   -160.62
REMARK 500    VAL A 369       59.89     30.76
REMARK 500    ASN A 442      -27.14    -32.98
REMARK 500    GLU A 464        4.15    -69.53
REMARK 500    VAL A 472      -89.72   -110.49
REMARK 500    ASN S   8       66.07   -115.62
REMARK 500    TYR S  12       51.86   -140.47
REMARK 500    GLU S  13     -139.12     51.43
REMARK 500    LEU S  15      -16.55     79.30
REMARK 500    SER S  16        7.99    -65.51
REMARK 500    ASP S  20      120.27    -34.46
REMARK 500    LYS S  35      -36.74    -33.62
REMARK 500    LYS S  71     -119.30     52.37
REMARK 500    ALA S  93      -55.99    101.45
REMARK 500    ASN S 106       -9.80    -57.78
REMARK 500    SER S 114      133.61   -173.20
REMARK 500    TYR S 118      121.14   -170.88
REMARK 500    SER B  10      145.86     99.23
REMARK 500    VAL B  11      109.64     74.81
REMARK 500    LYS B  21      -41.57    -29.62
REMARK 500    PRO B  46      -67.06     -6.94
REMARK 500    GLU B  52      -63.39    -93.80
REMARK 500    SER B  62      -75.83   -144.86
REMARK 500    THR B  65     -166.36   -123.34
REMARK 500    THR B  75     -157.57   -117.27
REMARK 500    ARG B  86      144.39    166.87
REMARK 500    ASP B  95       65.67      6.43
REMARK 500    SER B 119      -72.44    -72.24
REMARK 500    LYS B 146       -6.65    -57.73
REMARK 500    ARG B 167      152.02    146.96
REMARK 500    LYS B 177      -72.34    -42.53
REMARK 500    ASN B 207      -94.00   -119.80
REMARK 500    MET B 212      119.47   -169.86
REMARK 500    TYR B 239      106.43    -54.83
REMARK 500
REMARK 500 THIS ENTRY HAS     141 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ARG A  86        24.0      L          L   OUTSIDE RANGE
REMARK 500    HIS A 153        24.5      L          L   OUTSIDE RANGE
REMARK 500    ILE A 155        23.4      L          L   OUTSIDE RANGE
REMARK 500    LYS A 334        24.7      L          L   OUTSIDE RANGE
REMARK 500    MET A 387        24.6      L          L   OUTSIDE RANGE
REMARK 500    GLN S   2        24.1      L          L   OUTSIDE RANGE
REMARK 500    ILE S   7        21.1      L          L   OUTSIDE RANGE
REMARK 500    ARG S 100        45.2      L          L   OUTSIDE RANGE
REMARK 500    ARG B  86        24.3      L          L   OUTSIDE RANGE
REMARK 500    LEU B 180        46.1      L          L   OUTSIDE RANGE
REMARK 500    LEU B 371        46.1      L          L   OUTSIDE RANGE
REMARK 500    GLN T   2        23.5      L          L   OUTSIDE RANGE
REMARK 500    ILE T   7        21.0      L          L   OUTSIDE RANGE
REMARK 500    ARG C  86        24.3      L          L   OUTSIDE RANGE
REMARK 500    LYS C 334        24.5      L          L   OUTSIDE RANGE
REMARK 500    ASP C 351        24.6      L          L   OUTSIDE RANGE
REMARK 500    GLN U   2        23.5      L          L   OUTSIDE RANGE
REMARK 500    ILE U   7        20.1      L          L   OUTSIDE RANGE
REMARK 500    PRO U  73        46.8      L          L   OUTSIDE RANGE
REMARK 500    ARG D  86        23.4      L          L   OUTSIDE RANGE
REMARK 500    ILE D 155        24.2      L          L   OUTSIDE RANGE
REMARK 500    LEU D 371        46.3      L          L   OUTSIDE RANGE
REMARK 500    GLN V   2        24.8      L          L   OUTSIDE RANGE
REMARK 500    ILE V   7        19.7      L          L   OUTSIDE RANGE
REMARK 500    PRO V 120        46.1      L          L   OUTSIDE RANGE
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 491  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 204   OE1
REMARK 620 2 CAP A 490   O2  155.5
REMARK 620 3 CAP A 490   O4  115.3  71.0
REMARK 620 4 CAP A 490   O7   99.8  55.9  88.2
REMARK 620 5 FMT A 492   O1  107.5  91.4 108.7 136.8
REMARK 620 6 FMT A 492   O2  132.3  71.9  59.7 125.8  49.2
REMARK 620 7 ASP A 203   OD1  72.8  93.6 158.2  70.2  86.5 131.3
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 491  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B 490   O2
REMARK 620 2 CAP B 490   O4   65.2
REMARK 620 3 CAP B 490   O7   59.2  88.5
REMARK 620 4 FMT B 492   O1   96.2 110.8 139.6
REMARK 620 5 FMT B 492   O2   67.5  65.6 126.6  46.7
REMARK 620 6 GLU B 204   OE1 159.4 106.6 103.2 104.4 128.1
REMARK 620 7 ASP B 203   OD1 103.7 159.5  71.0  86.8 128.0  77.6
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG C 491  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT C 492   O1
REMARK 620 2 FMT C 492   O2   58.9
REMARK 620 3 GLU C 204   OE1 105.0 124.8
REMARK 620 4 CAP C 490   O4  125.3  66.6 102.4
REMARK 620 5 CAP C 490   O7  141.8 137.0  90.1  83.4
REMARK 620 6 CAP C 490   O2  110.2  85.4 142.6  67.1  53.9
REMARK 620 7 ASP C 203   OD1  86.8 143.8  71.8 147.1  64.6  97.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG D 491  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP D 490   O4
REMARK 620 2 GLU D 204   OE1 113.6
REMARK 620 3 CAP D 490   O7   77.4  89.8
REMARK 620 4 FMT D 492   O2   63.6 145.8 120.4
REMARK 620 5 FMT D 492   O1  122.5 114.0 132.2  58.9
REMARK 620 6 CAP D 490   O2   61.0 140.2  50.5  71.1  98.2
REMARK 620 7 ASP D 203   OD1 140.1  68.3  62.7 137.7  87.4  91.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: catalytic site
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: catalytic site
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: catalytic site
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: catalytic site
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 492
DBREF  4RUB A    1   477  UNP    P00876   RBL_TOBAC        1    477
DBREF  4RUB S    1   123  UNP    P69249   RBS_TOBAC       58    180
DBREF  4RUB B    1   477  UNP    P00876   RBL_TOBAC        1    477
DBREF  4RUB T    1   123  UNP    P69249   RBS_TOBAC       58    180
DBREF  4RUB C    1   477  UNP    P00876   RBL_TOBAC        1    477
DBREF  4RUB U    1   123  UNP    P69249   RBS_TOBAC       58    180
DBREF  4RUB D    1   477  UNP    P00876   RBL_TOBAC        1    477
DBREF  4RUB V    1   123  UNP    P69249   RBS_TOBAC       58    180
SEQADV 4RUB GLY S   88  UNP  P69249    GLU   145 CONFLICT
SEQADV 4RUB GLY T   88  UNP  P69249    GLU   145 CONFLICT
SEQADV 4RUB GLY U   88  UNP  P69249    GLU   145 CONFLICT
SEQADV 4RUB GLY V   88  UNP  P69249    GLU   145 CONFLICT
SEQRES   1 A  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 A  477  LYS ALA GLY VAL LYS GLU TYR LYS LEU THR TYR TYR THR
SEQRES   3 A  477  PRO GLU TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 A  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 A  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 A  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 A  477  ARG TYR LYS GLY ARG CYS TYR ARG ILE GLU ARG VAL VAL
SEQRES   8 A  477  GLY GLU LYS ASP GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 A  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 A  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 A  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 A  477  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 A  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 A  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 A  477  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 A  477  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 A  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 A  477  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 A  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 A  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 A  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 A  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 A  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 A  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 A  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 A  477  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 A  477  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 A  477  ASP PHE VAL GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 A  477  THR GLN ASP TRP VAL SER LEU PRO GLY VAL LEU PRO VAL
SEQRES  30 A  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 A  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 A  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 A  477  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL LYS
SEQRES  34 A  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA GLN GLU GLY ASN
SEQRES  35 A  477  GLU ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 A  477  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE VAL PHE ASN
SEQRES  37 A  477  PHE ALA ALA VAL ASP VAL LEU ASP LYS
SEQRES   1 S  123  MET GLN VAL TRP PRO PRO ILE ASN LYS LYS LYS TYR GLU
SEQRES   2 S  123  THR LEU SER TYR LEU PRO ASP LEU SER GLN GLU GLN LEU
SEQRES   3 S  123  LEU SER GLU VAL GLU TYR LEU LEU LYS ASN GLY TRP VAL
SEQRES   4 S  123  PRO CYS LEU GLU PHE GLU THR GLU HIS GLY PHE VAL TYR
SEQRES   5 S  123  ARG GLU ASN ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 S  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 S  123  ASP ALA THR GLN VAL LEU ALA GLU VAL GLY GLU ALA LYS
SEQRES   8 S  123  LYS ALA TYR PRO GLN ALA TRP ILE ARG ILE ILE GLY PHE
SEQRES   9 S  123  ASP ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 S  123  TYR LYS PRO GLU GLY TYR
SEQRES   1 B  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 B  477  LYS ALA GLY VAL LYS GLU TYR LYS LEU THR TYR TYR THR
SEQRES   3 B  477  PRO GLU TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 B  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 B  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 B  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 B  477  ARG TYR LYS GLY ARG CYS TYR ARG ILE GLU ARG VAL VAL
SEQRES   8 B  477  GLY GLU LYS ASP GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 B  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 B  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 B  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 B  477  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 B  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 B  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 B  477  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 B  477  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 B  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 B  477  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 B  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 B  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 B  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 B  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 B  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 B  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 B  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 B  477  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 B  477  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 B  477  ASP PHE VAL GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 B  477  THR GLN ASP TRP VAL SER LEU PRO GLY VAL LEU PRO VAL
SEQRES  30 B  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 B  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 B  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 B  477  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL LYS
SEQRES  34 B  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA GLN GLU GLY ASN
SEQRES  35 B  477  GLU ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 B  477  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE VAL PHE ASN
SEQRES  37 B  477  PHE ALA ALA VAL ASP VAL LEU ASP LYS
SEQRES   1 T  123  MET GLN VAL TRP PRO PRO ILE ASN LYS LYS LYS TYR GLU
SEQRES   2 T  123  THR LEU SER TYR LEU PRO ASP LEU SER GLN GLU GLN LEU
SEQRES   3 T  123  LEU SER GLU VAL GLU TYR LEU LEU LYS ASN GLY TRP VAL
SEQRES   4 T  123  PRO CYS LEU GLU PHE GLU THR GLU HIS GLY PHE VAL TYR
SEQRES   5 T  123  ARG GLU ASN ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 T  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 T  123  ASP ALA THR GLN VAL LEU ALA GLU VAL GLY GLU ALA LYS
SEQRES   8 T  123  LYS ALA TYR PRO GLN ALA TRP ILE ARG ILE ILE GLY PHE
SEQRES   9 T  123  ASP ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 T  123  TYR LYS PRO GLU GLY TYR
SEQRES   1 C  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 C  477  LYS ALA GLY VAL LYS GLU TYR LYS LEU THR TYR TYR THR
SEQRES   3 C  477  PRO GLU TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 C  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 C  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 C  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 C  477  ARG TYR LYS GLY ARG CYS TYR ARG ILE GLU ARG VAL VAL
SEQRES   8 C  477  GLY GLU LYS ASP GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 C  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 C  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 C  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 C  477  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 C  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 C  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 C  477  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 C  477  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 C  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 C  477  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 C  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 C  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 C  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 C  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 C  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 C  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 C  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 C  477  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 C  477  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 C  477  ASP PHE VAL GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 C  477  THR GLN ASP TRP VAL SER LEU PRO GLY VAL LEU PRO VAL
SEQRES  30 C  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 C  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 C  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 C  477  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL LYS
SEQRES  34 C  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA GLN GLU GLY ASN
SEQRES  35 C  477  GLU ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 C  477  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE VAL PHE ASN
SEQRES  37 C  477  PHE ALA ALA VAL ASP VAL LEU ASP LYS
SEQRES   1 U  123  MET GLN VAL TRP PRO PRO ILE ASN LYS LYS LYS TYR GLU
SEQRES   2 U  123  THR LEU SER TYR LEU PRO ASP LEU SER GLN GLU GLN LEU
SEQRES   3 U  123  LEU SER GLU VAL GLU TYR LEU LEU LYS ASN GLY TRP VAL
SEQRES   4 U  123  PRO CYS LEU GLU PHE GLU THR GLU HIS GLY PHE VAL TYR
SEQRES   5 U  123  ARG GLU ASN ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 U  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 U  123  ASP ALA THR GLN VAL LEU ALA GLU VAL GLY GLU ALA LYS
SEQRES   8 U  123  LYS ALA TYR PRO GLN ALA TRP ILE ARG ILE ILE GLY PHE
SEQRES   9 U  123  ASP ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 U  123  TYR LYS PRO GLU GLY TYR
SEQRES   1 D  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 D  477  LYS ALA GLY VAL LYS GLU TYR LYS LEU THR TYR TYR THR
SEQRES   3 D  477  PRO GLU TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 D  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 D  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 D  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 D  477  ARG TYR LYS GLY ARG CYS TYR ARG ILE GLU ARG VAL VAL
SEQRES   8 D  477  GLY GLU LYS ASP GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 D  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 D  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 D  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 D  477  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 D  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 D  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 D  477  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 D  477  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 D  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 D  477  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 D  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 D  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 D  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 D  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 D  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 D  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 D  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 D  477  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 D  477  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 D  477  ASP PHE VAL GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 D  477  THR GLN ASP TRP VAL SER LEU PRO GLY VAL LEU PRO VAL
SEQRES  30 D  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 D  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 D  477  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 D  477  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL LYS
SEQRES  34 D  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA GLN GLU GLY ASN
SEQRES  35 D  477  GLU ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 D  477  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE VAL PHE ASN
SEQRES  37 D  477  PHE ALA ALA VAL ASP VAL LEU ASP LYS
SEQRES   1 V  123  MET GLN VAL TRP PRO PRO ILE ASN LYS LYS LYS TYR GLU
SEQRES   2 V  123  THR LEU SER TYR LEU PRO ASP LEU SER GLN GLU GLN LEU
SEQRES   3 V  123  LEU SER GLU VAL GLU TYR LEU LEU LYS ASN GLY TRP VAL
SEQRES   4 V  123  PRO CYS LEU GLU PHE GLU THR GLU HIS GLY PHE VAL TYR
SEQRES   5 V  123  ARG GLU ASN ASN LYS SER PRO GLY TYR TYR ASP GLY ARG
SEQRES   6 V  123  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS THR
SEQRES   7 V  123  ASP ALA THR GLN VAL LEU ALA GLU VAL GLY GLU ALA LYS
SEQRES   8 V  123  LYS ALA TYR PRO GLN ALA TRP ILE ARG ILE ILE GLY PHE
SEQRES   9 V  123  ASP ASN VAL ARG GLN VAL GLN CYS ILE SER PHE ILE ALA
SEQRES  10 V  123  TYR LYS PRO GLU GLY TYR
HET     MG  A 491       1
HET     MG  B 491       1
HET     MG  C 491       1
HET     MG  D 491       1
HET    CAP  A 490      21
HET    CAP  B 490      21
HET    CAP  C 490      21
HET    CAP  D 490      21
HET    FMT  A 492       3
HET    FMT  B 492       3
HET    FMT  C 492       3
HET    FMT  D 492       3
HETNAM      MG MAGNESIUM ION
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM     FMT FORMIC ACID
FORMUL   9   MG    4(MG 2+)
FORMUL  13  CAP    4(C6 H14 O13 P2)
FORMUL  17  FMT    4(C H2 O2)
HELIX    1  N1 PRO A   50  ALA A   59  1                                  10
HELIX    2  N2 VAL A  113  VAL A  121  1                                   9
HELIX    3  N3 PRO A  142  VAL A  145  1                                   4
HELIX    4  N4 ILE A  155  LEU A  162  1                                   8
HELIX    5  B1 ALA A  182  ARG A  194  1                                  13
HELIX    6  B2 TRP A  214  THR A  232  1                                  19
HELIX    7  B3 CYS A  247  LEU A  260  1                                  14
HELIX    8 A4A TYR A  269  GLY A  272  1                                   4
HELIX    9 A4B PHE A  274  ASN A  287  1                                  14
HELIX   10 A5A HIS A  298  ASP A  302  1                                   5
HELIX   11 A5B PHE A  311  SER A  321  1                                  11
HELIX   12  B6 GLU A  336  ARG A  350  1                                  15
HELIX   13  B7 MET A  387  PHE A  394  1                                   8
HELIX   14  B8 ASN A  413  ASN A  432  1                                  20
HELIX   15  C1 LEU A  437  TRP A  451  1                                  15
HELIX   16  C2 PRO A  453  VAL A  466  1                                  14
HELIX   17  S1 GLN S   23  LYS S   35  1                                  13
HELIX   18  S2 ALA S   80  ALA S   93  1                                  14
HELIX   19  N1 PRO B   50  ALA B   59  1                                  10
HELIX   20  N2 VAL B  113  VAL B  121  1                                   9
HELIX   21  N3 PRO B  142  VAL B  145  1                                   4
HELIX   22  N4 ILE B  155  LEU B  162  1                                   8
HELIX   23  B1 ALA B  182  ARG B  194  1                                  13
HELIX   24  B2 TRP B  214  THR B  232  1                                  19
HELIX   25  B3 CYS B  247  LEU B  260  1                                  14
HELIX   26 B4A TYR B  269  GLY B  272  1                                   4
HELIX   27 B4B PHE B  274  ASN B  287  1                                  14
HELIX   28 B5A HIS B  298  ASP B  302  1                                   5
HELIX   29 B5B PHE B  311  SER B  321  1                                  11
HELIX   30  B6 GLU B  336  ARG B  350  1                                  15
HELIX   31  B7 MET B  387  PHE B  394  1                                   8
HELIX   32  B8 ASN B  413  ASN B  432  1                                  20
HELIX   33  C1 LEU B  437  TRP B  451  1                                  15
HELIX   34  C2 PRO B  453  VAL B  466  1                                  14
HELIX   35  S1 GLN T   23  LYS T   35  1                                  13
HELIX   36  S2 ALA T   80  ALA T   93  1                                  14
HELIX   37  N1 PRO C   50  ALA C   59  1                                  10
HELIX   38  N2 VAL C  113  VAL C  121  1                                   9
HELIX   39  N3 PRO C  142  VAL C  145  1                                   4
HELIX   40  N4 ILE C  155  LEU C  162  1                                   8
HELIX   41  B1 ALA C  182  ARG C  194  1                                  13
HELIX   42  B2 TRP C  214  THR C  232  1                                  19
HELIX   43  B3 CYS C  247  LEU C  260  1                                  14
HELIX   44 C4A TYR C  269  GLY C  272  1                                   4
HELIX   45 C4B PHE C  274  ASN C  287  1                                  14
HELIX   46 C5A HIS C  298  ASP C  302  1                                   5
HELIX   47 C5B PHE C  311  SER C  321  1                                  11
HELIX   48  B6 GLU C  336  ARG C  350  1                                  15
HELIX   49  B7 MET C  387  PHE C  394  1                                   8
HELIX   50  B8 ASN C  413  ASN C  432  1                                  20
HELIX   51  C1 LEU C  437  TRP C  451  1                                  15
HELIX   52  C2 PRO C  453  VAL C  466  1                                  14
HELIX   53  S1 GLN U   23  LYS U   35  1                                  13
HELIX   54  S2 ALA U   80  ALA U   93  1                                  14
HELIX   55  N1 PRO D   50  ALA D   59  1                                  10
HELIX   56  N2 VAL D  113  VAL D  121  1                                   9
HELIX   57  N3 PRO D  142  VAL D  145  1                                   4
HELIX   58  N4 ILE D  155  LEU D  162  1                                   8
HELIX   59  B1 ALA D  182  ARG D  194  1                                  13
HELIX   60  B2 TRP D  214  THR D  232  1                                  19
HELIX   61  B3 CYS D  247  LEU D  260  1                                  14
HELIX   62 D4A TYR D  269  GLY D  272  1                                   4
HELIX   63 D4B PHE D  274  ASN D  287  1                                  14
HELIX   64 D5A HIS D  298  ASP D  302  1                                   5
HELIX   65 D5B PHE D  311  SER D  321  1                                  11
HELIX   66  B6 GLU D  336  ARG D  350  1                                  15
HELIX   67  B7 MET D  387  PHE D  394  1                                   8
HELIX   68  B8 ASN D  413  ASN D  432  1                                  20
HELIX   69  C1 LEU D  437  TRP D  451  1                                  15
HELIX   70  C2 PRO D  453  VAL D  466  1                                  14
HELIX   71  S1 GLN V   23  LYS V   35  1                                  13
HELIX   72  S2 ALA V   80  ALA V   93  1                                  14
SHEET    1  NA 4 ILE A  36  PRO A  44  0
SHEET    2  NA 4 ARG A  83  ARG A  89  1
SHEET    3  NA 4 TYR A  97  TYR A 103 -1
SHEET    4  NA 4 LEU A 130  ARG A 139  1
SHEET    1  SA 4 VAL S  39  GLU S  45  0
SHEET    2  SA 4 THR S  68  TRP S  70 -1
SHEET    3  SA 4 TRP S  98  ASP S 105  1
SHEET    4  SA 4 VAL S 110  TYR S 118 -1
SHEET    1  NB 4 ILE B  36  PRO B  44  0
SHEET    2  NB 4 ARG B  83  ARG B  89  1
SHEET    3  NB 4 TYR B  97  TYR B 103 -1
SHEET    4  NB 4 LEU B 130  ARG B 139  1
SHEET    1  ST 4 VAL T  39  GLU T  45  0
SHEET    2  ST 4 THR T  68  TRP T  70 -1
SHEET    3  ST 4 TRP T  98  ASP T 105  1
SHEET    4  ST 4 VAL T 110  TYR T 118 -1
SHEET    1  NC 4 ILE C  36  PRO C  44  0
SHEET    2  NC 4 ARG C  83  ARG C  89  1
SHEET    3  NC 4 TYR C  97  TYR C 103 -1
SHEET    4  NC 4 LEU C 130  ARG C 139  1
SHEET    1  SU 4 VAL U  39  GLU U  45  0
SHEET    2  SU 4 THR U  68  TRP U  70 -1
SHEET    3  SU 4 TRP U  98  ASP U 105  1
SHEET    4  SU 4 VAL U 110  TYR U 118 -1
SHEET    1  ND 4 ILE D  36  PRO D  44  0
SHEET    2  ND 4 ARG D  83  ARG D  89  1
SHEET    3  ND 4 TYR D  97  TYR D 103 -1
SHEET    4  ND 4 LEU D 130  ARG D 139  1
SHEET    1  SV 4 VAL V  39  GLU V  45  0
SHEET    2  SV 4 THR V  68  TRP V  70 -1
SHEET    3  SV 4 TRP V  98  ASP V 105  1
SHEET    4  SV 4 VAL V 110  TYR V 118 -1
SSBOND   1 CYS A  247    CYS D  247                          1555   1555  2.02
SSBOND   2 CYS A  449    CYS A  459                          1555   1555  2.37
SSBOND   3 CYS B  247    CYS C  247                          1555   1555  1.76
SSBOND   4 CYS B  449    CYS B  459                          1555   1555  2.23
SSBOND   5 CYS C  449    CYS C  459                          1555   1555  2.02
SSBOND   6 CYS D  449    CYS D  459                          1555   1555  2.15
LINK         NZ  LYS A 201                 C   FMT A 492     1555   1555  1.24
LINK         NZ  LYS B 201                 C   FMT B 492     1555   1555  1.27
LINK         NZ  LYS C 201                 C   FMT C 492     1555   1555  1.29
LINK         NZ  LYS D 201                 C   FMT D 492     1555   1555  1.28
LINK        MG    MG A 491                 OE1 GLU A 204     1555   1555  1.86
LINK        MG    MG A 491                 O2  CAP A 490     1555   1555  2.33
LINK        MG    MG A 491                 O4  CAP A 490     1555   1555  2.11
LINK        MG    MG A 491                 O7  CAP A 490     1555   1555  2.17
LINK        MG    MG A 491                 O1  FMT A 492     1555   1555  2.28
LINK        MG    MG A 491                 O2  FMT A 492     1555   1555  2.54
LINK        MG    MG A 491                 OD1 ASP A 203     1555   1555  2.27
LINK        MG    MG B 491                 O2  CAP B 490     1555   1555  2.16
LINK        MG    MG B 491                 O4  CAP B 490     1555   1555  2.05
LINK        MG    MG B 491                 O7  CAP B 490     1555   1555  2.16
LINK        MG    MG B 491                 O1  FMT B 492     1555   1555  2.50
LINK        MG    MG B 491                 O2  FMT B 492     1555   1555  2.91
LINK        MG    MG B 491                 OE1 GLU B 204     1555   1555  1.88
LINK        MG    MG B 491                 OD1 ASP B 203     1555   1555  2.20
LINK        MG    MG C 491                 O1  FMT C 492     1555   1555  2.23
LINK        MG    MG C 491                 O2  FMT C 492     1555   1555  2.64
LINK        MG    MG C 491                 OE1 GLU C 204     1555   1555  2.08
LINK        MG    MG C 491                 O4  CAP C 490     1555   1555  2.10
LINK        MG    MG C 491                 O7  CAP C 490     1555   1555  2.49
LINK        MG    MG C 491                 O2  CAP C 490     1555   1555  2.10
LINK        MG    MG C 491                 OD1 ASP C 203     1555   1555  2.43
LINK         O4  CAP D 490                MG    MG D 491     1555   1555  2.05
LINK        MG    MG D 491                 OE1 GLU D 204     1555   1555  1.78
LINK        MG    MG D 491                 O7  CAP D 490     1555   1555  2.68
LINK        MG    MG D 491                 O2  FMT D 492     1555   1555  2.50
LINK        MG    MG D 491                 O1  FMT D 492     1555   1555  2.30
LINK        MG    MG D 491                 O2  CAP D 490     1555   1555  2.49
LINK        MG    MG D 491                 OD1 ASP D 203     1555   1555  2.44
CISPEP   1 LYS A  175    PRO A  176          0        -1.04
CISPEP   2 LYS B  175    PRO B  176          0         0.41
CISPEP   3 LYS C  175    PRO C  176          0        -0.59
CISPEP   4 LYS D  175    PRO D  176          0        -1.49
SITE     1 CTA 13 LYS A 175  LYS A 177  LYS A 201  ASP A 203
SITE     2 CTA 13 GLU A 204  HIS A 294  ARG A 295  HIS A 298
SITE     3 CTA 13 HIS A 327  SER A 379  FMT A 492  CAP A 490
SITE     4 CTA 13  MG A 491
SITE     1 CTB 13 LYS B 175  LYS B 177  LYS B 201  ASP B 203
SITE     2 CTB 13 GLU B 204  HIS B 294  ARG B 295  HIS B 298
SITE     3 CTB 13 HIS B 327  SER B 379  FMT B 492  CAP B 490
SITE     4 CTB 13  MG B 491
SITE     1 CTC 13 LYS C 175  LYS C 177  LYS C 201  ASP C 203
SITE     2 CTC 13 GLU C 204  HIS C 294  ARG C 295  HIS C 298
SITE     3 CTC 13 HIS C 327  SER C 379  FMT C 492  CAP C 490
SITE     4 CTC 13  MG C 491
SITE     1 CTD 13 LYS D 175  LYS D 177  LYS D 201  ASP D 203
SITE     2 CTD 13 GLU D 204  HIS D 294  ARG D 295  HIS D 298
SITE     3 CTD 13 HIS D 327  SER D 379  FMT D 492  CAP D 490
SITE     4 CTD 13  MG D 491
SITE     1 AC1  5 ASP A 203  GLU A 204  HIS A 294  CAP A 490
SITE     2 AC1  5 FMT A 492
SITE     1 AC2  5 ASP B 203  GLU B 204  HIS B 294  CAP B 490
SITE     2 AC2  5 FMT B 492
SITE     1 AC3  5 ASP C 203  GLU C 204  HIS C 294  CAP C 490
SITE     2 AC3  5 FMT C 492
SITE     1 AC4  5 ASP D 203  GLU D 204  HIS D 294  CAP D 490
SITE     2 AC4  5 FMT D 492
SITE     1 AC5 19 THR A 173  LYS A 175  ASP A 203  GLU A 204
SITE     2 AC5 19 HIS A 294  ARG A 295  HIS A 327  LYS A 334
SITE     3 AC5 19 LEU A 335  SER A 379  GLY A 380  GLY A 381
SITE     4 AC5 19 GLY A 403  GLY A 404   MG A 491  FMT A 492
SITE     5 AC5 19 THR D  65  TRP D  66  ASN D 123
SITE     1 AC6 19 THR B 173  LYS B 175  ASP B 203  GLU B 204
SITE     2 AC6 19 HIS B 294  ARG B 295  HIS B 327  LYS B 334
SITE     3 AC6 19 LEU B 335  SER B 379  GLY B 380  GLY B 381
SITE     4 AC6 19 GLY B 403  GLY B 404   MG B 491  FMT B 492
SITE     5 AC6 19 THR C  65  TRP C  66  ASN C 123
SITE     1 AC7 19 THR B  65  ASN B 123  THR C 173  LYS C 175
SITE     2 AC7 19 LYS C 177  ASP C 203  GLU C 204  HIS C 294
SITE     3 AC7 19 ARG C 295  HIS C 327  LYS C 334  LEU C 335
SITE     4 AC7 19 SER C 379  GLY C 380  GLY C 381  GLY C 403
SITE     5 AC7 19 GLY C 404   MG C 491  FMT C 492
SITE     1 AC8 19 THR A  65  TRP A  66  ASN A 123  THR D 173
SITE     2 AC8 19 LYS D 175  ASP D 203  GLU D 204  HIS D 294
SITE     3 AC8 19 ARG D 295  HIS D 327  LYS D 334  LEU D 335
SITE     4 AC8 19 SER D 379  GLY D 380  GLY D 381  GLY D 403
SITE     5 AC8 19 GLY D 404   MG D 491  FMT D 492
SITE     1 AC9  9 THR A 173  LYS A 201  ASP A 202  ASP A 203
SITE     2 AC9  9 GLU A 204  HIS A 294  HIS A 327  CAP A 490
SITE     3 AC9  9  MG A 491
SITE     1 BC1  9 THR B 173  LYS B 201  ASP B 202  ASP B 203
SITE     2 BC1  9 GLU B 204  HIS B 294  HIS B 327  CAP B 490
SITE     3 BC1  9  MG B 491
SITE     1 BC2  9 THR C 173  LYS C 201  ASP C 202  ASP C 203
SITE     2 BC2  9 GLU C 204  HIS C 294  HIS C 327  CAP C 490
SITE     3 BC2  9  MG C 491
SITE     1 BC3  9 THR D 173  LYS D 201  ASP D 202  ASP D 203
SITE     2 BC3  9 GLU D 204  HIS D 294  HIS D 327  CAP D 490
SITE     3 BC3  9  MG D 491
CRYST1  204.600  204.600  117.400  90.00  90.00 120.00 P 31 2 1     24
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      0.004888  0.002822  0.000000        0.00000
SCALE2      0.000000  0.005644  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008518        0.00000
MTRIX1   1 -1.000000  0.000000  0.000000      154.00000    1
MTRIX2   1  0.000000 -0.813100  0.582100      -22.78000    1
MTRIX3   1  0.000000  0.582100  0.813100        7.31000    1
MTRIX1   2 -1.000000  0.000000  0.000000      154.00000    1
MTRIX2   2  0.000000 -0.582100 -0.813100       31.82000    1
MTRIX3   2  0.000000 -0.813100  0.582100       16.36000    1
      
PROCHECK
Go to PROCHECK summary
 References