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PDBsum entry 1bya

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Hydrolase(o-glycosyl) PDB id
1bya
Jmol
Contents
Protein chain
491 a.a.
Ligands
SO4
Waters ×320
HEADER    HYDROLASE(O-GLYCOSYL)                   25-JAN-94   1BYA
TITLE     CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH
TITLE    2 BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR
TITLE    3 APPARENT ROLE IN CATALYSIS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.2;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE   3 ORGANISM_COMMON: SOYBEAN;
SOURCE   4 ORGANISM_TAXID: 3847
KEYWDS    HYDROLASE(O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.MIKAMI,M.DEGANO,E.J.HEHRE,J.C.SACCHETTINI
REVDAT   3   24-FEB-09 1BYA    1       VERSN
REVDAT   2   01-APR-03 1BYA    1       JRNL
REVDAT   1   31-JUL-94 1BYA    0
JRNL        AUTH   B.MIKAMI,M.DEGANO,E.J.HEHRE,J.C.SACCHETTINI
JRNL        TITL   CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED
JRNL        TITL 2 WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE
JRNL        TITL 3 COMPONENTS AND THEIR APPARENT ROLES IN CATALYSIS.
JRNL        REF    BIOCHEMISTRY                  V.  33  7779 1994
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   8011643
JRNL        DOI    10.1021/BI00191A005
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   B.MIKAMI,E.J.HEHRE,M.SATO,Y.KATSUBE,M.HIROSE,
REMARK   1  AUTH 2 Y.MORITA,J.C.SACCHETTINI
REMARK   1  TITL   THE 2.0-ANGSTROMS RESOLUTION STRUCTURE OF SOYBEAN
REMARK   1  TITL 2 BETA-AMYLASE COMPLEXED WITH ALPHA-CYCLODEXTRIN
REMARK   1  REF    BIOCHEMISTRY                  V.  32  6836 1993
REMARK   1  REFN                   ISSN 0006-2960
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT, X-PLOR
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 45035
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169
REMARK   3   R VALUE            (WORKING SET) : 0.169
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  USING ALL DATA, NO SIGMA CUTOFF.
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            : 3929
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 320
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1BYA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
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       48.06667
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       96.13333
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       96.13333
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       48.06667
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ALA A     1
REMARK 465     THR A     2
REMARK 465     SER A     3
REMARK 465     ASP A     4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    PHE A   200     N    ARG A   202              1.82
REMARK 500   OE2  GLU A   178     OD1  ASN A   340              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    GLU A  30   CD    GLU A  30   OE1     0.083
REMARK 500    GLU A  37   CD    GLU A  37   OE2     0.106
REMARK 500    GLU A  60   CD    GLU A  60   OE2     0.072
REMARK 500    GLU A 116   CD    GLU A 116   OE1     0.084
REMARK 500    GLU A 152   CD    GLU A 152   OE2     0.070
REMARK 500    GLU A 163   CD    GLU A 163   OE2     0.105
REMARK 500    GLU A 170   CD    GLU A 170   OE1     0.082
REMARK 500    GLU A 178   CD    GLU A 178   OE1     0.117
REMARK 500    GLU A 205   CD    GLU A 205   OE1     0.075
REMARK 500    GLU A 228   CD    GLU A 228   OE1     0.067
REMARK 500    GLU A 230   CD    GLU A 230   OE2     0.077
REMARK 500    GLU A 243   CD    GLU A 243   OE1     0.079
REMARK 500    GLU A 280   CD    GLU A 280   OE1     0.069
REMARK 500    GLU A 306   CD    GLU A 306   OE1     0.089
REMARK 500    GLU A 311   CD    GLU A 311   OE2     0.074
REMARK 500    GLU A 361   CD    GLU A 361   OE1     0.070
REMARK 500    GLU A 471   CD    GLU A 471   OE2     0.096
REMARK 500    GLU A 475   CD    GLU A 475   OE1     0.081
REMARK 500    GLU A 488   CD    GLU A 488   OE2     0.110
REMARK 500    GLY A 495   N     GLY A 495   CA      1.220
REMARK 500    GLY A 495   CA    GLY A 495   C       1.720
REMARK 500    GLY A 495   C     GLY A 495   O       4.966
REMARK 500    GLY A 495   C     GLY A 495   OXT     1.557
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    ASP A  31   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ASP A  33   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    LEU A  86   CB  -  CA  -  C   ANGL. DEV. =  12.2 DEGREES
REMARK 500    ASP A 120   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 140   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ARG A 148   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ASP A 156   CB  -  CG  -  OD1 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP A 156   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ARG A 162   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A 167   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ASP A 167   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 188   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 202   CB  -  CA  -  C   ANGL. DEV. =  14.0 DEGREES
REMARK 500    ARG A 202   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ASP A 234   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 234   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A 240   CB  -  CG  -  OD1 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ASP A 240   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP A 279   CB  -  CG  -  OD1 ANGL. DEV. =  -8.7 DEGREES
REMARK 500    ASP A 279   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    TYR A 316   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ASP A 321   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ASP A 321   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ASP A 323   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 323   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ARG A 330   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 330   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500    MET A 346   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES
REMARK 500    ARG A 347   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ASP A 374   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A 385   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A 387   CB  -  CG  -  OD1 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ARG A 420   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ASP A 446   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ASP A 446   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    GLY A 495   N   -  CA  -  C   ANGL. DEV. = -40.8 DEGREES
REMARK 500    GLY A 495   CA  -  C   -  O   ANGL. DEV. =  47.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ILE A 102      -85.82    -34.66
REMARK 500    TYR A 134      145.61   -173.14
REMARK 500    ASP A 140      -39.20    -38.85
REMARK 500    PHE A 145       75.51   -100.90
REMARK 500    ALA A 184       18.07     59.91
REMARK 500    TRP A 198      128.29    -39.23
REMARK 500    PHE A 200      -94.75    -48.82
REMARK 500    PRO A 201       26.06    -54.63
REMARK 500    HIS A 308       56.17     37.98
REMARK 500    ARG A 420      131.36     88.11
REMARK 500    LYS A 428      -71.70    -47.89
REMARK 500    ASP A 494       82.46    -52.80
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  11         0.07    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    GLU A 133         10.99
REMARK 500    VAL A 241         12.68
REMARK 500    GLN A 276         11.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 545        DISTANCE =  6.60 ANGSTROMS
REMARK 525    HOH A 634        DISTANCE =  5.68 ANGSTROMS
REMARK 525    HOH A 716        DISTANCE =  7.67 ANGSTROMS
REMARK 525    HOH A 721        DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH A 782        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH A 815        DISTANCE =  6.72 ANGSTROMS
REMARK 525    HOH A 818        DISTANCE =  5.52 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 951
DBREF  1BYA A    1   495  UNP    P10538   AMYB_SOYBN       1    495
SEQRES   1 A  495  ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES   2 A  495  VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES   3 A  495  ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES   4 A  495  LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES   5 A  495  ASP VAL TRP TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES   6 A  495  GLN TYR ASP TRP ARG ALA TYR ARG SER LEU PHE GLN LEU
SEQRES   7 A  495  VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES   8 A  495  PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES   9 A  495  ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES  10 A  495  ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES  11 A  495  ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES  12 A  495  ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES  13 A  495  TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES  14 A  495  GLU SER GLY LEU ILE ILE ASP ILE GLU VAL GLY LEU GLY
SEQRES  15 A  495  PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES  16 A  495  GLN GLY TRP GLU PHE PRO ARG ILE GLY GLU PHE GLN CYS
SEQRES  17 A  495  TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES  18 A  495  ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES  19 A  495  ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES  20 A  495  PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES  21 A  495  PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES  22 A  495  GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES  23 A  495  GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES  24 A  495  HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES  25 A  495  THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES  26 A  495  ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES  27 A  495  LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES  28 A  495  PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES  29 A  495  GLN VAL LEU SER GLY GLY TRP ARG GLU ASP ILE ARG VAL
SEQRES  30 A  495  ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES  31 A  495  TYR ASN GLN ILE ILE LEU ASN ALA LYS PRO GLN GLY VAL
SEQRES  32 A  495  ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES  33 A  495  THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES  34 A  495  ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES  35 A  495  ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES  36 A  495  HIS ALA ILE THR PRO LEU LYS PRO SER ALA PRO LYS ILE
SEQRES  37 A  495  PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR LEU
SEQRES  38 A  495  PRO PHE PRO TRP LEU PRO GLU THR ASP MET LYS VAL ASP
SEQRES  39 A  495  GLY
HET    SO4  A 951       5
HETNAM     SO4 SULFATE ION
FORMUL   2  SO4    O4 S 2-
FORMUL   3  HOH   *320(H2 O)
HELIX    1  A1 PRO A   32  ALA A   45  1                                  14
HELIX    2  A2 ARG A   70  GLU A   81  1                                  12
HELIX    3  A3 GLN A  109  SER A  117  1                                   9
HELIX    4  A4 ALA A  150  GLU A  170  1                                  21
HELIX    5  A5 LYS A  211  ALA A  224  1                                  14
HELIX    6  A6 LYS A  258  ALA A  284  1                                  27
HELIX    7  A7 ALA A  309  THR A  313  1                                   5
HELIX    8  A8 TYR A  325  ARG A  334  1                                  10
HELIX    9  A9 PRO A  359  GLU A  373  1                                  15
HELIX   10 A10 ASP A  387  LYS A  399  1                                  13
HELIX   11 A11 GLN A  427  HIS A  442  1                                  16
HELIX   12 A12 PRO A  469  GLU A  475  1                                   7
SHEET    1  S1 8 PRO A  13  LEU A  20  0
SHEET    2  S1 8 GLY A  49  TRP A  55  1  O  MET A  51   N  LEU A  18
SHEET    3  S1 8 THR A  85  SER A  91  1  O  GLN A  87   N  VAL A  52
SHEET    4  S1 8 ASP A 176  LEU A 181  1  O  ASP A 176   N  ALA A  88
SHEET    5  S1 8 VAL A 290  VAL A 296  1  O  LYS A 291   N  ILE A 177
SHEET    6  S1 8 ALA A 337  CYS A 343  1  O  ILE A 338   N  ILE A 294
SHEET    7  S1 8 ILE A 375  ASN A 381  1  O  ALA A 378   N  PHE A 341
SHEET    8  S1 8 GLY A 415  LEU A 419  1  N  THR A 417   O  GLY A 379
SITE     1 AC1  3 HIS A 146  ARG A 326  ARG A 372
CRYST1   86.200   86.200  144.200  90.00  90.00 120.00 P 31 2 1      6
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      0.011601  0.006698  0.000000        0.00000
SCALE2      0.000000  0.013396  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006935        0.00000
      
PROCHECK
Go to PROCHECK summary
 References