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PDBsum entry 1mwo

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Hydrolase PDB id
1mwo
Jmol
Contents
Protein chain
434 a.a. *
Metals
_CA
_ZN ×6
Waters ×398
* Residue conservation analysis
HEADER    HYDROLASE                               30-SEP-02   1MWO
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE HYPERTHERMOSTABLE
TITLE    2 PYROCOOCUS WOESEI ALPHA-AMYLASE
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: PYROCOCCUS WOESEI;
SOURCE   3 ORGANISM_TAXID: 2262;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS    (BETA/ALPHA)8-BARREL, ALPHA-AMYLASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.LINDEN,O.MAYANS,W.MEYER-KLAUCKE,G.ANTRANIKIAN,M.WILMANNS
REVDAT   2   24-FEB-09 1MWO    1       VERSN
REVDAT   1   10-JUN-03 1MWO    0
JRNL        AUTH   A.LINDEN,O.MAYANS,W.MEYER-KLAUCKE,G.ANTRANIKIAN,
JRNL        AUTH 2 M.WILMANNS
JRNL        TITL   DIFFERENTIAL REGULATION OF A HYPERTHERMOPHILIC
JRNL        TITL 2 ALPHA-AMYLASE WITH A NOVEL (CA,ZN) TWO-METAL
JRNL        TITL 3 CENTER BY ZINC
JRNL        REF    J.BIOL.CHEM.                  V. 278  9875 2003
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12482867
JRNL        DOI    10.1074/JBC.M211339200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
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)   (%) : 95.3
REMARK   3   NUMBER OF REFLECTIONS             : 25967
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.190
REMARK   3   FREE R VALUE                     : 0.224
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 995
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            : 3569
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 7
REMARK   3   SOLVENT ATOMS            : 398
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 27.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -8.71300
REMARK   3    B22 (A**2) : 4.14900
REMARK   3    B33 (A**2) : 4.56300
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) : 0.26
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) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.32
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  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1MWO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-02.
REMARK 100 THE RCSB ID CODE IS RCSB017254.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : X11
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91
REMARK 200  MONOCHROMATOR                  : TRIANGULAR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26004
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.06000
REMARK 200   FOR THE DATA SET  : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.17800
REMARK 200   FOR SHELL         : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-MME 550, ZINC SULFATE, MES, PH
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
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       31.44000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.14450
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.10000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.14450
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.44000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.10000
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     GLY A   435
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    TYR A   3     -100.89   -113.99
REMARK 500    ALA A  15       40.53    -78.60
REMARK 500    PHE A  16     -178.84   -172.96
REMARK 500    TRP A 177      -21.73   -153.75
REMARK 500    SER A 179      165.31    168.47
REMARK 500    ASN A 257       31.27   -148.72
REMARK 500    ASP A 291       74.17   -156.67
REMARK 500    GLU A 319      -60.72   -141.38
REMARK 500    TYR A 346      143.87   -172.71
REMARK 500    ASP A 358     -163.99   -125.49
REMARK 500    LEU A 364     -178.46   -170.65
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 569        DISTANCE =  6.95 ANGSTROMS
REMARK 525    HOH A 707        DISTANCE =  7.86 ANGSTROMS
REMARK 525    HOH A 728        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH A 750        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH A 768        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH A 815        DISTANCE =  5.32 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                              ZN A 438  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A  33   NZ
REMARK 620 2 GLU A  36   OE1 109.5
REMARK 620 3 GLU A 318   OE2 112.6  96.0
REMARK 620 4 LYS A 323   NZ  128.1 113.3  90.7
REMARK 620 5 GLU A 318   OE1  78.3 152.2  57.2  77.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 440  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  80   OE2
REMARK 620 2 GLU A  88   OE2 111.2
REMARK 620 3 GLU A 253   OE1  83.0  86.8
REMARK 620 4 GLU A 253   OE2 115.1 114.2  56.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 442  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 110   ND2
REMARK 620 2 ASP A 155   OD1 153.0
REMARK 620 3 ASP A 155   OD2 129.8  52.0
REMARK 620 4 GLY A 157   O    82.7  79.1 125.1
REMARK 620 5 ASP A 164   OD1 131.2  72.2  88.1 100.4
REMARK 620 6 ASP A 164   OD2  82.9 110.5 140.3  73.8  52.6
REMARK 620 7 GLY A 202   O    71.7  86.6  71.4  83.9 157.0 148.2
REMARK 620 8 HOH A 478   O    78.0 124.4  80.0 154.8  80.9  87.8 104.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 436  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 147   NE2
REMARK 620 2 HIS A 152   NE2 102.4
REMARK 620 3 CYS A 166   SG  116.2 115.3
REMARK 620 4 HOH A 816   O   109.6 100.4 111.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 441  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 222   OE2
REMARK 620 2 HOH A 553   O   152.7
REMARK 620 3 HOH A 822   O   109.2  92.0
REMARK 620 4 HOH A 655   O    81.3  82.1  89.2
REMARK 620 5 GLU A 222   OE1  56.9 100.2 165.7  85.1
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 437  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 252   OD1
REMARK 620 2 ASP A 256   OD2  99.3
REMARK 620 3 ILE A 292   O   107.1  99.4
REMARK 620 4 GLU A  87   OE1  98.3  93.6 149.1
REMARK 620 5 GLU A  87   OE2 139.6 113.5  90.7  58.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 439  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 347   OD2
REMARK 620 2 ASP A 349   OD1 104.3
REMARK 620 3 GLU A 350   OE1 105.2 119.7
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 436
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 437
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 438
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 439
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 440
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 441
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 442
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MXD   RELATED DB: PDB
REMARK 900 ALPHA AMYLASE WITH CARBOHYDRATES
REMARK 900 RELATED ID: 1MXG   RELATED DB: PDB
REMARK 900 ALPHA AMYLASE WITH CARBOHYDRATES
DBREF  1MWO A    1   435  UNP    O08452   O08452_PYRFU    26    460
SEQRES   1 A  435  ALA LYS TYR LEU GLU LEU GLU GLU GLY GLY VAL ILE MET
SEQRES   2 A  435  GLN ALA PHE TYR TRP ASP VAL PRO GLY GLY GLY ILE TRP
SEQRES   3 A  435  TRP ASP HIS ILE ARG SER LYS ILE PRO GLU TRP TYR GLU
SEQRES   4 A  435  ALA GLY ILE SER ALA ILE TRP LEU PRO PRO PRO SER LYS
SEQRES   5 A  435  GLY MET SER GLY GLY TYR SER MET GLY TYR ASP PRO TYR
SEQRES   6 A  435  ASP TYR PHE ASP LEU GLY GLU TYR TYR GLN LYS GLY THR
SEQRES   7 A  435  VAL GLU THR ARG PHE GLY SER LYS GLU GLU LEU VAL ARG
SEQRES   8 A  435  LEU ILE GLN THR ALA HIS ALA TYR GLY ILE LYS VAL ILE
SEQRES   9 A  435  ALA ASP VAL VAL ILE ASN HIS ARG ALA GLY GLY ASP LEU
SEQRES  10 A  435  GLU TRP ASN PRO PHE VAL GLY ASP TYR THR TRP THR ASP
SEQRES  11 A  435  PHE SER LYS VAL ALA SER GLY LYS TYR THR ALA ASN TYR
SEQRES  12 A  435  LEU ASP PHE HIS PRO ASN GLU LEU HIS CYS CYS ASP GLU
SEQRES  13 A  435  GLY THR PHE GLY GLY PHE PRO ASP ILE CYS HIS HIS LYS
SEQRES  14 A  435  GLU TRP ASP GLN TYR TRP LEU TRP LYS SER ASN GLU SER
SEQRES  15 A  435  TYR ALA ALA TYR LEU ARG SER ILE GLY PHE ASP GLY TRP
SEQRES  16 A  435  ARG PHE ASP TYR VAL LYS GLY TYR GLY ALA TRP VAL VAL
SEQRES  17 A  435  ARG ASP TRP LEU ASN TRP TRP GLY GLY TRP ALA VAL GLY
SEQRES  18 A  435  GLU TYR TRP ASP THR ASN VAL ASP ALA LEU LEU SER TRP
SEQRES  19 A  435  ALA TYR GLU SER GLY ALA LYS VAL PHE ASP PHE PRO LEU
SEQRES  20 A  435  TYR TYR LYS MET ASP GLU ALA PHE ASP ASN ASN ASN ILE
SEQRES  21 A  435  PRO ALA LEU VAL TYR ALA LEU GLN ASN GLY GLN THR VAL
SEQRES  22 A  435  VAL SER ARG ASP PRO PHE LYS ALA VAL THR PHE VAL ALA
SEQRES  23 A  435  ASN HIS ASP THR ASP ILE ILE TRP ASN LYS TYR PRO ALA
SEQRES  24 A  435  TYR ALA PHE ILE LEU THR TYR GLU GLY GLN PRO VAL ILE
SEQRES  25 A  435  PHE TYR ARG ASP PHE GLU GLU TRP LEU ASN LYS ASP LYS
SEQRES  26 A  435  LEU ILE ASN LEU ILE TRP ILE HIS ASP HIS LEU ALA GLY
SEQRES  27 A  435  GLY SER THR THR ILE VAL TYR TYR ASP ASN ASP GLU LEU
SEQRES  28 A  435  ILE PHE VAL ARG ASN GLY ASP SER ARG ARG PRO GLY LEU
SEQRES  29 A  435  ILE THR TYR ILE ASN LEU SER PRO ASN TRP VAL GLY ARG
SEQRES  30 A  435  TRP VAL TYR VAL PRO LYS PHE ALA GLY ALA CYS ILE HIS
SEQRES  31 A  435  GLU TYR THR GLY ASN LEU GLY GLY TRP VAL ASP LYS ARG
SEQRES  32 A  435  VAL ASP SER SER GLY TRP VAL TYR LEU GLU ALA PRO PRO
SEQRES  33 A  435  HIS ASP PRO ALA ASN GLY TYR TYR GLY TYR SER VAL TRP
SEQRES  34 A  435  SER TYR CYS GLY VAL GLY
HET     ZN  A 436       1
HET     ZN  A 437       1
HET     ZN  A 438       1
HET     ZN  A 439       1
HET     ZN  A 440       1
HET     ZN  A 441       1
HET     CA  A 442       1
HETNAM      ZN ZINC ION
HETNAM      CA CALCIUM ION
FORMUL   2   ZN    6(ZN 2+)
FORMUL   8   CA    CA 2+
FORMUL   9  HOH   *398(H2 O)
HELIX    1   1 GLU A    5  GLY A    9  5                                   5
HELIX    2   2 ILE A   25  GLY A   41  1                                  17
HELIX    3   3 SER A   55  SER A   59  5                                   5
HELIX    4   4 SER A   85  TYR A   99  1                                  15
HELIX    5   5 ASN A  142  PHE A  146  5                                   5
HELIX    6   6 LYS A  169  TRP A  177  1                                   9
HELIX    7   7 SER A  182  ILE A  190  1                                   9
HELIX    8   8 TYR A  199  TYR A  203  5                                   5
HELIX    9   9 GLY A  204  GLY A  216  1                                  13
HELIX   10  10 ASN A  227  GLY A  239  1                                  13
HELIX   11  11 ASP A  244  ASP A  256  1                                  13
HELIX   12  12 ASN A  259  ASN A  269  1                                  11
HELIX   13  13 THR A  272  ASP A  277  1                                   6
HELIX   14  14 ASN A  295  TYR A  306  1                                  12
HELIX   15  15 TYR A  314  GLU A  319  1                                   6
HELIX   16  16 ASN A  322  LEU A  336  1                                  15
HELIX   17  17 PRO A  382  ALA A  385  5                                   4
HELIX   18  18 PRO A  419  GLY A  422  5                                   4
SHEET    1   A 9 ILE A  12  GLN A  14  0
SHEET    2   A 9 ALA A  44  LEU A  47  1  O  TRP A  46   N  MET A  13
SHEET    3   A 9 LYS A 102  VAL A 107  1  O  ILE A 104   N  ILE A  45
SHEET    4   A 9 GLY A 194  PHE A 197  1  O  ARG A 196   N  ALA A 105
SHEET    5   A 9 ALA A 219  GLY A 221  1  O  VAL A 220   N  PHE A 197
SHEET    6   A 9 LYS A 241  PHE A 243  1  O  LYS A 241   N  GLY A 221
SHEET    7   A 9 ALA A 281  PHE A 284  1  O  VAL A 282   N  VAL A 242
SHEET    8   A 9 GLN A 309  PHE A 313  1  O  VAL A 311   N  THR A 283
SHEET    9   A 9 ILE A  12  GLN A  14  1  N  ILE A  12   O  ILE A 312
SHEET    1   B 2 LYS A  52  GLY A  53  0
SHEET    2   B 2 PRO A  64  ASP A  66 -1  O  TYR A  65   N  LYS A  52
SHEET    1   C 2 ASP A 116  ASN A 120  0
SHEET    2   C 2 ASP A 125  ASP A 130 -1  O  ASP A 130   N  ASP A 116
SHEET    1   D 6 THR A 341  TYR A 346  0
SHEET    2   D 6 GLU A 350  ARG A 355 -1  O  VAL A 354   N  THR A 342
SHEET    3   D 6 LEU A 364  ASN A 369 -1  O  ILE A 368   N  LEU A 351
SHEET    4   D 6 TYR A 426  TYR A 431 -1  O  TRP A 429   N  ILE A 365
SHEET    5   D 6 ALA A 387  GLU A 391 -1  N  HIS A 390   O  SER A 430
SHEET    6   D 6 ASP A 401  VAL A 404 -1  O  VAL A 404   N  ALA A 387
SHEET    1   E 2 VAL A 375  TYR A 380  0
SHEET    2   E 2 TRP A 409  ALA A 414 -1  O  LEU A 412   N  ARG A 377
SHEET    1   F 2 HIS A 417  ASP A 418  0
SHEET    2   F 2 TYR A 423  TYR A 424 -1  O  TYR A 423   N  ASP A 418
SSBOND   1 CYS A  153    CYS A  154                          1555   1555  2.06
SSBOND   2 CYS A  388    CYS A  432                          1555   1555  2.04
LINK         NZ  LYS A  33                ZN    ZN A 438     1555   1555  2.10
LINK         OE1 GLU A  36                ZN    ZN A 438     1555   1555  1.94
LINK         OE2 GLU A  80                ZN    ZN A 440     1555   1555  1.93
LINK         OE2 GLU A  88                ZN    ZN A 440     1555   1555  1.93
LINK         ND2 ASN A 110                CA    CA A 442     1555   1555  2.59
LINK         NE2 HIS A 147                ZN    ZN A 436     1555   1555  2.03
LINK         NE2 HIS A 152                ZN    ZN A 436     1555   1555  1.94
LINK         OD1 ASP A 155                CA    CA A 442     1555   1555  2.63
LINK         OD2 ASP A 155                CA    CA A 442     1555   1555  2.34
LINK         O   GLY A 157                CA    CA A 442     1555   1555  2.30
LINK         OD1 ASP A 164                CA    CA A 442     1555   1555  2.27
LINK         OD2 ASP A 164                CA    CA A 442     1555   1555  2.62
LINK         SG  CYS A 166                ZN    ZN A 436     1555   1555  2.32
LINK         O   GLY A 202                CA    CA A 442     1555   1555  2.32
LINK         OE2 GLU A 222                ZN    ZN A 441     1555   1555  2.13
LINK         OD1 ASP A 252                ZN    ZN A 437     1555   1555  1.88
LINK         OD2 ASP A 256                ZN    ZN A 437     1555   1555  1.96
LINK         O   ILE A 292                ZN    ZN A 437     1555   1555  2.15
LINK         OE2 GLU A 318                ZN    ZN A 438     1555   1555  2.18
LINK         OD2 ASP A 347                ZN    ZN A 439     1555   1555  1.77
LINK         OD1 ASP A 349                ZN    ZN A 439     1555   1555  1.99
LINK         OE1 GLU A 350                ZN    ZN A 439     1555   1555  2.15
LINK        ZN    ZN A 436                 O   HOH A 816     1555   1555  1.98
LINK        ZN    ZN A 441                 O   HOH A 553     1555   1555  2.19
LINK        ZN    ZN A 441                 O   HOH A 822     1555   1555  2.14
LINK        CA    CA A 442                 O   HOH A 478     1555   1555  2.53
LINK        ZN    ZN A 438                 NZ  LYS A 323     1555   1555  2.61
LINK        ZN    ZN A 438                 OE1 GLU A 318     1555   1555  2.40
LINK        ZN    ZN A 441                 O   HOH A 655     1555   1555  2.42
LINK        ZN    ZN A 441                 OE1 GLU A 222     1555   1555  2.45
LINK        ZN    ZN A 437                 OE1 GLU A  87     1555   3645  2.50
LINK        ZN    ZN A 437                 OE2 GLU A  87     1555   3645  1.87
LINK        ZN    ZN A 440                 OE1 GLU A 253     1555   3655  2.50
LINK        ZN    ZN A 440                 OE2 GLU A 253     1555   3655  2.03
CISPEP   1 HIS A  147    PRO A  148          0        -0.02
SITE     1 AC1  4 HIS A 147  HIS A 152  CYS A 166  HOH A 816
SITE     1 AC2  5 GLU A  87  ASP A 252  ASP A 256  ILE A 292
SITE     2 AC2  5 ILE A 293
SITE     1 AC3  4 LYS A  33  GLU A  36  GLU A 318  LYS A 323
SITE     1 AC4  4 ASP A 347  ASP A 349  GLU A 350  ARG A 377
SITE     1 AC5  3 GLU A  80  GLU A  88  GLU A 253
SITE     1 AC6  5 GLU A 222  ASP A 289  HOH A 553  HOH A 655
SITE     2 AC6  5 HOH A 822
SITE     1 AC7  6 ASN A 110  ASP A 155  GLY A 157  ASP A 164
SITE     2 AC7  6 GLY A 202  HOH A 478
CRYST1   62.880   78.200  106.289  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      0.015903  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012788  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009408        0.00000
      
PROCHECK
Go to PROCHECK summary
 References