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PDBsum entry 3rub

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Top Page protein ligands Protein-protein interface(s) links
Lyase(carbon-carbon) PDB id
3rub
Jmol
Contents
Protein chains
441 a.a. *
123 a.a. *
Ligands
SO4 ×3
ASN
Waters ×216
* Residue conservation analysis
HEADER    LYASE(CARBON-CARBON)                    25-MAY-90   3RUB
TITLE     CRYSTAL STRUCTURE OF THE UNACTIVATED FORM OF RIBULOSE-1,5-BISPHOSPHATE
TITLE    2 CARBOXYLASE(SLASH)OXYGENASE FROM TOBACCO REFINED AT 2.0-ANGSTROMS
TITLE    3 RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, FORM III;
COMPND   3 CHAIN: L;
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 III;
COMPND   8 CHAIN: S;
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: TOBACCO;
SOURCE   4 ORGANISM_TAXID: 4097;
SOURCE   5 MOL_ID: 2
KEYWDS    LYASE(CARBON-CARBON)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.SCHREUDER,D.CASCIO,P.M.G.CURMI,M.S.CHAPMAN,S.W.SUH,D.S.EISENBERG
REVDAT   6   13-JUL-11 3RUB    1       VERSN
REVDAT   5   25-AUG-09 3RUB    1       SOURCE
REVDAT   4   24-FEB-09 3RUB    1       VERSN
REVDAT   3   01-APR-03 3RUB    1       JRNL
REVDAT   2   30-APR-94 3RUB    1       SOURCE
REVDAT   1   15-OCT-92 3RUB    0
JRNL        AUTH   P.M.CURMI,D.CASCIO,R.M.SWEET,D.EISENBERG,H.SCHREUDER
JRNL        TITL   CRYSTAL STRUCTURE OF THE UNACTIVATED FORM OF
JRNL        TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM TOBACCO
JRNL        TITL 3 REFINED AT 2.0-A RESOLUTION.
JRNL        REF    J.BIOL.CHEM.                  V. 267 16980 1992
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   1512238
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   H.SCHREUDER,P.M.G.CURMI,D.CASCIO,D.EISENBERG
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE INACTIVE FORM OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE
REMARK   1  TITL 3 (RUBIS/CO): DISULFIDE BONDS AND ACTIVE SITE REGION
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.S.CHAPMAN,S.W.SUH,P.M.G.CURMI,D.CASCIO,W.W.SMITH,
REMARK   1  AUTH 2 D.S.EISENBERG
REMARK   1  TITL   TERTIARY STRUCTURE OF PLANT RUBIS/CO: DOMAINS AND THEIR
REMARK   1  TITL 2 CONTACTS
REMARK   1  REF    SCIENCE                       V. 241    71 1988
REMARK   1  REFN                   ISSN 0036-8075
REMARK   1 REFERENCE 3
REMARK   1  AUTH   M.S.CHAPMAN,S.W.SUH,D.CASCIO,W.W.SMITH,D.EISENBERG
REMARK   1  TITL   SLIDING-LAYER CONFORMATIONAL CHANGE LIMITED BY THE
REMARK   1  TITL 2 QUATERNARY STRUCTURE OF PLANT RUBIS/CO
REMARK   1  REF    NATURE                        V. 329   354 1987
REMARK   1  REFN                   ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 43088
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) : 0.171
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) : 47792
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4484
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 216
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:
REMARK   3  RESIDUES 64-68 OF THE LARGE SUBUNIT ARE COMPLETELY
REMARK   3  DISORDERED.  NO COORDINATES ARE PRESENTED FOR THESE
REMARK   3  RESIDUES.
REMARK   3  RESIDUES 90 - 96 AND 330 - 340 OF THE LARGE SUBUNIT
REMARK   3  AND RESIDUES 104 - 110 OF THE SMALL SUBUNIT HAVE
REMARK   3  VERY HIGH TEMPERATURE FACTORS.
REMARK   4
REMARK   4 3RUB 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   (%): 56.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   -X,Y,-Z
REMARK 290       6555   X,-Y,-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       74.35000
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       68.75000
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       74.35000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       68.75000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       74.35000
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       68.75000
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       74.35000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       68.75000
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.35000
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       68.75000
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.35000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       68.75000
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       74.35000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       68.75000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       74.35000
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       74.35000
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       68.75000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 95280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 120450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -696.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, S
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      148.70000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      148.70000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      148.70000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      148.70000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000      148.70000
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000      137.50000
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000      148.70000
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      137.50000
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000      137.50000
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000      148.70000
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000      148.70000
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000      137.50000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH L 518  LIES ON A SPECIAL POSITION.
REMARK 375      HOH L 604  LIES ON A SPECIAL POSITION.
REMARK 375      HOH L 665  LIES ON A SPECIAL POSITION.
REMARK 375      HOH L 514  LIES ON A SPECIAL POSITION.
REMARK 375      HOH L 539  LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THERE ARE SALT BRIDGES BETWEEN THE FOLLOWING ATOMS AND
REMARK 400 SYMMETRY RELATED ATOMS.   (THE 'A' AND 'D' DENOTE ACCEPTOR
REMARK 400 AND DONOR RESPECTIVELY).
REMARK 400
REMARK 400      ATOM 1                     ATOM 2
REMARK 400 OE1 GLU L 109 (A)         NH1 ARG S  53 (D)
REMARK 400 OE1 GLU L 110 (A)         NH1 ARG L 213 (D)
REMARK 400 THE COORDINATES OF THIS SYMMETRY RELATED ATOM 2 CAN BE
REMARK 400 OBTAINED FROM THE COORDINATES IN THIS ENTRY BY THE
REMARK 400 FOLLOWING TRANSFORMATION:
REMARK 400
REMARK 400   0       1       0       0
REMARK 400   1       0       0   +   0
REMARK 400   0       0      -1     137.5
REMARK 400
REMARK 400      ATOM 1                     ATOM 2
REMARK 400 OE2 GLU L 110             NZ  LYS L 146
REMARK 400 THE COORDINATES OF THIS SYMMETRY RELATED ATOM 2 CAN BE
REMARK 400 OBTAINED FROM THE COORDINATES IN THIS ENTRY BY THE
REMARK 400 FOLLOWING TRANSFORMATION:
REMARK 400
REMARK 400  -1       0       0     148.7
REMARK 400   0       1       0   +   0
REMARK 400   0       0      -1     137.5
REMARK 400
REMARK 400      ATOM 1                     ATOM 2
REMARK 400 NZ  LYS L 161 (D)         OD1 ASP L 216 (A)
REMARK 400 NH1 ARG L 258 (D)         OE1 GLU L  59 (A)
REMARK 400 THE COORDINATES OF THIS SYMMETRY RELATED ATOM 2 CAN BE
REMARK 400 OBTAINED FROM THE COORDINATES IN THIS ENTRY BY THE
REMARK 400 FOLLOWING TRANSFORMATION:
REMARK 400
REMARK 400   0      -1       0     148.7
REMARK 400   1       0       0   +   0
REMARK 400   0       0       1       0
REMARK 400      ATOM 1                     ATOM 2
REMARK 400 NH1 ARG L 187 (D)         OE1 GLU S  43 (A)
REMARK 400 OE1 GLU L 223 (A)         NH2 ARG S  65 (D)
REMARK 400 NZ  LYS L 252 (D)         OD2 ASP L 286 (A)
REMARK 400 THE COORDINATES OF THIS SYMMETRY RELATED ATOM 2 CAN BE
REMARK 400 OBTAINED FROM THE COORDINATES IN THIS ENTRY BY THE
REMARK 400 FOLLOWING TRANSFORMATION:
REMARK 400
REMARK 400   1       0       0       0
REMARK 400   0      -1       0  +  148.7
REMARK 400   0       0       1       0
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 L     1
REMARK 465     SER L     2
REMARK 465     PRO L     3
REMARK 465     GLN L     4
REMARK 465     THR L     5
REMARK 465     GLU L     6
REMARK 465     THR L     7
REMARK 465     LYS L     8
REMARK 465     ALA L     9
REMARK 465     SER L    10
REMARK 465     VAL L    11
REMARK 465     GLY L    12
REMARK 465     PHE L    13
REMARK 465     LYS L    14
REMARK 465     ALA L    15
REMARK 465     GLY L    16
REMARK 465     VAL L    17
REMARK 465     LYS L    18
REMARK 465     GLU L    19
REMARK 465     TYR L    20
REMARK 465     LYS L    21
REMARK 465     GLY L    64
REMARK 465     THR L    65
REMARK 465     TRP L    66
REMARK 465     THR L    67
REMARK 465     THR L    68
REMARK 465     ASN L   468
REMARK 465     PHE L   469
REMARK 465     ALA L   470
REMARK 465     ALA L   471
REMARK 465     VAL L   472
REMARK 465     ASP L   473
REMARK 465     VAL L   474
REMARK 465     LEU L   475
REMARK 465     ASP L   476
REMARK 465     LYS L   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     MET L 405    CB   CG   SD   CE
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   C    PHE L   467     N    ASN L   493              1.24
REMARK 500   OD1  ASP S    79     OG1  THR S    81              2.12
REMARK 500   O    PHE L   467     N    ASN L   493              2.19
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   OG1  THR L    71     O    LYS L   175     7556     2.13
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    GLY L 322   N     GLY L 322   CA     -0.091
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    LEU L  22   CB  -  CA  -  C   ANGL. DEV. =  15.1 DEGREES
REMARK 500    LEU L  22   CA  -  CB  -  CG  ANGL. DEV. =  22.7 DEGREES
REMARK 500    GLN L  30   C   -  N   -  CA  ANGL. DEV. =  15.3 DEGREES
REMARK 500    ARG L  41   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG L  41   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG L  79   N   -  CA  -  CB  ANGL. DEV. =  10.9 DEGREES
REMARK 500    ARG L  79   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES
REMARK 500    ARG L  83   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    TYR L  85   CB  -  CG  -  CD1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG L  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG L  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    TYR L  97   CB  -  CG  -  CD1 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    MET L 116   CG  -  SD  -  CE  ANGL. DEV. =  10.7 DEGREES
REMARK 500    ARG L 134   CD  -  NE  -  CZ  ANGL. DEV. = -12.4 DEGREES
REMARK 500    ARG L 134   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES
REMARK 500    LEU L 133   O   -  C   -  N   ANGL. DEV. =  10.4 DEGREES
REMARK 500    ARG L 139   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG L 159   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    LEU L 180   N   -  CA  -  CB  ANGL. DEV. = -13.2 DEGREES
REMARK 500    TYR L 185   CB  -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES
REMARK 500    TYR L 185   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    CYS L 192   CB  -  CA  -  C   ANGL. DEV. =   7.8 DEGREES
REMARK 500    ASP L 198   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP L 203   CB  -  CG  -  OD2 ANGL. DEV. =  -9.4 DEGREES
REMARK 500    VAL L 206   CA  -  CB  -  CG2 ANGL. DEV. =  11.2 DEGREES
REMARK 500    ARG L 213   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG L 217   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ARG L 217   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG L 253   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG L 258   CA  -  CB  -  CG  ANGL. DEV. =  19.6 DEGREES
REMARK 500    ARG L 285   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP L 286   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ASP L 302   CB  -  CG  -  OD2 ANGL. DEV. =   8.2 DEGREES
REMARK 500    ARG L 312   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ARG L 312   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG L 339   CD  -  NE  -  CZ  ANGL. DEV. =  12.7 DEGREES
REMARK 500    ARG L 339   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ASP L 347   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG L 350   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ARG L 360   NE  -  CZ  -  NH1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    TYR L 363   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    HIS L 383   CA  -  CB  -  CG  ANGL. DEV. = -11.8 DEGREES
REMARK 500    ASP L 396   CB  -  CG  -  OD2 ANGL. DEV. =  -8.4 DEGREES
REMARK 500    GLN L 401   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES
REMARK 500    GLN L 401   CA  -  CB  -  CG  ANGL. DEV. =  19.8 DEGREES
REMARK 500    ARG L 421   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG L 421   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.9 DEGREES
REMARK 500    ARG L 435   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    GLU L 440   OE1 -  CD  -  OE2 ANGL. DEV. =   8.5 DEGREES
REMARK 500    SER L 452   N   -  CA  -  CB  ANGL. DEV. =   9.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      64 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    GLU L  60       32.10    -95.93
REMARK 500    SER L  62      -52.32   -147.86
REMARK 500    ARG L  86      134.12   -175.79
REMARK 500    LYS L  94      -89.02    -57.39
REMARK 500    ASP L  95       40.69    -93.11
REMARK 500    ALA L 129        1.36    -59.86
REMARK 500    HIS L 153      -55.15   -132.95
REMARK 500    ASN L 207      -93.11   -121.93
REMARK 500    MET L 212      105.74   -167.19
REMARK 500    MET L 297       -8.51     83.72
REMARK 500    VAL L 332      109.73    -47.10
REMARK 500    ASP L 357       92.24   -169.26
REMARK 500    VAL L 369       55.02     32.78
REMARK 500    THR L 406      -65.77    -95.87
REMARK 500    GLU S  13     -154.99     74.08
REMARK 500    GLU S  47      -60.31   -105.00
REMARK 500    LYS S  71     -131.18     57.85
REMARK 500    ALA S  80      -15.98    -48.10
REMARK 500    SER S 114      111.05   -174.09
REMARK 500    TYR S 118      136.47   -172.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     ASN L  493
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC RESIDUES
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ASN L 493
DBREF  3RUB L    1   477  UNP    P00876   RBL_TOBAC        1    477
DBREF  3RUB S    1   123  UNP    P69249   RBS_TOBAC       58    180
SEQADV 3RUB VAL L  377  UNP  P00876    GLU   377 CONFLICT
SEQADV 3RUB MET L  405  UNP  P00876    GLY   405 CONFLICT
SEQRES   1 L  477  MET SER PRO GLN THR GLU THR LYS ALA SER VAL GLY PHE
SEQRES   2 L  477  LYS ALA GLY VAL LYS GLU TYR LYS LEU THR TYR TYR THR
SEQRES   3 L  477  PRO GLU TYR GLN THR LYS ASP THR ASP ILE LEU ALA ALA
SEQRES   4 L  477  PHE ARG VAL THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES   5 L  477  ALA GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES   6 L  477  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES   7 L  477  ARG TYR LYS GLY ARG CYS TYR ARG ILE GLU ARG VAL VAL
SEQRES   8 L  477  GLY GLU LYS ASP GLN TYR ILE ALA TYR VAL ALA TYR PRO
SEQRES   9 L  477  LEU ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES  10 L  477  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES  11 L  477  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES  12 L  477  TYR VAL LYS THR PHE GLN GLY PRO PRO HIS GLY ILE GLN
SEQRES  13 L  477  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG PRO LEU
SEQRES  14 L  477  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES  15 L  477  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES  16 L  477  GLY LEU ASP PHE THR LYS ASP ASP GLU ASN VAL ASN SER
SEQRES  17 L  477  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE CYS
SEQRES  18 L  477  ALA GLU ALA LEU TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES  19 L  477  ILE LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES  20 L  477  GLU GLU MET ILE LYS ARG ALA VAL PHE ALA ARG GLU LEU
SEQRES  21 L  477  GLY VAL PRO ILE VAL MET HIS ASP TYR LEU THR GLY GLY
SEQRES  22 L  477  PHE THR ALA ASN THR SER LEU ALA HIS TYR CYS ARG ASP
SEQRES  23 L  477  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES  24 L  477  VAL ILE ASP ARG GLN LYS ASN HIS GLY ILE HIS PHE ARG
SEQRES  25 L  477  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES  26 L  477  ILE HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES  27 L  477  ARG ASP ILE THR LEU GLY PHE VAL ASP LEU LEU ARG ASP
SEQRES  28 L  477  ASP PHE VAL GLU GLN ASP ARG SER ARG GLY ILE TYR PHE
SEQRES  29 L  477  THR GLN ASP TRP VAL SER LEU PRO GLY VAL LEU PRO VAL
SEQRES  30 L  477  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES  31 L  477  THR GLU ILE PHE GLY ASP ASP SER VAL LEU GLN PHE GLY
SEQRES  32 L  477  GLY MET THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES  33 L  477  ALA VAL ALA ASN ARG VAL ALA LEU GLU ALA CYS VAL LYS
SEQRES  34 L  477  ALA ARG ASN GLU GLY ARG ASP LEU ALA GLN GLU GLY ASN
SEQRES  35 L  477  GLU ILE ILE ARG GLU ALA CYS LYS TRP SER PRO GLU LEU
SEQRES  36 L  477  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE VAL PHE ASN
SEQRES  37 L  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 GLU 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
HET    SO4  L 490       5
HET    SO4  L 491       5
HET    SO4  L 492       5
HET    ASN  L 493       1
HETNAM     SO4 SULFATE ION
HETNAM     ASN ASPARAGINE
FORMUL   3  SO4    3(O4 S 2-)
FORMUL   6  ASN    C4 H8 N2 O3
FORMUL   7  HOH   *216(H2 O)
HELIX    1  N1 PRO L   50  ALA L   59  1                                  10
HELIX    2  N2 VAL L  113  VAL L  121  1                                   9
HELIX    3  N3 PRO L  142  VAL L  145  1                                   4
HELIX    4  N4 ILE L  155  LEU L  162  1                                   8
HELIX    5  B1 ALA L  182  ARG L  194  1                                  13
HELIX    6  B2 TRP L  214  THR L  232  1                                  19
HELIX    7  B3 CYS L  247  LEU L  260  1                                  14
HELIX    8 B4A TYR L  269  GLY L  272  1                                   4
HELIX    9 B4B PHE L  274  ASN L  287  1                                  14
HELIX   10 B5A HIS L  298  ASP L  302  1                                   5
HELIX   11 B5B PHE L  311  SER L  321  1                                  11
HELIX   12  B6 GLU L  336  ARG L  350  1                                  15
HELIX   13  B7 MET L  387  PHE L  394  1                                   8
HELIX   14  B8 ASN L  413  ASN L  432  1                                  20
HELIX   15  C1 LEU L  437  TRP L  451  1                                  15
HELIX   16  C2 PRO L  453  VAL L  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
SHEET    1   N 4 ILE L  36  PRO L  44  0
SHEET    2   N 4 ARG L  83  ARG L  89  1
SHEET    3   N 4 TYR L  97  TYR L 103 -1
SHEET    4   N 4 LEU L 130  ARG L 139  1
SHEET    1   S 4 VAL S  39  GLU S  45  0
SHEET    2   S 4 THR S  68  TRP S  70 -1
SHEET    3   S 4 TRP S  98  ASP S 105  1
SHEET    4   S 4 VAL S 110  TYR S 118 -1
SSBOND   1 CYS L  172    CYS L  192                          1555   1555  2.13
SSBOND   2 CYS L  247    CYS L  247                          1555   7556  1.88
CISPEP   1 LYS L  175    PRO L  176          0         1.12
SITE     1 CAT 13 LYS L 175  LYS L 177  LYS L 201  ASP L 203
SITE     2 CAT 13 GLU L 204  HIS L 294  ARG L 295  HIS L 298
SITE     3 CAT 13 HIS L 327  SER L 379  SO4 L 490  SO4 L 491
SITE     4 CAT 13 SO4 L 492
SITE     1 AC1  6 GLY L 380  GLY L 381  GLY L 403  GLY L 404
SITE     2 AC1  6 HOH L 608  HOH L 668
SITE     1 AC2  4 ARG L 295  HIS L 298  GLY L 329  HOH L 636
SITE     1 AC3  5 ARG L 134  LYS L 305  HIS L 310  ILE L 341
SITE     2 AC3  5 HOH L 578
SITE     1 AC4  3 LYS L 463  GLU L 464  PHE L 467
CRYST1  148.700  148.700  137.500  90.00  90.00  90.00 I 4 2 2      16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.006725  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006725  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007273        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

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