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PDBsum entry 1vep

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Hydrolase PDB id
1vep
Jmol
Contents
Protein chain
516 a.a.
Ligands
GLC-BGC
GLC-GLC ×3
Metals
_CA
Waters ×271
HEADER    HYDROLASE                               03-APR-04   1VEP
TITLE     CRYSTAL STRUCTURE ANALYSIS OF TRIPLE (T47M/Y164E/T328N)
TITLE    2 /MALTOSE OF BACILLUS CEREUS BETA-AMYLASE AT PH 6.5
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN MALTOHYDROLASE, GLYCOSIDE
COMPND   5 HYDROLASE FAMILY 14;
COMPND   6 EC: 3.2.1.2;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE   3 ORGANISM_TAXID: 1396;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HMS174;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS    BETA-ALPHA-BARRELS, OPTIMUM PH, T47M/Y164E/T328N, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.HIRATA,M.ADACHI,S.UTSUMI,B.MIKAMI
REVDAT   3   04-AUG-09 1VEP    1       FORMUL HET    HETATM HETNAM
REVDAT   3 2                   1       LINK   SITE
REVDAT   2   24-FEB-09 1VEP    1       VERSN
REVDAT   1   24-MAY-05 1VEP    0
JRNL        AUTH   A.HIRATA,M.ADACHI,S.UTSUMI,B.MIKAMI
JRNL        TITL   ENGINEERING OF THE PH OPTIMUM OF BACILLUS CEREUS
JRNL        TITL 2 BETA-AMYLASE: CONVERSION OF THE PH OPTIMUM FROM A
JRNL        TITL 3 BACTERIAL TYPE TO A HIGHER-PLANT TYPE
JRNL        REF    BIOCHEMISTRY                  V.  43 12523 2004
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   15449941
JRNL        DOI    10.1021/BI049173H
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.06 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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) : 2.06
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.90
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 464417.640
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.3
REMARK   3   NUMBER OF REFLECTIONS             : 36666
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) : 0.183
REMARK   3   FREE R VALUE                     : 0.226
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3670
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.06
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.19
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.80
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4681
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170
REMARK   3   BIN FREE R VALUE                    : 0.3550
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 515
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4200
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 93
REMARK   3   SOLVENT ATOMS            : 271
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 8.40
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.50
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -7.51000
REMARK   3    B22 (A**2) : 10.21000
REMARK   3    B33 (A**2) : -2.70000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -3.23000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24
REMARK   3   ESD FROM SIGMAA              (A) : 0.35
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.30
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.82
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.270 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.990 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.170 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.160 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.32
REMARK   3   BSOL        : 44.70
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_REP.PARAM
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  4  : ION.PARAM
REMARK   3  PARAMETER FILE  5  : CIS_PEPTIDE.PARAM
REMARK   3  PARAMETER FILE  6  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP
REMARK   3  TOPOLOGY FILE  4   : ION.TOP
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1VEP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-APR-04.
REMARK 100 THE RCSB ID CODE IS RCSB006535.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-03
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : MACSCIENCE
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200  DATA SCALING SOFTWARE          : SAINT
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53224
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.700
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90
REMARK 200  COMPLETENESS FOR SHELL     (%) : 36.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 58.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, AMMONIUM SULFATE,
REMARK 280  POTASSIUM PHOSPHATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       46.34750
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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   OE2  GLU A   172     O4   GLC A   902              2.19
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    GLU A  56       45.42   -143.84
REMARK 500    ASP A  98       61.17   -116.11
REMARK 500    ASN A 100       84.93   -155.05
REMARK 500    GLN A 193       55.69   -118.70
REMARK 500    ASN A 243      -12.70   -160.74
REMARK 500    LYS A 337      -62.84   -129.03
REMARK 500    TYR A 398      -67.56    -17.31
REMARK 500    THR A 510     -155.28   -151.66
REMARK 500
REMARK 500 REMARK: NULL
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 930  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  56   OE2
REMARK 620 2 ASP A  60   OD1  96.6
REMARK 620 3 GLN A  61   OE1  84.4  98.8
REMARK 620 4 GLU A 141   OE1 108.4  83.5 166.8
REMARK 620 5 GLU A 144   OE1 158.5  95.0  76.1  90.8
REMARK 620 6 HOH A 757   O    77.7 162.5  97.1  82.7  95.8
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 900
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 901
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 902
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 903
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 904
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 905
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 906
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 907
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 930
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VEM   RELATED DB: PDB
REMARK 900 BETA-AMYLASE AT THE OPTIMUM PH 6.5
REMARK 900 RELATED ID: 1VEN   RELATED DB: PDB
REMARK 900 Y164E/MALTOSE OF BACILUS CEREUS BETA-AMYLASE AT PH 4.6
REMARK 900 RELATED ID: 1VEO   RELATED DB: PDB
REMARK 900 Y164F/MALTOSE OF BACILLUS CEREUS BETA-AMYLASE AT PH 4.6
DBREF  1VEP A    1   516  UNP    P36924   AMYB_BACCE      31    546
SEQADV 1VEP MET A   47  UNP  P36924    THR    77 ENGINEERED
SEQADV 1VEP GLU A  164  UNP  P36924    TYR   194 ENGINEERED
SEQADV 1VEP ASN A  328  UNP  P36924    THR   358 ENGINEERED
SEQRES   1 A  516  ALA VAL ASN GLY LYS GLY MET ASN PRO ASP TYR LYS ALA
SEQRES   2 A  516  TYR LEU MET ALA PRO LEU LYS LYS ILE PRO GLU VAL THR
SEQRES   3 A  516  ASN TRP GLU THR PHE GLU ASN ASP LEU ARG TRP ALA LYS
SEQRES   4 A  516  GLN ASN GLY PHE TYR ALA ILE MET VAL ASP PHE TRP TRP
SEQRES   5 A  516  GLY ASP MET GLU LYS ASN GLY ASP GLN GLN PHE ASP PHE
SEQRES   6 A  516  SER TYR ALA GLN ARG PHE ALA GLN SER VAL LYS ASN ALA
SEQRES   7 A  516  GLY MET LYS MET ILE PRO ILE ILE SER THR HIS GLN CYS
SEQRES   8 A  516  GLY GLY ASN VAL GLY ASP ASP CYS ASN VAL PRO ILE PRO
SEQRES   9 A  516  SER TRP VAL TRP ASN GLN LYS SER ASP ASP SER LEU TYR
SEQRES  10 A  516  PHE LYS SER GLU THR GLY THR VAL ASN LYS GLU THR LEU
SEQRES  11 A  516  ASN PRO LEU ALA SER ASP VAL ILE ARG LYS GLU TYR GLY
SEQRES  12 A  516  GLU LEU TYR THR ALA PHE ALA ALA ALA MET LYS PRO TYR
SEQRES  13 A  516  LYS ASP VAL ILE ALA LYS ILE GLU LEU SER GLY GLY PRO
SEQRES  14 A  516  ALA GLY GLU LEU ARG TYR PRO SER TYR THR THR SER ASP
SEQRES  15 A  516  GLY THR GLY TYR PRO SER ARG GLY LYS PHE GLN ALA TYR
SEQRES  16 A  516  THR GLU PHE ALA LYS SER LYS PHE ARG LEU TRP VAL LEU
SEQRES  17 A  516  ASN LYS TYR GLY SER LEU ASN GLU VAL ASN LYS ALA TRP
SEQRES  18 A  516  GLY THR LYS LEU ILE SER GLU LEU ALA ILE LEU PRO PRO
SEQRES  19 A  516  SER ASP GLY GLU GLN PHE LEU MET ASN GLY TYR LEU SER
SEQRES  20 A  516  MET TYR GLY LYS ASP TYR LEU GLU TRP TYR GLN GLY ILE
SEQRES  21 A  516  LEU GLU ASN HIS THR LYS LEU ILE GLY GLU LEU ALA HIS
SEQRES  22 A  516  ASN ALA PHE ASP THR THR PHE GLN VAL PRO ILE GLY ALA
SEQRES  23 A  516  LYS ILE ALA GLY VAL HIS TRP GLN TYR ASN ASN PRO THR
SEQRES  24 A  516  ILE PRO HIS GLY ALA GLU LYS PRO ALA GLY TYR ASN ASP
SEQRES  25 A  516  TYR SER HIS LEU LEU ASP ALA PHE LYS SER ALA LYS LEU
SEQRES  26 A  516  ASP VAL ASN PHE THR CYS LEU GLU MET THR ASP LYS GLY
SEQRES  27 A  516  SER TYR PRO GLU TYR SER MET PRO LYS THR LEU VAL GLN
SEQRES  28 A  516  ASN ILE ALA THR LEU ALA ASN GLU LYS GLY ILE VAL LEU
SEQRES  29 A  516  ASN GLY GLU ASN ALA LEU SER ILE GLY ASN GLU GLU GLU
SEQRES  30 A  516  TYR LYS ARG VAL ALA GLU MET ALA PHE ASN TYR ASN PHE
SEQRES  31 A  516  ALA GLY PHE THR LEU LEU ARG TYR GLN ASP VAL MET TYR
SEQRES  32 A  516  ASN ASN SER LEU MET GLY LYS PHE LYS ASP LEU LEU GLY
SEQRES  33 A  516  VAL THR PRO VAL MET GLN THR ILE VAL VAL LYS ASN VAL
SEQRES  34 A  516  PRO THR THR ILE GLY ASP THR VAL TYR ILE THR GLY ASN
SEQRES  35 A  516  ARG ALA GLU LEU GLY SER TRP ASP THR LYS GLN TYR PRO
SEQRES  36 A  516  ILE GLN LEU TYR TYR ASP SER HIS SER ASN ASP TRP ARG
SEQRES  37 A  516  GLY ASN VAL VAL LEU PRO ALA GLU ARG ASN ILE GLU PHE
SEQRES  38 A  516  LYS ALA PHE ILE LYS SER LYS ASP GLY THR VAL LYS SER
SEQRES  39 A  516  TRP GLN THR ILE GLN GLN SER TRP ASN PRO VAL PRO LEU
SEQRES  40 A  516  LYS THR THR SER HIS THR SER SER TRP
HET    GLC  A 900      11
HET    BGC  A 901      12
HET    GLC  A 902      11
HET    GLC  A 903      12
HET    GLC  A 904      11
HET    GLC  A 905      12
HET    GLC  A 906      11
HET    GLC  A 907      12
HET     CA  A 930       1
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     BGC BETA-D-GLUCOSE
HETNAM      CA CALCIUM ION
FORMUL   2  GLC    7(C6 H12 O6)
FORMUL   2  BGC    C6 H12 O6
FORMUL   6   CA    CA 2+
FORMUL   7  HOH   *271(H2 O)
HELIX    1   1 ALA A    1  LYS A    5  5                                   5
HELIX    2   2 LYS A   21  VAL A   25  5                                   5
HELIX    3   3 ASN A   27  ASN A   41  1                                  15
HELIX    4   4 TRP A   52  GLU A   56  1                                   5
HELIX    5   5 PHE A   65  ALA A   78  1                                  14
HELIX    6   6 PRO A  104  LYS A  111  5                                   8
HELIX    7   7 ALA A  134  LYS A  154  1                                  21
HELIX    8   8 PRO A  155  ILE A  160  5                                   6
HELIX    9   9 GLY A  168  GLU A  172  5                                   5
HELIX   10  10 THR A  196  GLY A  212  1                                  17
HELIX   11  11 SER A  213  GLY A  222  1                                  10
HELIX   12  12 SER A  227  ILE A  231  5                                   5
HELIX   13  13 ASP A  236  ASN A  243  1                                   8
HELIX   14  14 GLY A  244  LEU A  246  5                                   3
HELIX   15  15 SER A  247  ASP A  277  1                                  31
HELIX   16  16 ALA A  304  GLY A  309  1                                   6
HELIX   17  17 ASP A  312  LYS A  324  1                                  13
HELIX   18  18 MET A  345  GLY A  361  1                                  17
HELIX   19  19 ASN A  374  TYR A  388  1                                  15
HELIX   20  20 ARG A  397  TYR A  403  1                                   7
HELIX   21  21 ASN A  404  LEU A  415  1                                  12
HELIX   22  22 ARG A  443  GLY A  447  5                                   5
SHEET    1   A 9 LYS A  12  MET A  16  0
SHEET    2   A 9 PHE A  43  TRP A  51  1  O  TYR A  44   N  ALA A  13
SHEET    3   A 9 LYS A  81  SER A  87  1  O  ILE A  85   N  VAL A  48
SHEET    4   A 9 ILE A 163  LEU A 165  1  O  GLU A 164   N  PRO A  84
SHEET    5   A 9 ILE A 284  LYS A 287  1  O  GLY A 285   N  LEU A 165
SHEET    6   A 9 ASP A 326  PHE A 329  1  O  ASP A 326   N  ILE A 284
SHEET    7   A 9 LEU A 364  GLU A 367  1  O  ASN A 365   N  PHE A 329
SHEET    8   A 9 GLY A 392  LEU A 395  1  O  THR A 394   N  GLY A 366
SHEET    9   A 9 LYS A  12  MET A  16  1  N  TYR A  14   O  PHE A 393
SHEET    1   B 2 PHE A 118  LYS A 119  0
SHEET    2   B 2 VAL A 125  ASN A 126 -1  O  ASN A 126   N  PHE A 118
SHEET    1   C 4 TYR A 459  ASP A 461  0
SHEET    2   C 4 ASP A 466  PRO A 474 -1  O  ARG A 468   N  TYR A 459
SHEET    3   C 4 PRO A 419  LYS A 427 -1  N  GLN A 422   O  VAL A 471
SHEET    4   C 4 SER A 511  SER A 515  1  O  HIS A 512   N  THR A 423
SHEET    1   D 4 ILE A 456  GLN A 457  0
SHEET    2   D 4 THR A 436  GLY A 441 -1  N  ILE A 439   O  ILE A 456
SHEET    3   D 4 ILE A 479  LYS A 486 -1  O  LYS A 486   N  THR A 436
SHEET    4   D 4 VAL A 492  TRP A 495 -1  O  LYS A 493   N  ILE A 485
SHEET    1   E 4 ILE A 456  GLN A 457  0
SHEET    2   E 4 THR A 436  GLY A 441 -1  N  ILE A 439   O  ILE A 456
SHEET    3   E 4 ILE A 479  LYS A 486 -1  O  LYS A 486   N  THR A 436
SHEET    4   E 4 GLN A 500  TRP A 502 -1  O  GLN A 500   N  PHE A 481
SSBOND   1 CYS A   91    CYS A   99                          1555   1555  2.03
LINK         OE2 GLU A  56                CA    CA A 930     1555   1555  2.64
LINK         OD1 ASP A  60                CA    CA A 930     1555   1555  2.31
LINK         OE1 GLN A  61                CA    CA A 930     1555   1555  2.84
LINK         OE1 GLU A 141                CA    CA A 930     1555   1555  2.61
LINK         OE1 GLU A 144                CA    CA A 930     1555   1555  2.63
LINK         C1  GLC A 900                 O4  BGC A 901     1555   1555  1.40
LINK         C1  GLC A 902                 O4  GLC A 903     1555   1555  1.40
LINK         C1  GLC A 904                 O4  GLC A 905     1555   1555  1.40
LINK         C1  GLC A 906                 O4  GLC A 907     1555   1555  1.40
LINK        CA    CA A 930                 O   HOH A 757     1555   1555  2.66
CISPEP   1 TYR A  186    PRO A  187          0         0.46
CISPEP   2 TYR A  340    PRO A  341          0        -0.30
CISPEP   3 LEU A  396    ARG A  397          0         0.67
CISPEP   4 ASN A  503    PRO A  504          0        -0.12
SITE     1 AC1 10 MET A  16  ASP A  49  TRP A  51  HIS A  89
SITE     2 AC1 10 ASP A  97  ARG A 397  HOH A 535  HOH A 536
SITE     3 AC1 10 HOH A 586  BGC A 901
SITE     1 AC2 10 ALA A 170  GLU A 172  LYS A 287  THR A 330
SITE     2 AC2 10 GLU A 367  ALA A 369  HOH A 642  HOH A 651
SITE     3 AC2 10 GLC A 900  GLC A 902
SITE     1 AC3 10 GLU A 172  ARG A 174  TYR A 178  GLY A 290
SITE     2 AC3 10 HIS A 292  THR A 330  CYS A 331  HOH A 586
SITE     3 AC3 10 BGC A 901  GLC A 903
SITE     1 AC4  6 VAL A  95  TYR A 186  HIS A 292  LEU A 370
SITE     2 AC4  6 HOH A 604  GLC A 902
SITE     1 AC5 10 TRP A 221  ALA A 230  ILE A 231  LEU A 232
SITE     2 AC5 10 PRO A 233  SER A 235  TYR A 249  HOH A 584
SITE     3 AC5 10 HOH A 683  GLC A 905
SITE     1 AC6  8 THR A 223  PRO A 234  GLN A 239  PHE A 240
SITE     2 AC6  8 GLY A 244  TYR A 249  HOH A 569  GLC A 904
SITE     1 AC7  4 TRP A 449  LYS A 482  GLN A 499  GLC A 907
SITE     1 AC8  3 LYS A 482  TRP A 495  GLC A 906
SITE     1 AC9  6 GLU A  56  ASP A  60  GLN A  61  GLU A 141
SITE     2 AC9  6 GLU A 144  HOH A 757
CRYST1   57.450   92.695   65.755  90.00 102.37  90.00 P 1 21 1      2
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      0.017406  0.000000  0.003818        0.00000
SCALE2      0.000000  0.010788  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015569        0.00000
      
PROCHECK
Go to PROCHECK summary
 References