spacer
spacer

PDBsum entry 1b1y

Go to PDB code: 
Top Page protein ligands links
Hydrolase PDB id
1b1y
Jmol
Contents
Protein chain
500 a.a. *
Ligands
GLC-BGC
BGC
Waters ×140
* Residue conservation analysis
HEADER    HYDROLASE                               25-NOV-98   1B1Y
TITLE     SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (BETA-AMYLASE);
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.2;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE;
SOURCE   3 ORGANISM_TAXID: 4513;
SOURCE   4 VARIANT: CV. HARUNA;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: JM 109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PB927
KEYWDS    HYDROLASE(O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.MIKAMI,H.J.YOON,N.YOSHIGI
REVDAT   4   25-AUG-09 1B1Y    1       HET
REVDAT   3   24-FEB-09 1B1Y    1       VERSN
REVDAT   2   22-DEC-99 1B1Y    4       HEADER COMPND REMARK JRNL
REVDAT   2 2                   4       ATOM   SOURCE SEQRES
REVDAT   1   02-DEC-98 1B1Y    0
JRNL        AUTH   B.MIKAMI,H.J.YOON,N.YOSHIGI
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE SEVENFOLD MUTANT OF
JRNL        TITL 2 BARLEY BETA-AMYLASE WITH INCREASED THERMOSTABILITY
JRNL        TITL 3 AT 2.5 A RESOLUTION.
JRNL        REF    J.MOL.BIOL.                   V. 285  1235 1999
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9918723
JRNL        DOI    10.1006/JMBI.1998.2379
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   N.YOSHIGI,Y.OKADA,H.MAEBA,H.SAHARA,T.TAMAKI
REMARK   1  TITL   CONSTRUCTION OF A PLASMID USED FOR THE EXPRESSION
REMARK   1  TITL 2 OF A SEVENFOLD-MUTANT BARLEY BETA-AMYLASE WITH
REMARK   1  TITL 3 INCREASED THERMOSTABILITY IN ESCHERICHIA COLI AND
REMARK   1  TITL 4 PROPERTIES OF THE SEVENFOLD-MUTANT BETA-AMYLASE
REMARK   1  REF    J.BIOCHEM.(TOKYO)             V. 118   562 1995
REMARK   1  REFN                   ISSN 0021-924X
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
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) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.9
REMARK   3   NUMBER OF REFLECTIONS             : 18732
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.187
REMARK   3   FREE R VALUE                     : 0.256
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.61
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 45.60
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1182
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840
REMARK   3   BIN FREE R VALUE                    : 0.3280
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.14
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 119
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            : 3973
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 35
REMARK   3   SOLVENT ATOMS            : 140
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.14
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -2.89000
REMARK   3    B22 (A**2) : -2.89000
REMARK   3    B33 (A**2) : 5.79000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.00
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) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 3.24
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.77
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.22
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  : PARAM19X.PRO
REMARK   3  PARAMETER FILE  2  : PARAM1.CHO
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH1.CHO
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1B1Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-98.
REMARK 100 THE RCSB ID CODE IS RCSB000158.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-96
REMARK 200  TEMPERATURE           (KELVIN) : 291
REMARK 200  PH                             : 7.1
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : CARBON
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22631
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3
REMARK 200  DATA REDUNDANCY                : 5.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08600
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1BTC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HUNGING DROP VAPOR DIFFUSION
REMARK 280  AGAINST 0.1 M PIPES PH 7.1, 0.1 M MGAC2 AND 14% PEG 6000 WITH
REMARK 280  A PROTEIN CONCENTRATION OF 3 MG/ML., VAPOR DIFFUSION - HANGING
REMARK 280  DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-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      125.25500
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       36.05500
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       36.05500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      187.88250
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       36.05500
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       36.05500
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       62.62750
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       36.05500
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.05500
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      187.88250
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       36.05500
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.05500
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       62.62750
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      125.25500
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 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  91   NE2   HIS A  91   CD2    -0.071
REMARK 500    HIS A 125   NE2   HIS A 125   CD2    -0.071
REMARK 500    HIS A 224   NE2   HIS A 224   CD2    -0.068
REMARK 500    HIS A 271   NE2   HIS A 271   CD2    -0.069
REMARK 500    HIS A 306   NE2   HIS A 306   CD2    -0.069
REMARK 500    HIS A 333   NE2   HIS A 333   CD2    -0.077
REMARK 500    HIS A 409   NE2   HIS A 409   CD2    -0.070
REMARK 500    HIS A 440   NE2   HIS A 440   CD2    -0.080
REMARK 500    HIS A 483   NE2   HIS A 483   CD2    -0.067
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    ARG A  34   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    TRP A  53   CD1 -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    TRP A  53   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP A  54   CD1 -  CG  -  CD2 ANGL. DEV. =   5.3 DEGREES
REMARK 500    TRP A  54   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    VAL A  57   CA  -  C   -  N   ANGL. DEV. =  13.7 DEGREES
REMARK 500    VAL A  57   O   -  C   -  N   ANGL. DEV. =  -9.7 DEGREES
REMARK 500    TRP A  67   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP A  67   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    LEU A  84   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES
REMARK 500    TRP A 108   CD1 -  CG  -  CD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    TRP A 108   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP A 108   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 110   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 110   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    TYR A 121   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 146   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 146   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    LEU A 179   CA  -  CB  -  CG  ANGL. DEV. =  16.5 DEGREES
REMARK 500    TRP A 196   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    TRP A 196   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP A 227   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    TRP A 227   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    ARG A 258   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    TRP A 263   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TRP A 263   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP A 299   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    TRP A 299   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 300   CD1 -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    TRP A 300   CB  -  CG  -  CD1 ANGL. DEV. =  -8.0 DEGREES
REMARK 500    TRP A 300   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.7 DEGREES
REMARK 500    TRP A 300   CG  -  CD2 -  CE3 ANGL. DEV. =   5.8 DEGREES
REMARK 500    TYR A 315   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    ARG A 328   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG A 345   CA  -  CB  -  CG  ANGL. DEV. = -15.4 DEGREES
REMARK 500    TRP A 369   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TRP A 369   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 369   CG  -  CD2 -  CE3 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A 370   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 370   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ARG A 383   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A 418   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ARG A 418   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 445   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 457   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 457   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    ASP A  19       62.79   -117.02
REMARK 500    SER A  22      179.81    -40.06
REMARK 500    VAL A  23        6.73    -69.17
REMARK 500    ASN A  24       50.37   -156.09
REMARK 500    LYS A  29       20.99    -67.11
REMARK 500    VAL A  57      -89.32    -65.07
REMARK 500    GLU A  58       30.31    -67.60
REMARK 500    LYS A  63       14.29     55.08
REMARK 500    MET A  88       82.81    -69.96
REMARK 500    PHE A  90       28.75    -73.66
REMARK 500    ASP A 118       13.36    -67.89
REMARK 500    PHE A 143       64.82   -102.99
REMARK 500    ALA A 182        5.40     58.73
REMARK 500    LEU A 185       99.94    -68.42
REMARK 500    ARG A 186     -176.58    179.76
REMARK 500    CYS A 206       31.37   -143.38
REMARK 500    HIS A 224       64.07   -112.97
REMARK 500    PRO A 230      105.72    -50.31
REMARK 500    LEU A 284      102.96    -49.56
REMARK 500    ALA A 307      -61.32    -29.62
REMARK 500    ALA A 342      -35.82    -37.33
REMARK 500    PRO A 350      129.74    -35.82
REMARK 500    ASN A 442        7.58     56.80
REMARK 500    SER A 463      172.95    -53.42
REMARK 500    PRO A 490     -120.71   -138.39
REMARK 500    MET A 494      -49.56   -137.23
REMARK 500    PRO A 501      135.29    -39.30
REMARK 500    THR A 502      -96.86    -72.88
REMARK 500    CYS A 503      -43.15   -164.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLY A  405     PRO A  406                  143.86
REMARK 500 GLY A  500     PRO A  501                 -128.27
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 210         0.07    SIDE_CHAIN
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 620        DISTANCE =  5.47 ANGSTROMS
REMARK 525    HOH A 626        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH A 632        DISTANCE =  6.76 ANGSTROMS
REMARK 525    HOH A 634        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH A 637        DISTANCE =  6.12 ANGSTROMS
REMARK 525    HOH A 643        DISTANCE = 12.48 ANGSTROMS
REMARK 525    HOH A 646        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH A 652        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A 653        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH A 655        DISTANCE =  6.28 ANGSTROMS
REMARK 525    HOH A 662        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH A 663        DISTANCE =  7.15 ANGSTROMS
REMARK 525    HOH A 664        DISTANCE =  6.87 ANGSTROMS
REMARK 525    HOH A 678        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH A 680        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH A 686        DISTANCE =  5.91 ANGSTROMS
REMARK 525    HOH A 695        DISTANCE =  6.67 ANGSTROMS
REMARK 525    HOH A 701        DISTANCE =  6.86 ANGSTROMS
REMARK 525    HOH A 709        DISTANCE =  7.26 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 550
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 551
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 552
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 REF.2 AND REF.3
DBREF  1B1Y A    5   504  UNP    P16098   AMYB_HORVU       5    504
SEQADV 1B1Y MET A    5  UNP  P16098    VAL     5 CONFLICT
SEQADV 1B1Y LEU A  185  UNP  P16098    MET   185 ENGINEERED
SEQADV 1B1Y ALA A  295  UNP  P16098    SER   295 ENGINEERED
SEQADV 1B1Y VAL A  297  UNP  P16098    ILE   297 ENGINEERED
SEQADV 1B1Y PRO A  350  UNP  P16098    SER   350 ENGINEERED
SEQADV 1B1Y PRO A  351  UNP  P16098    SER   351 ENGINEERED
SEQADV 1B1Y ASP A  352  UNP  P16098    GLN   352 ENGINEERED
SEQADV 1B1Y SER A  376  UNP  P16098    ALA   376 ENGINEERED
SEQADV 1B1Y ILE A  475  UNP  P16098    LEU   475 CONFLICT
SEQRES   1 A  500  MET LYS GLY ASN TYR VAL GLN VAL TYR VAL MET LEU PRO
SEQRES   2 A  500  LEU ASP ALA VAL SER VAL ASN ASN ARG PHE GLU LYS GLY
SEQRES   3 A  500  ASP GLU LEU ARG ALA GLN LEU ARG LYS LEU VAL GLU ALA
SEQRES   4 A  500  GLY VAL ASP GLY VAL MET VAL ASP VAL TRP TRP GLY LEU
SEQRES   5 A  500  VAL GLU GLY LYS GLY PRO LYS ALA TYR ASP TRP SER ALA
SEQRES   6 A  500  TYR LYS GLN LEU PHE GLU LEU VAL GLN LYS ALA GLY LEU
SEQRES   7 A  500  LYS LEU GLN ALA ILE MET SER PHE HIS GLN CYS GLY GLY
SEQRES   8 A  500  ASN VAL GLY ASP ALA VAL ASN ILE PRO ILE PRO GLN TRP
SEQRES   9 A  500  VAL ARG ASP VAL GLY THR ARG ASP PRO ASP ILE PHE TYR
SEQRES  10 A  500  THR ASP GLY HIS GLY THR ARG ASN ILE GLU TYR LEU THR
SEQRES  11 A  500  LEU GLY VAL ASP ASN GLN PRO LEU PHE HIS GLY ARG SER
SEQRES  12 A  500  ALA VAL GLN MET TYR ALA ASP TYR MET THR SER PHE ARG
SEQRES  13 A  500  GLU ASN MET LYS ASP PHE LEU ASP ALA GLY VAL ILE VAL
SEQRES  14 A  500  ASP ILE GLU VAL GLY LEU GLY PRO ALA GLY GLU LEU ARG
SEQRES  15 A  500  TYR PRO SER TYR PRO GLN SER HIS GLY TRP SER PHE PRO
SEQRES  16 A  500  GLY ILE GLY GLU PHE ILE CYS TYR ASP LYS TYR LEU GLN
SEQRES  17 A  500  ALA ASP PHE LYS ALA ALA ALA ALA ALA VAL GLY HIS PRO
SEQRES  18 A  500  GLU TRP GLU PHE PRO ASN ASP ALA GLY GLN TYR ASN ASP
SEQRES  19 A  500  THR PRO GLU ARG THR GLN PHE PHE ARG ASP ASN GLY THR
SEQRES  20 A  500  TYR LEU SER GLU LYS GLY ARG PHE PHE LEU ALA TRP TYR
SEQRES  21 A  500  SER ASN ASN LEU ILE LYS HIS GLY ASP ARG ILE LEU ASP
SEQRES  22 A  500  GLU ALA ASN LYS VAL PHE LEU GLY TYR LYS VAL GLN LEU
SEQRES  23 A  500  ALA ILE LYS ILE ALA GLY VAL HIS TRP TRP TYR LYS VAL
SEQRES  24 A  500  PRO SER HIS ALA ALA GLU LEU THR ALA GLY TYR TYR ASN
SEQRES  25 A  500  LEU HIS ASP ARG ASP GLY TYR ARG THR ILE ALA ARG MET
SEQRES  26 A  500  LEU LYS ARG HIS ARG ALA SER ILE ASN PHE THR CYS ALA
SEQRES  27 A  500  GLU MET ARG ASP SER GLU GLN PRO PRO ASP ALA MET SER
SEQRES  28 A  500  ALA PRO GLU GLU LEU VAL GLN GLN VAL LEU SER ALA GLY
SEQRES  29 A  500  TRP ARG GLU GLY LEU ASN VAL SER CYS GLU ASN ALA LEU
SEQRES  30 A  500  PRO ARG TYR ASP PRO THR ALA TYR ASN THR ILE LEU ARG
SEQRES  31 A  500  ASN ALA ARG PRO HIS GLY ILE ASN GLN SER GLY PRO PRO
SEQRES  32 A  500  GLU HIS LYS LEU PHE GLY PHE THR TYR LEU ARG LEU SER
SEQRES  33 A  500  ASN GLN LEU VAL GLU GLY GLN ASN TYR VAL ASN PHE LYS
SEQRES  34 A  500  THR PHE VAL ASP ARG MET HIS ALA ASN LEU PRO ARG ASP
SEQRES  35 A  500  PRO TYR VAL ASP PRO MET ALA PRO LEU PRO ARG SER GLY
SEQRES  36 A  500  PRO GLU ILE SER ILE GLU MET ILE LEU GLN ALA ALA GLN
SEQRES  37 A  500  PRO LYS ILE GLN PRO PHE PRO PHE GLN GLU HIS THR ASP
SEQRES  38 A  500  LEU PRO VAL GLY PRO THR GLY GLY MET GLY GLY GLN ALA
SEQRES  39 A  500  GLU GLY PRO THR CYS GLY
HET    GLC  A 550      11
HET    BGC  A 551      12
HET    BGC  A 552      12
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     BGC BETA-D-GLUCOSE
FORMUL   2  GLC    C6 H12 O6
FORMUL   2  BGC    2(C6 H12 O6)
FORMUL   4  HOH   *140(H2 O)
HELIX    1   1 LYS A    6  ASN A    8  5                                   3
HELIX    2   2 LYS A   29  GLU A   42  5                                  14
HELIX    3   3 VAL A   57  LYS A   60  5                                   4
HELIX    4   4 SER A   68  ALA A   80  1                                  13
HELIX    5   5 GLN A  107  ARG A  115  1                                   9
HELIX    6   6 PRO A  117  ILE A  119  5                                   3
HELIX    7   7 LEU A  135  VAL A  137  5                                   3
HELIX    8   8 ALA A  148  ALA A  169  1                                  22
HELIX    9   9 PRO A  181  GLY A  183  5                                   3
HELIX   10  10 GLN A  192  HIS A  194  5                                   3
HELIX   11  11 LYS A  209  ALA A  221  1                                  13
HELIX   12  12 PRO A  240  ARG A  242  5                                   3
HELIX   13  13 THR A  251  LEU A  253  5                                   3
HELIX   14  14 GLU A  255  PHE A  283  1                                  29
HELIX   15  15 ALA A  307  ALA A  312  1                                   6
HELIX   16  16 ARG A  324  LEU A  330  1                                   7
HELIX   17  17 ASP A  346  GLU A  348  5                                   3
HELIX   18  18 PRO A  357  ARG A  370  1                                  14
HELIX   19  19 PRO A  386  ALA A  396  1                                  11
HELIX   20  20 GLY A  426  HIS A  440  1                                  15
HELIX   21  21 ILE A  464  ALA A  470  1                                   7
SHEET    1   A 8 GLY A 413  TYR A 416  0
SHEET    2   A 8 GLN A  11  MET A  15  1  N  GLN A  11   O  PHE A 414
SHEET    3   A 8 GLY A  47  TRP A  53  1  N  GLY A  47   O  VAL A  14
SHEET    4   A 8 LYS A  83  SER A  89  1  N  LYS A  83   O  VAL A  48
SHEET    5   A 8 ILE A 172  VAL A 177  1  N  VAL A 173   O  LEU A  84
SHEET    6   A 8 GLN A 289  ILE A 294  1  N  GLN A 289   O  ILE A 175
SHEET    7   A 8 SER A 336  PHE A 339  1  N  SER A 336   O  ILE A 292
SHEET    8   A 8 VAL A 375  CYS A 377  1  N  SER A 376   O  ILE A 337
SHEET    1   B 2 PHE A 120  THR A 122  0
SHEET    2   B 2 ARG A 128  LEU A 133 -1  N  TYR A 132   O  TYR A 121
LINK         C1  GLC A 550                 O4  BGC A 551     1555   1555  1.43
CISPEP   1 PHE A  198    PRO A  199          0         9.25
CISPEP   2 LEU A  417    ARG A  418          0         0.16
CISPEP   3 GLN A  472    PRO A  473          0       -11.44
SITE     1 AC1 13 MET A  15  ASP A  51  TRP A  53  ILE A  87
SITE     2 AC1 13 HIS A  91  ASN A  96  ASP A  99  ALA A 182
SITE     3 AC1 13 ARG A 418  BGC A 551  HOH A 658  HOH A 684
SITE     4 AC1 13 HOH A 728
SITE     1 AC2  9 VAL A  97  ALA A 182  GLU A 184  LYS A 293
SITE     2 AC2  9 THR A 340  GLU A 378  ALA A 380  GLC A 550
SITE     3 AC2  9 HOH A 684
SITE     1 AC3  4 GLN A 192  PHE A 198  HIS A 298  HOH A 718
CRYST1   72.110   72.110  250.510  90.00  90.00  90.00 P 43 21 2     8
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      0.013868  0.000000  0.000000        0.00000
SCALE2      0.000000  0.013868  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003992        0.00000
      
PROCHECK
Go to PROCHECK summary
 References

 

spacer

spacer