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PDBsum entry 1amy

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Hydrolase (o-glycosyl) PDB id
1amy
Jmol
Contents
Protein chain
403 a.a.
Metals
_CA ×3
Waters ×152
HEADER    HYDROLASE (O-GLYCOSYL)                  10-MAR-94   1AMY
TITLE     CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE;
SOURCE   3 ORGANISM_TAXID: 4513
KEYWDS    HYDROLASE (O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.KADZIOLA,R.HASER
REVDAT   3   24-FEB-09 1AMY    1       VERSN
REVDAT   2   01-APR-03 1AMY    1       JRNL
REVDAT   1   13-MAY-95 1AMY    0
JRNL        AUTH   A.KADZIOLA,J.ABE,B.SVENSSON,R.HASER
JRNL        TITL   CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY
JRNL        TITL 2 ALPHA-AMYLASE.
JRNL        REF    J.MOL.BIOL.                   V. 239   104 1994
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   8196040
JRNL        DOI    10.1006/JMBI.1994.1354
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   F.VALLEE,A.KADZIOLA,Y.BOURNE,J.-I.ABE,B.SVENSSON,
REMARK   1  AUTH 2 R.HASER
REMARK   1  TITL   CHARACTERIZATION, CRYSTALLIZATION AND
REMARK   1  TITL 2 CRYSTALLOGRAPHIC PRELIMINARY DATA OF THE COMPLEX
REMARK   1  TITL 3 BETWEEN BARLEY ALPHA-AMYLASE AND THE BIFUNCTIONAL
REMARK   1  TITL 4 ALPHA-AMYLASE(SLASH)SUBTILISIN INHIBITOR FROM
REMARK   1  TITL 5 BARLEY SEEDS
REMARK   1  REF    J.MOL.BIOL.                   V. 236   368 1994
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   M.SOGAARD,A.KADZIOLA,R.HASER,B.SVENSSON
REMARK   1  TITL   SITE-DIRECTED MUTAGENESIS OF HISTIDINE 93,
REMARK   1  TITL 2 ASPARTIC ACID 180, GLUTAMIC ACID 20 5, HISTIDINE
REMARK   1  TITL 3 290, AND ASPARTIC ACID 291 AT THE ACTIVE SITE AND
REMARK   1  TITL 4 TRYPTOPHAN 279 AT THE RAW STARCH BINDING SITE IN
REMARK   1  TITL 5 BARLEY ALPHA-AMYLASE 1
REMARK   1  REF    J.BIOL.CHEM.                  V. 268 22480 1993
REMARK   1  REFN                   ISSN 0021-9258
REMARK   2
REMARK   2 RESOLUTION.    2.80 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) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000
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             : 18303
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) : 0.153
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            : 3184
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 3
REMARK   3   SOLVENT ATOMS            : 152
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) : 0.016
REMARK   3   BOND ANGLES            (DEGREES) : 3.30
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:  IN A FINAL 2FOBS-FCALC MAP NO
REMARK   3  DENSITY WAS SEEN FOR THE SIDE CHAINS OF LYS 158, TYR 378, AND
REMARK   3  LYS 389.
REMARK   4
REMARK   4 1AMY 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   (%): 73.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.67
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       26.53333
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       53.06667
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       53.06667
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       26.53333
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE STRUCTURE CAN BE DESCRIBED AS CONSISTING OF THREE
REMARK 400 DOMAINS:  A CENTRAL DOMAIN (A) FORMING AN
REMARK 400 ALPHA-BETA-8-BARREL (GLN 1 - ILE 88 AND ASN 153 - HIS 344)
REMARK 400 WITH A PROTRUDING IRREGULARLY STRUCTURED LOOP DOMAIN (B)
REMARK 400 (VAL 89 - LEU 152) AND A C-TERMINAL DOMAIN (C) (LYS 351 -
REMARK 400 ILE 403) FORMING AN ANTI-PARALLEL FIVE STRANDED
REMARK 400 BETA-SHEET.
REMARK 400
REMARK 400 THE ACTIVE CATALYTIC SITE CLEFT (AS) HAS BEEN LOCATED TO
REMARK 400 THE C-TERMINAL END OF THE CENTRAL BETA-BARREL AROUND
REMARK 400 RESIDUES ASP 179, GLU 204 AND ASP 289.
REMARK 400
REMARK 400 A RAW STARCH BINDING SITE (SS) HAS BEEN LOCATED AT THE
REMARK 400 SURFACE AROUND RESIDUES TRP 276 AND TRP 277.
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  14   NE2   HIS A  14   CD2    -0.070
REMARK 500    HIS A  36   NE2   HIS A  36   CD2    -0.080
REMARK 500    HIS A  92   NE2   HIS A  92   CD2    -0.079
REMARK 500    HIS A  97   NE2   HIS A  97   CD2    -0.075
REMARK 500    HIS A 151   NE2   HIS A 151   CD2    -0.067
REMARK 500    HIS A 224   NE2   HIS A 224   CD2    -0.072
REMARK 500    HIS A 288   NE2   HIS A 288   CD2    -0.071
REMARK 500    HIS A 314   NE2   HIS A 314   CD2    -0.079
REMARK 500    HIS A 324   NE2   HIS A 324   CD2    -0.071
REMARK 500    HIS A 344   NE2   HIS A 344   CD2    -0.076
REMARK 500    HIS A 347   NE2   HIS A 347   CD2    -0.074
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    GLN A   1   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES
REMARK 500    LEU A   3   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    TRP A   9   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    TRP A   9   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP A  12   CD1 -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    TRP A  12   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP A  12   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A  18   CD1 -  CG  -  CD2 ANGL. DEV. =   7.6 DEGREES
REMARK 500    TRP A  18   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    TRP A  18   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES
REMARK 500    TRP A  38   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A  38   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP A  38   CG  -  CD2 -  CE3 ANGL. DEV. =   5.5 DEGREES
REMARK 500    MET A  52   CG  -  SD  -  CE  ANGL. DEV. =  -9.9 DEGREES
REMARK 500    ARG A 101   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    TRP A 118   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES
REMARK 500    TRP A 118   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES
REMARK 500    ARG A 155   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    TRP A 163   CD1 -  CG  -  CD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    TRP A 163   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    TRP A 163   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP A 166   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    TRP A 166   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES
REMARK 500    TRP A 176   CD1 -  CG  -  CD2 ANGL. DEV. =   8.4 DEGREES
REMARK 500    TRP A 176   CB  -  CG  -  CD1 ANGL. DEV. =  -8.3 DEGREES
REMARK 500    TRP A 176   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    TRP A 176   CE2 -  CD2 -  CG  ANGL. DEV. =  -7.2 DEGREES
REMARK 500    TRP A 176   CG  -  CD2 -  CE3 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ARG A 177   CA  -  CB  -  CG  ANGL. DEV. = -15.6 DEGREES
REMARK 500    TRP A 206   CD1 -  CG  -  CD2 ANGL. DEV. =   5.0 DEGREES
REMARK 500    TRP A 206   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.8 DEGREES
REMARK 500    TRP A 231   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    TRP A 231   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TRP A 261   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 261   CB  -  CG  -  CD1 ANGL. DEV. =  -8.7 DEGREES
REMARK 500    TRP A 261   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP A 261   CG  -  CD2 -  CE3 ANGL. DEV. =   6.6 DEGREES
REMARK 500    TRP A 277   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    TRP A 277   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TRP A 297   CD1 -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES
REMARK 500    TRP A 297   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES
REMARK 500    TRP A 297   CG  -  CD2 -  CE3 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    MET A 305   CG  -  SD  -  CE  ANGL. DEV. = -11.5 DEGREES
REMARK 500    TRP A 328   CD1 -  CG  -  CD2 ANGL. DEV. =   8.1 DEGREES
REMARK 500    TRP A 328   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    TRP A 328   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 336   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 336   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    ARG A 341   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      56 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    LEU A  56      -38.55    -38.75
REMARK 500    ARG A 101      -33.15    157.87
REMARK 500    TYR A 104       86.25    -69.88
REMARK 500    ARG A 125      -53.48    -19.54
REMARK 500    ASP A 132       30.03    -97.68
REMARK 500    ALA A 169      -72.38    -67.77
REMARK 500    GLU A 197       77.15     30.35
REMARK 500    ASP A 214      -15.33   -177.77
REMARK 500    TRP A 277       61.93   -154.25
REMARK 500    SER A 292     -146.09     59.30
REMARK 500    TRP A 297       68.22   -167.51
REMARK 500    PRO A 300      111.64    -35.85
REMARK 500    PRO A 315     -177.60    -56.75
REMARK 500    TYR A 322      -68.67    -29.81
REMARK 500    ASN A 348      -65.22      4.86
REMARK 500    LEU A 361      118.48   -163.65
REMARK 500    ASP A 367       25.59     44.20
REMARK 500    ASN A 382      -20.25    -37.74
REMARK 500    ASP A 396       52.13   -170.78
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 660        DISTANCE =  9.93 ANGSTROMS
REMARK 525    HOH A 668        DISTANCE =  7.19 ANGSTROMS
REMARK 525    HOH A 722        DISTANCE = 12.51 ANGSTROMS
REMARK 525    HOH A 728        DISTANCE =  6.82 ANGSTROMS
REMARK 525    HOH A 731        DISTANCE = 14.56 ANGSTROMS
REMARK 525    HOH A 732        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A 739        DISTANCE =  6.15 ANGSTROMS
REMARK 525    HOH A 742        DISTANCE =  5.70 ANGSTROMS
REMARK 525    HOH A 744        DISTANCE =  6.15 ANGSTROMS
REMARK 525    HOH A 750        DISTANCE = 13.50 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 500  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 630   O
REMARK 620 2 ASP A 138   OD1  78.7
REMARK 620 3 ASP A 138   OD2  85.3  49.7
REMARK 620 4 ASN A  91   OD1  86.0 160.7 141.2
REMARK 620 5 ALA A 141   O   171.0  93.6  86.2 102.5
REMARK 620 6 GLY A 183   O   101.6  85.5 132.8  86.1  82.1
REMARK 620 7 ASP A 148   OD2  90.0 121.8  72.8  69.4  90.3 152.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 501  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 108   OE1
REMARK 620 2 THR A 111   O   112.9
REMARK 620 3 ASP A 113   O   163.2  81.1
REMARK 620 4 ASP A 117   OD1  68.3 138.0 108.2
REMARK 620 5 ASP A 117   OD2  70.0 171.4  94.8  50.5
REMARK 620 6 HOH A 604   O   118.7  75.2  72.8  69.3 111.0
REMARK 620 7 HOH A 656   O    68.4  76.3 108.1 133.2  98.0 150.9
REMARK 620 8 GLU A 108   OE2  46.2  77.3 150.4  76.3 109.0  82.2  86.2
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 502  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 142   OD1
REMARK 620 2 ASP A 142   OD2  39.8
REMARK 620 3 PHE A 143   O    91.4  71.5
REMARK 620 4 ASP A 148   OD1  62.4  95.6  86.0
REMARK 620 5 ALA A 146   O   151.6 163.9  94.0  90.2
REMARK 620 6 ASP A 127   OD1  73.5  76.9 144.8 112.7 114.6
REMARK 620 7 GLY A 144   O   127.0  87.7  56.7 139.4  78.3 107.5
REMARK 620 8 ASP A 127   OD2  79.8 110.4 159.4  73.5  85.7  49.8 142.4
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET PRESENTED AS *A* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY AN EIGHT-STRANDED BETA-BARREL.  THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND
REMARK 700 LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: SS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
DBREF  1AMY A    1   403  UNP    P04063   AMY2_HORVU      25    427
SEQRES   1 A  403  GLN VAL LEU PHE GLN GLY PHE ASN TRP GLU SER TRP LYS
SEQRES   2 A  403  HIS ASN GLY GLY TRP TYR ASN PHE LEU MET GLY LYS VAL
SEQRES   3 A  403  ASP ASP ILE ALA ALA ALA GLY ILE THR HIS VAL TRP LEU
SEQRES   4 A  403  PRO PRO ALA SER GLN SER VAL ALA GLU GLN GLY TYR MET
SEQRES   5 A  403  PRO GLY ARG LEU TYR ASP LEU ASP ALA SER LYS TYR GLY
SEQRES   6 A  403  ASN LYS ALA GLN LEU LYS SER LEU ILE GLY ALA LEU HIS
SEQRES   7 A  403  GLY LYS GLY VAL LYS ALA ILE ALA ASP ILE VAL ILE ASN
SEQRES   8 A  403  HIS ARG THR ALA GLU HIS LYS ASP GLY ARG GLY ILE TYR
SEQRES   9 A  403  CYS ILE PHE GLU GLY GLY THR PRO ASP ALA ARG LEU ASP
SEQRES  10 A  403  TRP GLY PRO HIS MET ILE CYS ARG ASP ASP ARG PRO TYR
SEQRES  11 A  403  ALA ASP GLY THR GLY ASN PRO ASP THR GLY ALA ASP PHE
SEQRES  12 A  403  GLY ALA ALA PRO ASP ILE ASP HIS LEU ASN LEU ARG VAL
SEQRES  13 A  403  GLN LYS GLU LEU VAL GLU TRP LEU ASN TRP LEU LYS ALA
SEQRES  14 A  403  ASP ILE GLY PHE ASP GLY TRP ARG PHE ASP PHE ALA LYS
SEQRES  15 A  403  GLY TYR SER ALA ASP VAL ALA LYS ILE TYR ILE ASP ARG
SEQRES  16 A  403  SER GLU PRO SER PHE ALA VAL ALA GLU ILE TRP THR SER
SEQRES  17 A  403  LEU ALA TYR GLY GLY ASP GLY LYS PRO ASN LEU ASN GLN
SEQRES  18 A  403  ASP GLN HIS ARG GLN GLU LEU VAL ASN TRP VAL ASP LYS
SEQRES  19 A  403  VAL GLY GLY LYS GLY PRO ALA THR THR PHE ASP PHE THR
SEQRES  20 A  403  THR LYS GLY ILE LEU ASN VAL ALA VAL GLU GLY GLU LEU
SEQRES  21 A  403  TRP ARG LEU ARG GLY THR ASP GLY LYS ALA PRO GLY MET
SEQRES  22 A  403  ILE GLY TRP TRP PRO ALA LYS ALA VAL THR PHE VAL ASP
SEQRES  23 A  403  ASN HIS ASP THR GLY SER THR GLN HIS MET TRP PRO PHE
SEQRES  24 A  403  PRO SER ASP ARG VAL MET GLN GLY TYR ALA TYR ILE LEU
SEQRES  25 A  403  THR HIS PRO GLY THR PRO CYS ILE PHE TYR ASP HIS PHE
SEQRES  26 A  403  PHE ASP TRP GLY LEU LYS GLU GLU ILE ASP ARG LEU VAL
SEQRES  27 A  403  SER VAL ARG THR ARG HIS GLY ILE HIS ASN GLU SER LYS
SEQRES  28 A  403  LEU GLN ILE ILE GLU ALA ASP ALA ASP LEU TYR LEU ALA
SEQRES  29 A  403  GLU ILE ASP GLY LYS VAL ILE VAL LYS LEU GLY PRO ARG
SEQRES  30 A  403  TYR ASP VAL GLY ASN LEU ILE PRO GLY GLY PHE LYS VAL
SEQRES  31 A  403  ALA ALA HIS GLY ASN ASP TYR ALA VAL TRP GLU LYS ILE
HET     CA  A 500       1
HET     CA  A 501       1
HET     CA  A 502       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    3(CA 2+)
FORMUL   5  HOH   *152(H2 O)
HELIX    1  A1 GLY A   17  ALA A   32  1NO H. BOND BET. G24-O & D27-N     16
HELIX    2  A2 ASN A   66  LYS A   80  1                                  15
HELIX    3  A3 ASN A  153  ASP A  170  1                                  18
HELIX    4  A4 SER A  185  GLU A  197  1                                  13
HELIX    5  A5 GLN A  221  GLY A  236  1                                  16
HELIX    6 A6A PHE A  246  VAL A  256  1                                  11
HELIX    7 A6B MET A  273  TRP A  277  1                                   5
HELIX    8 A7A ASN A  287  GLY A  291  1                                   5
HELIX    9 A7B VAL A  304  HIS A  314  1                                  11
HELIX   10 A8A TYR A  322  ASP A  327  1                                   6
HELIX   11 A8B LEU A  330  HIS A  344  1                                  15
SHEET    1   A 9 VAL A   2  GLY A   6  0
SHEET    2   A 9 THR A  35  LEU A  39  1  N  TRP A  38   O  PHE A   4
SHEET    3   A 9 LYS A  83  ILE A  88  1  N  ILE A  85   O  VAL A  37
SHEET    4   A 9 GLY A 175  ASP A 179  1  N  ARG A 177   O  ALA A  86
SHEET    5   A 9 PHE A 200  GLU A 204  1  N  VAL A 202   O  TRP A 176
SHEET    6   A 9 THR A 243  ASP A 245  1  N  PHE A 244   O  ALA A 203
SHEET    7   A 9 LYS A 280  THR A 283  1  N  VAL A 282   O  THR A 243
SHEET    8   A 9 THR A 317  TYR A 322  1  N  CYS A 319   O  THR A 283
SHEET    9   A 9 VAL A   2  GLY A   6  1  N  GLN A   5   O  ILE A 320
SHEET    1   C 5 LYS A 351  ASP A 358  0
SHEET    2   C 5 LEU A 361  ASP A 367 -1  N  GLU A 365   O  GLN A 353
SHEET    3   C 5 LYS A 369  GLY A 375 -1  N  VAL A 372   O  ALA A 364
SHEET    4   C 5 ASP A 396  ILE A 403 -1  N  TRP A 400   O  ILE A 371
SHEET    5   C 5 GLY A 387  GLY A 394 -1  N  ALA A 392   O  VAL A 399
LINK        CA    CA A 500                 O   HOH A 630     1555   1555  2.12
LINK        CA    CA A 500                 OD1 ASP A 138     1555   1555  2.33
LINK        CA    CA A 500                 OD2 ASP A 138     1555   1555  2.75
LINK        CA    CA A 500                 OD1 ASN A  91     1555   1555  2.11
LINK        CA    CA A 500                 O   ALA A 141     1555   1555  2.09
LINK        CA    CA A 500                 O   GLY A 183     1555   1555  2.11
LINK        CA    CA A 500                 OD2 ASP A 148     1555   1555  2.60
LINK        CA    CA A 501                 OE1 GLU A 108     1555   1555  2.91
LINK        CA    CA A 501                 O   THR A 111     1555   1555  2.37
LINK        CA    CA A 501                 O   ASP A 113     1555   1555  2.23
LINK        CA    CA A 501                 OD1 ASP A 117     1555   1555  2.59
LINK        CA    CA A 501                 OD2 ASP A 117     1555   1555  2.39
LINK        CA    CA A 501                 O   HOH A 604     1555   1555  2.21
LINK        CA    CA A 501                 O   HOH A 656     1555   1555  2.07
LINK        CA    CA A 501                 OE2 GLU A 108     1555   1555  2.58
LINK        CA    CA A 502                 OD1 ASP A 142     1555   1555  2.77
LINK        CA    CA A 502                 OD2 ASP A 142     1555   1555  3.36
LINK        CA    CA A 502                 O   PHE A 143     1555   1555  2.20
LINK        CA    CA A 502                 OD1 ASP A 148     1555   1555  2.47
LINK        CA    CA A 502                 O   ALA A 146     1555   1555  2.23
LINK        CA    CA A 502                 OD1 ASP A 127     1555   1555  2.59
LINK        CA    CA A 502                 O   GLY A 144     1555   1555  3.26
LINK        CA    CA A 502                 OD2 ASP A 127     1555   1555  2.45
CISPEP   1 ARG A  128    PRO A  129          0         7.48
SITE     1  AS  3 ASP A 179  GLU A 204  ASP A 289
SITE     1  SS  2 TRP A 276  TRP A 277
SITE     1 AC1  6 ASN A  91  ASP A 138  ALA A 141  ASP A 148
SITE     2 AC1  6 GLY A 183  HOH A 630
SITE     1 AC2  6 GLU A 108  THR A 111  ASP A 113  ASP A 117
SITE     2 AC2  6 HOH A 604  HOH A 656
SITE     1 AC3  6 ASP A 127  ASP A 142  PHE A 143  GLY A 144
SITE     2 AC3  6 ALA A 146  ASP A 148
CRYST1  135.200  135.200   79.600  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      0.007396  0.004270  0.000000        0.00000
SCALE2      0.000000  0.008541  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012563        0.00000
      
PROCHECK
Go to PROCHECK summary
 References