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PDBsum entry 1bga

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Top Page protein Protein-protein interface(s) links
Glycosidase PDB id
1bga
Jmol
Contents
Protein chains
447 a.a. *
Waters ×1541
* Residue conservation analysis
HEADER    GLYCOSIDASE                             04-APR-97   1BGA
TITLE     BETA-GLUCOSIDASE A FROM BACILLUS POLYMYXA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-GLUCOSIDASE A;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: BGA;
COMPND   5 EC: 3.2.1.21;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PAENIBACILLUS POLYMYXA;
SOURCE   3 ORGANISM_TAXID: 1406;
SOURCE   4 ATCC: 842;
SOURCE   5 GENE: BGLA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: JM109 (DE3);
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PUC DERIVATIVE
KEYWDS    FAMILY 1 BETA-GLUCOSIDASE, GLYCOSYL HYDROLASE, GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.SANZ-APARICIO,J.A.HERMOSO,M.MARTINEZ-RIPOLL,J.POLAINA
REVDAT   2   24-FEB-09 1BGA    1       VERSN
REVDAT   1   15-APR-98 1BGA    0
JRNL        AUTH   J.SANZ-APARICIO,J.A.HERMOSO,M.MARTINEZ-RIPOLL,
JRNL        AUTH 2 J.L.LEQUERICA,J.POLAINA
JRNL        TITL   CRYSTAL STRUCTURE OF BETA-GLUCOSIDASE A FROM
JRNL        TITL 2 BACILLUS POLYMYXA: INSIGHTS INTO THE CATALYTIC
JRNL        TITL 3 ACTIVITY IN FAMILY 1 GLYCOSYL HYDROLASES.
JRNL        REF    J.MOL.BIOL.                   V. 275   491 1998
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   9466926
JRNL        DOI    10.1006/JMBI.1997.1467
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.SANZ-APARICIO,A.ROMERO,M.MARTINEZ-RIPOLL,
REMARK   1  AUTH 2 A.MADARRO,A.FLORS,J.POLAINA
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK   1  TITL 2 ANALYSIS OF A TYPE I BETA-GLUCOSIDASE ENCODED BY
REMARK   1  TITL 3 THE BGLA GENE OF BACILLUS POLYMYXA
REMARK   1  REF    J.MOL.BIOL.                   V. 240   267 1994
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1 REFERENCE 2
REMARK   1  AUTH   E.PAINBENI,S.VALLES,J.POLAINA,A.FLORS
REMARK   1  TITL   PURIFICATION AND CHARACTERIZATION OF A BACILLUS
REMARK   1  TITL 2 POLYMYXA BETA-GLUCOSIDASE EXPRESSED IN ESCHERICHIA
REMARK   1  TITL 3 COLI
REMARK   1  REF    J.BACTERIOL.                  V. 174  3087 1992
REMARK   1  REFN                   ISSN 0021-9193
REMARK   2
REMARK   2 RESOLUTION.    2.40 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) : 2.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 78.7
REMARK   3   NUMBER OF REFLECTIONS             : 92319
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) : 0.200
REMARK   3   FREE R VALUE                     : 0.270
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8408
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500
REMARK   3   BIN FREE R VALUE                    : 0.3000
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.00
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            : 14576
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 16
REMARK   3   SOLVENT ATOMS            : 1441
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.60
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) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.51
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.35
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 : RESTRAINTS
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  : PARAMCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSD.PRO
REMARK   3  TOPOLOGY FILE  2   : AMTOPH19.SOL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1BGA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : OCT-96
REMARK 200  TEMPERATURE           (KELVIN) : 176
REMARK 200  PH                             : 8.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : LURE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.983
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 117344
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.540
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 4.700
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : 0.08000
REMARK 200   FOR THE DATA SET  : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000
REMARK 200  R SYM FOR SHELL            (I) : 0.30000
REMARK 200   FOR SHELL         : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.843
REMARK 200 STARTING MODEL: PDB ENTRY 1CBG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 1.3 M
REMARK 280  NA/K PHOSPHATE, PH 8.3, 5 MICRO-L PROTEIN, 14 MG/ML, 5 MICRO-L
REMARK 280  RESERVOIR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-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        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000      102.73000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      102.73000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       77.93000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      102.73000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      102.73000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       77.93000
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      102.73000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      102.73000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       77.93000
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      102.73000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.73000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       77.93000
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      155.86000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 430   CD    GLU A 430   OE2     0.074
REMARK 500    GLU B 430   CD    GLU B 430   OE2     0.073
REMARK 500    GLU C 430   CD    GLU C 430   OE2     0.067
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    ALA A  24       62.34   -159.52
REMARK 500    ALA A  54     -122.29     46.56
REMARK 500    PRO A  83        1.04    -62.30
REMARK 500    TRP A 122      -12.36     79.84
REMARK 500    HIS A 155      -86.49    -32.10
REMARK 500    GLU A 166       65.59     62.12
REMARK 500    TYR A 296      -44.14   -135.00
REMARK 500    SER A 399      105.98     83.65
REMARK 500    TRP A 406     -126.49     45.41
REMARK 500    ALA B  24       62.51   -159.81
REMARK 500    ALA B  54     -123.02     48.12
REMARK 500    PRO B  83        1.35    -62.84
REMARK 500    TRP B 122      -10.97     78.78
REMARK 500    HIS B 155      -86.78    -31.55
REMARK 500    GLU B 166       66.03     62.24
REMARK 500    TYR B 296      -44.19   -134.16
REMARK 500    ASN B 353      119.92   -162.23
REMARK 500    SER B 399      106.10     83.04
REMARK 500    TRP B 406     -125.45     44.50
REMARK 500    PHE B 421       -9.81    -59.97
REMARK 500    ALA C  24       63.43   -161.01
REMARK 500    ALA C  54     -121.31     48.09
REMARK 500    PRO C  83        0.32    -62.96
REMARK 500    TRP C 122      -11.26     77.97
REMARK 500    HIS C 155      -86.70    -31.58
REMARK 500    GLU C 166       65.35     60.96
REMARK 500    SER C 247      -60.22   -109.54
REMARK 500    TYR C 296      -43.13   -133.45
REMARK 500    SER C 399      105.60     83.38
REMARK 500    TRP C 406     -125.71     44.36
REMARK 500    ALA D  24       62.66   -159.62
REMARK 500    ALA D  54     -121.15     47.72
REMARK 500    PRO D  83        0.44    -63.22
REMARK 500    TRP D 122      -12.92     79.34
REMARK 500    HIS D 155      -87.82    -30.63
REMARK 500    GLU D 166       65.33     61.07
REMARK 500    TYR D 296      -43.73   -134.04
REMARK 500    SER D 399      105.32     83.80
REMARK 500    TRP D 406     -126.17     44.55
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 C 465        DISTANCE =  6.32 ANGSTROMS
REMARK 525    HOH D 477        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH B 561        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH C 626        DISTANCE =  6.43 ANGSTROMS
REMARK 525    HOH C 629        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH A 694        DISTANCE =  6.64 ANGSTROMS
REMARK 525    HOH D 701        DISTANCE =  6.71 ANGSTROMS
REMARK 525    HOH A 704        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH D 739        DISTANCE =  8.07 ANGSTROMS
REMARK 525    HOH C 740        DISTANCE =  6.98 ANGSTROMS
REMARK 525    HOH A 753        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH C 759        DISTANCE =  5.90 ANGSTROMS
REMARK 525    HOH D 769        DISTANCE =  6.30 ANGSTROMS
REMARK 525    HOH B 773        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH C 788        DISTANCE =  6.14 ANGSTROMS
REMARK 525    HOH B 798        DISTANCE =  6.77 ANGSTROMS
REMARK 525    HOH D 814        DISTANCE =  5.78 ANGSTROMS
REMARK 525    HOH A 825        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH B 828        DISTANCE =  5.74 ANGSTROMS
DBREF  1BGA A    2   448  UNP    P22073   BGLA_PAEPO       2    448
DBREF  1BGA B    2   448  UNP    P22073   BGLA_PAEPO       2    448
DBREF  1BGA C    2   448  UNP    P22073   BGLA_PAEPO       2    448
DBREF  1BGA D    2   448  UNP    P22073   BGLA_PAEPO       2    448
SEQRES   1 A  447  THR ILE PHE GLN PHE PRO GLN ASP PHE MET TRP GLY THR
SEQRES   2 A  447  ALA THR ALA ALA TYR GLN ILE GLU GLY ALA TYR GLN GLU
SEQRES   3 A  447  ASP GLY ARG GLY LEU SER ILE TRP ASP THR PHE ALA HIS
SEQRES   4 A  447  THR PRO GLY LYS VAL PHE ASN GLY ASP ASN GLY ASN VAL
SEQRES   5 A  447  ALA CYS ASP SER TYR HIS ARG TYR GLU GLU ASP ILE ARG
SEQRES   6 A  447  LEU MET LYS GLU LEU GLY ILE ARG THR TYR ARG PHE SER
SEQRES   7 A  447  VAL SER TRP PRO ARG ILE PHE PRO ASN GLY ASP GLY GLU
SEQRES   8 A  447  VAL ASN GLN GLU GLY LEU ASP TYR TYR HIS ARG VAL VAL
SEQRES   9 A  447  ASP LEU LEU ASN ASP ASN GLY ILE GLU PRO PHE CYS THR
SEQRES  10 A  447  LEU TYR HIS TRP ASP LEU PRO GLN ALA LEU GLN ASP ALA
SEQRES  11 A  447  GLY GLY TRP GLY ASN ARG ARG THR ILE GLN ALA PHE VAL
SEQRES  12 A  447  GLN PHE ALA GLU THR MET PHE ARG GLU PHE HIS GLY LYS
SEQRES  13 A  447  ILE GLN HIS TRP LEU THR PHE ASN GLU PRO TRP CYS ILE
SEQRES  14 A  447  ALA PHE LEU SER ASN MET LEU GLY VAL HIS ALA PRO GLY
SEQRES  15 A  447  LEU THR ASN LEU GLN THR ALA ILE ASP VAL GLY HIS HIS
SEQRES  16 A  447  LEU LEU VAL ALA HIS GLY LEU SER VAL ARG ARG PHE ARG
SEQRES  17 A  447  GLU LEU GLY THR SER GLY GLN ILE GLY ILE ALA PRO ASN
SEQRES  18 A  447  VAL SER TRP ALA VAL PRO TYR SER THR SER GLU GLU ASP
SEQRES  19 A  447  LYS ALA ALA CYS ALA ARG THR ILE SER LEU HIS SER ASP
SEQRES  20 A  447  TRP PHE LEU GLN PRO ILE TYR GLN GLY SER TYR PRO GLN
SEQRES  21 A  447  PHE LEU VAL ASP TRP PHE ALA GLU GLN GLY ALA THR VAL
SEQRES  22 A  447  PRO ILE GLN ASP GLY ASP MET ASP ILE ILE GLY GLU PRO
SEQRES  23 A  447  ILE ASP MET ILE GLY ILE ASN TYR TYR SER MET SER VAL
SEQRES  24 A  447  ASN ARG PHE ASN PRO GLU ALA GLY PHE LEU GLN SER GLU
SEQRES  25 A  447  GLU ILE ASN MET GLY LEU PRO VAL THR ASP ILE GLY TRP
SEQRES  26 A  447  PRO VAL GLU SER ARG GLY LEU TYR GLU VAL LEU HIS TYR
SEQRES  27 A  447  LEU GLN LYS TYR GLY ASN ILE ASP ILE TYR ILE THR GLU
SEQRES  28 A  447  ASN GLY ALA CYS ILE ASN ASP GLU VAL VAL ASN GLY LYS
SEQRES  29 A  447  VAL GLN ASP ASP ARG ARG ILE SER TYR MET GLN GLN HIS
SEQRES  30 A  447  LEU VAL GLN VAL HIS ARG THR ILE HIS ASP GLY LEU HIS
SEQRES  31 A  447  VAL LYS GLY TYR MET ALA TRP SER LEU LEU ASP ASN PHE
SEQRES  32 A  447  GLU TRP ALA GLU GLY TYR ASN MET ARG PHE GLY MET ILE
SEQRES  33 A  447  HIS VAL ASP PHE ARG THR GLN VAL ARG THR PRO LYS GLU
SEQRES  34 A  447  SER TYR TYR TRP TYR ARG ASN VAL VAL SER ASN ASN TRP
SEQRES  35 A  447  LEU GLU THR ARG ARG
SEQRES   1 B  447  THR ILE PHE GLN PHE PRO GLN ASP PHE MET TRP GLY THR
SEQRES   2 B  447  ALA THR ALA ALA TYR GLN ILE GLU GLY ALA TYR GLN GLU
SEQRES   3 B  447  ASP GLY ARG GLY LEU SER ILE TRP ASP THR PHE ALA HIS
SEQRES   4 B  447  THR PRO GLY LYS VAL PHE ASN GLY ASP ASN GLY ASN VAL
SEQRES   5 B  447  ALA CYS ASP SER TYR HIS ARG TYR GLU GLU ASP ILE ARG
SEQRES   6 B  447  LEU MET LYS GLU LEU GLY ILE ARG THR TYR ARG PHE SER
SEQRES   7 B  447  VAL SER TRP PRO ARG ILE PHE PRO ASN GLY ASP GLY GLU
SEQRES   8 B  447  VAL ASN GLN GLU GLY LEU ASP TYR TYR HIS ARG VAL VAL
SEQRES   9 B  447  ASP LEU LEU ASN ASP ASN GLY ILE GLU PRO PHE CYS THR
SEQRES  10 B  447  LEU TYR HIS TRP ASP LEU PRO GLN ALA LEU GLN ASP ALA
SEQRES  11 B  447  GLY GLY TRP GLY ASN ARG ARG THR ILE GLN ALA PHE VAL
SEQRES  12 B  447  GLN PHE ALA GLU THR MET PHE ARG GLU PHE HIS GLY LYS
SEQRES  13 B  447  ILE GLN HIS TRP LEU THR PHE ASN GLU PRO TRP CYS ILE
SEQRES  14 B  447  ALA PHE LEU SER ASN MET LEU GLY VAL HIS ALA PRO GLY
SEQRES  15 B  447  LEU THR ASN LEU GLN THR ALA ILE ASP VAL GLY HIS HIS
SEQRES  16 B  447  LEU LEU VAL ALA HIS GLY LEU SER VAL ARG ARG PHE ARG
SEQRES  17 B  447  GLU LEU GLY THR SER GLY GLN ILE GLY ILE ALA PRO ASN
SEQRES  18 B  447  VAL SER TRP ALA VAL PRO TYR SER THR SER GLU GLU ASP
SEQRES  19 B  447  LYS ALA ALA CYS ALA ARG THR ILE SER LEU HIS SER ASP
SEQRES  20 B  447  TRP PHE LEU GLN PRO ILE TYR GLN GLY SER TYR PRO GLN
SEQRES  21 B  447  PHE LEU VAL ASP TRP PHE ALA GLU GLN GLY ALA THR VAL
SEQRES  22 B  447  PRO ILE GLN ASP GLY ASP MET ASP ILE ILE GLY GLU PRO
SEQRES  23 B  447  ILE ASP MET ILE GLY ILE ASN TYR TYR SER MET SER VAL
SEQRES  24 B  447  ASN ARG PHE ASN PRO GLU ALA GLY PHE LEU GLN SER GLU
SEQRES  25 B  447  GLU ILE ASN MET GLY LEU PRO VAL THR ASP ILE GLY TRP
SEQRES  26 B  447  PRO VAL GLU SER ARG GLY LEU TYR GLU VAL LEU HIS TYR
SEQRES  27 B  447  LEU GLN LYS TYR GLY ASN ILE ASP ILE TYR ILE THR GLU
SEQRES  28 B  447  ASN GLY ALA CYS ILE ASN ASP GLU VAL VAL ASN GLY LYS
SEQRES  29 B  447  VAL GLN ASP ASP ARG ARG ILE SER TYR MET GLN GLN HIS
SEQRES  30 B  447  LEU VAL GLN VAL HIS ARG THR ILE HIS ASP GLY LEU HIS
SEQRES  31 B  447  VAL LYS GLY TYR MET ALA TRP SER LEU LEU ASP ASN PHE
SEQRES  32 B  447  GLU TRP ALA GLU GLY TYR ASN MET ARG PHE GLY MET ILE
SEQRES  33 B  447  HIS VAL ASP PHE ARG THR GLN VAL ARG THR PRO LYS GLU
SEQRES  34 B  447  SER TYR TYR TRP TYR ARG ASN VAL VAL SER ASN ASN TRP
SEQRES  35 B  447  LEU GLU THR ARG ARG
SEQRES   1 C  447  THR ILE PHE GLN PHE PRO GLN ASP PHE MET TRP GLY THR
SEQRES   2 C  447  ALA THR ALA ALA TYR GLN ILE GLU GLY ALA TYR GLN GLU
SEQRES   3 C  447  ASP GLY ARG GLY LEU SER ILE TRP ASP THR PHE ALA HIS
SEQRES   4 C  447  THR PRO GLY LYS VAL PHE ASN GLY ASP ASN GLY ASN VAL
SEQRES   5 C  447  ALA CYS ASP SER TYR HIS ARG TYR GLU GLU ASP ILE ARG
SEQRES   6 C  447  LEU MET LYS GLU LEU GLY ILE ARG THR TYR ARG PHE SER
SEQRES   7 C  447  VAL SER TRP PRO ARG ILE PHE PRO ASN GLY ASP GLY GLU
SEQRES   8 C  447  VAL ASN GLN GLU GLY LEU ASP TYR TYR HIS ARG VAL VAL
SEQRES   9 C  447  ASP LEU LEU ASN ASP ASN GLY ILE GLU PRO PHE CYS THR
SEQRES  10 C  447  LEU TYR HIS TRP ASP LEU PRO GLN ALA LEU GLN ASP ALA
SEQRES  11 C  447  GLY GLY TRP GLY ASN ARG ARG THR ILE GLN ALA PHE VAL
SEQRES  12 C  447  GLN PHE ALA GLU THR MET PHE ARG GLU PHE HIS GLY LYS
SEQRES  13 C  447  ILE GLN HIS TRP LEU THR PHE ASN GLU PRO TRP CYS ILE
SEQRES  14 C  447  ALA PHE LEU SER ASN MET LEU GLY VAL HIS ALA PRO GLY
SEQRES  15 C  447  LEU THR ASN LEU GLN THR ALA ILE ASP VAL GLY HIS HIS
SEQRES  16 C  447  LEU LEU VAL ALA HIS GLY LEU SER VAL ARG ARG PHE ARG
SEQRES  17 C  447  GLU LEU GLY THR SER GLY GLN ILE GLY ILE ALA PRO ASN
SEQRES  18 C  447  VAL SER TRP ALA VAL PRO TYR SER THR SER GLU GLU ASP
SEQRES  19 C  447  LYS ALA ALA CYS ALA ARG THR ILE SER LEU HIS SER ASP
SEQRES  20 C  447  TRP PHE LEU GLN PRO ILE TYR GLN GLY SER TYR PRO GLN
SEQRES  21 C  447  PHE LEU VAL ASP TRP PHE ALA GLU GLN GLY ALA THR VAL
SEQRES  22 C  447  PRO ILE GLN ASP GLY ASP MET ASP ILE ILE GLY GLU PRO
SEQRES  23 C  447  ILE ASP MET ILE GLY ILE ASN TYR TYR SER MET SER VAL
SEQRES  24 C  447  ASN ARG PHE ASN PRO GLU ALA GLY PHE LEU GLN SER GLU
SEQRES  25 C  447  GLU ILE ASN MET GLY LEU PRO VAL THR ASP ILE GLY TRP
SEQRES  26 C  447  PRO VAL GLU SER ARG GLY LEU TYR GLU VAL LEU HIS TYR
SEQRES  27 C  447  LEU GLN LYS TYR GLY ASN ILE ASP ILE TYR ILE THR GLU
SEQRES  28 C  447  ASN GLY ALA CYS ILE ASN ASP GLU VAL VAL ASN GLY LYS
SEQRES  29 C  447  VAL GLN ASP ASP ARG ARG ILE SER TYR MET GLN GLN HIS
SEQRES  30 C  447  LEU VAL GLN VAL HIS ARG THR ILE HIS ASP GLY LEU HIS
SEQRES  31 C  447  VAL LYS GLY TYR MET ALA TRP SER LEU LEU ASP ASN PHE
SEQRES  32 C  447  GLU TRP ALA GLU GLY TYR ASN MET ARG PHE GLY MET ILE
SEQRES  33 C  447  HIS VAL ASP PHE ARG THR GLN VAL ARG THR PRO LYS GLU
SEQRES  34 C  447  SER TYR TYR TRP TYR ARG ASN VAL VAL SER ASN ASN TRP
SEQRES  35 C  447  LEU GLU THR ARG ARG
SEQRES   1 D  447  THR ILE PHE GLN PHE PRO GLN ASP PHE MET TRP GLY THR
SEQRES   2 D  447  ALA THR ALA ALA TYR GLN ILE GLU GLY ALA TYR GLN GLU
SEQRES   3 D  447  ASP GLY ARG GLY LEU SER ILE TRP ASP THR PHE ALA HIS
SEQRES   4 D  447  THR PRO GLY LYS VAL PHE ASN GLY ASP ASN GLY ASN VAL
SEQRES   5 D  447  ALA CYS ASP SER TYR HIS ARG TYR GLU GLU ASP ILE ARG
SEQRES   6 D  447  LEU MET LYS GLU LEU GLY ILE ARG THR TYR ARG PHE SER
SEQRES   7 D  447  VAL SER TRP PRO ARG ILE PHE PRO ASN GLY ASP GLY GLU
SEQRES   8 D  447  VAL ASN GLN GLU GLY LEU ASP TYR TYR HIS ARG VAL VAL
SEQRES   9 D  447  ASP LEU LEU ASN ASP ASN GLY ILE GLU PRO PHE CYS THR
SEQRES  10 D  447  LEU TYR HIS TRP ASP LEU PRO GLN ALA LEU GLN ASP ALA
SEQRES  11 D  447  GLY GLY TRP GLY ASN ARG ARG THR ILE GLN ALA PHE VAL
SEQRES  12 D  447  GLN PHE ALA GLU THR MET PHE ARG GLU PHE HIS GLY LYS
SEQRES  13 D  447  ILE GLN HIS TRP LEU THR PHE ASN GLU PRO TRP CYS ILE
SEQRES  14 D  447  ALA PHE LEU SER ASN MET LEU GLY VAL HIS ALA PRO GLY
SEQRES  15 D  447  LEU THR ASN LEU GLN THR ALA ILE ASP VAL GLY HIS HIS
SEQRES  16 D  447  LEU LEU VAL ALA HIS GLY LEU SER VAL ARG ARG PHE ARG
SEQRES  17 D  447  GLU LEU GLY THR SER GLY GLN ILE GLY ILE ALA PRO ASN
SEQRES  18 D  447  VAL SER TRP ALA VAL PRO TYR SER THR SER GLU GLU ASP
SEQRES  19 D  447  LYS ALA ALA CYS ALA ARG THR ILE SER LEU HIS SER ASP
SEQRES  20 D  447  TRP PHE LEU GLN PRO ILE TYR GLN GLY SER TYR PRO GLN
SEQRES  21 D  447  PHE LEU VAL ASP TRP PHE ALA GLU GLN GLY ALA THR VAL
SEQRES  22 D  447  PRO ILE GLN ASP GLY ASP MET ASP ILE ILE GLY GLU PRO
SEQRES  23 D  447  ILE ASP MET ILE GLY ILE ASN TYR TYR SER MET SER VAL
SEQRES  24 D  447  ASN ARG PHE ASN PRO GLU ALA GLY PHE LEU GLN SER GLU
SEQRES  25 D  447  GLU ILE ASN MET GLY LEU PRO VAL THR ASP ILE GLY TRP
SEQRES  26 D  447  PRO VAL GLU SER ARG GLY LEU TYR GLU VAL LEU HIS TYR
SEQRES  27 D  447  LEU GLN LYS TYR GLY ASN ILE ASP ILE TYR ILE THR GLU
SEQRES  28 D  447  ASN GLY ALA CYS ILE ASN ASP GLU VAL VAL ASN GLY LYS
SEQRES  29 D  447  VAL GLN ASP ASP ARG ARG ILE SER TYR MET GLN GLN HIS
SEQRES  30 D  447  LEU VAL GLN VAL HIS ARG THR ILE HIS ASP GLY LEU HIS
SEQRES  31 D  447  VAL LYS GLY TYR MET ALA TRP SER LEU LEU ASP ASN PHE
SEQRES  32 D  447  GLU TRP ALA GLU GLY TYR ASN MET ARG PHE GLY MET ILE
SEQRES  33 D  447  HIS VAL ASP PHE ARG THR GLN VAL ARG THR PRO LYS GLU
SEQRES  34 D  447  SER TYR TYR TRP TYR ARG ASN VAL VAL SER ASN ASN TRP
SEQRES  35 D  447  LEU GLU THR ARG ARG
FORMUL   5  HOH   *1541(H2 O)
HELIX    1   1 ALA A   18  ILE A   21  1                                   4
HELIX    2   2 GLU A   27  GLY A   29  5                                   3
HELIX    3   3 ILE A   34  ALA A   39  1                                   6
HELIX    4   4 PHE A   46  GLY A   48  5                                   3
HELIX    5   5 SER A   57  GLU A   70  1                                  14
HELIX    6   6 TRP A   82  ILE A   85  1                                   4
HELIX    7   7 GLN A   95  ASN A  111  1                                  17
HELIX    8   8 GLN A  126  ASP A  130  1                                   5
HELIX    9   9 GLY A  133  GLY A  135  5                                   3
HELIX   10  10 ARG A  138  GLU A  153  1                                  16
HELIX   11  11 HIS A  155  LYS A  157  5                                   3
HELIX   12  12 PRO A  167  ASN A  175  1                                   9
HELIX   13  13 LEU A  187  GLU A  210  1                                  24
HELIX   14  14 GLU A  233  HIS A  246  1                                  14
HELIX   15  15 ASP A  248  GLN A  256  1                                   9
HELIX   16  16 GLN A  261  GLN A  270  1                                  10
HELIX   17  17 ASP A  280  ILE A  284  1                                   5
HELIX   18  18 GLY A  308  LEU A  310  5                                   3
HELIX   19  19 SER A  330  TYR A  343  5                                  14
HELIX   20  20 ASP A  369  ASP A  388  1                                  20
HELIX   21  21 TRP A  406  ASN A  411  5                                   6
HELIX   22  22 GLU A  430  ASN A  441  1                                  12
HELIX   23  23 ALA B   18  ILE B   21  1                                   4
HELIX   24  24 GLU B   27  GLY B   29  5                                   3
HELIX   25  25 ILE B   34  ALA B   39  1                                   6
HELIX   26  26 PHE B   46  GLY B   48  5                                   3
HELIX   27  27 SER B   57  GLU B   70  1                                  14
HELIX   28  28 TRP B   82  ILE B   85  1                                   4
HELIX   29  29 GLN B   95  ASN B  111  1                                  17
HELIX   30  30 GLN B  126  ASP B  130  1                                   5
HELIX   31  31 GLY B  133  GLY B  135  5                                   3
HELIX   32  32 ARG B  138  GLU B  153  1                                  16
HELIX   33  33 HIS B  155  LYS B  157  5                                   3
HELIX   34  34 PRO B  167  ASN B  175  1                                   9
HELIX   35  35 LEU B  187  LEU B  211  1                                  25
HELIX   36  36 GLU B  233  HIS B  246  1                                  14
HELIX   37  37 ASP B  248  GLN B  256  1                                   9
HELIX   38  38 GLN B  261  GLN B  270  1                                  10
HELIX   39  39 ASP B  280  ILE B  284  1                                   5
HELIX   40  40 SER B  330  TYR B  343  5                                  14
HELIX   41  41 ASP B  369  HIS B  387  1                                  19
HELIX   42  42 TRP B  406  GLU B  408  5                                   3
HELIX   43  43 GLU B  430  ASN B  441  1                                  12
HELIX   44  44 ALA C   18  ILE C   21  1                                   4
HELIX   45  45 GLU C   27  GLY C   29  5                                   3
HELIX   46  46 ILE C   34  ALA C   39  1                                   6
HELIX   47  47 PHE C   46  GLY C   48  5                                   3
HELIX   48  48 SER C   57  GLU C   70  1                                  14
HELIX   49  49 TRP C   82  ILE C   85  1                                   4
HELIX   50  50 GLN C   95  ASN C  111  1                                  17
HELIX   51  51 GLN C  126  ASP C  130  1                                   5
HELIX   52  52 GLY C  133  GLY C  135  5                                   3
HELIX   53  53 ARG C  137  GLU C  153  5                                  17
HELIX   54  54 HIS C  155  LYS C  157  5                                   3
HELIX   55  55 PRO C  167  ASN C  175  1                                   9
HELIX   56  56 LEU C  187  LEU C  211  1                                  25
HELIX   57  57 GLU C  233  HIS C  246  1                                  14
HELIX   58  58 ASP C  248  GLN C  256  1                                   9
HELIX   59  59 GLN C  261  GLN C  270  1                                  10
HELIX   60  60 ASP C  280  ILE C  284  1                                   5
HELIX   61  61 SER C  330  TYR C  343  5                                  14
HELIX   62  62 ASP C  369  HIS C  387  1                                  19
HELIX   63  63 TRP C  406  GLU C  408  5                                   3
HELIX   64  64 GLU C  430  ASN C  441  1                                  12
HELIX   65  65 ALA D   18  ILE D   21  1                                   4
HELIX   66  66 GLU D   27  GLY D   29  5                                   3
HELIX   67  67 ILE D   34  ALA D   39  1                                   6
HELIX   68  68 PHE D   46  GLY D   48  5                                   3
HELIX   69  69 SER D   57  GLU D   70  1                                  14
HELIX   70  70 TRP D   82  ILE D   85  1                                   4
HELIX   71  71 GLN D   95  ASN D  111  1                                  17
HELIX   72  72 GLN D  126  ASP D  130  1                                   5
HELIX   73  73 GLY D  133  GLY D  135  5                                   3
HELIX   74  74 ARG D  137  GLU D  153  1                                  17
HELIX   75  75 HIS D  155  LYS D  157  5                                   3
HELIX   76  76 PRO D  167  ASN D  175  1                                   9
HELIX   77  77 LEU D  187  LEU D  211  1                                  25
HELIX   78  78 GLU D  233  HIS D  246  1                                  14
HELIX   79  79 ASP D  248  GLN D  256  1                                   9
HELIX   80  80 GLN D  261  GLN D  270  1                                  10
HELIX   81  81 ASP D  280  ILE D  284  1                                   5
HELIX   82  82 SER D  330  TYR D  343  5                                  14
HELIX   83  83 ASP D  369  ASP D  388  1                                  20
HELIX   84  84 TRP D  406  ASN D  411  5                                   6
HELIX   85  85 GLU D  430  ASN D  441  1                                  12
SHEET    1   A 2 ILE A   3  GLN A   5  0
SHEET    2   A 2 TRP A 443  GLU A 445 -1  N  LEU A 444   O  PHE A   4
SHEET    1   B 9 GLY A 394  TRP A 398  0
SHEET    2   B 9 MET A  11  ALA A  15  1  N  MET A  11   O  TYR A 395
SHEET    3   B 9 THR A  75  SER A  79  1  N  THR A  75   O  THR A  14
SHEET    4   B 9 GLU A 114  THR A 118  1  N  GLU A 114   O  TYR A  76
SHEET    5   B 9 HIS A 160  LEU A 162  1  N  HIS A 160   O  CYS A 117
SHEET    6   B 9 GLN A 216  ASN A 222  1  N  GLN A 216   O  TRP A 161
SHEET    7   B 9 MET A 290  ASN A 294  1  N  MET A 290   O  ILE A 219
SHEET    8   B 9 ILE A 348  GLU A 352  1  N  TYR A 349   O  ILE A 291
SHEET    9   B 9 VAL A 392  TYR A 395  1  N  LYS A 393   O  ILE A 348
SHEET    1   C 3 ALA A 226  PRO A 228  0
SHEET    2   C 3 SER A 299  PHE A 303  1  N  SER A 299   O  VAL A 227
SHEET    3   C 3 SER A 312  ILE A 315 -1  N  ILE A 315   O  VAL A 300
SHEET    1   D 2 ILE A 417  ASP A 420  0
SHEET    2   D 2 VAL A 425  PRO A 428 -1  N  THR A 427   O  HIS A 418
SHEET    1   E 2 ILE B   3  GLN B   5  0
SHEET    2   E 2 TRP B 443  GLU B 445 -1  N  LEU B 444   O  PHE B   4
SHEET    1   F 9 GLY B 394  TRP B 398  0
SHEET    2   F 9 MET B  11  ALA B  15  1  N  MET B  11   O  TYR B 395
SHEET    3   F 9 THR B  75  SER B  79  1  N  THR B  75   O  THR B  14
SHEET    4   F 9 GLU B 114  THR B 118  1  N  GLU B 114   O  TYR B  76
SHEET    5   F 9 HIS B 160  LEU B 162  1  N  HIS B 160   O  CYS B 117
SHEET    6   F 9 GLN B 216  ASN B 222  1  N  GLN B 216   O  TRP B 161
SHEET    7   F 9 MET B 290  ASN B 294  1  N  MET B 290   O  ILE B 219
SHEET    8   F 9 ILE B 348  GLU B 352  1  N  TYR B 349   O  ILE B 291
SHEET    9   F 9 VAL B 392  TYR B 395  1  N  LYS B 393   O  ILE B 348
SHEET    1   G 3 ALA B 226  PRO B 228  0
SHEET    2   G 3 SER B 299  PHE B 303  1  N  SER B 299   O  VAL B 227
SHEET    3   G 3 SER B 312  ILE B 315 -1  N  ILE B 315   O  VAL B 300
SHEET    1   H 2 ILE B 417  ASP B 420  0
SHEET    2   H 2 VAL B 425  PRO B 428 -1  N  THR B 427   O  HIS B 418
SHEET    1   I 2 ILE C   3  GLN C   5  0
SHEET    2   I 2 TRP C 443  GLU C 445 -1  N  LEU C 444   O  PHE C   4
SHEET    1   J 9 GLY C 394  TRP C 398  0
SHEET    2   J 9 MET C  11  ALA C  15  1  N  MET C  11   O  TYR C 395
SHEET    3   J 9 THR C  75  SER C  79  1  N  THR C  75   O  THR C  14
SHEET    4   J 9 GLU C 114  THR C 118  1  N  GLU C 114   O  TYR C  76
SHEET    5   J 9 HIS C 160  LEU C 162  1  N  HIS C 160   O  CYS C 117
SHEET    6   J 9 GLN C 216  ASN C 222  1  N  GLN C 216   O  TRP C 161
SHEET    7   J 9 MET C 290  ASN C 294  1  N  MET C 290   O  ILE C 219
SHEET    8   J 9 ILE C 348  GLU C 352  1  N  TYR C 349   O  ILE C 291
SHEET    9   J 9 VAL C 392  TYR C 395  1  N  LYS C 393   O  ILE C 348
SHEET    1   K 3 ALA C 226  PRO C 228  0
SHEET    2   K 3 SER C 299  PHE C 303  1  N  SER C 299   O  VAL C 227
SHEET    3   K 3 SER C 312  ILE C 315 -1  N  ILE C 315   O  VAL C 300
SHEET    1   L 2 ILE C 417  ASP C 420  0
SHEET    2   L 2 VAL C 425  PRO C 428 -1  N  THR C 427   O  HIS C 418
SHEET    1   M 2 ILE D   3  GLN D   5  0
SHEET    2   M 2 TRP D 443  GLU D 445 -1  N  LEU D 444   O  PHE D   4
SHEET    1   N 9 GLY D 394  TRP D 398  0
SHEET    2   N 9 MET D  11  ALA D  15  1  N  MET D  11   O  TYR D 395
SHEET    3   N 9 THR D  75  SER D  79  1  N  THR D  75   O  THR D  14
SHEET    4   N 9 GLU D 114  THR D 118  1  N  GLU D 114   O  TYR D  76
SHEET    5   N 9 HIS D 160  LEU D 162  1  N  HIS D 160   O  CYS D 117
SHEET    6   N 9 GLN D 216  ASN D 222  1  N  GLN D 216   O  TRP D 161
SHEET    7   N 9 MET D 290  ASN D 294  1  N  MET D 290   O  ILE D 219
SHEET    8   N 9 ILE D 348  GLU D 352  1  N  TYR D 349   O  ILE D 291
SHEET    9   N 9 VAL D 392  TYR D 395  1  N  LYS D 393   O  ILE D 348
SHEET    1   O 3 ALA D 226  PRO D 228  0
SHEET    2   O 3 SER D 299  PHE D 303  1  N  SER D 299   O  VAL D 227
SHEET    3   O 3 SER D 312  ILE D 315 -1  N  ILE D 315   O  VAL D 300
SHEET    1   P 2 ILE D 417  ASP D 420  0
SHEET    2   P 2 VAL D 425  PRO D 428 -1  N  THR D 427   O  HIS D 418
CISPEP   1 ALA A  181    PRO A  182          0         0.96
CISPEP   2 ALA B  181    PRO B  182          0        -0.01
CISPEP   3 ALA C  181    PRO C  182          0        -1.11
CISPEP   4 ALA D  181    PRO D  182          0         0.89
CRYST1  205.460  205.460  155.860  90.00  90.00  90.00 P 42 21 2    32
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      0.004867  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004867  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006416        0.00000
MTRIX1   1 -0.003907 -0.999992  0.000477      100.85710    1
MTRIX2   1  0.999971 -0.003904  0.006489       -0.45350    1
MTRIX3   1 -0.006487  0.000502  0.999979        0.22540    1
MTRIX1   2 -0.999873  0.002548 -0.015757      101.69910    1
MTRIX2   2 -0.002653 -0.999975  0.006625      100.07450    1
MTRIX3   2 -0.015740  0.006666  0.999854        0.22180    1
MTRIX1   3 -0.002523  0.999869 -0.015986        1.28930    1
MTRIX2   3 -0.999997 -0.002534 -0.000679      100.81960    1
MTRIX3   3 -0.000719  0.015984  0.999872       -0.93910    1
      
PROCHECK
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 References