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PDBsum entry 2guy

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Hydrolase PDB id
2guy
Jmol
Contents
Protein chain
476 a.a.
Ligands
NAG-NAG-BMA
Metals
_CA
Waters ×564
HEADER    HYDROLASE                               02-MAY-06   2GUY
TITLE     ORTHORHOMBIC CRYSTAL STRUCTURE (SPACE GROUP P21212) OF ASPERGILLUS
TITLE    2 NIGER ALPHA-AMYLASE AT 1.6 A RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ALPHA-AMYLASE A;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: TAKA-AMYLASE A, TAA, 1,4- ALPHA-D-GLUCAN GLUCANOHYDROLASE;
COMPND   5 EC: 3.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE   3 ORGANISM_TAXID: 5062
KEYWDS    (BETA-ALPHA) 8 BARREL, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.VUJICIC ZAGAR
REVDAT   3   13-JUL-11 2GUY    1       VERSN
REVDAT   2   24-FEB-09 2GUY    1       VERSN
REVDAT   1   15-AUG-06 2GUY    0
JRNL        AUTH   A.VUJICIC-ZAGAR,B.W.DIJKSTRA
JRNL        TITL   MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE
JRNL        TITL 2 IN COMPLEX WITH MALTOSE AT 1.8 ANGSTROMS RESOLUTION.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   716 2006
JRNL        REFN                   ESSN 1744-3091
JRNL        PMID   16880540
JRNL        DOI    10.1107/S1744309106024729
REMARK   2
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9
REMARK   3   NUMBER OF REFLECTIONS             : 60711
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 + TEST SET) : 0.165
REMARK   3   R VALUE            (WORKING SET) : 0.164
REMARK   3   FREE R VALUE                     : 0.196
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3245
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.59
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3418
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.80
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520
REMARK   3   BIN FREE R VALUE SET COUNT          : 183
REMARK   3   BIN FREE R VALUE                    : 0.2720
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3686
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 40
REMARK   3   SOLVENT ATOMS            : 564
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.31
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.79000
REMARK   3    B22 (A**2) : 1.08000
REMARK   3    B33 (A**2) : -0.29000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.085
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.205
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3828 ; 0.014 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5234 ; 1.483 ; 1.952
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   475 ; 5.772 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;35.711 ;25.115
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   567 ;13.725 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;10.104 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   579 ; 0.110 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2950 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1903 ; 0.217 ; 0.300
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2703 ; 0.324 ; 0.500
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   815 ; 0.172 ; 0.500
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.030 ; 0.500
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.235 ; 0.300
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    98 ; 0.279 ; 0.500
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2394 ; 1.158 ; 2.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3805 ; 1.726 ; 3.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1659 ; 1.482 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1429 ; 2.129 ; 3.000
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 1
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A     1        A   476
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5739   6.5953  18.7641
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0168 T22:  -0.0169
REMARK   3      T33:  -0.0373 T12:   0.0354
REMARK   3      T13:   0.0160 T23:  -0.0221
REMARK   3    L TENSOR
REMARK   3      L11:   1.0247 L22:   0.8174
REMARK   3      L33:   0.6026 L12:  -0.3997
REMARK   3      L13:   0.0484 L23:  -0.2453
REMARK   3    S TENSOR
REMARK   3      S11:   0.1099 S12:   0.1992 S13:   0.0083
REMARK   3      S21:  -0.0613 S22:  -0.1166 S23:  -0.0204
REMARK   3      S31:  -0.0035 S32:  -0.0366 S33:   0.0068
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2GUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-06.
REMARK 100 THE RCSB ID CODE IS RCSB037580.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-AUG-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID23-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91835
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PRODC
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65130
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.07900
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) : 1.59
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.55600
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 7TAA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M NA-ACETATE, 0.1M NA
REMARK 280  -CACODYLATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       51.39950
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.61400
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.39950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.61400
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A1252  LIES ON A SPECIAL POSITION.
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     SER A   477
REMARK 465     SER A   478
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NZ   LYS A   412     CE1  TYR A   419              2.02
REMARK 500   O    HOH A  1147     O    HOH A  1521              2.09
REMARK 500   O    HOH A  1177     O    HOH A  1443              2.12
REMARK 500   O    HOH A  1311     O    HOH A  1375              2.12
REMARK 500   OE1  GLU A   109     O    HOH A  1452              2.13
REMARK 500   O    HOH A  1112     O    HOH A  1446              2.17
REMARK 500   OG   SER A   422     ND2  ASN A   450              2.17
REMARK 500   O    HOH A  1134     O    HOH A  1566              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A  1227     O    HOH A  1302     2555     2.03
REMARK 500   O    HOH A  1428     O    HOH A  1441     3556     2.13
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    ALA A  78       45.81    -79.57
REMARK 500    TRP A  83       61.50   -119.95
REMARK 500    GLN A  85      -34.80   -130.64
REMARK 500    ALA A 329      121.60    -36.03
REMARK 500    ASP A 340      126.94    -33.64
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 A1123        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A1444        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A1470        DISTANCE =  6.13 ANGSTROMS
REMARK 525    HOH A1540        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH A1555        DISTANCE =  5.04 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 601  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1050   O
REMARK 620 2 GLU A 162   O    73.9
REMARK 620 3 ASP A 175   OD2  88.7  78.1
REMARK 620 4 HOH A1026   O   144.2  72.5  96.4
REMARK 620 5 HOH A1194   O   144.7 132.4  77.4  70.4
REMARK 620 6 ASP A 175   OD1  68.3 115.7  51.7 139.5  77.8
REMARK 620 7 ASN A 121   OD1  88.7 152.1 124.0 116.4  73.4  75.8
REMARK 620 8 HIS A 210   O    80.1  81.7 159.0  83.0 121.4 136.1  73.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7TAA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FAMILY 13 ALPHA AMYLASE FROM
REMARK 900 ASPERGILLUS ORYZAE IN COMPLEX WITH ACARBOSE
REMARK 900 RELATED ID: 6TAA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN A DIFFERENT
REMARK 900 CRYSTAL FORM
REMARK 900 RELATED ID: 2TAA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN A DIFFERENT
REMARK 900 CRYSTAL FORM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CURRENTLY THERE IS NO AMINOACID SEQUENCE DATABASE REFERENCE
REMARK 999 AVAILABLE FOR THE PROTEIN
DBREF  2GUY A    1   478  UNP    P0C1B3   AMYA1_ASPOR     22    499
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER
MODRES 2GUY ASN A  197  ASN  GLYCOSYLATION SITE
HET    NAG  A1000      14
HET    NAG  A1001      14
HET    BMA  A1002      11
HET     CA  A 601       1
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BMA BETA-D-MANNOSE
HETNAM      CA CALCIUM ION
FORMUL   2  NAG    2(C8 H15 N O6)
FORMUL   2  BMA    C6 H12 O6
FORMUL   3   CA    CA 2+
FORMUL   4  HOH   *564(H2 O)
HELIX    1   1 THR A    2  ARG A    7  1                                   6
HELIX    2   2 LEU A   15  ALA A   20  1                                   6
HELIX    3   3 ASN A   31  GLN A   35  5                                   5
HELIX    4   4 THR A   41  LYS A   48  1                                   8
HELIX    5   5 LYS A   48  GLY A   54  1                                   7
HELIX    6   6 THR A   96  ARG A  110  1                                  15
HELIX    7   7 ALA A  128  VAL A  132  5                                   5
HELIX    8   8 ASP A  133  PHE A  137  5                                   5
HELIX    9   9 SER A  142  PHE A  146  5                                   5
HELIX   10  10 ASP A  157  CYS A  164  1                                   8
HELIX   11  11 LYS A  180  SER A  199  1                                  20
HELIX   12  12 THR A  207  VAL A  211  5                                   5
HELIX   13  13 GLN A  212  ASP A  214  5                                   3
HELIX   14  14 PHE A  215  GLY A  224  1                                  10
HELIX   15  15 ASP A  235  CYS A  240  1                                   6
HELIX   16  16 PRO A  241  VAL A  245  5                                   5
HELIX   17  17 ASN A  251  LYS A  263  1                                  13
HELIX   18  18 SER A  268  CYS A  283  1                                  16
HELIX   19  19 ASP A  285  LEU A  288  5                                   4
HELIX   20  20 ARG A  300  TYR A  304  5                                   5
HELIX   21  21 ASP A  307  ASN A  321  1                                  15
HELIX   22  22 GLY A  330  HIS A  334  5                                   5
HELIX   23  23 ALA A  346  GLY A  351  5                                   6
HELIX   24  24 SER A  356  ASP A  376  1                                  21
HELIX   25  25 GLU A  467  ALA A  470  5                                   4
SHEET    1   A 8 GLY A 248  VAL A 249  0
SHEET    2   A 8 TYR A 226  GLY A 229  1  N  GLY A 229   O  GLY A 248
SHEET    3   A 8 GLY A 202  ILE A 205  1  N  ILE A 205   O  ILE A 228
SHEET    4   A 8 TYR A 113  VAL A 118  1  N  VAL A 118   O  ARG A 204
SHEET    5   A 8 ALA A  59  ILE A  62  1  N  ILE A  60   O  MET A 115
SHEET    6   A 8 ILE A  11  LEU A  14  1  N  LEU A  14   O  TRP A  61
SHEET    7   A 8 ILE A 324  TYR A 328  1  O  PRO A 325   N  ILE A  11
SHEET    8   A 8 GLY A 290  THR A 291  1  N  THR A 291   O  ILE A 326
SHEET    1   B 2 THR A  66  GLN A  68  0
SHEET    2   B 2 GLN A  84  LEU A  90 -1  O  GLN A  85   N  ALA A  67
SHEET    1   C 3 TYR A 125  ASP A 126  0
SHEET    2   C 3 VAL A 171  LEU A 173 -1  O  SER A 172   N  TYR A 125
SHEET    3   C 3 LEU A 166  GLY A 167 -1  N  LEU A 166   O  LEU A 173
SHEET    1   D 6 TRP A 385  ASP A 390  0
SHEET    2   D 6 THR A 393  LYS A 398 -1  O  ALA A 395   N  TYR A 388
SHEET    3   D 6 ILE A 405  SER A 410 -1  O  LEU A 409   N  ILE A 394
SHEET    4   D 6 ARG A 461  PRO A 465 -1  O  LEU A 463   N  VAL A 406
SHEET    5   D 6 GLN A 433  GLU A 436 -1  N  THR A 435   O  TYR A 464
SHEET    6   D 6 THR A 441  THR A 444 -1  O  VAL A 443   N  LEU A 434
SHEET    1   E 2 TYR A 419  LEU A 423  0
SHEET    2   E 2 VAL A 451  MET A 455 -1  O  MET A 455   N  TYR A 419
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.13
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.49
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.04
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  2.05
LINK         ND2 ASN A 197                 C1  NAG A1000     1555   1555  1.45
LINK         O4  NAG A1000                 C1  NAG A1001     1555   1555  1.44
LINK         O4  NAG A1001                 C1  BMA A1002     1555   1555  1.46
LINK        CA    CA A 601                 O   HOH A1050     1555   1555  2.51
LINK        CA    CA A 601                 O   GLU A 162     1555   1555  2.44
LINK        CA    CA A 601                 OD2 ASP A 175     1555   1555  2.50
LINK        CA    CA A 601                 O   HOH A1026     1555   1555  2.48
LINK        CA    CA A 601                 O   HOH A1194     1555   1555  2.43
LINK        CA    CA A 601                 OD1 ASP A 175     1555   1555  2.61
LINK        CA    CA A 601                 OD1 ASN A 121     1555   1555  2.38
LINK        CA    CA A 601                 O   HIS A 210     1555   1555  2.41
CISPEP   1 LYS A  138    PRO A  139          0         4.88
CISPEP   2 ASP A  340    PRO A  341          0         5.20
SITE     1 AC1  7 TYR A  88  TRP A 190  SER A 193  ASN A 197
SITE     2 AC1  7 NAG A1001  HOH A1080  HOH A1246
SITE     1 AC2  3 NAG A1000  BMA A1002  HOH A1367
SITE     1 AC3  1 NAG A1001
SITE     1 AC4  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210
SITE     2 AC4  7 HOH A1026  HOH A1050  HOH A1194
CRYST1  102.799   63.228   74.456  90.00  90.00  90.00 P 21 21 2     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      0.009728  0.000000  0.000000        0.00000
SCALE2      0.000000  0.015816  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013431        0.00000
      
PROCHECK
Go to PROCHECK summary
 References