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PDBsum entry 1jd9

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Hydrolase PDB id
1jd9
Jmol
Contents
Protein chain
448 a.a. *
Metals
_CA
Waters ×190
* Residue conservation analysis
HEADER    HYDROLASE                               13-JUN-01   1JD9
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300Q OF
TITLE    2 PSEUDOALTEROMONAS HALOPLANCTIS 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;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOALTEROMONAS HALOPLANKTIS;
SOURCE   3 ORGANISM_TAXID: 228;
SOURCE   4 STRAIN: A23;
SOURCE   5 GENE: AMY;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PUC12;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PAH12WT;
SOURCE  11 EXPRESSION_SYSTEM_GENE: HB101
KEYWDS    ALPHA-BETA BARREL, GLYCOSYL HYDROLASE, ALLOSTERIC ACTIVATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.AGHAJARI,R.HASER
REVDAT   2   24-FEB-09 1JD9    1       VERSN
REVDAT   1   18-SEP-02 1JD9    0
JRNL        AUTH   N.AGHAJARI,G.FELLER,C.GERDAY,R.HASER
JRNL        TITL   STRUCTURAL BASIS OF ALPHA-AMYLASE ACTIVATION BY
JRNL        TITL 2 CHLORIDE
JRNL        REF    PROTEIN SCI.                  V.  11  1435 2002
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   12021442
JRNL        DOI    10.1110/PS.0202602
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   N.AGHAJARI,G.FELLER,C.GERDAY,R.HASER
REMARK   1  TITL   STRUCTURES OF THE PSYCHROPHILIC ALTEROMONAS
REMARK   1  TITL 2 HALOPLANCTIS ALPHA-AMYLASE GIVE INSIGHTS INTO COLD
REMARK   1  TITL 3 ADAPTATION AT A MOLECULAR LEVEL
REMARK   1  REF    STRUCTURE                     V.   6  1503 1998
REMARK   1  REFN                   ISSN 0969-2126
REMARK   1 REFERENCE 2
REMARK   1  AUTH   N.AGHAJARI,G.FELLER,C.GERDAY,R.HASER
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE PSYCHROPHILIC
REMARK   1  TITL 2 ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS IN ITS
REMARK   1  TITL 3 NATIVE FORM AND COMPLEXED WITH AN INHIBITOR
REMARK   1  REF    PROTEIN SCI.                  V.   7   564 1998
REMARK   1  REFN                   ISSN 0961-8368
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.843
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.70
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)   (%) : 82.4
REMARK   3   NUMBER OF REFLECTIONS             : 16727
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) : 0.180
REMARK   3   FREE R VALUE                     : 0.245
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1680
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) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350
REMARK   3   BIN FREE R VALUE                    : 0.3640
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 23
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            : 3443
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 1
REMARK   3   SOLVENT ATOMS            : 190
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 32.92
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) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1JD9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUN-01.
REMARK 100 THE RCSB ID CODE IS RCSB013647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-DEC-97
REMARK 200  TEMPERATURE           (KELVIN) : 288
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : COLLIMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16759
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.030
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.8
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.21600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 3.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 39.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.56400
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1AQH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, HEPES, PH 7, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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       57.70000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.70000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       35.75000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.20000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.75000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.20000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       57.70000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.75000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.20000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.70000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.75000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.20000
REMARK 290   SMTRY3   8  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 A1429  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     THR A   449
REMARK 465     SER A   450
REMARK 465     SER A   451
REMARK 465     ALA A   452
REMARK 465     SER A   453
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     GLU A 118    CG   CD   OE1  OE2
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    THR A   3      -14.24   -146.30
REMARK 500    GLU A  10       15.16     56.23
REMARK 500    TYR A  23      -55.40   -129.83
REMARK 500    SER A  59     -168.86   -123.17
REMARK 500    ASN A 129       57.08   -148.36
REMARK 500    ASP A 130       72.81   -179.98
REMARK 500    LEU A 241        1.22    -68.31
REMARK 500    ASP A 310      106.77    -54.55
REMARK 500    PHE A 329       -3.14     60.29
REMARK 500    ALA A 330     -129.36    -99.70
REMARK 500    ASN A 332     -113.27   -113.02
REMARK 500    ALA A 353        7.94    -68.90
REMARK 500    ASN A 355       83.41   -159.77
REMARK 500    TRP A 356       25.33    -78.92
REMARK 500    ASN A 360       61.23     39.58
REMARK 500    THR A 365       -3.66     75.97
REMARK 500    ASN A 366     -100.61   -134.03
REMARK 500    VAL A 404       -5.02    -59.07
REMARK 500    ASN A 432       77.98   -153.28
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 A1260        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH A1298        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH A1299        DISTANCE =  6.96 ANGSTROMS
REMARK 525    HOH A1418        DISTANCE =  7.40 ANGSTROMS
REMARK 525    HOH A1419        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH A1420        DISTANCE =  5.14 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 800  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A  88   OD1
REMARK 620 2 GLN A 135   O   149.9
REMARK 620 3 ASP A 144   OD1  82.8 121.5
REMARK 620 4 HIS A 178   O    64.8  85.1 135.7
REMARK 620 5 HOH A1117   O    98.0  80.2  63.8  90.6
REMARK 620 6 ASP A 144   OD2 130.9  79.0  53.8 163.8  83.4
REMARK 620 7 HOH A1118   O   109.1  64.5 141.2  80.5 144.1  95.6
REMARK 620 8 HOH A1437   O    70.3 125.1  84.7 109.4 147.8  82.8  66.4
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 CA A 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQH   RELATED DB: PDB
REMARK 900 1AQH CONTAINS THE SAME PROTEIN(WILD TYPE).
REMARK 900 RELATED ID: 1AQM   RELATED DB: PDB
REMARK 900 1AQM CONTAINS THE SAME PROTEIN COMPLEXED WITH TRIS.
REMARK 900 RELATED ID: 1JD7   RELATED DB: PDB
REMARK 900 1JD7 CONTAINS THE SAME PROTEIN(K300R MUTANT).
REMARK 900 RELATED ID: 1B0I   RELATED DB: PDB
REMARK 900 1B0I CONTAINS THE SAME PROTEIN WITH ANOTHER CRYSTAL FORM.
REMARK 900 RELATED ID: 1G94   RELATED DB: PDB
REMARK 900 1G94 CONTAINS THE SAME PROTEIN COMPLEXED WITH HEPTA-
REMARK 900 SACCHARIDE AND TRIS.
REMARK 900 RELATED ID: 1G9H   RELATED DB: PDB
REMARK 900 1G9H CONTAINS THE SAME PROTEIN COMPLEXED WITH TRI-
REMARK 900 SACCHARIDE AND TRIS.
DBREF  1JD9 A    1   453  UNP    P29957   AMY_ALTHA       25    477
SEQADV 1JD9 GLN A  300  UNP  P29957    LYS   324 ENGINEERED
SEQRES   1 A  453  THR PRO THR THR PHE VAL HIS LEU PHE GLU TRP ASN TRP
SEQRES   2 A  453  GLN ASP VAL ALA GLN GLU CYS GLU GLN TYR LEU GLY PRO
SEQRES   3 A  453  LYS GLY TYR ALA ALA VAL GLN VAL SER PRO PRO ASN GLU
SEQRES   4 A  453  HIS ILE THR GLY SER GLN TRP TRP THR ARG TYR GLN PRO
SEQRES   5 A  453  VAL SER TYR GLU LEU GLN SER ARG GLY GLY ASN ARG ALA
SEQRES   6 A  453  GLN PHE ILE ASP MET VAL ASN ARG CYS SER ALA ALA GLY
SEQRES   7 A  453  VAL ASP ILE TYR VAL ASP THR LEU ILE ASN HIS MET ALA
SEQRES   8 A  453  ALA GLY SER GLY THR GLY THR ALA GLY ASN SER PHE GLY
SEQRES   9 A  453  ASN LYS SER PHE PRO ILE TYR SER PRO GLN ASP PHE HIS
SEQRES  10 A  453  GLU SER CYS THR ILE ASN ASN SER ASP TYR GLY ASN ASP
SEQRES  11 A  453  ARG TYR ARG VAL GLN ASN CYS GLU LEU VAL GLY LEU ALA
SEQRES  12 A  453  ASP LEU ASP THR ALA SER ASN TYR VAL GLN ASN THR ILE
SEQRES  13 A  453  ALA ALA TYR ILE ASN ASP LEU GLN ALA ILE GLY VAL LYS
SEQRES  14 A  453  GLY PHE ARG PHE ASP ALA SER LYS HIS VAL ALA ALA SER
SEQRES  15 A  453  ASP ILE GLN SER LEU MET ALA LYS VAL ASN GLY SER PRO
SEQRES  16 A  453  VAL VAL PHE GLN GLU VAL ILE ASP GLN GLY GLY GLU ALA
SEQRES  17 A  453  VAL GLY ALA SER GLU TYR LEU SER THR GLY LEU VAL THR
SEQRES  18 A  453  GLU PHE LYS TYR SER THR GLU LEU GLY ASN THR PHE ARG
SEQRES  19 A  453  ASN GLY SER LEU ALA TRP LEU SER ASN PHE GLY GLU GLY
SEQRES  20 A  453  TRP GLY PHE MET PRO SER SER SER ALA VAL VAL PHE VAL
SEQRES  21 A  453  ASP ASN HIS ASP ASN GLN ARG GLY HIS GLY GLY ALA GLY
SEQRES  22 A  453  ASN VAL ILE THR PHE GLU ASP GLY ARG LEU TYR ASP LEU
SEQRES  23 A  453  ALA ASN VAL PHE MET LEU ALA TYR PRO TYR GLY TYR PRO
SEQRES  24 A  453  GLN VAL MET SER SER TYR ASP PHE HIS GLY ASP THR ASP
SEQRES  25 A  453  ALA GLY GLY PRO ASN VAL PRO VAL HIS ASN ASN GLY ASN
SEQRES  26 A  453  LEU GLU CYS PHE ALA SER ASN TRP LYS CYS GLU HIS ARG
SEQRES  27 A  453  TRP SER TYR ILE ALA GLY GLY VAL ASP PHE ARG ASN ASN
SEQRES  28 A  453  THR ALA ASP ASN TRP ALA VAL THR ASN TRP TRP ASP ASN
SEQRES  29 A  453  THR ASN ASN GLN ILE SER PHE GLY ARG GLY SER SER GLY
SEQRES  30 A  453  HIS MET ALA ILE ASN LYS GLU ASP SER THR LEU THR ALA
SEQRES  31 A  453  THR VAL GLN THR ASP MET ALA SER GLY GLN TYR CYS ASN
SEQRES  32 A  453  VAL LEU LYS GLY GLU LEU SER ALA ASP ALA LYS SER CYS
SEQRES  33 A  453  SER GLY GLU VAL ILE THR VAL ASN SER ASP GLY THR ILE
SEQRES  34 A  453  ASN LEU ASN ILE GLY ALA TRP ASP ALA MET ALA ILE HIS
SEQRES  35 A  453  LYS ASN ALA LYS LEU ASN THR SER SER ALA SER
HET     CA  A 800       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    CA 2+
FORMUL   3  HOH   *190(H2 O)
HELIX    1   1 ASN A   12  TYR A   23  1                                  12
HELIX    2   2 TYR A   23  GLY A   28  1                                   6
HELIX    3   3 GLN A   45  GLN A   51  5                                   7
HELIX    4   4 ASN A   63  GLY A   78  1                                  16
HELIX    5   5 SER A  112  ASP A  115  5                                   4
HELIX    6   6 SER A  125  ASP A  130  1                                   6
HELIX    7   7 ASP A  130  CYS A  137  1                                   8
HELIX    8   8 SER A  149  GLY A  167  1                                  19
HELIX    9   9 ALA A  175  VAL A  179  5                                   5
HELIX   10  10 ALA A  180  VAL A  191  1                                  12
HELIX   11  11 GLY A  210  LEU A  215  5                                   6
HELIX   12  12 GLU A  222  GLY A  236  1                                  15
HELIX   13  13 SER A  237  PHE A  244  5                                   8
HELIX   14  14 GLY A  245  GLY A  249  5                                   5
HELIX   15  15 PRO A  252  SER A  254  5                                   3
HELIX   16  16 THR A  277  ASP A  280  5                                   4
HELIX   17  17 GLY A  281  TYR A  294  1                                  14
HELIX   18  18 CYS A  335  ARG A  338  5                                   4
HELIX   19  19 TRP A  339  ASN A  351  1                                  13
SHEET    1   A 8 ALA A 256  VAL A 257  0
SHEET    2   A 8 LEU A 219  THR A 221  1  O  VAL A 220   N  VAL A 257
SHEET    3   A 8 VAL A 196  GLN A 199  1  O  VAL A 197   N  LEU A 219
SHEET    4   A 8 GLY A 170  ASP A 174  1  O  PHE A 171   N  PHE A 198
SHEET    5   A 8 ASP A  80  LEU A  86  1  O  ILE A  81   N  GLY A 170
SHEET    6   A 8 ALA A  31  VAL A  34  1  O  VAL A  32   N  TYR A  82
SHEET    7   A 8 PHE A   5  LEU A   8  1  O  VAL A   6   N  GLN A  33
SHEET    8   A 8 GLN A 300  SER A 303  1  N  VAL A 301   O  PHE A   5
SHEET    1   B 2 HIS A  89  MET A  90  0
SHEET    2   B 2 ALA A 143  ASP A 144 -1  O  ALA A 143   N  MET A  90
SHEET    1   C 2 GLY A  95  THR A  96  0
SHEET    2   C 2 SER A 102  PHE A 103 -1  O  PHE A 103   N  GLY A  95
SHEET    1   D 2 HIS A 321  ASN A 322  0
SHEET    2   D 2 ASN A 325  LEU A 326 -1  O  ASN A 325   N  ASN A 322
SHEET    1   E 4 THR A 359  ASP A 363  0
SHEET    2   E 4 GLN A 368  GLY A 372 -1  O  SER A 370   N  TRP A 362
SHEET    3   E 4 GLY A 377  ASN A 382 -1  N  MET A 379   O  PHE A 371
SHEET    4   E 4 ASP A 437  HIS A 442 -1  O  ASP A 437   N  ASN A 382
SHEET    1   F 2 THR A 391  GLN A 393  0
SHEET    2   F 2 THR A 428  ASN A 430 -1  N  ILE A 429   O  VAL A 392
SHEET    1   G 2 GLY A 399  CYS A 402  0
SHEET    2   G 2 VAL A 420  VAL A 423 -1  N  ILE A 421   O  TYR A 401
SSBOND   1 CYS A   20    CYS A   74                          1555   1555  2.04
SSBOND   2 CYS A  120    CYS A  137                          1555   1555  2.03
SSBOND   3 CYS A  328    CYS A  335                          1555   1555  2.03
SSBOND   4 CYS A  402    CYS A  416                          1555   1555  2.03
LINK        CA    CA A 800                 OD1 ASN A  88     1555   1555  2.27
LINK        CA    CA A 800                 O   GLN A 135     1555   1555  2.52
LINK        CA    CA A 800                 OD1 ASP A 144     1555   1555  2.47
LINK        CA    CA A 800                 O   HIS A 178     1555   1555  2.37
LINK        CA    CA A 800                 O   HOH A1117     1555   1555  2.75
LINK        CA    CA A 800                 OD2 ASP A 144     1555   1555  2.38
LINK        CA    CA A 800                 O   HOH A1118     1555   1555  2.39
LINK        CA    CA A 800                 O   HOH A1437     1555   1555  2.51
SITE     1 AC1  7 ASN A  88  GLN A 135  ASP A 144  HIS A 178
SITE     2 AC1  7 HOH A1117  HOH A1118  HOH A1437
CRYST1   71.500  138.400  115.400  90.00  90.00  90.00 C 2 2 21      8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.013986  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007225  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008666        0.00000
      
PROCHECK
Go to PROCHECK summary
 References