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PDBsum entry 1q6f

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Hydrolase PDB id
1q6f
Jmol
Contents
Protein chain
490 a.a. *
Ligands
BGC-BGC-GLC
GLC-BGC
SO4 ×2
Waters ×247
* Residue conservation analysis
HEADER    HYDROLASE                               13-AUG-03   1Q6F
TITLE     CRYSTAL STRUCTURE OF SOYBEAN BETA-AMYLASE MUTANT (E178Y)
TITLE    2 WITH INCREASED PH OPTIMUM AT PH 7.1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 EC: 3.2.1.2;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE   3 ORGANISM_COMMON: SOYBEAN;
SOURCE   4 ORGANISM_TAXID: 3847;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PKK233-2
KEYWDS    BETA-ALPHA-BARRELS, BETA-AMYLASE, MALTOSE COMPLEX,
KEYWDS   2 INCREASED PH OPTIMUM, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.HIRATA,M.ADACHI,A.SEKINE,Y.N.KANG,S.UTSUMI,B.MIKAMI
REVDAT   2   24-FEB-09 1Q6F    1       VERSN
REVDAT   1   24-FEB-04 1Q6F    0
JRNL        AUTH   A.HIRATA,M.ADACHI,A.SEKINE,Y.N.KANG,S.UTSUMI,
JRNL        AUTH 2 B.MIKAMI
JRNL        TITL   STRUCTURAL AND ENZYMATIC ANALYSIS OF SOYBEAN
JRNL        TITL 2 {BETA}-AMYLASE MUTANTS WITH INCREASED PH OPTIMUM
JRNL        REF    J.BIOL.CHEM.                  V. 279  7287 2004
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   14638688
JRNL        DOI    10.1074/JBC.M309411200
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 498594.430
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 81.1
REMARK   3   NUMBER OF REFLECTIONS             : 30486
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) : 0.171
REMARK   3   FREE R VALUE                     : 0.208
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 3050
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3563
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330
REMARK   3   BIN FREE R VALUE                    : 0.2740
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 387
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3950
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 91
REMARK   3   SOLVENT ATOMS            : 247
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 8.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.26000
REMARK   3    B22 (A**2) : 2.26000
REMARK   3    B33 (A**2) : -4.51000
REMARK   3    B12 (A**2) : 4.64000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21
REMARK   3   ESD FROM SIGMAA              (A) : 0.21
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) : 0.25
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) : 22.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
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) : 1.210 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.820 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.190 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.100 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.33
REMARK   3   BSOL        : 50.50
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 1Q6F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-AUG-03.
REMARK 100 THE RCSB ID CODE IS RCSB019974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-99
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 7.1
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          : 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   : 39656
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.650
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08400
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.9
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   (%): 52.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.1, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.41333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       96.82667
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       96.82667
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.41333
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 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     ALA A     1
REMARK 465     THR A     2
REMARK 465     SER A     3
REMARK 465     ASP A     4
REMARK 465     SER A     5
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    ASP A  31       76.01   -119.22
REMARK 500    GLU A  60       41.15   -107.96
REMARK 500    ASN A 118       85.01   -154.85
REMARK 500    PHE A 145       77.41   -103.55
REMARK 500    PRO A 201       52.68   -105.36
REMARK 500    THR A 342       39.39    -85.83
REMARK 500    CYS A 343       84.60   -168.33
REMARK 500    PRO A 466      154.48    -49.72
REMARK 500    ASP A 494      -90.87    103.26
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 A 675        DISTANCE =  7.24 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 GLC 496 AND ALTERNATE POSITION A OF BGC 497
REMARK 600 ARE BOUND EACH OTHER.
REMARK 600 ALSO, GLC 496 AND ALTERNATE POSITION B OF GLC 1497,
REMARK 600 GLC 498 AND 499 WHICH PLACE ALTERNATE POSITION A,
REMARK 600 GLC 498 AND 499 WHICH PLACE ALTERNATE POSITION B
REMARK 600 ARE BOUND EACH OTHER.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 496
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 497
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 1497
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 498
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC A 499
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 900
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q6C   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH MALTOSE
REMARK 900 RELATED ID: 1Q6D   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, M51T MUTANT
REMARK 900 RELATED ID: 1Q6E   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, E178Y MUTANT AT PH 5.4
REMARK 900 RELATED ID: 1Q6G   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, N340T MUTANT
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONFLICT BASED ON A REASONABLE SPECIFIC ACTIVITY
REMARK 999 OF CRUDE EXTRACT.
REMARK 999 THE REFFERENCE IS JOURNAL OF BIOLOGICAL CHEMISTRY (1998)
REMARK 999 273, 19859-19865.
DBREF  1Q6F A    1   495  GB     902938   BAA09462         2    496
SEQADV 1Q6F LEU A   76  GB   902938    PHE    77 SEE REMARK 999
SEQADV 1Q6F TYR A  178  GB   902938    GLU   179 ENGINEERED
SEQRES   1 A  495  ALA THR SER ASP SER ASN MET LEU LEU ASN TYR VAL PRO
SEQRES   2 A  495  VAL TYR VAL MET LEU PRO LEU GLY VAL VAL ASN VAL ASP
SEQRES   3 A  495  ASN VAL PHE GLU ASP PRO ASP GLY LEU LYS GLU GLN LEU
SEQRES   4 A  495  LEU GLN LEU ARG ALA ALA GLY VAL ASP GLY VAL MET VAL
SEQRES   5 A  495  ASP VAL TRP TRP GLY ILE ILE GLU LEU LYS GLY PRO LYS
SEQRES   6 A  495  GLN TYR ASP TRP ARG ALA TYR ARG SER LEU LEU GLN LEU
SEQRES   7 A  495  VAL GLN GLU CYS GLY LEU THR LEU GLN ALA ILE MET SER
SEQRES   8 A  495  PHE HIS GLN CYS GLY GLY ASN VAL GLY ASP ILE VAL ASN
SEQRES   9 A  495  ILE PRO ILE PRO GLN TRP VAL LEU ASP ILE GLY GLU SER
SEQRES  10 A  495  ASN HIS ASP ILE PHE TYR THR ASN ARG SER GLY THR ARG
SEQRES  11 A  495  ASN LYS GLU TYR LEU THR VAL GLY VAL ASP ASN GLU PRO
SEQRES  12 A  495  ILE PHE HIS GLY ARG THR ALA ILE GLU ILE TYR SER ASP
SEQRES  13 A  495  TYR MET LYS SER PHE ARG GLU ASN MET SER ASP PHE LEU
SEQRES  14 A  495  GLU SER GLY LEU ILE ILE ASP ILE TYR VAL GLY LEU GLY
SEQRES  15 A  495  PRO ALA GLY GLU LEU ARG TYR PRO SER TYR PRO GLN SER
SEQRES  16 A  495  GLN GLY TRP GLU PHE PRO GLY ILE GLY GLU PHE GLN CYS
SEQRES  17 A  495  TYR ASP LYS TYR LEU LYS ALA ASP PHE LYS ALA ALA VAL
SEQRES  18 A  495  ALA ARG ALA GLY HIS PRO GLU TRP GLU LEU PRO ASP ASP
SEQRES  19 A  495  ALA GLY LYS TYR ASN ASP VAL PRO GLU SER THR GLY PHE
SEQRES  20 A  495  PHE LYS SER ASN GLY THR TYR VAL THR GLU LYS GLY LYS
SEQRES  21 A  495  PHE PHE LEU THR TRP TYR SER ASN LYS LEU LEU ASN HIS
SEQRES  22 A  495  GLY ASP GLN ILE LEU ASP GLU ALA ASN LYS ALA PHE LEU
SEQRES  23 A  495  GLY CYS LYS VAL LYS LEU ALA ILE LYS VAL SER GLY ILE
SEQRES  24 A  495  HIS TRP TRP TYR LYS VAL GLU ASN HIS ALA ALA GLU LEU
SEQRES  25 A  495  THR ALA GLY TYR TYR ASN LEU ASN ASP ARG ASP GLY TYR
SEQRES  26 A  495  ARG PRO ILE ALA ARG MET LEU SER ARG HIS HIS ALA ILE
SEQRES  27 A  495  LEU ASN PHE THR CYS LEU GLU MET ARG ASP SER GLU GLN
SEQRES  28 A  495  PRO SER ASP ALA LYS SER GLY PRO GLN GLU LEU VAL GLN
SEQRES  29 A  495  GLN VAL LEU SER GLY GLY TRP ARG GLU ASP ILE ARG VAL
SEQRES  30 A  495  ALA GLY GLU ASN ALA LEU PRO ARG TYR ASP ALA THR ALA
SEQRES  31 A  495  TYR ASN GLN ILE ILE LEU ASN ALA ARG PRO GLN GLY VAL
SEQRES  32 A  495  ASN ASN ASN GLY PRO PRO LYS LEU SER MET PHE GLY VAL
SEQRES  33 A  495  THR TYR LEU ARG LEU SER ASP ASP LEU LEU GLN LYS SER
SEQRES  34 A  495  ASN PHE ASN ILE PHE LYS LYS PHE VAL LEU LYS MET HIS
SEQRES  35 A  495  ALA ASP GLN ASP TYR CYS ALA ASN PRO GLN LYS TYR ASN
SEQRES  36 A  495  HIS ALA ILE THR PRO LEU LYS PRO SER ALA PRO LYS ILE
SEQRES  37 A  495  PRO ILE GLU VAL LEU LEU GLU ALA THR LYS PRO THR LEU
SEQRES  38 A  495  PRO PHE PRO TRP LEU PRO GLU THR ASP MET LYS VAL ASP
SEQRES  39 A  495  GLY
HET    BGC  A 496      11
HET    BGC  A 497      12
HET    GLC  A1497      12
HET    GLC  A 498      22
HET    BGC  A 499      24
HET    SO4  A 900       5
HET    SO4  A 901       5
HETNAM     BGC BETA-D-GLUCOSE
HETNAM     GLC ALPHA-D-GLUCOSE
HETNAM     SO4 SULFATE ION
FORMUL   2  BGC    3(C6 H12 O6)
FORMUL   2  GLC    2(C6 H12 O6)
FORMUL   4  SO4    2(O4 S 2-)
FORMUL   6  HOH   *247(H2 O)
HELIX    1   1 ASN A    6  TYR A   11  5                                   6
HELIX    2   2 ASP A   31  GLY A   46  1                                  16
HELIX    3   3 TRP A   56  GLU A   60  1                                   5
HELIX    4   4 TRP A   69  CYS A   82  1                                  14
HELIX    5   5 PRO A  108  ASN A  118  1                                  11
HELIX    6   6 VAL A  137  ASP A  140  5                                   4
HELIX    7   7 THR A  149  MET A  165  1                                  17
HELIX    8   8 MET A  165  SER A  171  1                                   7
HELIX    9   9 GLY A  182  GLU A  186  5                                   5
HELIX   10  10 PRO A  193  GLY A  197  5                                   5
HELIX   11  11 ASP A  210  ALA A  224  1                                  15
HELIX   12  12 VAL A  241  THR A  245  5                                   5
HELIX   13  13 GLY A  252  VAL A  255  5                                   4
HELIX   14  14 THR A  256  LEU A  286  1                                  31
HELIX   15  15 HIS A  308  GLY A  315  1                                   8
HELIX   16  16 TYR A  325  HIS A  335  1                                  11
HELIX   17  17 ARG A  347  GLN A  351  5                                   5
HELIX   18  18 PRO A  352  LYS A  356  5                                   5
HELIX   19  19 GLY A  358  GLU A  373  1                                  16
HELIX   20  20 ASP A  387  ARG A  399  1                                  13
HELIX   21  21 SER A  422  GLN A  427  1                                   6
HELIX   22  22 GLN A  427  HIS A  442  1                                  16
HELIX   23  23 ASN A  450  ASN A  455  5                                   6
HELIX   24  24 PRO A  469  LEU A  474  1                                   6
HELIX   25  25 GLU A  475  LYS A  478  5                                   4
SHEET    1   A 9 VAL A  14  MET A  17  0
SHEET    2   A 9 GLY A  49  TRP A  55  1  O  MET A  51   N  VAL A  16
SHEET    3   A 9 THR A  85  SER A  91  1  O  ILE A  89   N  VAL A  52
SHEET    4   A 9 ILE A 174  VAL A 179  1  O  TYR A 178   N  MET A  90
SHEET    5   A 9 LYS A 291  VAL A 296  1  O  LYS A 291   N  ILE A 177
SHEET    6   A 9 ILE A 338  PHE A 341  1  O  ASN A 340   N  VAL A 296
SHEET    7   A 9 VAL A 377  GLU A 380  1  O  ALA A 378   N  PHE A 341
SHEET    8   A 9 GLY A 415  TYR A 418  1  O  THR A 417   N  GLY A 379
SHEET    9   A 9 VAL A  14  MET A  17  1  N  TYR A  15   O  TYR A 418
SHEET    1   B 2 PHE A 122  THR A 124  0
SHEET    2   B 2 ARG A 130  LEU A 135 -1  O  ASN A 131   N  TYR A 123
LINK         C1  BGC A 496                 O4 ABGC A 497     1555   1555  1.40
LINK         C1  BGC A 496                 O4 BGLC A1497     1555   1555  1.40
LINK         C1 AGLC A 498                 O4 ABGC A 499     1555   1555  1.40
LINK         C1 BGLC A 498                 O4 BBGC A 499     1555   1555  1.40
CISPEP   1 PHE A  200    PRO A  201          0         0.58
CISPEP   2 LEU A  419    ARG A  420          0         0.17
SITE     1 AC1 11 LEU A  20  ASP A  53  TRP A  55  HIS A  93
SITE     2 AC1 11 ASP A 101  ARG A 420  BGC A 497  HOH A 593
SITE     3 AC1 11 HOH A 594  HOH A 599  GLC A1497
SITE     1 AC2 12 ALA A 184  LYS A 295  THR A 342  GLU A 380
SITE     2 AC2 12 ASN A 381  ALA A 382  LEU A 419  BGC A 496
SITE     3 AC2 12 GLC A 498  HOH A 500  HOH A 581  HOH A 594
SITE     1 AC3 12 VAL A  99  ALA A 184  GLU A 186  LYS A 295
SITE     2 AC3 12 THR A 342  GLU A 380  ALA A 382  BGC A 496
SITE     3 AC3 12 GLC A 498  HOH A 500  HOH A 581  HOH A 594
SITE     1 AC4 16 GLU A 186  ARG A 188  TYR A 192  TRP A 198
SITE     2 AC4 16 PHE A 200  SER A 297  GLY A 298  HIS A 300
SITE     3 AC4 16 TRP A 301  THR A 342  CYS A 343  MET A 346
SITE     4 AC4 16 BGC A 497  BGC A 499  HOH A 596  GLC A1497
SITE     1 AC5  7 VAL A  99  GLN A 194  HIS A 300  MET A 346
SITE     2 AC5  7 LEU A 383  GLC A 498  HOH A 596
SITE     1 AC6  4 GLN A  77  ARG A 372  THR A 480  LEU A 481
SITE     1 AC7  4 HIS A 146  ARG A 326  ARG A 372  LYS A 478
CRYST1   86.818   86.818  145.240  90.00  90.00 120.00 P 31 2 1      6
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      0.011518  0.006650  0.000000        0.00000
SCALE2      0.000000  0.013300  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006885        0.00000
      
PROCHECK
Go to PROCHECK summary
 References