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PDBsum entry 1j18

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Hydrolase PDB id
1j18
Jmol
Contents
Protein chain
516 a.a. *
Ligands
GLC-GLC-GLC-GLC
GLC-BGC ×2
SO4
ACY
Metals
_CA
Waters ×395
* Residue conservation analysis
HEADER    HYDROLASE                               02-DEC-02   1J18
TITLE     CRYSTAL STRUCTURE OF A BETA-AMYLASE FROM BACILLUS CEREUS
TITLE    2 VAR. MYCOIDES COCRYSTALLIZED WITH MALTOSE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN MALTOHYDROLASE;
COMPND   5 EC: 3.2.1.2;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE   3 ORGANISM_TAXID: 1396;
SOURCE   4 STRAIN: VAR. MYCOIDES;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS    BETA-AMYLASE, AMYLASE, COMPLEX, TIM BAREL, MALTOSE,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    H.MIYAKE,G.KURISU,M.KUSUNOKI,S.NISHIMURA,S.KITAMURA,Y.NITTA
REVDAT   4   28-JUL-09 1J18    1       HETATM HETNAM
REVDAT   3   24-FEB-09 1J18    1       VERSN
REVDAT   2   03-JUN-03 1J18    1       SOURCE
REVDAT   1   27-MAY-03 1J18    0
JRNL        AUTH   H.MIYAKE,G.KURISU,M.KUSUNOKI,S.NISHIMURA,
JRNL        AUTH 2 S.KITAMURA,Y.NITTA
JRNL        TITL   CRYSTAL STRUCTURE OF A CATALYTIC SITE MUTANT OF
JRNL        TITL 2 BETA-AMYLASE FROM BACILLUS CEREUS VAR. MYCOIDES
JRNL        TITL 3 COCRYSTALLIZED WITH MALTOPENTAOSE
JRNL        REF    BIOCHEMISTRY                  V.  42  5574 2003
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12741813
JRNL        DOI    10.1021/BI020712X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.00 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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1239672.270
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8
REMARK   3   NUMBER OF REFLECTIONS             : 43133
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) : 0.181
REMARK   3   FREE R VALUE                     : 0.221
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 2129
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6840
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130
REMARK   3   BIN FREE R VALUE                    : 0.2650
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 323
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4119
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 98
REMARK   3   SOLVENT ATOMS            : 399
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -5.54000
REMARK   3    B22 (A**2) : 7.34000
REMARK   3    B33 (A**2) : -1.80000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -4.81000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20
REMARK   3   ESD FROM SIGMAA              (A) : 0.14
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) : 0.26
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.19
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.005
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90
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) : 4.020 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.480 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.650 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.990 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.38
REMARK   3   BSOL        : 57.77
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_BEAMY_PARAM
REMARK   3  PARAMETER FILE  2  : ION.PARAM
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  5  : ACY_XPLOR_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   : ACY_XPLOR_TOP
REMARK   3  TOPOLOGY FILE  6   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1J18 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-03.
REMARK 100 THE RCSB ID CODE IS RCSB005502.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-DEC-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-18B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 43133
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.05600
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) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, AMMONUIM SULFATE,
REMARK 280  MALTOSE, ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 293K
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       44.66550
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   O1   GLC A   602     O4   GLC A   603              2.10
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       45.79   -152.86
REMARK 500    CYS A  99     -179.65   -176.59
REMARK 500    ASN A 100       82.62   -161.65
REMARK 500    PRO A 104      122.37    -37.89
REMARK 500    ASP A 113     -159.12    -96.49
REMARK 500    ASN A 243      -18.47   -149.08
REMARK 500    CYS A 331       83.68   -153.42
REMARK 500    LYS A 337      -60.56   -120.36
REMARK 500    TYR A 398      -70.95    -14.70
REMARK 500    ASN A 404       87.19   -153.62
REMARK 500    THR A 497      -74.16    -47.78
REMARK 500    THR A 510     -144.25   -154.21
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 A1082        DISTANCE =  5.14 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE ELECTRON DENSITY OF GLC 602 SUGGESTS
REMARK 600 THE EXISTENCE OF ALPHA- AND BETA-MALTOSE.
REMARK 600 WHEN ALPHA- OR BETA-MALTOSE BINDS AT SUBSITES -2
REMARK 600 AND -1, THE OTHER MALTOSE MOLECULE CANNOT BIND TO
REMARK 600 SUBSITES +1 AND +2 AT THE SAME TIME
REMARK 600 BECAUSE THE DISTANCE BETWEEN THE C1 ATOM OF GLC 602
REMARK 600 AND THE O4 ATOM OF GLC 603 IS TOO SHORT (1.7 A),
REMARK 600 UNLESS A CONDENSATION BETWEEN THE MALTOSE
REMARK 600 MOLECULES OCCURS.
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 A1500  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  56   OE2
REMARK 620 2 ASP A  60   OD1 100.3
REMARK 620 3 GLN A  61   OE1  73.6 100.4
REMARK 620 4 GLU A 141   OE1 114.4  81.0 171.6
REMARK 620 5 GLU A 144   OE1 148.1  96.6  76.8  94.8
REMARK 620 6 HOH A1051   O    71.7 159.7  95.3  85.4  99.6
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 601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 602
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 603
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 604
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 606
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 607
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 611
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 612
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1500
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1501
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5BCA   RELATED DB: PDB
REMARK 900 5BCA CONTAINS THE SAME PROTEIN COMPLEXED WITH MALTOSE.
DBREF  1J18 A    1   516  UNP    P36924   AMYB_BACCE      31    546
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 THR 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 TYR 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 THR 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 601      11
HET    GLC  A 602      12
HET    GLC  A 603      11
HET    GLC  A 604      12
HET    GLC  A 606      11
HET    BGC  A 607      12
HET    GLC  A 611      11
HET    BGC  A 612      12
HET     CA  A1500       1
HET    SO4  A1501       5
HET    ACY  A1502       4
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     BGC BETA-D-GLUCOSE
HETNAM      CA CALCIUM ION
HETNAM     SO4 SULFATE ION
HETNAM     ACY ACETIC ACID
FORMUL   2  GLC    6(C6 H12 O6)
FORMUL   4  BGC    2(C6 H12 O6)
FORMUL   6   CA    CA 2+
FORMUL   7  SO4    O4 S 2-
FORMUL   8  ACY    C2 H4 O2
FORMUL   9  HOH   *395(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  GLN A  110  5                                   7
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  ALA A  323  1                                  12
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 MET A  82  SER A  87  1  O  ILE A  83   N  ILE A  46
SHEET    4   A 9 ILE A 163  LEU A 165  1  O  TYR A 164   N  PRO A  84
SHEET    5   A 9 ILE A 284  ILE A 288  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  VAL A 327
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 3 VAL A 492  TRP A 495  0
SHEET    2   C 3 ILE A 479  LYS A 486 -1  N  ILE A 485   O  SER A 494
SHEET    3   C 3 GLN A 500  TRP A 502 -1  O  GLN A 500   N  PHE A 481
SHEET    1   D 7 VAL A 492  TRP A 495  0
SHEET    2   D 7 ILE A 479  LYS A 486 -1  N  ILE A 485   O  SER A 494
SHEET    3   D 7 THR A 436  GLY A 441 -1  N  TYR A 438   O  PHE A 484
SHEET    4   D 7 ILE A 456  ASP A 461 -1  O  LEU A 458   N  VAL A 437
SHEET    5   D 7 ASP A 466  PRO A 474 -1  O  ARG A 468   N  TYR A 459
SHEET    6   D 7 PRO A 419  LYS A 427 -1  N  ILE A 424   O  GLY A 469
SHEET    7   D 7 SER A 511  SER A 515  1  O  HIS A 512   N  VAL A 425
SSBOND   1 CYS A   91    CYS A   99                          1555   1555  2.03
LINK         OE2 GLU A  56                CA    CA A1500     1555   1555  2.86
LINK         OD1 ASP A  60                CA    CA A1500     1555   1555  2.24
LINK         OE1 GLN A  61                CA    CA A1500     1555   1555  2.74
LINK         OE1 GLU A 141                CA    CA A1500     1555   1555  2.55
LINK         OE1 GLU A 144                CA    CA A1500     1555   1555  2.38
LINK         C1  GLC A 601                 O4  GLC A 602     1555   1555  1.38
LINK         C1  GLC A 602                 O4  GLC A 603     1555   1555  1.74
LINK         C1  GLC A 603                 O4  GLC A 604     1555   1555  1.41
LINK         C1  GLC A 606                 O4  BGC A 607     1555   1555  1.40
LINK         C1  GLC A 611                 O4  BGC A 612     1555   1555  1.40
LINK        CA    CA A1500                 O   HOH A1051     1555   1555  2.49
CISPEP   1 TYR A  186    PRO A  187          0         0.29
CISPEP   2 TYR A  340    PRO A  341          0         0.38
CISPEP   3 LEU A  396    ARG A  397          0         1.02
CISPEP   4 ASN A  503    PRO A  504          0        -0.56
SITE     1 AC1 10 ASP A  49  TRP A  51  HIS A  89  ASP A  97
SITE     2 AC1 10 ALA A 170  ARG A 397  GLC A 602  HOH A 704
SITE     3 AC1 10 HOH A 730  HOH A 815
SITE     1 AC2 14 VAL A  95  ALA A 170  GLU A 172  LYS A 287
SITE     2 AC2 14 THR A 330  GLU A 367  ALA A 369  LEU A 396
SITE     3 AC2 14 GLC A 601  GLC A 603  HOH A 724  HOH A 783
SITE     4 AC2 14 HOH A 815  HOH A1084
SITE     1 AC3 12 ALA A 170  GLU A 172  ARG A 174  TYR A 178
SITE     2 AC3 12 GLY A 290  HIS A 292  TRP A 293  THR A 330
SITE     3 AC3 12 CYS A 331  GLC A 602  GLC A 604  HOH A 815
SITE     1 AC4  6 VAL A  95  TYR A 186  HIS A 292  LEU A 370
SITE     2 AC4  6 GLC A 603  HOH A 966
SITE     1 AC5  9 ALA A 230  ILE A 231  LEU A 232  PRO A 233
SITE     2 AC5  9 SER A 235  TYR A 249  BGC A 607  HOH A 790
SITE     3 AC5  9 HOH A 935
SITE     1 AC6  9 THR A 223  PRO A 234  GLN A 239  PHE A 240
SITE     2 AC6  9 GLY A 244  TYR A 249  GLC A 606  HOH A 727
SITE     3 AC6  9 HOH A 797
SITE     1 AC7  5 TRP A 449  GLN A 499  BGC A 612  HOH A 956
SITE     2 AC7  5 HOH A1094
SITE     1 AC8  4 LYS A 482  TRP A 495  GLC A 611  HOH A 956
SITE     1 AC9  6 GLU A  56  ASP A  60  GLN A  61  GLU A 141
SITE     2 AC9  6 GLU A 144  HOH A1051
SITE     1 BC1  4 ASN A 404  ASN A 405  SER A 406  HOH A1007
SITE     1 BC2  8 ASN A 131  LEU A 133  TYR A 175  GLN A 193
SITE     2 BC2  8 ALA A 194  ALA A 199  ILE A 260  HOH A 703
CRYST1   56.808   89.331   65.394  90.00 102.32  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      0.017603  0.000000  0.003845        0.00000
SCALE2      0.000000  0.011194  0.000000        0.00000
SCALE3      0.000000  0.000000  0.015652        0.00000
      
PROCHECK
Go to PROCHECK summary
 References