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PDBsum entry 1kxh

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Hydrolase PDB id
1kxh
Jmol
Contents
Protein chain
448 a.a. *
Ligands
ACR
Metals
_CL
_CA
Waters ×205
* Residue conservation analysis
HEADER    HYDROLASE                               31-JAN-02   1KXH
TITLE     CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN AN INACTIVE MUTANT OF
TITLE    2 PSYCHROPHILIC ALPHA-AMYLASE (D174N) AND ACARBOSE
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    (BETA/ALPHA)8 BARREL, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    N.AGHAJARI,R.HASER
REVDAT   4   13-JUL-11 1KXH    1       VERSN
REVDAT   3   24-FEB-09 1KXH    1       VERSN
REVDAT   2   12-JUL-05 1KXH    1       DBREF  SEQADV REMARK
REVDAT   1   19-JUN-02 1KXH    0
JRNL        AUTH   N.AGHAJARI,M.ROTH,R.HASER
JRNL        TITL   CRYSTALLOGRAPHIC EVIDENCE OF A TRANSGLYCOSYLATION REACTION:
JRNL        TITL 2 TERNARY COMPLEXES OF A PSYCHROPHILIC ALPHA-AMYLASE.
JRNL        REF    BIOCHEMISTRY                  V.  41  4273
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   11914073
JRNL        DOI    10.1021/BI0160516
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  TITL   STRUCTURES OF THE PSYCHROPHILIC ALTEROMONAS HALOPLANCTIS
REMARK   1  TITL 2 ALPHA-AMYLASE GIVE INSIGHTS INTO COLD ADAPTATION AT A
REMARK   1  TITL 3 MOLECULAR LEVEL
REMARK   1  REF    STRUCTURE                     V.   6  1503 1998
REMARK   1  REFN                   ISSN 0969-2126
REMARK   1 REFERENCE 2
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE PSYCHROPHILIC ALPHA-AMYLASE FROM
REMARK   1  TITL 2 ALTEROMONAS HALOPLANCTIS IN ITS NATIVE FORM AND COMPLEXED
REMARK   1  TITL 3 WITH AN INHIBITOR
REMARK   1  REF    PROTEIN SCI.                  V.   7   564 1998
REMARK   1  REFN                   ISSN 0961-8368
REMARK   2
REMARK   2 RESOLUTION.    2.30 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) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.70
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 22031
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) : 0.138
REMARK   3   FREE R VALUE                     : 0.188
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2410
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            : 3444
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 46
REMARK   3   SOLVENT ATOMS            : 205
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 24.17
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) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.57
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 1KXH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-02.
REMARK 100 THE RCSB ID CODE IS RCSB015437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-99
REMARK 200  TEMPERATURE           (KELVIN) : 277
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          : ENRAF-NONIUS FR591
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS
REMARK 200  OPTICS                         : MIRRORS
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   : 24442
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.700
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6
REMARK 200  DATA REDUNDANCY                : 3.900
REMARK 200  R MERGE                    (I) : 0.09200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.700
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 1AQM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, HEPES, PH 7, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 293K
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       57.65000
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       57.65000
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       35.55000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.95000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.55000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.95000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       57.65000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.55000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.95000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.65000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.55000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.95000
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 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    TYR A  23      -60.25   -129.49
REMARK 500    PRO A 295       46.63    -77.78
REMARK 500    PHE A 329      -13.15     69.94
REMARK 500    ALA A 330     -131.10    -98.79
REMARK 500    ASN A 332     -110.24   -112.38
REMARK 500    THR A 365       -1.79     76.60
REMARK 500    ASN A 366     -108.21   -137.66
REMARK 500    ASN A 432       71.38   -154.18
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 A1180        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A1318        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH A1321        DISTANCE =  5.66 ANGSTROMS
REMARK 525    HOH A1384        DISTANCE =  5.43 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   154.8
REMARK 620 3 HIS A 178   O    75.7  79.4
REMARK 620 4 HOH A1107   O    98.2  74.9  83.5
REMARK 620 5 ASP A 144   OD1  77.2 120.4 137.5  68.6
REMARK 620 6 ASP A 144   OD2 122.9  80.3 156.2  79.3  48.4
REMARK 620 7 HOH A1091   O    74.9 124.1 125.0 145.9  77.4  77.1
REMARK 620 8 HOH A1108   O   112.5  68.8  84.9 143.3 136.1  99.1  65.5
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 ACR A 598
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G94   RELATED DB: PDB
REMARK 900 COMPLEX NATIVE AHA/ACARBOSE/TRIS
REMARK 900 RELATED ID: 1G9H   RELATED DB: PDB
REMARK 900 COMPLEX NATIVE AHA/COMPONENT II/TRIS
REMARK 900 RELATED ID: 1AQH   RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE OF WILDTYPE AHA
REMARK 900 RELATED ID: 1AQM   RELATED DB: PDB
REMARK 900 COMPLEX NATIVE AHA/TRIS
REMARK 900 RELATED ID: 1BOI   RELATED DB: PDB
REMARK 900 NATIVE STRUCTURE OF RECOMBINANT AHA
DBREF  1KXH A    1   448  UNP    P29957   AMY_ALTHA       25    472
SEQADV 1KXH ASN A  174  UNP  P29957    ASP   198 ENGINEERED
SEQRES   1 A  448  THR PRO THR THR PHE VAL HIS LEU PHE GLU TRP ASN TRP
SEQRES   2 A  448  GLN ASP VAL ALA GLN GLU CYS GLU GLN TYR LEU GLY PRO
SEQRES   3 A  448  LYS GLY TYR ALA ALA VAL GLN VAL SER PRO PRO ASN GLU
SEQRES   4 A  448  HIS ILE THR GLY SER GLN TRP TRP THR ARG TYR GLN PRO
SEQRES   5 A  448  VAL SER TYR GLU LEU GLN SER ARG GLY GLY ASN ARG ALA
SEQRES   6 A  448  GLN PHE ILE ASP MET VAL ASN ARG CYS SER ALA ALA GLY
SEQRES   7 A  448  VAL ASP ILE TYR VAL ASP THR LEU ILE ASN HIS MET ALA
SEQRES   8 A  448  ALA GLY SER GLY THR GLY THR ALA GLY ASN SER PHE GLY
SEQRES   9 A  448  ASN LYS SER PHE PRO ILE TYR SER PRO GLN ASP PHE HIS
SEQRES  10 A  448  GLU SER CYS THR ILE ASN ASN SER ASP TYR GLY ASN ASP
SEQRES  11 A  448  ARG TYR ARG VAL GLN ASN CYS GLU LEU VAL GLY LEU ALA
SEQRES  12 A  448  ASP LEU ASP THR ALA SER ASN TYR VAL GLN ASN THR ILE
SEQRES  13 A  448  ALA ALA TYR ILE ASN ASP LEU GLN ALA ILE GLY VAL LYS
SEQRES  14 A  448  GLY PHE ARG PHE ASN ALA SER LYS HIS VAL ALA ALA SER
SEQRES  15 A  448  ASP ILE GLN SER LEU MET ALA LYS VAL ASN GLY SER PRO
SEQRES  16 A  448  VAL VAL PHE GLN GLU VAL ILE ASP GLN GLY GLY GLU ALA
SEQRES  17 A  448  VAL GLY ALA SER GLU TYR LEU SER THR GLY LEU VAL THR
SEQRES  18 A  448  GLU PHE LYS TYR SER THR GLU LEU GLY ASN THR PHE ARG
SEQRES  19 A  448  ASN GLY SER LEU ALA TRP LEU SER ASN PHE GLY GLU GLY
SEQRES  20 A  448  TRP GLY PHE MET PRO SER SER SER ALA VAL VAL PHE VAL
SEQRES  21 A  448  ASP ASN HIS ASP ASN GLN ARG GLY HIS GLY GLY ALA GLY
SEQRES  22 A  448  ASN VAL ILE THR PHE GLU ASP GLY ARG LEU TYR ASP LEU
SEQRES  23 A  448  ALA ASN VAL PHE MET LEU ALA TYR PRO TYR GLY TYR PRO
SEQRES  24 A  448  LYS VAL MET SER SER TYR ASP PHE HIS GLY ASP THR ASP
SEQRES  25 A  448  ALA GLY GLY PRO ASN VAL PRO VAL HIS ASN ASN GLY ASN
SEQRES  26 A  448  LEU GLU CYS PHE ALA SER ASN TRP LYS CYS GLU HIS ARG
SEQRES  27 A  448  TRP SER TYR ILE ALA GLY GLY VAL ASP PHE ARG ASN ASN
SEQRES  28 A  448  THR ALA ASP ASN TRP ALA VAL THR ASN TRP TRP ASP ASN
SEQRES  29 A  448  THR ASN ASN GLN ILE SER PHE GLY ARG GLY SER SER GLY
SEQRES  30 A  448  HIS MET ALA ILE ASN LYS GLU ASP SER THR LEU THR ALA
SEQRES  31 A  448  THR VAL GLN THR ASP MET ALA SER GLY GLN TYR CYS ASN
SEQRES  32 A  448  VAL LEU LYS GLY GLU LEU SER ALA ASP ALA LYS SER CYS
SEQRES  33 A  448  SER GLY GLU VAL ILE THR VAL ASN SER ASP GLY THR ILE
SEQRES  34 A  448  ASN LEU ASN ILE GLY ALA TRP ASP ALA MET ALA ILE HIS
SEQRES  35 A  448  LYS ASN ALA LYS LEU ASN
HET    ACR  A 598      44
HET     CA  A 800       1
HET     CL  A 900       1
HETNAM     ACR ALPHA-ACARBOSE
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
HETSYN     ACR 1,4-DEOXY-4-((5-HYDROXYMETHYL-2,3,4-TRIHYDROXYCYCLOHEX-
HETSYN   2 ACR  5,6-ENYL)AMINO)FRUCTOSE
FORMUL   2  ACR    C25 H43 N O18
FORMUL   3   CA    CA 2+
FORMUL   4   CL    CL 1-
FORMUL   5  HOH   *205(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  ALA A   77  1                                  15
HELIX    5   5 SER A  112  PHE A  116  5                                   5
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  LYS A  190  1                                  11
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 ASP A  264  GLY A  268  5                                   5
HELIX   17  17 THR A  277  ASP A  280  5                                   4
HELIX   18  18 GLY A  281  TYR A  294  1                                  14
HELIX   19  19 CYS A  335  ARG A  338  5                                   4
HELIX   20  20 TRP A  339  THR A  352  1                                  14
SHEET    1   A 9 PHE A   5  LEU A   8  0
SHEET    2   A 9 ALA A  31  VAL A  34  1  O  GLN A  33   N  VAL A   6
SHEET    3   A 9 ASP A  80  LEU A  86  1  O  TYR A  82   N  VAL A  32
SHEET    4   A 9 GLY A 170  ASN A 174  1  O  ARG A 172   N  THR A  85
SHEET    5   A 9 VAL A 196  GLN A 199  1  O  PHE A 198   N  PHE A 171
SHEET    6   A 9 LEU A 219  THR A 221  1  O  LEU A 219   N  GLN A 199
SHEET    7   A 9 ALA A 256  VAL A 258  1  O  VAL A 257   N  VAL A 220
SHEET    8   A 9 TYR A 298  SER A 303  1  O  LYS A 300   N  VAL A 258
SHEET    9   A 9 PHE A   5  LEU A   8  1  N  PHE A   5   O  VAL A 301
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  GLY A 372   N  THR A 359
SHEET    3   E 4 GLY A 377  ASN A 382 -1  O  MET A 379   N  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  O  ILE A 429   N  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  O  ILE A 421   N  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  2.02
SSBOND   4 CYS A  402    CYS A  416                          1555   1555  2.04
LINK        CA    CA A 800                 OD1 ASN A  88     1555   1555  2.37
LINK        CA    CA A 800                 O   GLN A 135     1555   1555  2.55
LINK        CA    CA A 800                 O   HIS A 178     1555   1555  2.46
LINK        CA    CA A 800                 O   HOH A1107     1555   1555  2.59
LINK        CA    CA A 800                 OD1 ASP A 144     1555   1555  2.73
LINK        CA    CA A 800                 OD2 ASP A 144     1555   1555  2.60
LINK        CA    CA A 800                 O   HOH A1091     1555   1555  2.47
LINK        CA    CA A 800                 O   HOH A1108     1555   1555  2.39
SITE     1 AC1 13 TRP A  47  TYR A  50  GLN A  51  HIS A  89
SITE     2 AC1 13 VAL A 140  ASN A 174  ALA A 175  ASN A 192
SITE     3 AC1 13 GLU A 200  ASP A 264  HIS A 269  HOH A1128
SITE     4 AC1 13 HOH A1375
SITE     1 AC2  7 ASN A  88  GLN A 135  ASP A 144  HIS A 178
SITE     2 AC2  7 HOH A1091  HOH A1107  HOH A1108
SITE     1 AC3  3 ARG A 172  ASN A 262  LYS A 300
CRYST1   71.100  139.900  115.300  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      0.014065  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007148  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008673        0.00000
      
PROCHECK
Go to PROCHECK summary
 References