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PDBsum entry 1rld

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Top Page protein Protein-protein interface(s) links
Lyase(carbon-carbon) PDB id
1rld
Jmol
Contents
Protein chains
441 a.a. *
123 a.a. *
* Residue conservation analysis
HEADER    LYASE(CARBON-CARBON)                    10-DEC-93   1RLD
TITLE     SOLID-STATE PHASE TRANSITION IN THE CRYSTAL STRUCTURE OF RIBULOSE 1,5-
TITLE    2 BIPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE
COMPND   3 CHAIN);
COMPND   4 CHAIN: A, B;
COMPND   5 EC: 4.1.1.39;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL
COMPND   9 CHAIN);
COMPND  10 CHAIN: S, T;
COMPND  11 EC: 4.1.1.39;
COMPND  12 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    K.Y.J.ZHANG,D.EISENBERG
REVDAT   3   13-JUL-11 1RLD    1       VERSN
REVDAT   2   24-FEB-09 1RLD    1       VERSN
REVDAT   1   30-APR-94 1RLD    0
JRNL        AUTH   K.Y.ZHANG,D.EISENBERG
JRNL        TITL   SOLID-STATE PHASE TRANSITION IN THE CRYSTAL STRUCTURE OF
JRNL        TITL 2 RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   258 1994
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   15299436
JRNL        DOI    10.1107/S090744499301306X
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   P.M.G.CURMI,D.CASCIO,R.M.SWEET,D.EISENBERG,H.SCHREUDER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE UNACTIVATED FORM OF
REMARK   1  TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM
REMARK   1  TITL 3 TOBACCO REFINED AT 2.0 ANGSTROMS RESOLUTION
REMARK   1  REF    J.BIOL.CHEM.                  V. 267 16980 1992
REMARK   1  REFN                   ISSN 0021-9258
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.EISENBERG
REMARK   1  TITL   TERTIARY STRUCTURE OF PLANT RUBISCO: DOMAIN AND THEIR
REMARK   1  TITL 2 CONTACTS
REMARK   1  REF    SCIENCE                       V. 244    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 RUBISCO
REMARK   1  REF    NATURE                        V. 329   354 1987
REMARK   1  REFN                   ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 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 SET) : 0.211
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   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 8970
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
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  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.018
REMARK   3   BOND ANGLES            (DEGREES) : 3.83
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  RESIDUES 64 - 68 ARE COMPLETELY DISORDERED.  RESIDUES
REMARK   3  90 - 96, 330 - 340 AND 604 - 610 HAVE VERY HIGH TEMPERATURE
REMARK   3  FACTORS.
REMARK   4
REMARK   4 1RLD 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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   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       76.50500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       76.50500
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.72500
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       76.50500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       76.50500
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.72500
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       76.50500
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       76.50500
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       56.72500
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       76.50500
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       76.50500
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       56.72500
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 TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAINS B AND T WHEN
REMARK 300 APPLIED TO CHAINS A AND S, RESPECTIVELY.
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: 88990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 121000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -323.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S, B, T
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        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000
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        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A    64
REMARK 465     THR A    65
REMARK 465     TRP A    66
REMARK 465     THR A    67
REMARK 465     THR A    68
REMARK 465     GLY B    64
REMARK 465     THR B    65
REMARK 465     TRP B    66
REMARK 465     THR B    67
REMARK 465     THR B    68
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    HIS A 153   NE2   HIS A 153   CD2    -0.067
REMARK 500    HIS A 238   NE2   HIS A 238   CD2    -0.092
REMARK 500    HIS A 292   NE2   HIS A 292   CD2    -0.075
REMARK 500    HIS A 294   NE2   HIS A 294   CD2    -0.068
REMARK 500    HIS A 298   NE2   HIS A 298   CD2    -0.086
REMARK 500    HIS A 310   NE2   HIS A 310   CD2    -0.067
REMARK 500    HIS A 325   NE2   HIS A 325   CD2    -0.068
REMARK 500    HIS A 386   NE2   HIS A 386   CD2    -0.080
REMARK 500    HIS S 548   NE2   HIS S 548   CD2    -0.072
REMARK 500    HIS B 238   NE2   HIS B 238   CD2    -0.102
REMARK 500    HIS B 267   NE2   HIS B 267   CD2    -0.068
REMARK 500    HIS B 292   NE2   HIS B 292   CD2    -0.068
REMARK 500    HIS B 310   NE2   HIS B 310   CD2    -0.070
REMARK 500    HIS B 325   NE2   HIS B 325   CD2    -0.067
REMARK 500    HIS B 327   NE2   HIS B 327   CD2    -0.075
REMARK 500    HIS B 409   NE2   HIS B 409   CD2    -0.069
REMARK 500    HIS T 548   NE2   HIS T 548   CD2    -0.073
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    LYS A  32   CA  -  CB  -  CG  ANGL. DEV. =  13.3 DEGREES
REMARK 500    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    VAL A  69   N   -  CA  -  C   ANGL. DEV. =  23.4 DEGREES
REMARK 500    TRP A  70   CA  -  CB  -  CG  ANGL. DEV. =  12.2 DEGREES
REMARK 500    TRP A  70   CB  -  CG  -  CD2 ANGL. DEV. =   8.9 DEGREES
REMARK 500    TRP A  70   CB  -  CG  -  CD1 ANGL. DEV. = -11.6 DEGREES
REMARK 500    TRP A  70   NE1 -  CE2 -  CZ2 ANGL. DEV. =  -8.6 DEGREES
REMARK 500    TRP A  70   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TRP A  70   CG  -  CD2 -  CE3 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    TYR A 144   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    TYR A 165   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 167   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    LEU A 180   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    TYR A 185   CB  -  CG  -  CD2 ANGL. DEV. =   4.1 DEGREES
REMARK 500    TYR A 185   CB  -  CG  -  CD1 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG A 187   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    TYR A 190   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ASP A 202   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    GLU A 204   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES
REMARK 500    VAL A 206   CG1 -  CB  -  CG2 ANGL. DEV. = -11.0 DEGREES
REMARK 500    ARG A 213   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    TRP A 214   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES
REMARK 500    ARG A 215   NE  -  CZ  -  NH1 ANGL. DEV. =   7.8 DEGREES
REMARK 500    ARG A 215   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    PHE A 218   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    LEU A 219   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    ARG A 253   CG  -  CD  -  NE  ANGL. DEV. = -14.3 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A 253   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 258   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    VAL A 262   CA  -  CB  -  CG2 ANGL. DEV. =   9.6 DEGREES
REMARK 500    TYR A 283   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    ARG A 319   CB  -  CG  -  CD  ANGL. DEV. =  16.2 DEGREES
REMARK 500    ARG A 319   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ARG A 358   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    TRP A 368   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A 368   CB  -  CG  -  CD1 ANGL. DEV. =  -8.5 DEGREES
REMARK 500    TRP A 368   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    VAL A 384   N   -  CA  -  C   ANGL. DEV. =  18.5 DEGREES
REMARK 500    VAL A 384   CA  -  C   -  O   ANGL. DEV. = -14.8 DEGREES
REMARK 500    TRP A 385   CA  -  CB  -  CG  ANGL. DEV. =  26.5 DEGREES
REMARK 500    TRP A 385   CB  -  CG  -  CD2 ANGL. DEV. =   9.5 DEGREES
REMARK 500    TRP A 385   CB  -  CG  -  CD1 ANGL. DEV. = -13.9 DEGREES
REMARK 500    TRP A 385   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.5 DEGREES
REMARK 500    TRP A 385   CG  -  CD2 -  CE3 ANGL. DEV. =   7.1 DEGREES
REMARK 500    VAL A 384   CA  -  C   -  N   ANGL. DEV. =  20.4 DEGREES
REMARK 500    TRP A 411   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     161 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  61      -34.26   -158.72
REMARK 500    TRP A  70      -82.27    129.43
REMARK 500    ASP A  72      -24.40    -32.84
REMARK 500    LYS A  94     -153.52    155.56
REMARK 500    ASP A 106       -7.99    -52.01
REMARK 500    ILE A 120      -72.55   -104.47
REMARK 500    PHE A 125        9.44    -59.42
REMARK 500    HIS A 153      -65.53   -137.10
REMARK 500    LYS A 177      -73.35    -63.37
REMARK 500    ASN A 207     -109.91   -126.77
REMARK 500    GLU A 223      -73.56    -50.84
REMARK 500    ASN A 241       94.10    -66.11
REMARK 500    ARG A 295       42.98   -100.10
REMARK 500    MET A 297       -7.94     80.78
REMARK 500    PHE A 311      -28.58    -35.84
REMARK 500    ASP A 357       89.27   -153.54
REMARK 500    VAL A 369       45.58     24.93
REMARK 500    SER A 370       30.66     75.88
REMARK 500    THR A 406      -69.99   -109.40
REMARK 500    PRO A 410      -53.86    -16.92
REMARK 500    GLU A 433       62.98   -103.74
REMARK 500    VAL A 466     -123.90    -89.42
REMARK 500    GLU S 513     -130.04     58.28
REMARK 500    HIS S 548      114.91    119.49
REMARK 500    GLU S 554      -54.73   -131.51
REMARK 500    ASN S 556      144.35   -177.14
REMARK 500    PRO S 559      107.23    -44.66
REMARK 500    LYS S 571     -119.11     55.68
REMARK 500    ALA S 597      154.53    -43.19
REMARK 500    SER S 614      104.79   -170.10
REMARK 500    SER B  61      -33.97   -158.79
REMARK 500    TRP B  70      -82.95    128.52
REMARK 500    ASP B  72      -24.64    -33.74
REMARK 500    LYS B  94     -153.30    155.37
REMARK 500    ASP B 106       -8.36    -51.14
REMARK 500    ILE B 120      -72.06   -104.80
REMARK 500    PHE B 125        9.43    -58.60
REMARK 500    ALA B 129       21.65    -74.63
REMARK 500    HIS B 153      -65.25   -136.79
REMARK 500    LYS B 177      -73.95    -63.51
REMARK 500    ASN B 207     -110.54   -127.87
REMARK 500    GLU B 223      -73.34    -49.87
REMARK 500    ASN B 241       93.23    -67.17
REMARK 500    ARG B 295       41.33   -100.21
REMARK 500    MET B 297       -9.70     82.05
REMARK 500    PHE B 311      -28.42    -35.53
REMARK 500    LEU B 314       -9.65    -55.12
REMARK 500    ASP B 357       89.87   -154.20
REMARK 500    VAL B 369       45.56     26.13
REMARK 500    SER B 370       30.49     75.22
REMARK 500
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A 239         0.08    SIDE CHAIN
REMARK 500    TYR A 283         0.07    SIDE CHAIN
REMARK 500    TYR B 239         0.07    SIDE CHAIN
REMARK 500    TYR B 283         0.07    SIDE CHAIN
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    VAL A  69        20.6      L          L   OUTSIDE RANGE
REMARK 500    ILE A 362        46.5      L          L   OUTSIDE RANGE
REMARK 500    VAL A 384        21.8      L          L   OUTSIDE RANGE
REMARK 500    TRP A 385        24.2      L          L   OUTSIDE RANGE
REMARK 500    GLU S 547        24.8      L          L   OUTSIDE RANGE
REMARK 500    VAL B  69        20.9      L          L   OUTSIDE RANGE
REMARK 500    ILE B 362        45.6      L          L   OUTSIDE RANGE
REMARK 500    VAL B 384        21.5      L          L   OUTSIDE RANGE
REMARK 500    TRP B 385        24.4      L          L   OUTSIDE RANGE
REMARK 500    GLU T 547        24.5      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE ADVISORY NOTICE:
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999      SWISS-PROT ENTRY NAME: RBL_TOBAC
REMARK 999
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE
REMARK 999        GLN    229            GLU     A    229
REMARK 999        GLU    377            VAL     A    377
REMARK 999        GLN    229            GLU     B    229
REMARK 999        GLU    377            VAL     B    377
DBREF  1RLD A   22   467  UNP    P00876   RBL_TOBAC       22    467
DBREF  1RLD S  501   623  UNP    P69249   RBS_TOBAC       58    180
DBREF  1RLD B   22   467  UNP    P00876   RBL_TOBAC       22    467
DBREF  1RLD T  501   623  UNP    P69249   RBS_TOBAC       58    180
SEQADV 1RLD GLU A  229  UNP  P00876    GLN   229 CONFLICT
SEQADV 1RLD VAL A  377  UNP  P00876    GLU   377 CONFLICT
SEQADV 1RLD GLU B  229  UNP  P00876    GLN   229 CONFLICT
SEQADV 1RLD VAL B  377  UNP  P00876    GLU   377 CONFLICT
SEQRES   1 A  446  LEU THR TYR TYR THR PRO GLU TYR GLN THR LYS ASP THR
SEQRES   2 A  446  ASP ILE LEU ALA ALA PHE ARG VAL THR PRO GLN PRO GLY
SEQRES   3 A  446  VAL PRO PRO GLU GLU ALA GLY ALA ALA VAL ALA ALA GLU
SEQRES   4 A  446  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP GLY
SEQRES   5 A  446  LEU THR SER LEU ASP ARG TYR LYS GLY ARG CYS TYR ARG
SEQRES   6 A  446  ILE GLU ARG VAL VAL GLY GLU LYS ASP GLN TYR ILE ALA
SEQRES   7 A  446  TYR VAL ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   8 A  446  VAL THR ASN MET PHE THR SER ILE VAL GLY ASN VAL PHE
SEQRES   9 A  446  GLY PHE LYS ALA LEU ARG ALA LEU ARG LEU GLU ASP LEU
SEQRES  10 A  446  ARG ILE PRO PRO ALA TYR VAL LYS THR PHE GLN GLY PRO
SEQRES  11 A  446  PRO HIS GLY ILE GLN VAL GLU ARG ASP LYS LEU ASN LYS
SEQRES  12 A  446  TYR GLY ARG PRO LEU LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  13 A  446  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  14 A  446  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  15 A  446  GLU ASN VAL ASN SER GLN PRO PHE MET ARG TRP ARG ASP
SEQRES  16 A  446  ARG PHE LEU PHE CYS ALA GLU ALA LEU TYR LYS ALA GLU
SEQRES  17 A  446  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN ALA
SEQRES  18 A  446  THR ALA GLY THR CYS GLU GLU MET ILE LYS ARG ALA VAL
SEQRES  19 A  446  PHE ALA ARG GLU LEU GLY VAL PRO ILE VAL MET HIS ASP
SEQRES  20 A  446  TYR LEU THR GLY GLY PHE THR ALA ASN THR SER LEU ALA
SEQRES  21 A  446  HIS TYR CYS ARG ASP ASN GLY LEU LEU LEU HIS ILE HIS
SEQRES  22 A  446  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN LYS ASN HIS
SEQRES  23 A  446  GLY ILE HIS PHE ARG VAL LEU ALA LYS ALA LEU ARG MET
SEQRES  24 A  446  SER GLY GLY ASP HIS ILE HIS SER GLY THR VAL VAL GLY
SEQRES  25 A  446  LYS LEU GLU GLY GLU ARG ASP ILE THR LEU GLY PHE VAL
SEQRES  26 A  446  ASP LEU LEU ARG ASP ASP PHE VAL GLU GLN ASP ARG SER
SEQRES  27 A  446  ARG GLY ILE TYR PHE THR GLN ASP TRP VAL SER LEU PRO
SEQRES  28 A  446  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  29 A  446  HIS MET PRO ALA LEU THR GLU ILE PHE GLY ASP ASP SER
SEQRES  30 A  446  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  31 A  446  GLY ASN ALA PRO GLY ALA VAL ALA ASN ARG VAL ALA LEU
SEQRES  32 A  446  GLU ALA CYS VAL LYS ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  33 A  446  ALA GLN GLU GLY ASN GLU ILE ILE ARG GLU ALA CYS LYS
SEQRES  34 A  446  TRP SER PRO GLU LEU ALA ALA ALA CYS GLU VAL TRP LYS
SEQRES  35 A  446  GLU ILE VAL PHE
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
SEQRES   1 B  446  LEU THR TYR TYR THR PRO GLU TYR GLN THR LYS ASP THR
SEQRES   2 B  446  ASP ILE LEU ALA ALA PHE ARG VAL THR PRO GLN PRO GLY
SEQRES   3 B  446  VAL PRO PRO GLU GLU ALA GLY ALA ALA VAL ALA ALA GLU
SEQRES   4 B  446  SER SER THR GLY THR TRP THR THR VAL TRP THR ASP GLY
SEQRES   5 B  446  LEU THR SER LEU ASP ARG TYR LYS GLY ARG CYS TYR ARG
SEQRES   6 B  446  ILE GLU ARG VAL VAL GLY GLU LYS ASP GLN TYR ILE ALA
SEQRES   7 B  446  TYR VAL ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES   8 B  446  VAL THR ASN MET PHE THR SER ILE VAL GLY ASN VAL PHE
SEQRES   9 B  446  GLY PHE LYS ALA LEU ARG ALA LEU ARG LEU GLU ASP LEU
SEQRES  10 B  446  ARG ILE PRO PRO ALA TYR VAL LYS THR PHE GLN GLY PRO
SEQRES  11 B  446  PRO HIS GLY ILE GLN VAL GLU ARG ASP LYS LEU ASN LYS
SEQRES  12 B  446  TYR GLY ARG PRO LEU LEU GLY CYS THR ILE LYS PRO LYS
SEQRES  13 B  446  LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES  14 B  446  GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES  15 B  446  GLU ASN VAL ASN SER GLN PRO PHE MET ARG TRP ARG ASP
SEQRES  16 B  446  ARG PHE LEU PHE CYS ALA GLU ALA LEU TYR LYS ALA GLU
SEQRES  17 B  446  ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN ALA
SEQRES  18 B  446  THR ALA GLY THR CYS GLU GLU MET ILE LYS ARG ALA VAL
SEQRES  19 B  446  PHE ALA ARG GLU LEU GLY VAL PRO ILE VAL MET HIS ASP
SEQRES  20 B  446  TYR LEU THR GLY GLY PHE THR ALA ASN THR SER LEU ALA
SEQRES  21 B  446  HIS TYR CYS ARG ASP ASN GLY LEU LEU LEU HIS ILE HIS
SEQRES  22 B  446  ARG ALA MET HIS ALA VAL ILE ASP ARG GLN LYS ASN HIS
SEQRES  23 B  446  GLY ILE HIS PHE ARG VAL LEU ALA LYS ALA LEU ARG MET
SEQRES  24 B  446  SER GLY GLY ASP HIS ILE HIS SER GLY THR VAL VAL GLY
SEQRES  25 B  446  LYS LEU GLU GLY GLU ARG ASP ILE THR LEU GLY PHE VAL
SEQRES  26 B  446  ASP LEU LEU ARG ASP ASP PHE VAL GLU GLN ASP ARG SER
SEQRES  27 B  446  ARG GLY ILE TYR PHE THR GLN ASP TRP VAL SER LEU PRO
SEQRES  28 B  446  GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES  29 B  446  HIS MET PRO ALA LEU THR GLU ILE PHE GLY ASP ASP SER
SEQRES  30 B  446  VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES  31 B  446  GLY ASN ALA PRO GLY ALA VAL ALA ASN ARG VAL ALA LEU
SEQRES  32 B  446  GLU ALA CYS VAL LYS ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES  33 B  446  ALA GLN GLU GLY ASN GLU ILE ILE ARG GLU ALA CYS LYS
SEQRES  34 B  446  TRP SER PRO GLU LEU ALA ALA ALA CYS GLU VAL TRP LYS
SEQRES  35 B  446  GLU ILE VAL PHE
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 GLU 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
HELIX    1  N1 PRO A   50  ALA A   59  1                                  10
HELIX    2  N2 VAL A  113  SER A  119  1                                   7
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 B4A TYR A  269  GLY A  272  1                                   4
HELIX    9 B4B PHE A  274  ASN A  287  1                                  14
HELIX   10 B5A HIS A  298  ASP A  302  1                                   5
HELIX   11 B5B PHE A  311  SER A  321  1                                  11
HELIX   12  B6 ARG A  339  ARG A  350  1                                  12
HELIX   13  B7 MET A  387  PHE A  394  1                                   8
HELIX   14 B7A GLY A  404  LEU A  407  1                                   4
HELIX   15  B8 ASN A  413  ASN A  432  1                                  20
HELIX   16  C1 LEU A  437  TRP A  451  1                                  15
HELIX   17  C2 PRO A  453  LYS A  463  1                                  11
HELIX   18  S1 GLN S  523  ASN S  536  1                                  14
HELIX   19  S2 ALA S  580  ALA S  593  1                                  14
HELIX   20  N1 PRO B   50  ALA B   59  1                                  10
HELIX   21  N2 VAL B  113  SER B  119  1                                   7
HELIX   22  N3 PRO B  142  VAL B  145  1                                   4
HELIX   23  N4 ILE B  155  LEU B  162  1                                   8
HELIX   24  B1 ALA B  182  ARG B  194  1                                  13
HELIX   25  B2 TRP B  214  THR B  232  1                                  19
HELIX   26  B3 CYS B  247  LEU B  260  1                                  14
HELIX   27 B4A TYR B  269  GLY B  272  1                                   4
HELIX   28 B4B PHE B  274  ASN B  287  1                                  14
HELIX   29 B5A HIS B  298  ASP B  302  1                                   5
HELIX   30 B5B PHE B  311  SER B  321  1                                  11
HELIX   31  B6 ARG B  339  ARG B  350  1                                  12
HELIX   32  B7 MET B  387  PHE B  394  1                                   8
HELIX   33 B7A GLY B  404  LEU B  407  1                                   4
HELIX   34  B8 ASN B  413  ASN B  432  1                                  20
HELIX   35  C1 LEU B  437  TRP B  451  1                                  15
HELIX   36  C2 PRO B  453  LYS B  463  1                                  11
HELIX   37  S1 GLN T  523  ASN T  536  1                                  14
HELIX   38  S2 ALA T  580  ALA T  593  1                                  14
SHEET    1 S1A 4 ASP A  35  PRO A  44  0
SHEET    2 S1A 4 ARG A  83  VAL A  90  1
SHEET    3 S1A 4 GLN A  96  PRO A 104 -1
SHEET    4 S1A 4 LEU A 130  ARG A 139  1
SHEET    1 S2A 8 LEU A 169  THR A 173  0
SHEET    2 S2A 8 PHE A 199  LYS A 201  1
SHEET    3 S2A 8 GLY A 237  ASN A 241  1
SHEET    4 S2A 8 ILE A 264  ASP A 268  1
SHEET    5 S2A 8 LEU A 290  HIS A 294  1
SHEET    6 S2A 8 HIS A 325  GLY A 329  1
SHEET    7 S2A 8 LEU A 375  SER A 379  1
SHEET    8 S2A 8 VAL A 399  PHE A 402  1
SHEET    1 S1B 4 ASP B  35  PRO B  44  0
SHEET    2 S1B 4 ARG B  83  VAL B  90  1
SHEET    3 S1B 4 GLN B  96  PRO B 104 -1
SHEET    4 S1B 4 LEU B 130  ARG B 139  1
SHEET    1 S2B 8 LEU B 169  THR B 173  0
SHEET    2 S2B 8 PHE B 199  LYS B 201  1
SHEET    3 S2B 8 GLY B 237  ASN B 241  1
SHEET    4 S2B 8 ILE B 264  ASP B 268  1
SHEET    5 S2B 8 LEU B 290  HIS B 294  1
SHEET    6 S2B 8 HIS B 325  GLY B 329  1
SHEET    7 S2B 8 LEU B 375  SER B 379  1
SHEET    8 S2B 8 VAL B 399  PHE B 402  1
SHEET    1 S1S 4 VAL S 539  GLU S 545  0
SHEET    2 S1S 4 THR S 568  TRP S 570 -1
SHEET    3 S1S 4 TRP S 598  ASP S 605  1
SHEET    4 S1S 4 VAL S 610  TYR S 618 -1
SHEET    1 S1T 4 VAL T 539  GLU T 545  0
SHEET    2 S1T 4 THR T 568  TRP T 570 -1
SHEET    3 S1T 4 TRP T 598  ASP T 605  1
SHEET    4 S1T 4 VAL T 610  TYR T 618 -1
SSBOND   1 CYS A  172    CYS A  192                          1555   1555  2.04
SSBOND   2 CYS A  247    CYS B  247                          1555   1555  1.91
SSBOND   3 CYS A  449    CYS A  459                          1555   1555  1.88
SSBOND   4 CYS B  172    CYS B  192                          1555   1555  2.02
SSBOND   5 CYS B  449    CYS B  459                          1555   1555  1.98
CISPEP   1 LYS A  175    PRO A  176          0         0.28
CISPEP   2 LYS B  175    PRO B  176          0        -0.28
SITE     1 CAT 10 LYS A 175  LYS A 201  LYS A 177  ASP A 203
SITE     2 CAT 10 GLU A 204  HIS A 294  HIS A 327  ARG A 295
SITE     3 CAT 10 HIS A 298  SER A 379
CRYST1  153.010  153.010  113.450  90.00  90.00  90.00 I 4          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      0.006536  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006536  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008814        0.00000
MTRIX1   1  0.133535 -0.991044  0.000337       -0.01860    1
MTRIX2   1 -0.991044 -0.133535 -0.000161       -0.00140    1
MTRIX3   1 -0.000115 -0.000355 -1.000000        0.03590    1
      
PROCHECK
Go to PROCHECK summary
 References