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PDBsum entry 1ppi

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Hydrolase (o-glycosyl) PDB id
1ppi
Jmol
Contents
Protein chain
496 a.a.
Ligands
GLC-GLC-DAF-BGC
Metals
_CA
_CL
Waters ×393
HEADER    HYDROLASE (O-GLYCOSYL)                  22-FEB-94   1PPI
TITLE     THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE
TITLE    2 STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH
TITLE    3 A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS
TITLE    4 RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 TISSUE: PANCREAS
KEYWDS    HYDROLASE (O-GLYCOSYL)
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.QIAN,R.HASER,F.PAYAN
REVDAT   4   08-SEP-09 1PPI    1       HETATM HETNAM
REVDAT   3   25-AUG-09 1PPI    1       SOURCE
REVDAT   2   24-FEB-09 1PPI    1       VERSN
REVDAT   1   24-MAY-95 1PPI    0
JRNL        AUTH   M.QIAN,R.HASER,G.BUISSON,E.DUEE,F.PAYAN
JRNL        TITL   THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE.
JRNL        TITL 2 STRUCTURE OF THE COMPLEX OF A PANCREATIC
JRNL        TITL 3 ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED
JRNL        TITL 4 TO 2.2-A RESOLUTION.
JRNL        REF    BIOCHEMISTRY                  V.  33  6284 1994
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   8193143
JRNL        DOI    10.1021/BI00186A031
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.QIAN,R.HASER,F.PAYAN
REMARK   1  TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF PIG
REMARK   1  TITL 2 PANCREATIC ALPHA-AMYLASE AT 2.1 ANGSTROMS
REMARK   1  TITL 3 RESOLUTION
REMARK   1  REF    J.MOL.BIOL.                   V. 231   785 1993
REMARK   1  REFN                   ISSN 0022-2836
REMARK   2
REMARK   2 RESOLUTION.    2.20 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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
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             : 25018
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            : 3908
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 57
REMARK   3   SOLVENT ATOMS            : 393
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) : 0.015
REMARK   3   BOND ANGLES            (DEGREES) : 2.90
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: NULL
REMARK   4
REMARK   4 1PPI 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   (%): 46.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
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       28.15000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.70000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.90000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.70000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.15000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.90000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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    TYR A   2   CE1   TYR A   2   CZ     -0.083
REMARK 500    HIS A  15   NE2   HIS A  15   CD2    -0.078
REMARK 500    HIS A 201   NE2   HIS A 201   CD2    -0.075
REMARK 500    HIS A 386   NE2   HIS A 386   CD2    -0.079
REMARK 500    HIS A 491   NE2   HIS A 491   CD2    -0.068
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    TYR A   2   CB  -  CG  -  CD1 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ARG A  10   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    TRP A  19   CD1 -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES
REMARK 500    TRP A  19   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A  20   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    TRP A  21   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    TRP A  21   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES
REMARK 500    TRP A  21   CG  -  CD2 -  CE3 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ARG A  30   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    TRP A  58   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES
REMARK 500    TRP A  58   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TRP A  59   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TRP A  59   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A  72   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ARG A  72   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG A 124   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 124   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    TRP A 134   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP A 134   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 176   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ARG A 176   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500    ARG A 195   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG A 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TRP A 203   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    TRP A 203   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 221   CD1 -  CG  -  CD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    TRP A 221   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 227   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG A 252   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG A 252   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 269   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    TRP A 269   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES
REMARK 500    TRP A 280   CD1 -  CG  -  CD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    TRP A 280   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES
REMARK 500    TRP A 284   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    TRP A 284   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 316   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES
REMARK 500    TRP A 316   CB  -  CG  -  CD1 ANGL. DEV. =  -8.9 DEGREES
REMARK 500    TRP A 316   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TRP A 316   CG  -  CD2 -  CE3 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ARG A 337   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    TYR A 342   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG A 343   NE  -  CZ  -  NH1 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ARG A 343   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.4 DEGREES
REMARK 500    TRP A 344   CD1 -  CG  -  CD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    TRP A 344   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TRP A 357   CD1 -  CG  -  CD2 ANGL. DEV. =   5.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      67 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  16       76.80   -102.61
REMARK 500    TYR A  31      -60.91   -143.38
REMARK 500    MET A 102     -145.04   -107.95
REMARK 500    VAL A 163       44.17     29.71
REMARK 500    ALA A 224      -72.28    -35.29
REMARK 500    ASP A 317       63.58   -115.44
REMARK 500    ASP A 381       19.33     57.33
REMARK 500    SER A 414     -102.78   -127.36
REMARK 500    PRO A 486       38.59    -73.20
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 630        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH A 761        DISTANCE =  5.89 ANGSTROMS
REMARK 525    HOH A 782        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A 815        DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH A 870A       DISTANCE =  5.55 ANGSTROMS
REMARK 525    HOH A 880A       DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH A 894A       DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH A 913A       DISTANCE =  6.52 ANGSTROMS
REMARK 525    HOH A 915A       DISTANCE =  7.79 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ACARBOSE IS A PSEUDOSACCHARRIDE THAT IS ACTED ON BY THE
REMARK 600 ENZYME.  THIS YIELDS A FIVE-UNIT PRODUCT PRESENT IN THE
REMARK 600 ACTIVE SITE CLEFT OF THE COMPLEX.  THE FINAL LIGAND
REMARK 600 OBSERVED IN THIS STRUCTURE PROBABLY IS THE RESULT OF
REMARK 600 SUCCESSIVE EVENTS LIKE HYDROLYSIS TRANSGLOCOSYLATION AND
REMARK 600 CONDENSATION THAT MAY OCCUR IN THE ACTIVE CENTER OF PPA.
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 ASP A 167   OD2
REMARK 620 2 HOH A 520   O    73.5
REMARK 620 3 HOH A 539   O    99.1  65.0
REMARK 620 4 HOH A 527   O    83.9 143.8 148.3
REMARK 620 5 HIS A 201   O   157.0 127.5  84.6  81.4
REMARK 620 6 ASP A 167   OD1  48.3  77.4 137.0  66.5 137.1
REMARK 620 7 ARG A 158   O    78.9 123.7  72.5  77.3  80.7 116.6
REMARK 620 8 ASN A 100   OD1 123.6  74.0 107.2  96.8  75.9  80.3 156.5
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE 1
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE 2
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE 3
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE 4
REMARK 800 SITE_IDENTIFIER: AS5
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE 5
REMARK 800 SITE_IDENTIFIER: CAL
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE
REMARK 800 SITE_IDENTIFIER: CLO
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CHLORIDE BINDING SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 990
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 991
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAF A 992
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 993
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 498
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
DBREF  1PPI A    1   496  UNP    P00690   AMYP_PIG         1    496
SEQADV 1PPI VAL A   49  UNP  P00690    ILE    49 CONFLICT
SEQADV 1PPI LYS A  243  UNP  P00690    GLN   243 CONFLICT
SEQADV 1PPI SER A  310  UNP  P00690    ALA   310 CONFLICT
SEQRES   1 A  496  GLN TYR ALA PRO GLN THR GLN SER GLY ARG THR SER ILE
SEQRES   2 A  496  VAL HIS LEU PHE GLU TRP ARG TRP VAL ASP ILE ALA LEU
SEQRES   3 A  496  GLU CYS GLU ARG TYR LEU GLY PRO LYS GLY PHE GLY GLY
SEQRES   4 A  496  VAL GLN VAL SER PRO PRO ASN GLU ASN VAL VAL VAL THR
SEQRES   5 A  496  ASN PRO SER ARG PRO TRP TRP GLU ARG TYR GLN PRO VAL
SEQRES   6 A  496  SER TYR LYS LEU CYS THR ARG SER GLY ASN GLU ASN GLU
SEQRES   7 A  496  PHE ARG ASP MET VAL THR ARG CYS ASN ASN VAL GLY VAL
SEQRES   8 A  496  ARG ILE TYR VAL ASP ALA VAL ILE ASN HIS MET CYS GLY
SEQRES   9 A  496  SER GLY ALA ALA ALA GLY THR GLY THR THR CYS GLY SER
SEQRES  10 A  496  TYR CYS ASN PRO GLY SER ARG GLU PHE PRO ALA VAL PRO
SEQRES  11 A  496  TYR SER ALA TRP ASP PHE ASN ASP GLY LYS CYS LYS THR
SEQRES  12 A  496  ALA SER GLY GLY ILE GLU SER TYR ASN ASP PRO TYR GLN
SEQRES  13 A  496  VAL ARG ASP CYS GLN LEU VAL GLY LEU LEU ASP LEU ALA
SEQRES  14 A  496  LEU GLU LYS ASP TYR VAL ARG SER MET ILE ALA ASP TYR
SEQRES  15 A  496  LEU ASN LYS LEU ILE ASP ILE GLY VAL ALA GLY PHE ARG
SEQRES  16 A  496  ILE ASP ALA SER LYS HIS MET TRP PRO GLY ASP ILE LYS
SEQRES  17 A  496  ALA VAL LEU ASP LYS LEU HIS ASN LEU ASN THR ASN TRP
SEQRES  18 A  496  PHE PRO ALA GLY SER ARG PRO PHE ILE PHE GLN GLU VAL
SEQRES  19 A  496  ILE ASP LEU GLY GLY GLU ALA ILE LYS SER SER GLU TYR
SEQRES  20 A  496  PHE GLY ASN GLY ARG VAL THR GLU PHE LYS TYR GLY ALA
SEQRES  21 A  496  LYS LEU GLY THR VAL VAL ARG LYS TRP SER GLY GLU LYS
SEQRES  22 A  496  MET SER TYR LEU LYS ASN TRP GLY GLU GLY TRP GLY PHE
SEQRES  23 A  496  MET PRO SER ASP ARG ALA LEU VAL PHE VAL ASP ASN HIS
SEQRES  24 A  496  ASP ASN GLN ARG GLY HIS GLY ALA GLY GLY SER SER ILE
SEQRES  25 A  496  LEU THR PHE TRP ASP ALA ARG LEU TYR LYS VAL ALA VAL
SEQRES  26 A  496  GLY PHE MET LEU ALA HIS PRO TYR GLY PHE THR ARG VAL
SEQRES  27 A  496  MET SER SER TYR ARG TRP ALA ARG ASN PHE VAL ASN GLY
SEQRES  28 A  496  GLU ASP VAL ASN ASP TRP ILE GLY PRO PRO ASN ASN ASN
SEQRES  29 A  496  GLY VAL ILE LYS GLU VAL THR ILE ASN ALA ASP THR THR
SEQRES  30 A  496  CYS GLY ASN ASP TRP VAL CYS GLU HIS ARG TRP ARG GLU
SEQRES  31 A  496  ILE ARG ASN MET VAL TRP PHE ARG ASN VAL VAL ASP GLY
SEQRES  32 A  496  GLU PRO PHE ALA ASN TRP TRP ASP ASN GLY SER ASN GLN
SEQRES  33 A  496  VAL ALA PHE GLY ARG GLY ASN ARG GLY PHE ILE VAL PHE
SEQRES  34 A  496  ASN ASN ASP ASP TRP GLN LEU SER SER THR LEU GLN THR
SEQRES  35 A  496  GLY LEU PRO GLY GLY THR TYR CYS ASP VAL ILE SER GLY
SEQRES  36 A  496  ASP LYS VAL GLY ASN SER CYS THR GLY ILE LYS VAL TYR
SEQRES  37 A  496  VAL SER SER ASP GLY THR ALA GLN PHE SER ILE SER ASN
SEQRES  38 A  496  SER ALA GLU ASP PRO PHE ILE ALA ILE HIS ALA GLU SER
SEQRES  39 A  496  LYS LEU
HET    GLC  A 990      11
HET    GLC  A 991      11
HET    DAF  A 992      21
HET    BGC  A 993      12
HET     CL  A 498       1
HET     CA  A 500       1
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     DAF 1,4-DEOXY-4-((5-HYDROXYMETHYL-2,3,4-TRIHYDROXYCYCLOHEX-
HETNAM   2 DAF  5-ENYL)AMINO)FRUCTOSE
HETNAM     BGC BETA-D-GLUCOSE
HETNAM      CL CHLORIDE ION
HETNAM      CA CALCIUM ION
FORMUL   2  GLC    2(C6 H12 O6)
FORMUL   2  DAF    C13 H23 N O7
FORMUL   2  BGC    C6 H12 O6
FORMUL   3   CL    CL 1-
FORMUL   4   CA    CA 2+
FORMUL   5  HOH   *393(H2 O)
HELIX    1 A1A ARG A   20  ARG A   30  1                                  11
HELIX    2 A1B TYR A   31  GLY A   36  1                                   6
HELIX    3  H1 PRO A   57  GLN A   63  13 CONSECUTIVE BETA TURNS           7
HELIX    4  A2 ASN A   75  ARG A   92  1                                  18
HELIX    5  H2 ASN A  120  ARG A  124  12 CONSECUTIVE BETA TURNS           5
HELIX    6  A3 LYS A  172  GLY A  190  1                                  19
HELIX    7  A4 TRP A  203  ASP A  212  1                                  10
HELIX    8  A5 SER A  244  ASN A  250  5                                   7
HELIX    9 A6A PHE A  256  LYS A  268  1                                  13
HELIX   10 A6B LYS A  273  TRP A  280  52 CONSECUTIVE BETA TURNS           8
HELIX   11  H3 GLY A  281  GLY A  285  52 CONSECUTIVE BETA TURNS           5
HELIX   12  H4 PRO A  288  ALA A  292  52 CONSECUTIVE BETA TURNS           5
HELIX   13  H5 ASP A  300  GLY A  304  52 CONSECUTIVE BETA TURNS           5
HELIX   14  A7 ASP A  317  HIS A  331  1                                  15
HELIX   15  H6 CYS A  384  TRP A  388  52 CONSECUTIVE BETA TURNS           5
HELIX   16  A8 TRP A  388  ASP A  402  1                                  15
HELIX   17  B1 ASP A  153  ASP A  159  1                                   7
SHEET    1  A1 8 SER A  12  LEU A  16  0
SHEET    2  A1 8 GLY A  38  VAL A  42  1  N  GLY A  38   O  SER A  12
SHEET    3  A1 8 ARG A  92  ALA A  97  1  N  ARG A  92   O  GLY A  38
SHEET    4  A1 8 ALA A 192  ASP A 197  1  N  ALA A 192   O  ILE A  93
SHEET    5  A1 8 PHE A 229  GLU A 233  1  N  PHE A 229   O  ALA A 192
SHEET    6  A1 8 ARG A 252  GLU A 255  1  N  ARG A 252   O  ILE A 230
SHEET    7  A1 8 ARG A 291  VAL A 294  1  O  ARG A 291   N  VAL A 253
SHEET    8  A1 8 PHE A 335  SER A 340  1  N  PHE A 335   O  ALA A 292
SHEET    1  A2 4 SER A  73  GLU A  76  0
SHEET    2  A2 4 LEU A  69  THR A  71 -1  O  CYS A  70   N  SER A  73
SHEET    3  A2 4 PRO A  45  VAL A  50 -1  O  PRO A  45   N  CYS A  70
SHEET    4  A2 4 GLY A 110  THR A 114 -1  N  THR A 114   O  ASN A  48
SHEET    1  A3 2 ASN A 347  VAL A 349  0
SHEET    2  A3 2 GLU A 352  VAL A 354 -1  N  VAL A 354   O  ASN A 347
SHEET    1  A4 2 THR A 371  ASN A 373  0
SHEET    2  A4 2 THR A 376  GLY A 379 -1  N  GLY A 379   O  THR A 371
SHEET    1  B1 4 GLY A 110  THR A 114  0
SHEET    2  B1 4 CYS A 119  PRO A 121 -1  O  CYS A 119   N  GLY A 110
SHEET    3  B1 4 ARG A 124  PRO A 127 -1  N  ARG A 124   O  PRO A 121
SHEET    4  B1 4 TYR A 131  ALA A 133 -1  N  ALA A 133   O  ARG A 124
SHEET    1  B2 3 ASN A 100  SER A 105  0
SHEET    2  B2 3 GLY A 164  ALA A 169 -1  N  LEU A 168   O  ASN A 100
SHEET    3  B2 3 ASP A 135  ASN A 137 -1  O  ASP A 135   N  ALA A 169
SHEET    1  B3 3 GLY A 146  ILE A 148  0
SHEET    2  B3 3 GLN A 161  LEU A 162  1  N  GLN A 161   O  GLY A 146
SHEET    3  B3 3 GLY A 164  ALA A 169  1  N  LEU A 165   O  LEU A 162
SHEET    1  C1 4 PRO A 405  ASN A 412  0
SHEET    2  C1 4 ASN A 415  GLY A 422 -1  O  GLN A 416   N  ASN A 412
SHEET    3  C1 4 ARG A 424  ASN A 431 -1  N  ASN A 431   O  ASN A 415
SHEET    4  C1 4 PRO A 486  ALA A 492 -1  O  PRO A 486   N  ASN A 430
SHEET    1  C2 4 LEU A 436  THR A 442  0
SHEET    2  C2 4 GLY A 473  ILE A 479 -1  O  GLY A 473   N  THR A 442
SHEET    3  C2 4 ILE A 465  SER A 470 -1  O  SER A 470   N  GLY A 473
SHEET    4  C2 4 GLY A 447  ASP A 451 -1  N  GLY A 447   O  VAL A 469
SHEET    1  C3 2 ASP A 456  VAL A 458  0
SHEET    2  C3 2 SER A 461  THR A 463 -1  N  THR A 463   O  ASP A 456
SSBOND   1 CYS A   28    CYS A   86                          1555   1555  2.03
SSBOND   2 CYS A   70    CYS A  115                          1555   1555  2.01
SSBOND   3 CYS A  141    CYS A  160                          1555   1555  2.03
SSBOND   4 CYS A  378    CYS A  384                          1555   1555  2.01
SSBOND   5 CYS A  450    CYS A  462                          1555   1555  2.03
LINK         C1  GLC A 990                 O4  GLC A 991     1555   1555  1.41
LINK         C1  GLC A 991                 O4H DAF A 992     1555   1555  1.41
LINK        CA    CA A 500                 OD2 ASP A 167     1555   1555  2.56
LINK        CA    CA A 500                 O   HOH A 520     1555   1555  2.29
LINK        CA    CA A 500                 O   HOH A 539     1555   1555  2.41
LINK        CA    CA A 500                 O   HOH A 527     1555   1555  2.51
LINK        CA    CA A 500                 O   HIS A 201     1555   1555  2.20
LINK        CA    CA A 500                 OD1 ASP A 167     1555   1555  2.59
LINK        CA    CA A 500                 O   ARG A 158     1555   1555  2.26
LINK        CA    CA A 500                 OD1 ASN A 100     1555   1555  2.32
LINK         C1  DAF A 992                 O4  BGC A 993     1555   1555  1.42
CISPEP   1 ASN A   53    PRO A   54          0        -6.53
CISPEP   2 VAL A  129    PRO A  130          0        -2.74
SITE     1 AS1  3 VAL A 163  GLN A  63  LEU A 165
SITE     1 AS2  3 HIS A 305  GLN A  63  TRP A  59
SITE     1 AS3  4 ASP A 300  HIS A 299  ASP A 197  HIS A 101
SITE     1 AS4  3 HIS A 201  GLU A 233  ASP A 300
SITE     1 AS5  2 GLU A 240  LYS A 200
SITE     1 CAL  4 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     1 CLO  3 ARG A 195  ASN A 298  ARG A 337
SITE     1 AC1 12 TRP A  59  GLN A  63  GLY A 104  VAL A 163
SITE     2 AC1 12 LEU A 165  HOH A 679  HOH A 864A HOH A 876A
SITE     3 AC1 12 HOH A 892A HOH A 918A HOH A 939A GLC A 991
SITE     1 AC2  8 TRP A  59  TYR A  62  GLN A  63  VAL A 163
SITE     2 AC2  8 HIS A 305  HOH A 659  GLC A 990  DAF A 992
SITE     1 AC3 13 TRP A  58  TYR A  62  HIS A 101  ARG A 195
SITE     2 AC3 13 ASP A 197  ALA A 198  HIS A 201  GLU A 233
SITE     3 AC3 13 HIS A 299  ASP A 300  GLY A 306  HOH A 930A
SITE     4 AC3 13 GLC A 991
SITE     1 AC4  8 TYR A 151  LYS A 200  ILE A 235  GLU A 240
SITE     2 AC4  8 GLY A 306  HOH A 883A HOH A 897A DAF A 992
SITE     1 AC5  3 ARG A 195  ASN A 298  ARG A 337
SITE     1 AC6  7 ASN A 100  ARG A 158  ASP A 167  HIS A 201
SITE     2 AC6  7 HOH A 520  HOH A 527  HOH A 539
CRYST1   56.300   87.800  103.400  90.00  90.00  90.00 P 21 21 21    4
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      0.017762  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011390  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009671        0.00000
      
PROCHECK
Go to PROCHECK summary
 References