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PDBsum entry 3ac0

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3ac0
Jmol
Contents
Protein chains
841 a.a.
Ligands
BGC ×4
Waters ×1564
HEADER    HYDROLASE                               25-DEC-09   3AC0
TITLE     CRYSTAL STRUCTURE OF BETA-GLUCOSIDASE FROM KLUYVEROMYCES MARXIANUS IN
TITLE    2 COMPLEX WITH GLUCOSE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA-GLUCOSIDASE I;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 EC: 3.2.1.21;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES MARXIANUS;
SOURCE   3 ORGANISM_COMMON: YEAST;
SOURCE   4 ORGANISM_TAXID: 4911;
SOURCE   5 STRAIN: NBRC1777;
SOURCE   6 GENE: BGL, BGLI;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS    GLYCOSIDE HYDROLASE FAMILY3 BETA-GLUCOSIDASE, PA14 DOMAIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.YOSHIDA,M.HIDAKA,S.FUSHINOBU,T.KATAYAMA,H.KUMAGAI
REVDAT   2   30-OCT-13 3AC0    1       JRNL   VERSN
REVDAT   1   11-AUG-10 3AC0    0
JRNL        AUTH   E.YOSHIDA,M.HIDAKA,S.FUSHINOBU,T.KOYANAGI,H.MINAMI,H.TAMAKI,
JRNL        AUTH 2 M.KITAOKA,T.KATAYAMA,H.KUMAGAI
JRNL        TITL   ROLE OF A PA14 DOMAIN IN DETERMINING SUBSTRATE SPECIFICITY
JRNL        TITL 2 OF A GLYCOSIDE HYDROLASE FAMILY 3 BETA-GLUCOSIDASE FROM
JRNL        TITL 3 KLUYVEROMYCES MARXIANUS.
JRNL        REF    BIOCHEM.J.                    V. 431    39 2010
JRNL        REFN                   ISSN 0264-6021
JRNL        PMID   20662765
JRNL        DOI    10.1042/BJ20100351
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   E.YOSHIDA,M.HIDAKA,S.FUSHINOBU,T.KOYANAGI,H.MINAMI,H.TAMAKI,
REMARK   1  AUTH 2 M.KITAOKA,T.KATAYAMA,H.KUMAGAI
REMARK   1  TITL   PURIFICATION, CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS
REMARK   1  TITL 2 OF BETA-GLUCOSIDASE FROM KLUYVEROMYCES MARXIANUS NBRC1777
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  65  1190 2009
REMARK   1  REFN                   ESSN 1744-3091
REMARK   1  PMID   19923748
REMARK   1  DOI    10.1107/S1744309109042948
REMARK   2
REMARK   2 RESOLUTION.    2.54 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0072
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.54
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 123171
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 + TEST SET) : 0.173
REMARK   3   R VALUE            (WORKING SET) : 0.169
REMARK   3   FREE R VALUE                     : 0.242
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6526
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.54
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.60
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8658
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.86
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320
REMARK   3   BIN FREE R VALUE SET COUNT          : 414
REMARK   3   BIN FREE R VALUE                    : 0.3440
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 26051
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 48
REMARK   3   SOLVENT ATOMS            : 1564
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.58000
REMARK   3    B22 (A**2) : -0.08000
REMARK   3    B33 (A**2) : 0.57000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.12000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.651
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.297
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 26630 ; 0.018 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 36005 ; 1.692 ; 1.962
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3311 ; 6.925 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1234 ;37.902 ;24.976
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4633 ;17.846 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   123 ;19.282 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3960 ; 0.112 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20150 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 16463 ; 0.787 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 26498 ; 1.478 ; 2.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 10167 ; 2.304 ; 3.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9507 ; 3.705 ; 4.500
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3AC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB029066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.1
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-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97831, 0.97928, 0.96405
REMARK 200  MONOCHROMATOR                  : SI 111
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129736
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.540
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.08900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM DIHYDROGEN PHOSPHATE, PEG
REMARK 280  8000, GLYCEROL, GLUCOSE, PH 5.1, VAPOR DIFFUSION, SITTING DROP,
REMARK 280  TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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   X+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      122.92350
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.20600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      122.92350
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       74.20600
REMARK 290   SMTRY3   4  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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 115630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
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 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     MET A     1
REMARK 465     GLY A   540
REMARK 465     LEU A   541
REMARK 465     VAL A   542
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     VAL B   422
REMARK 465     GLU B   423
REMARK 465     GLU B   424
REMARK 465     PHE B   445
REMARK 465     ASP B   446
REMARK 465     SER B   505
REMARK 465     PHE B   506
REMARK 465     CYS B   507
REMARK 465     PHE B   508
REMARK 465     THR B   538
REMARK 465     SER B   539
REMARK 465     GLY B   540
REMARK 465     LEU B   541
REMARK 465     VAL B   542
REMARK 465     GLY B   543
REMARK 465     GLU B   544
REMARK 465     PHE B   545
REMARK 465     GLY B   546
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     ALA C   406
REMARK 465     ASP C   407
REMARK 465     ALA C   408
REMARK 465     GLU C   450
REMARK 465     LYS C   451
REMARK 465     HIS C   499
REMARK 465     ASN C   500
REMARK 465     GLY C   540
REMARK 465     LEU C   541
REMARK 465     VAL C   542
REMARK 465     GLY C   543
REMARK 465     GLU C   544
REMARK 465     MET D     1
REMARK 465     SER D     2
REMARK 465     GLU D   423
REMARK 465     GLU D   424
REMARK 465     ARG D   425
REMARK 465     SER D   426
REMARK 465     ASP D   427
REMARK 465     ASP D   428
REMARK 465     GLU D   429
REMARK 465     GLU D   430
REMARK 465     GLY D   540
REMARK 465     LEU D   541
REMARK 465     VAL D   542
REMARK 465     GLY D   543
REMARK 465     GLU D   544
REMARK 465     PHE D   545
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   OE1  GLU B   816     OE2  GLU B   833              2.02
REMARK 500   O    ASN B   500     NH2  ARG B   515              2.07
REMARK 500   O    ASP C   155     OG1  THR C   685              2.17
REMARK 500
REMARK 500 REMARK: NULL
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 D 816   CG    GLU D 816   CD      0.100
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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   ATM2   ATM3
REMARK 500    ASP A  26   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    PRO A 176   C   -  N   -  CA  ANGL. DEV. =  -9.0 DEGREES
REMARK 500    ARG B 249   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    LEU B 579   CA  -  CB  -  CG  ANGL. DEV. =  19.6 DEGREES
REMARK 500    ARG B 769   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
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    ASP A  26     -157.32   -139.45
REMARK 500    THR A 103       51.31   -149.27
REMARK 500    ASP A 155      109.79    -45.49
REMARK 500    ASN A 185       69.28     39.58
REMARK 500    SER A 202        0.40    -69.76
REMARK 500    ILE A 209      -58.33   -127.17
REMARK 500    ARG A 213      -60.47    -93.55
REMARK 500    PHE A 227       -1.41     77.57
REMARK 500    GLN A 265      -50.09     73.44
REMARK 500    ASN A 297       41.29     36.66
REMARK 500    THR A 302       36.79    -99.03
REMARK 500    ASN A 329       54.16     34.58
REMARK 500    LYS A 349       71.07   -117.30
REMARK 500    SER A 387       21.20   -148.56
REMARK 500    SER A 397       32.36   -141.62
REMARK 500    ASN A 456       81.23   -162.90
REMARK 500    CYS A 507       68.12     63.26
REMARK 500    LEU A 583     -166.71   -100.30
REMARK 500    GLU A 590      138.59    -39.86
REMARK 500    LYS A 601     -133.60     55.87
REMARK 500    TRP A 642     -151.51     56.02
REMARK 500    ASP A 695     -125.95     54.28
REMARK 500    THR A 721     -167.91   -129.88
REMARK 500    ASP A 735       10.33   -154.65
REMARK 500    ASN A 745       98.93    -66.95
REMARK 500    ASN A 764       58.00   -143.94
REMARK 500    THR B 103       54.66   -144.09
REMARK 500    ILE B 209      -61.08   -120.25
REMARK 500    ARG B 213      -68.99    -90.66
REMARK 500    GLN B 265      -50.40     73.62
REMARK 500    ASN B 297       33.95     37.18
REMARK 500    ASN B 326       68.93   -157.35
REMARK 500    LYS B 349       72.03   -119.28
REMARK 500    SER B 387       20.31   -146.51
REMARK 500    ASP B 427      -38.92    -35.93
REMARK 500    LEU B 583     -163.87   -110.49
REMARK 500    LYS B 601     -130.49     58.31
REMARK 500    ASN B 616       46.10    -98.16
REMARK 500    TRP B 642     -160.70     73.71
REMARK 500    ASP B 695     -132.21     55.52
REMARK 500    ASN B 764       59.93   -149.27
REMARK 500    ASP C  26     -154.42   -140.22
REMARK 500    TRP C  28       -8.46   -144.74
REMARK 500    PHE C  55      -62.04    -97.04
REMARK 500    PHE C  74       36.99     39.65
REMARK 500    ILE C 209      -61.28   -108.71
REMARK 500    ARG C 213      -65.83    -94.59
REMARK 500    GLN C 265      -49.29     72.53
REMARK 500    ASN C 326       70.91   -162.40
REMARK 500    ASN C 329       38.83     34.93
REMARK 500
REMARK 500 THIS ENTRY HAS      86 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    GLN A 265        23.2      L          L   OUTSIDE RANGE
REMARK 500    GLN B 265        22.5      L          L   OUTSIDE RANGE
REMARK 500    GLN C 265        19.6      L          L   OUTSIDE RANGE
REMARK 500    CYS C 507        24.6      L          L   OUTSIDE RANGE
REMARK 500    GLN D 265        24.6      L          L   OUTSIDE RANGE
REMARK 500    CYS D 507        24.6      L          L   OUTSIDE RANGE
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 999        DISTANCE =  5.99 ANGSTROMS
REMARK 525    HOH D1370        DISTANCE =  5.99 ANGSTROMS
REMARK 525    HOH D1486        DISTANCE =  5.22 ANGSTROMS
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 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC B 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC C 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BGC D 5004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ABZ   RELATED DB: PDB
DBREF  3AC0 A    1   845  UNP    D1GCC6   D1GCC6_KLUMA     1    845
DBREF  3AC0 B    1   845  UNP    D1GCC6   D1GCC6_KLUMA     1    845
DBREF  3AC0 C    1   845  UNP    D1GCC6   D1GCC6_KLUMA     1    845
DBREF  3AC0 D    1   845  UNP    D1GCC6   D1GCC6_KLUMA     1    845
SEQRES   1 A  845  MET SER LYS PHE ASP VAL GLU GLN LEU LEU SER GLU LEU
SEQRES   2 A  845  ASN GLN ASP GLU LYS ILE SER LEU LEU SER ALA VAL ASP
SEQRES   3 A  845  PHE TRP HIS THR LYS LYS ILE GLU ARG LEU GLY ILE PRO
SEQRES   4 A  845  ALA VAL ARG VAL SER ASP GLY PRO ASN GLY ILE ARG GLY
SEQRES   5 A  845  THR LYS PHE PHE ASP GLY VAL PRO SER GLY CYS PHE PRO
SEQRES   6 A  845  ASN GLY THR GLY LEU ALA SER THR PHE ASP ARG ASP LEU
SEQRES   7 A  845  LEU GLU THR ALA GLY LYS LEU MET ALA LYS GLU SER ILE
SEQRES   8 A  845  ALA LYS ASN ALA ALA VAL ILE LEU GLY PRO THR THR ASN
SEQRES   9 A  845  MET GLN ARG GLY PRO LEU GLY GLY ARG GLY PHE GLU SER
SEQRES  10 A  845  PHE SER GLU ASP PRO TYR LEU ALA GLY MET ALA THR SER
SEQRES  11 A  845  SER VAL VAL LYS GLY MET GLN GLY GLU GLY ILE ALA ALA
SEQRES  12 A  845  THR VAL LYS HIS PHE VAL CYS ASN ASP LEU GLU ASP GLN
SEQRES  13 A  845  ARG PHE SER SER ASN SER ILE VAL SER GLU ARG ALA LEU
SEQRES  14 A  845  ARG GLU ILE TYR LEU GLU PRO PHE ARG LEU ALA VAL LYS
SEQRES  15 A  845  HIS ALA ASN PRO VAL CYS ILE MET THR ALA TYR ASN LYS
SEQRES  16 A  845  VAL ASN GLY GLU HIS CYS SER GLN SER LYS LYS LEU LEU
SEQRES  17 A  845  ILE ASP ILE LEU ARG ASP GLU TRP LYS TRP ASP GLY MET
SEQRES  18 A  845  LEU MET SER ASP TRP PHE GLY THR TYR THR THR ALA ALA
SEQRES  19 A  845  ALA ILE LYS ASN GLY LEU ASP ILE GLU PHE PRO GLY PRO
SEQRES  20 A  845  THR ARG TRP ARG THR ARG ALA LEU VAL SER HIS SER LEU
SEQRES  21 A  845  ASN SER ARG GLU GLN ILE THR THR GLU ASP VAL ASP ASP
SEQRES  22 A  845  ARG VAL ARG GLN VAL LEU LYS MET ILE LYS PHE VAL VAL
SEQRES  23 A  845  ASP ASN LEU GLU LYS THR GLY ILE VAL GLU ASN GLY PRO
SEQRES  24 A  845  GLU SER THR SER ASN ASN THR LYS GLU THR SER ASP LEU
SEQRES  25 A  845  LEU ARG LYS ILE ALA ALA ASP SER ILE VAL LEU LEU LYS
SEQRES  26 A  845  ASN LYS ASN ASN ILE LEU PRO LEU LYS LYS GLU ASP ASN
SEQRES  27 A  845  ILE ILE VAL ILE GLY PRO ASN ALA LYS ALA LYS THR SER
SEQRES  28 A  845  SER GLY GLY GLY SER ALA SER MET ASN SER TYR TYR VAL
SEQRES  29 A  845  VAL SER PRO TYR GLU GLY ILE VAL ASN LYS LEU GLY LYS
SEQRES  30 A  845  GLU VAL ASP TYR THR VAL GLY ALA TYR SER HIS LYS SER
SEQRES  31 A  845  ILE GLY GLY LEU ALA GLU SER SER LEU ILE ASP ALA ALA
SEQRES  32 A  845  LYS PRO ALA ASP ALA GLU ASN SER GLY LEU ILE ALA LYS
SEQRES  33 A  845  PHE TYR SER ASN PRO VAL GLU GLU ARG SER ASP ASP GLU
SEQRES  34 A  845  GLU PRO PHE HIS VAL THR LYS VAL ASN ARG SER ASN VAL
SEQRES  35 A  845  HIS LEU PHE ASP PHE LYS HIS GLU LYS VAL ASP PRO LYS
SEQRES  36 A  845  ASN PRO TYR PHE PHE VAL THR LEU THR GLY GLN TYR VAL
SEQRES  37 A  845  PRO GLN GLU ASP GLY ASP TYR ILE PHE SER LEU GLN VAL
SEQRES  38 A  845  TYR GLY SER GLY LEU PHE TYR LEU ASN ASP GLU LEU ILE
SEQRES  39 A  845  ILE ASP GLN LYS HIS ASN GLN GLU ARG GLY SER PHE CYS
SEQRES  40 A  845  PHE GLY ALA GLY THR LYS GLU ARG THR LYS LYS LEU THR
SEQRES  41 A  845  LEU LYS LYS GLY GLN VAL TYR ASN VAL ARG VAL GLU TYR
SEQRES  42 A  845  GLY SER GLY PRO THR SER GLY LEU VAL GLY GLU PHE GLY
SEQRES  43 A  845  ALA GLY GLY PHE GLN ALA GLY VAL ILE LYS ALA ILE ASP
SEQRES  44 A  845  ASP ASP GLU GLU ILE ARG ASN ALA ALA GLU LEU ALA ALA
SEQRES  45 A  845  LYS HIS ASP LYS ALA VAL LEU ILE ILE GLY LEU ASN GLY
SEQRES  46 A  845  GLU TRP GLU THR GLU GLY TYR ASP ARG GLU ASN MET ASP
SEQRES  47 A  845  LEU PRO LYS ARG THR ASN GLU LEU VAL ARG ALA VAL LEU
SEQRES  48 A  845  LYS ALA ASN PRO ASN THR VAL ILE VAL ASN GLN SER GLY
SEQRES  49 A  845  THR PRO VAL GLU PHE PRO TRP LEU GLU ASP ALA ASN ALA
SEQRES  50 A  845  LEU VAL GLN ALA TRP TYR GLY GLY ASN GLU LEU GLY ASN
SEQRES  51 A  845  ALA ILE ALA ASP VAL LEU TYR GLY ASP VAL VAL PRO ASN
SEQRES  52 A  845  GLY LYS LEU SER LEU SER TRP PRO PHE LYS LEU GLN ASP
SEQRES  53 A  845  ASN PRO ALA PHE LEU ASN PHE LYS THR GLU PHE GLY ARG
SEQRES  54 A  845  VAL ILE TYR GLY GLU ASP ILE PHE VAL GLY TYR ARG TYR
SEQRES  55 A  845  TYR GLU LYS LEU GLN ARG LYS VAL ALA PHE PRO PHE GLY
SEQRES  56 A  845  TYR GLY LEU SER TYR THR THR PHE GLU LEU ASP ILE SER
SEQRES  57 A  845  ASP PHE LYS VAL THR ASP ASP LYS ILE ALA ILE SER VAL
SEQRES  58 A  845  ASP VAL LYS ASN THR GLY ASP LYS PHE ALA GLY SER GLU
SEQRES  59 A  845  VAL VAL GLN VAL TYR PHE SER ALA LEU ASN SER LYS VAL
SEQRES  60 A  845  SER ARG PRO VAL LYS GLU LEU LYS GLY PHE GLU LYS VAL
SEQRES  61 A  845  HIS LEU GLU PRO GLY GLU LYS LYS THR VAL ASN ILE ASP
SEQRES  62 A  845  LEU GLU LEU LYS ASP ALA ILE SER TYR PHE ASN GLU GLU
SEQRES  63 A  845  LEU GLY LYS TRP HIS VAL GLU ALA GLY GLU TYR LEU VAL
SEQRES  64 A  845  SER VAL GLY THR SER SER ASP ASP ILE LEU SER VAL LYS
SEQRES  65 A  845  GLU PHE LYS VAL GLU LYS GLU LEU TYR TRP LYS GLY LEU
SEQRES   1 B  845  MET SER LYS PHE ASP VAL GLU GLN LEU LEU SER GLU LEU
SEQRES   2 B  845  ASN GLN ASP GLU LYS ILE SER LEU LEU SER ALA VAL ASP
SEQRES   3 B  845  PHE TRP HIS THR LYS LYS ILE GLU ARG LEU GLY ILE PRO
SEQRES   4 B  845  ALA VAL ARG VAL SER ASP GLY PRO ASN GLY ILE ARG GLY
SEQRES   5 B  845  THR LYS PHE PHE ASP GLY VAL PRO SER GLY CYS PHE PRO
SEQRES   6 B  845  ASN GLY THR GLY LEU ALA SER THR PHE ASP ARG ASP LEU
SEQRES   7 B  845  LEU GLU THR ALA GLY LYS LEU MET ALA LYS GLU SER ILE
SEQRES   8 B  845  ALA LYS ASN ALA ALA VAL ILE LEU GLY PRO THR THR ASN
SEQRES   9 B  845  MET GLN ARG GLY PRO LEU GLY GLY ARG GLY PHE GLU SER
SEQRES  10 B  845  PHE SER GLU ASP PRO TYR LEU ALA GLY MET ALA THR SER
SEQRES  11 B  845  SER VAL VAL LYS GLY MET GLN GLY GLU GLY ILE ALA ALA
SEQRES  12 B  845  THR VAL LYS HIS PHE VAL CYS ASN ASP LEU GLU ASP GLN
SEQRES  13 B  845  ARG PHE SER SER ASN SER ILE VAL SER GLU ARG ALA LEU
SEQRES  14 B  845  ARG GLU ILE TYR LEU GLU PRO PHE ARG LEU ALA VAL LYS
SEQRES  15 B  845  HIS ALA ASN PRO VAL CYS ILE MET THR ALA TYR ASN LYS
SEQRES  16 B  845  VAL ASN GLY GLU HIS CYS SER GLN SER LYS LYS LEU LEU
SEQRES  17 B  845  ILE ASP ILE LEU ARG ASP GLU TRP LYS TRP ASP GLY MET
SEQRES  18 B  845  LEU MET SER ASP TRP PHE GLY THR TYR THR THR ALA ALA
SEQRES  19 B  845  ALA ILE LYS ASN GLY LEU ASP ILE GLU PHE PRO GLY PRO
SEQRES  20 B  845  THR ARG TRP ARG THR ARG ALA LEU VAL SER HIS SER LEU
SEQRES  21 B  845  ASN SER ARG GLU GLN ILE THR THR GLU ASP VAL ASP ASP
SEQRES  22 B  845  ARG VAL ARG GLN VAL LEU LYS MET ILE LYS PHE VAL VAL
SEQRES  23 B  845  ASP ASN LEU GLU LYS THR GLY ILE VAL GLU ASN GLY PRO
SEQRES  24 B  845  GLU SER THR SER ASN ASN THR LYS GLU THR SER ASP LEU
SEQRES  25 B  845  LEU ARG LYS ILE ALA ALA ASP SER ILE VAL LEU LEU LYS
SEQRES  26 B  845  ASN LYS ASN ASN ILE LEU PRO LEU LYS LYS GLU ASP ASN
SEQRES  27 B  845  ILE ILE VAL ILE GLY PRO ASN ALA LYS ALA LYS THR SER
SEQRES  28 B  845  SER GLY GLY GLY SER ALA SER MET ASN SER TYR TYR VAL
SEQRES  29 B  845  VAL SER PRO TYR GLU GLY ILE VAL ASN LYS LEU GLY LYS
SEQRES  30 B  845  GLU VAL ASP TYR THR VAL GLY ALA TYR SER HIS LYS SER
SEQRES  31 B  845  ILE GLY GLY LEU ALA GLU SER SER LEU ILE ASP ALA ALA
SEQRES  32 B  845  LYS PRO ALA ASP ALA GLU ASN SER GLY LEU ILE ALA LYS
SEQRES  33 B  845  PHE TYR SER ASN PRO VAL GLU GLU ARG SER ASP ASP GLU
SEQRES  34 B  845  GLU PRO PHE HIS VAL THR LYS VAL ASN ARG SER ASN VAL
SEQRES  35 B  845  HIS LEU PHE ASP PHE LYS HIS GLU LYS VAL ASP PRO LYS
SEQRES  36 B  845  ASN PRO TYR PHE PHE VAL THR LEU THR GLY GLN TYR VAL
SEQRES  37 B  845  PRO GLN GLU ASP GLY ASP TYR ILE PHE SER LEU GLN VAL
SEQRES  38 B  845  TYR GLY SER GLY LEU PHE TYR LEU ASN ASP GLU LEU ILE
SEQRES  39 B  845  ILE ASP GLN LYS HIS ASN GLN GLU ARG GLY SER PHE CYS
SEQRES  40 B  845  PHE GLY ALA GLY THR LYS GLU ARG THR LYS LYS LEU THR
SEQRES  41 B  845  LEU LYS LYS GLY GLN VAL TYR ASN VAL ARG VAL GLU TYR
SEQRES  42 B  845  GLY SER GLY PRO THR SER GLY LEU VAL GLY GLU PHE GLY
SEQRES  43 B  845  ALA GLY GLY PHE GLN ALA GLY VAL ILE LYS ALA ILE ASP
SEQRES  44 B  845  ASP ASP GLU GLU ILE ARG ASN ALA ALA GLU LEU ALA ALA
SEQRES  45 B  845  LYS HIS ASP LYS ALA VAL LEU ILE ILE GLY LEU ASN GLY
SEQRES  46 B  845  GLU TRP GLU THR GLU GLY TYR ASP ARG GLU ASN MET ASP
SEQRES  47 B  845  LEU PRO LYS ARG THR ASN GLU LEU VAL ARG ALA VAL LEU
SEQRES  48 B  845  LYS ALA ASN PRO ASN THR VAL ILE VAL ASN GLN SER GLY
SEQRES  49 B  845  THR PRO VAL GLU PHE PRO TRP LEU GLU ASP ALA ASN ALA
SEQRES  50 B  845  LEU VAL GLN ALA TRP TYR GLY GLY ASN GLU LEU GLY ASN
SEQRES  51 B  845  ALA ILE ALA ASP VAL LEU TYR GLY ASP VAL VAL PRO ASN
SEQRES  52 B  845  GLY LYS LEU SER LEU SER TRP PRO PHE LYS LEU GLN ASP
SEQRES  53 B  845  ASN PRO ALA PHE LEU ASN PHE LYS THR GLU PHE GLY ARG
SEQRES  54 B  845  VAL ILE TYR GLY GLU ASP ILE PHE VAL GLY TYR ARG TYR
SEQRES  55 B  845  TYR GLU LYS LEU GLN ARG LYS VAL ALA PHE PRO PHE GLY
SEQRES  56 B  845  TYR GLY LEU SER TYR THR THR PHE GLU LEU ASP ILE SER
SEQRES  57 B  845  ASP PHE LYS VAL THR ASP ASP LYS ILE ALA ILE SER VAL
SEQRES  58 B  845  ASP VAL LYS ASN THR GLY ASP LYS PHE ALA GLY SER GLU
SEQRES  59 B  845  VAL VAL GLN VAL TYR PHE SER ALA LEU ASN SER LYS VAL
SEQRES  60 B  845  SER ARG PRO VAL LYS GLU LEU LYS GLY PHE GLU LYS VAL
SEQRES  61 B  845  HIS LEU GLU PRO GLY GLU LYS LYS THR VAL ASN ILE ASP
SEQRES  62 B  845  LEU GLU LEU LYS ASP ALA ILE SER TYR PHE ASN GLU GLU
SEQRES  63 B  845  LEU GLY LYS TRP HIS VAL GLU ALA GLY GLU TYR LEU VAL
SEQRES  64 B  845  SER VAL GLY THR SER SER ASP ASP ILE LEU SER VAL LYS
SEQRES  65 B  845  GLU PHE LYS VAL GLU LYS GLU LEU TYR TRP LYS GLY LEU
SEQRES   1 C  845  MET SER LYS PHE ASP VAL GLU GLN LEU LEU SER GLU LEU
SEQRES   2 C  845  ASN GLN ASP GLU LYS ILE SER LEU LEU SER ALA VAL ASP
SEQRES   3 C  845  PHE TRP HIS THR LYS LYS ILE GLU ARG LEU GLY ILE PRO
SEQRES   4 C  845  ALA VAL ARG VAL SER ASP GLY PRO ASN GLY ILE ARG GLY
SEQRES   5 C  845  THR LYS PHE PHE ASP GLY VAL PRO SER GLY CYS PHE PRO
SEQRES   6 C  845  ASN GLY THR GLY LEU ALA SER THR PHE ASP ARG ASP LEU
SEQRES   7 C  845  LEU GLU THR ALA GLY LYS LEU MET ALA LYS GLU SER ILE
SEQRES   8 C  845  ALA LYS ASN ALA ALA VAL ILE LEU GLY PRO THR THR ASN
SEQRES   9 C  845  MET GLN ARG GLY PRO LEU GLY GLY ARG GLY PHE GLU SER
SEQRES  10 C  845  PHE SER GLU ASP PRO TYR LEU ALA GLY MET ALA THR SER
SEQRES  11 C  845  SER VAL VAL LYS GLY MET GLN GLY GLU GLY ILE ALA ALA
SEQRES  12 C  845  THR VAL LYS HIS PHE VAL CYS ASN ASP LEU GLU ASP GLN
SEQRES  13 C  845  ARG PHE SER SER ASN SER ILE VAL SER GLU ARG ALA LEU
SEQRES  14 C  845  ARG GLU ILE TYR LEU GLU PRO PHE ARG LEU ALA VAL LYS
SEQRES  15 C  845  HIS ALA ASN PRO VAL CYS ILE MET THR ALA TYR ASN LYS
SEQRES  16 C  845  VAL ASN GLY GLU HIS CYS SER GLN SER LYS LYS LEU LEU
SEQRES  17 C  845  ILE ASP ILE LEU ARG ASP GLU TRP LYS TRP ASP GLY MET
SEQRES  18 C  845  LEU MET SER ASP TRP PHE GLY THR TYR THR THR ALA ALA
SEQRES  19 C  845  ALA ILE LYS ASN GLY LEU ASP ILE GLU PHE PRO GLY PRO
SEQRES  20 C  845  THR ARG TRP ARG THR ARG ALA LEU VAL SER HIS SER LEU
SEQRES  21 C  845  ASN SER ARG GLU GLN ILE THR THR GLU ASP VAL ASP ASP
SEQRES  22 C  845  ARG VAL ARG GLN VAL LEU LYS MET ILE LYS PHE VAL VAL
SEQRES  23 C  845  ASP ASN LEU GLU LYS THR GLY ILE VAL GLU ASN GLY PRO
SEQRES  24 C  845  GLU SER THR SER ASN ASN THR LYS GLU THR SER ASP LEU
SEQRES  25 C  845  LEU ARG LYS ILE ALA ALA ASP SER ILE VAL LEU LEU LYS
SEQRES  26 C  845  ASN LYS ASN ASN ILE LEU PRO LEU LYS LYS GLU ASP ASN
SEQRES  27 C  845  ILE ILE VAL ILE GLY PRO ASN ALA LYS ALA LYS THR SER
SEQRES  28 C  845  SER GLY GLY GLY SER ALA SER MET ASN SER TYR TYR VAL
SEQRES  29 C  845  VAL SER PRO TYR GLU GLY ILE VAL ASN LYS LEU GLY LYS
SEQRES  30 C  845  GLU VAL ASP TYR THR VAL GLY ALA TYR SER HIS LYS SER
SEQRES  31 C  845  ILE GLY GLY LEU ALA GLU SER SER LEU ILE ASP ALA ALA
SEQRES  32 C  845  LYS PRO ALA ASP ALA GLU ASN SER GLY LEU ILE ALA LYS
SEQRES  33 C  845  PHE TYR SER ASN PRO VAL GLU GLU ARG SER ASP ASP GLU
SEQRES  34 C  845  GLU PRO PHE HIS VAL THR LYS VAL ASN ARG SER ASN VAL
SEQRES  35 C  845  HIS LEU PHE ASP PHE LYS HIS GLU LYS VAL ASP PRO LYS
SEQRES  36 C  845  ASN PRO TYR PHE PHE VAL THR LEU THR GLY GLN TYR VAL
SEQRES  37 C  845  PRO GLN GLU ASP GLY ASP TYR ILE PHE SER LEU GLN VAL
SEQRES  38 C  845  TYR GLY SER GLY LEU PHE TYR LEU ASN ASP GLU LEU ILE
SEQRES  39 C  845  ILE ASP GLN LYS HIS ASN GLN GLU ARG GLY SER PHE CYS
SEQRES  40 C  845  PHE GLY ALA GLY THR LYS GLU ARG THR LYS LYS LEU THR
SEQRES  41 C  845  LEU LYS LYS GLY GLN VAL TYR ASN VAL ARG VAL GLU TYR
SEQRES  42 C  845  GLY SER GLY PRO THR SER GLY LEU VAL GLY GLU PHE GLY
SEQRES  43 C  845  ALA GLY GLY PHE GLN ALA GLY VAL ILE LYS ALA ILE ASP
SEQRES  44 C  845  ASP ASP GLU GLU ILE ARG ASN ALA ALA GLU LEU ALA ALA
SEQRES  45 C  845  LYS HIS ASP LYS ALA VAL LEU ILE ILE GLY LEU ASN GLY
SEQRES  46 C  845  GLU TRP GLU THR GLU GLY TYR ASP ARG GLU ASN MET ASP
SEQRES  47 C  845  LEU PRO LYS ARG THR ASN GLU LEU VAL ARG ALA VAL LEU
SEQRES  48 C  845  LYS ALA ASN PRO ASN THR VAL ILE VAL ASN GLN SER GLY
SEQRES  49 C  845  THR PRO VAL GLU PHE PRO TRP LEU GLU ASP ALA ASN ALA
SEQRES  50 C  845  LEU VAL GLN ALA TRP TYR GLY GLY ASN GLU LEU GLY ASN
SEQRES  51 C  845  ALA ILE ALA ASP VAL LEU TYR GLY ASP VAL VAL PRO ASN
SEQRES  52 C  845  GLY LYS LEU SER LEU SER TRP PRO PHE LYS LEU GLN ASP
SEQRES  53 C  845  ASN PRO ALA PHE LEU ASN PHE LYS THR GLU PHE GLY ARG
SEQRES  54 C  845  VAL ILE TYR GLY GLU ASP ILE PHE VAL GLY TYR ARG TYR
SEQRES  55 C  845  TYR GLU LYS LEU GLN ARG LYS VAL ALA PHE PRO PHE GLY
SEQRES  56 C  845  TYR GLY LEU SER TYR THR THR PHE GLU LEU ASP ILE SER
SEQRES  57 C  845  ASP PHE LYS VAL THR ASP ASP LYS ILE ALA ILE SER VAL
SEQRES  58 C  845  ASP VAL LYS ASN THR GLY ASP LYS PHE ALA GLY SER GLU
SEQRES  59 C  845  VAL VAL GLN VAL TYR PHE SER ALA LEU ASN SER LYS VAL
SEQRES  60 C  845  SER ARG PRO VAL LYS GLU LEU LYS GLY PHE GLU LYS VAL
SEQRES  61 C  845  HIS LEU GLU PRO GLY GLU LYS LYS THR VAL ASN ILE ASP
SEQRES  62 C  845  LEU GLU LEU LYS ASP ALA ILE SER TYR PHE ASN GLU GLU
SEQRES  63 C  845  LEU GLY LYS TRP HIS VAL GLU ALA GLY GLU TYR LEU VAL
SEQRES  64 C  845  SER VAL GLY THR SER SER ASP ASP ILE LEU SER VAL LYS
SEQRES  65 C  845  GLU PHE LYS VAL GLU LYS GLU LEU TYR TRP LYS GLY LEU
SEQRES   1 D  845  MET SER LYS PHE ASP VAL GLU GLN LEU LEU SER GLU LEU
SEQRES   2 D  845  ASN GLN ASP GLU LYS ILE SER LEU LEU SER ALA VAL ASP
SEQRES   3 D  845  PHE TRP HIS THR LYS LYS ILE GLU ARG LEU GLY ILE PRO
SEQRES   4 D  845  ALA VAL ARG VAL SER ASP GLY PRO ASN GLY ILE ARG GLY
SEQRES   5 D  845  THR LYS PHE PHE ASP GLY VAL PRO SER GLY CYS PHE PRO
SEQRES   6 D  845  ASN GLY THR GLY LEU ALA SER THR PHE ASP ARG ASP LEU
SEQRES   7 D  845  LEU GLU THR ALA GLY LYS LEU MET ALA LYS GLU SER ILE
SEQRES   8 D  845  ALA LYS ASN ALA ALA VAL ILE LEU GLY PRO THR THR ASN
SEQRES   9 D  845  MET GLN ARG GLY PRO LEU GLY GLY ARG GLY PHE GLU SER
SEQRES  10 D  845  PHE SER GLU ASP PRO TYR LEU ALA GLY MET ALA THR SER
SEQRES  11 D  845  SER VAL VAL LYS GLY MET GLN GLY GLU GLY ILE ALA ALA
SEQRES  12 D  845  THR VAL LYS HIS PHE VAL CYS ASN ASP LEU GLU ASP GLN
SEQRES  13 D  845  ARG PHE SER SER ASN SER ILE VAL SER GLU ARG ALA LEU
SEQRES  14 D  845  ARG GLU ILE TYR LEU GLU PRO PHE ARG LEU ALA VAL LYS
SEQRES  15 D  845  HIS ALA ASN PRO VAL CYS ILE MET THR ALA TYR ASN LYS
SEQRES  16 D  845  VAL ASN GLY GLU HIS CYS SER GLN SER LYS LYS LEU LEU
SEQRES  17 D  845  ILE ASP ILE LEU ARG ASP GLU TRP LYS TRP ASP GLY MET
SEQRES  18 D  845  LEU MET SER ASP TRP PHE GLY THR TYR THR THR ALA ALA
SEQRES  19 D  845  ALA ILE LYS ASN GLY LEU ASP ILE GLU PHE PRO GLY PRO
SEQRES  20 D  845  THR ARG TRP ARG THR ARG ALA LEU VAL SER HIS SER LEU
SEQRES  21 D  845  ASN SER ARG GLU GLN ILE THR THR GLU ASP VAL ASP ASP
SEQRES  22 D  845  ARG VAL ARG GLN VAL LEU LYS MET ILE LYS PHE VAL VAL
SEQRES  23 D  845  ASP ASN LEU GLU LYS THR GLY ILE VAL GLU ASN GLY PRO
SEQRES  24 D  845  GLU SER THR SER ASN ASN THR LYS GLU THR SER ASP LEU
SEQRES  25 D  845  LEU ARG LYS ILE ALA ALA ASP SER ILE VAL LEU LEU LYS
SEQRES  26 D  845  ASN LYS ASN ASN ILE LEU PRO LEU LYS LYS GLU ASP ASN
SEQRES  27 D  845  ILE ILE VAL ILE GLY PRO ASN ALA LYS ALA LYS THR SER
SEQRES  28 D  845  SER GLY GLY GLY SER ALA SER MET ASN SER TYR TYR VAL
SEQRES  29 D  845  VAL SER PRO TYR GLU GLY ILE VAL ASN LYS LEU GLY LYS
SEQRES  30 D  845  GLU VAL ASP TYR THR VAL GLY ALA TYR SER HIS LYS SER
SEQRES  31 D  845  ILE GLY GLY LEU ALA GLU SER SER LEU ILE ASP ALA ALA
SEQRES  32 D  845  LYS PRO ALA ASP ALA GLU ASN SER GLY LEU ILE ALA LYS
SEQRES  33 D  845  PHE TYR SER ASN PRO VAL GLU GLU ARG SER ASP ASP GLU
SEQRES  34 D  845  GLU PRO PHE HIS VAL THR LYS VAL ASN ARG SER ASN VAL
SEQRES  35 D  845  HIS LEU PHE ASP PHE LYS HIS GLU LYS VAL ASP PRO LYS
SEQRES  36 D  845  ASN PRO TYR PHE PHE VAL THR LEU THR GLY GLN TYR VAL
SEQRES  37 D  845  PRO GLN GLU ASP GLY ASP TYR ILE PHE SER LEU GLN VAL
SEQRES  38 D  845  TYR GLY SER GLY LEU PHE TYR LEU ASN ASP GLU LEU ILE
SEQRES  39 D  845  ILE ASP GLN LYS HIS ASN GLN GLU ARG GLY SER PHE CYS
SEQRES  40 D  845  PHE GLY ALA GLY THR LYS GLU ARG THR LYS LYS LEU THR
SEQRES  41 D  845  LEU LYS LYS GLY GLN VAL TYR ASN VAL ARG VAL GLU TYR
SEQRES  42 D  845  GLY SER GLY PRO THR SER GLY LEU VAL GLY GLU PHE GLY
SEQRES  43 D  845  ALA GLY GLY PHE GLN ALA GLY VAL ILE LYS ALA ILE ASP
SEQRES  44 D  845  ASP ASP GLU GLU ILE ARG ASN ALA ALA GLU LEU ALA ALA
SEQRES  45 D  845  LYS HIS ASP LYS ALA VAL LEU ILE ILE GLY LEU ASN GLY
SEQRES  46 D  845  GLU TRP GLU THR GLU GLY TYR ASP ARG GLU ASN MET ASP
SEQRES  47 D  845  LEU PRO LYS ARG THR ASN GLU LEU VAL ARG ALA VAL LEU
SEQRES  48 D  845  LYS ALA ASN PRO ASN THR VAL ILE VAL ASN GLN SER GLY
SEQRES  49 D  845  THR PRO VAL GLU PHE PRO TRP LEU GLU ASP ALA ASN ALA
SEQRES  50 D  845  LEU VAL GLN ALA TRP TYR GLY GLY ASN GLU LEU GLY ASN
SEQRES  51 D  845  ALA ILE ALA ASP VAL LEU TYR GLY ASP VAL VAL PRO ASN
SEQRES  52 D  845  GLY LYS LEU SER LEU SER TRP PRO PHE LYS LEU GLN ASP
SEQRES  53 D  845  ASN PRO ALA PHE LEU ASN PHE LYS THR GLU PHE GLY ARG
SEQRES  54 D  845  VAL ILE TYR GLY GLU ASP ILE PHE VAL GLY TYR ARG TYR
SEQRES  55 D  845  TYR GLU LYS LEU GLN ARG LYS VAL ALA PHE PRO PHE GLY
SEQRES  56 D  845  TYR GLY LEU SER TYR THR THR PHE GLU LEU ASP ILE SER
SEQRES  57 D  845  ASP PHE LYS VAL THR ASP ASP LYS ILE ALA ILE SER VAL
SEQRES  58 D  845  ASP VAL LYS ASN THR GLY ASP LYS PHE ALA GLY SER GLU
SEQRES  59 D  845  VAL VAL GLN VAL TYR PHE SER ALA LEU ASN SER LYS VAL
SEQRES  60 D  845  SER ARG PRO VAL LYS GLU LEU LYS GLY PHE GLU LYS VAL
SEQRES  61 D  845  HIS LEU GLU PRO GLY GLU LYS LYS THR VAL ASN ILE ASP
SEQRES  62 D  845  LEU GLU LEU LYS ASP ALA ILE SER TYR PHE ASN GLU GLU
SEQRES  63 D  845  LEU GLY LYS TRP HIS VAL GLU ALA GLY GLU TYR LEU VAL
SEQRES  64 D  845  SER VAL GLY THR SER SER ASP ASP ILE LEU SER VAL LYS
SEQRES  65 D  845  GLU PHE LYS VAL GLU LYS GLU LEU TYR TRP LYS GLY LEU
HET    BGC  A5001      12
HET    BGC  B5002      12
HET    BGC  C5003      12
HET    BGC  D5004      12
HETNAM     BGC BETA-D-GLUCOSE
FORMUL   5  BGC    4(C6 H12 O6)
FORMUL   9  HOH   *1564(H2 O)
HELIX    1   1 ASP A    5  LEU A   13  1                                   9
HELIX    2   2 ASN A   14  LEU A   22  1                                   9
HELIX    3   3 ILE A   33  GLY A   37  5                                   5
HELIX    4   4 ASN A   66  THR A   73  1                                   8
HELIX    5   5 ASP A   75  LYS A   93  1                                  19
HELIX    6   6 ARG A  113  SER A  117  5                                   5
HELIX    7   7 ASP A  121  GLU A  139  1                                  19
HELIX    8   8 SER A  165  ILE A  172  1                                   8
HELIX    9   9 LEU A  174  ASN A  185  1                                  12
HELIX   10  10 SER A  204  ILE A  209  1                                   6
HELIX   11  11 THR A  232  ASN A  238  1                                   7
HELIX   12  12 THR A  252  SER A  262  1                                  11
HELIX   13  13 THR A  267  ASN A  288  1                                  22
HELIX   14  14 ASN A  288  GLY A  293  1                                   6
HELIX   15  15 THR A  306  ILE A  321  1                                  16
HELIX   16  16 SER A  366  GLY A  376  1                                  11
HELIX   17  17 LEU A  394  SER A  398  5                                   5
HELIX   18  18 ASP A  559  LYS A  573  1                                  15
HELIX   19  19 ARG A  602  ASN A  614  1                                  13
HELIX   20  20 TRP A  631  ALA A  635  5                                   5
HELIX   21  21 GLU A  647  TYR A  657  1                                  11
HELIX   22  22 LYS A  673  ASN A  677  5                                   5
HELIX   23  23 GLY A  699  LEU A  706  1                                   8
HELIX   24  24 GLU A  795  SER A  801  1                                   7
HELIX   25  25 ASP B    5  LEU B   13  1                                   9
HELIX   26  26 ASN B   14  LEU B   21  1                                   8
HELIX   27  27 ILE B   33  GLY B   37  5                                   5
HELIX   28  28 ASN B   66  SER B   72  1                                   7
HELIX   29  29 ASP B   75  ALA B   92  1                                  18
HELIX   30  30 ASP B  121  GLU B  139  1                                  19
HELIX   31  31 SER B  165  ILE B  172  1                                   8
HELIX   32  32 LEU B  174  ASN B  185  1                                  12
HELIX   33  33 SER B  204  ILE B  209  1                                   6
HELIX   34  34 THR B  232  GLY B  239  1                                   8
HELIX   35  35 THR B  252  SER B  262  1                                  11
HELIX   36  36 THR B  267  ASN B  288  1                                  22
HELIX   37  37 ASN B  288  GLY B  293  1                                   6
HELIX   38  38 THR B  306  ILE B  321  1                                  16
HELIX   39  39 ASN B  328  ILE B  330  5                                   3
HELIX   40  40 SER B  366  GLY B  376  1                                  11
HELIX   41  41 LEU B  394  SER B  398  5                                   5
HELIX   42  42 ASP B  559  LYS B  573  1                                  15
HELIX   43  43 ARG B  602  ASN B  614  1                                  13
HELIX   44  44 TRP B  631  ALA B  635  5                                   5
HELIX   45  45 GLU B  647  TYR B  657  1                                  11
HELIX   46  46 LYS B  673  ASN B  677  5                                   5
HELIX   47  47 GLY B  699  GLN B  707  1                                   9
HELIX   48  48 LEU B  796  SER B  801  1                                   6
HELIX   49  49 ASP C    5  LEU C   13  1                                   9
HELIX   50  50 ASN C   14  LEU C   22  1                                   9
HELIX   51  51 ILE C   33  GLY C   37  5                                   5
HELIX   52  52 ASN C   66  THR C   73  1                                   8
HELIX   53  53 ASP C   75  ALA C   92  1                                  18
HELIX   54  54 ASP C  121  GLU C  139  1                                  19
HELIX   55  55 SER C  165  TYR C  173  1                                   9
HELIX   56  56 LEU C  174  ASN C  185  1                                  12
HELIX   57  57 SER C  204  ILE C  209  1                                   6
HELIX   58  58 THR C  232  GLY C  239  1                                   8
HELIX   59  59 THR C  252  SER C  262  1                                  11
HELIX   60  60 THR C  267  ASN C  288  1                                  22
HELIX   61  61 ASN C  288  GLY C  293  1                                   6
HELIX   62  62 THR C  306  ILE C  321  1                                  16
HELIX   63  63 ASN C  328  ILE C  330  5                                   3
HELIX   64  64 SER C  366  GLY C  376  1                                  11
HELIX   65  65 LEU C  394  SER C  398  5                                   5
HELIX   66  66 PRO C  421  ARG C  425  5                                   5
HELIX   67  67 SER C  505  ALA C  510  1                                   6
HELIX   68  68 GLY C  536  SER C  539  5                                   4
HELIX   69  69 ASP C  559  LYS C  573  1                                  15
HELIX   70  70 ARG C  602  ASN C  614  1                                  13
HELIX   71  71 TRP C  631  ALA C  635  5                                   5
HELIX   72  72 GLU C  647  TYR C  657  1                                  11
HELIX   73  73 LYS C  673  ASN C  677  5                                   5
HELIX   74  74 GLY C  699  GLN C  707  1                                   9
HELIX   75  75 GLU C  795  ILE C  800  1                                   6
HELIX   76  76 ASP D    5  LEU D   13  1                                   9
HELIX   77  77 ASN D   14  LEU D   22  1                                   9
HELIX   78  78 ILE D   33  GLY D   37  5                                   5
HELIX   79  79 ASN D   66  THR D   73  1                                   8
HELIX   80  80 ASP D   75  LYS D   93  1                                  19
HELIX   81  81 ARG D  113  SER D  117  5                                   5
HELIX   82  82 ASP D  121  GLU D  139  1                                  19
HELIX   83  83 SER D  165  ILE D  172  1                                   8
HELIX   84  84 TYR D  173  ASN D  185  1                                  13
HELIX   85  85 SER D  204  ILE D  209  1                                   6
HELIX   86  86 THR D  232  ASN D  238  1                                   7
HELIX   87  87 THR D  252  SER D  262  1                                  11
HELIX   88  88 THR D  267  ASP D  287  1                                  21
HELIX   89  89 ASN D  288  GLY D  293  1                                   6
HELIX   90  90 THR D  306  ASP D  319  1                                  14
HELIX   91  91 ASN D  328  ILE D  330  5                                   3
HELIX   92  92 SER D  366  GLY D  376  1                                  11
HELIX   93  93 GLY D  536  SER D  539  5                                   4
HELIX   94  94 ASP D  559  LYS D  573  1                                  15
HELIX   95  95 ARG D  602  ASN D  614  1                                  13
HELIX   96  96 TRP D  631  ALA D  635  5                                   5
HELIX   97  97 GLU D  647  TYR D  657  1                                  11
HELIX   98  98 LYS D  673  ASN D  677  5                                   5
HELIX   99  99 GLY D  699  GLN D  707  1                                   9
HELIX  100 100 LEU D  796  SER D  801  1                                   6
SHEET    1   A 2 VAL A  43  ASP A  45  0
SHEET    2   A 2 VAL A  97  LEU A  99  1  O  LEU A  99   N  SER A  44
SHEET    1   B 3 THR A 144  PHE A 148  0
SHEET    2   B 3 CYS A 188  THR A 191  1  O  MET A 190   N  PHE A 148
SHEET    3   B 3 MET A 221  MET A 223  1  O  MET A 223   N  THR A 191
SHEET    1   C 4 GLU A 199  HIS A 200  0
SHEET    2   C 4 LYS A 195  VAL A 196 -1  N  VAL A 196   O  GLU A 199
SHEET    3   C 4 ASN A 161  ILE A 163  1  N  SER A 162   O  LYS A 195
SHEET    4   C 4 ARG A 689  ILE A 691  1  O  VAL A 690   N  ILE A 163
SHEET    1   D 6 VAL A 322  ASN A 326  0
SHEET    2   D 6 ALA A 637  GLN A 640 -1  O  GLN A 640   N  VAL A 322
SHEET    3   D 6 THR A 617  GLN A 622  1  N  ILE A 619   O  ALA A 637
SHEET    4   D 6 LYS A 576  GLY A 582  1  N  LEU A 579   O  VAL A 620
SHEET    5   D 6 ILE A 339  ILE A 342  1  N  ILE A 342   O  VAL A 578
SHEET    6   D 6 ASP A 380  THR A 382  1  O  ASP A 380   N  VAL A 341
SHEET    1   E 6 HIS A 433  VAL A 437  0
SHEET    2   E 6 LEU A 413  TYR A 418 -1  N  LEU A 413   O  VAL A 437
SHEET    3   E 6 PHE A 460  TYR A 467 -1  O  THR A 462   N  LYS A 416
SHEET    4   E 6 TYR A 527  GLY A 534 -1  O  VAL A 531   N  LEU A 463
SHEET    5   E 6 SER A 484  LEU A 489 -1  N  TYR A 488   O  ARG A 530
SHEET    6   E 6 GLU A 492  GLN A 497 -1  O  ILE A 494   N  PHE A 487
SHEET    1   F 4 ASN A 441  HIS A 443  0
SHEET    2   F 4 GLY A 549  LYS A 556 -1  O  PHE A 550   N  VAL A 442
SHEET    3   F 4 GLY A 473  TYR A 482 -1  N  ILE A 476   O  ILE A 555
SHEET    4   F 4 ARG A 515  LEU A 521 -1  O  LEU A 519   N  TYR A 475
SHEET    1   G 3 PHE A 723  VAL A 732  0
SHEET    2   G 3 ILE A 737  ASN A 745 -1  O  LYS A 744   N  GLU A 724
SHEET    3   G 3 LYS A 787  LEU A 794 -1  O  VAL A 790   N  VAL A 741
SHEET    1   H 4 GLU A 773  LEU A 782  0
SHEET    2   H 4 GLY A 752  ALA A 762 -1  N  VAL A 758   O  GLY A 776
SHEET    3   H 4 GLY A 815  GLY A 822 -1  O  GLY A 822   N  GLN A 757
SHEET    4   H 4 ILE A 828  VAL A 836 -1  O  PHE A 834   N  TYR A 817
SHEET    1   I 3 TYR A 802  ASN A 804  0
SHEET    2   I 3 LYS A 809  VAL A 812 -1  O  HIS A 811   N  TYR A 802
SHEET    3   I 3 LEU A 840  TRP A 842 -1  O  LEU A 840   N  VAL A 812
SHEET    1   J 5 VAL B  43  ASP B  45  0
SHEET    2   J 5 VAL B  97  LEU B  99  1  O  LEU B  99   N  SER B  44
SHEET    3   J 5 ALA B 142  PHE B 148  1  O  ALA B 142   N  ILE B  98
SHEET    4   J 5 CYS B 188  THR B 191  1  O  MET B 190   N  PHE B 148
SHEET    5   J 5 MET B 221  SER B 224  1  O  MET B 223   N  THR B 191
SHEET    1   K 4 GLU B 199  HIS B 200  0
SHEET    2   K 4 LYS B 195  VAL B 196 -1  N  VAL B 196   O  GLU B 199
SHEET    3   K 4 ASN B 161  ILE B 163  1  N  SER B 162   O  LYS B 195
SHEET    4   K 4 ARG B 689  ILE B 691  1  O  VAL B 690   N  ILE B 163
SHEET    1   L 6 VAL B 322  ASN B 326  0
SHEET    2   L 6 ALA B 637  GLN B 640 -1  O  GLN B 640   N  VAL B 322
SHEET    3   L 6 THR B 617  GLN B 622  1  N  ILE B 619   O  ALA B 637
SHEET    4   L 6 LYS B 576  GLY B 582  1  N  LEU B 579   O  VAL B 620
SHEET    5   L 6 ILE B 339  ILE B 342  1  N  ILE B 342   O  VAL B 578
SHEET    6   L 6 ASP B 380  THR B 382  1  O  ASP B 380   N  VAL B 341
SHEET    1   M 6 HIS B 433  VAL B 437  0
SHEET    2   M 6 LEU B 413  TYR B 418 -1  N  LEU B 413   O  VAL B 437
SHEET    3   M 6 PHE B 460  TYR B 467 -1  O  THR B 462   N  LYS B 416
SHEET    4   M 6 TYR B 527  GLY B 534 -1  O  TYR B 533   N  VAL B 461
SHEET    5   M 6 SER B 484  LEU B 489 -1  N  SER B 484   O  GLY B 534
SHEET    6   M 6 GLU B 492  GLN B 497 -1  O  ILE B 494   N  PHE B 487
SHEET    1   N 4 ASN B 441  VAL B 442  0
SHEET    2   N 4 PHE B 550  LYS B 556 -1  O  PHE B 550   N  VAL B 442
SHEET    3   N 4 GLY B 473  VAL B 481 -1  N  ILE B 476   O  ILE B 555
SHEET    4   N 4 ARG B 515  LEU B 521 -1  O  LEU B 521   N  GLY B 473
SHEET    1   O 3 PHE B 723  VAL B 732  0
SHEET    2   O 3 LYS B 736  ASN B 745 -1  O  SER B 740   N  SER B 728
SHEET    3   O 3 LYS B 787  GLU B 795 -1  O  LEU B 794   N  ILE B 737
SHEET    1   P 4 GLU B 773  LEU B 782  0
SHEET    2   P 4 GLY B 752  ALA B 762 -1  N  VAL B 756   O  GLU B 778
SHEET    3   P 4 GLY B 815  GLY B 822 -1  O  SER B 820   N  TYR B 759
SHEET    4   P 4 ILE B 828  VAL B 836 -1  O  LYS B 832   N  VAL B 819
SHEET    1   Q 3 TYR B 802  ASN B 804  0
SHEET    2   Q 3 LYS B 809  VAL B 812 -1  O  LYS B 809   N  ASN B 804
SHEET    3   Q 3 LEU B 840  TRP B 842 -1  O  LEU B 840   N  VAL B 812
SHEET    1   R 5 VAL C  43  SER C  44  0
SHEET    2   R 5 VAL C  97  ILE C  98  1  O  VAL C  97   N  SER C  44
SHEET    3   R 5 ALA C 142  PHE C 148  1  O  ALA C 142   N  ILE C  98
SHEET    4   R 5 CYS C 188  THR C 191  1  O  CYS C 188   N  ALA C 143
SHEET    5   R 5 MET C 221  SER C 224  1  O  MET C 223   N  THR C 191
SHEET    1   S 4 GLU C 199  HIS C 200  0
SHEET    2   S 4 LYS C 195  VAL C 196 -1  N  VAL C 196   O  GLU C 199
SHEET    3   S 4 ASN C 161  ILE C 163  1  N  SER C 162   O  LYS C 195
SHEET    4   S 4 ARG C 689  ILE C 691  1  O  VAL C 690   N  ASN C 161
SHEET    1   T 6 VAL C 322  ASN C 326  0
SHEET    2   T 6 ALA C 637  GLN C 640 -1  O  LEU C 638   N  LEU C 324
SHEET    3   T 6 VAL C 618  GLN C 622  1  N  ASN C 621   O  VAL C 639
SHEET    4   T 6 LYS C 576  GLY C 582  1  N  LEU C 579   O  VAL C 618
SHEET    5   T 6 ILE C 339  ILE C 342  1  N  ILE C 342   O  ILE C 580
SHEET    6   T 6 ASP C 380  THR C 382  1  O  ASP C 380   N  VAL C 341
SHEET    1   U 6 HIS C 433  VAL C 437  0
SHEET    2   U 6 LEU C 413  TYR C 418 -1  N  ALA C 415   O  THR C 435
SHEET    3   U 6 PHE C 460  TYR C 467 -1  O  PHE C 460   N  TYR C 418
SHEET    4   U 6 TYR C 527  GLY C 534 -1  O  TYR C 533   N  VAL C 461
SHEET    5   U 6 SER C 484  LEU C 489 -1  N  TYR C 488   O  ARG C 530
SHEET    6   U 6 GLU C 492  ASP C 496 -1  O  ILE C 494   N  PHE C 487
SHEET    1   V 4 ASN C 441  HIS C 443  0
SHEET    2   V 4 GLY C 549  LYS C 556 -1  O  PHE C 550   N  VAL C 442
SHEET    3   V 4 GLY C 473  TYR C 482 -1  N  TYR C 482   O  GLY C 549
SHEET    4   V 4 ARG C 515  LEU C 521 -1  O  LEU C 521   N  GLY C 473
SHEET    1   W 3 GLU C 724  VAL C 732  0
SHEET    2   W 3 ILE C 737  LYS C 744 -1  O  ALA C 738   N  LYS C 731
SHEET    3   W 3 LYS C 787  LEU C 794 -1  O  LEU C 794   N  ILE C 737
SHEET    1   X 4 GLU C 773  LEU C 782  0
SHEET    2   X 4 GLY C 752  ALA C 762 -1  N  VAL C 756   O  GLU C 778
SHEET    3   X 4 GLY C 815  GLY C 822 -1  O  SER C 820   N  TYR C 759
SHEET    4   X 4 ILE C 828  VAL C 836 -1  O  LYS C 832   N  VAL C 819
SHEET    1   Y 3 SER C 801  ASN C 804  0
SHEET    2   Y 3 LYS C 809  VAL C 812 -1  O  LYS C 809   N  ASN C 804
SHEET    3   Y 3 LEU C 840  TRP C 842 -1  O  LEU C 840   N  VAL C 812
SHEET    1   Z 6 VAL D  43  ASP D  45  0
SHEET    2   Z 6 VAL D  97  LEU D  99  1  O  LEU D  99   N  SER D  44
SHEET    3   Z 6 ALA D 142  PHE D 148  1  O  ALA D 142   N  ILE D  98
SHEET    4   Z 6 CYS D 188  THR D 191  1  O  MET D 190   N  PHE D 148
SHEET    5   Z 6 MET D 221  TRP D 226  1  O  MET D 223   N  THR D 191
SHEET    6   Z 6 ILE D 242  PHE D 244  1  O  ILE D 242   N  LEU D 222
SHEET    1  AA 4 GLU D 199  HIS D 200  0
SHEET    2  AA 4 LYS D 195  VAL D 196 -1  N  VAL D 196   O  GLU D 199
SHEET    3  AA 4 ASN D 161  ILE D 163  1  N  SER D 162   O  LYS D 195
SHEET    4  AA 4 ARG D 689  ILE D 691  1  O  VAL D 690   N  ILE D 163
SHEET    1  AB 6 VAL D 322  ASN D 326  0
SHEET    2  AB 6 ALA D 637  GLN D 640 -1  O  GLN D 640   N  VAL D 322
SHEET    3  AB 6 THR D 617  GLN D 622  1  N  ILE D 619   O  ALA D 637
SHEET    4  AB 6 LYS D 576  GLY D 582  1  N  ILE D 581   O  VAL D 620
SHEET    5  AB 6 ILE D 339  ILE D 342  1  N  ILE D 342   O  VAL D 578
SHEET    6  AB 6 ASP D 380  THR D 382  1  O  ASP D 380   N  VAL D 341
SHEET    1  AC 6 HIS D 433  VAL D 437  0
SHEET    2  AC 6 LEU D 413  TYR D 418 -1  N  LEU D 413   O  VAL D 437
SHEET    3  AC 6 PHE D 460  TYR D 467 -1  O  THR D 464   N  ILE D 414
SHEET    4  AC 6 TYR D 527  GLY D 534 -1  O  TYR D 533   N  VAL D 461
SHEET    5  AC 6 SER D 484  LEU D 489 -1  N  SER D 484   O  GLY D 534
SHEET    6  AC 6 LEU D 493  GLN D 497 -1  O  ILE D 494   N  PHE D 487
SHEET    1  AD 4 ASN D 441  HIS D 443  0
SHEET    2  AD 4 GLY D 549  LYS D 556 -1  O  PHE D 550   N  VAL D 442
SHEET    3  AD 4 GLY D 473  TYR D 482 -1  N  GLN D 480   O  GLN D 551
SHEET    4  AD 4 ARG D 515  LEU D 521 -1  O  ARG D 515   N  LEU D 479
SHEET    1  AE 3 PHE D 723  VAL D 732  0
SHEET    2  AE 3 LYS D 736  ASN D 745 -1  O  SER D 740   N  ASP D 729
SHEET    3  AE 3 LYS D 787  GLU D 795 -1  O  LEU D 794   N  ILE D 737
SHEET    1  AF 4 GLU D 773  LEU D 782  0
SHEET    2  AF 4 GLY D 752  ALA D 762 -1  N  VAL D 756   O  GLU D 778
SHEET    3  AF 4 GLY D 815  GLY D 822 -1  O  SER D 820   N  TYR D 759
SHEET    4  AF 4 ILE D 828  VAL D 836 -1  O  LYS D 832   N  VAL D 819
SHEET    1  AG 3 TYR D 802  ASN D 804  0
SHEET    2  AG 3 LYS D 809  VAL D 812 -1  O  HIS D 811   N  TYR D 802
SHEET    3  AG 3 LEU D 840  TRP D 842 -1  O  LEU D 840   N  VAL D 812
CISPEP   1 ASP A   45    GLY A   46          0         2.95
CISPEP   2 GLY A  100    PRO A  101          0         1.40
CISPEP   3 LYS A  146    HIS A  147          0        -4.70
CISPEP   4 PHE A  148    VAL A  149          0         6.73
CISPEP   5 PHE A  244    PRO A  245          0        -8.19
CISPEP   6 GLY A  246    PRO A  247          0        -7.51
CISPEP   7 LEU A  331    PRO A  332          0        -1.15
CISPEP   8 ASP B   45    GLY B   46          0        -8.38
CISPEP   9 GLY B  100    PRO B  101          0         2.33
CISPEP  10 LYS B  146    HIS B  147          0        -3.67
CISPEP  11 PHE B  148    VAL B  149          0         4.53
CISPEP  12 PHE B  244    PRO B  245          0        -5.33
CISPEP  13 GLY B  246    PRO B  247          0        -0.14
CISPEP  14 LEU B  331    PRO B  332          0        -2.88
CISPEP  15 ASP C   45    GLY C   46          0        -1.91
CISPEP  16 GLY C  100    PRO C  101          0         4.93
CISPEP  17 LYS C  146    HIS C  147          0        -8.64
CISPEP  18 PHE C  148    VAL C  149          0        -1.78
CISPEP  19 PHE C  244    PRO C  245          0        -8.52
CISPEP  20 GLY C  246    PRO C  247          0        -2.79
CISPEP  21 LEU C  331    PRO C  332          0        -3.66
CISPEP  22 ASP D   45    GLY D   46          0         0.33
CISPEP  23 GLY D  100    PRO D  101          0         1.24
CISPEP  24 LYS D  146    HIS D  147          0        -6.59
CISPEP  25 PHE D  148    VAL D  149          0        10.18
CISPEP  26 PHE D  244    PRO D  245          0        -5.15
CISPEP  27 GLY D  246    PRO D  247          0        -5.71
CISPEP  28 LEU D  331    PRO D  332          0        -4.22
SITE     1 AC1 12 TRP A  28  ASP A  45  LEU A  99  ARG A 113
SITE     2 AC1 12 LYS A 146  HIS A 147  MET A 190  TYR A 193
SITE     3 AC1 12 ASP A 225  TRP A 226  SER A 356  GLU A 590
SITE     1 AC2 10 ASP B  45  LEU B  99  ARG B 113  LYS B 146
SITE     2 AC2 10 HIS B 147  TYR B 193  ASP B 225  TRP B 226
SITE     3 AC2 10 SER B 356  GLU B 590
SITE     1 AC3 12 TRP C  28  ASP C  45  LEU C  99  ARG C 113
SITE     2 AC3 12 LYS C 146  HIS C 147  MET C 190  TYR C 193
SITE     3 AC3 12 ASP C 225  TRP C 226  SER C 356  GLU C 590
SITE     1 AC4 11 TRP D  28  ASP D  45  LEU D  99  ARG D 113
SITE     2 AC4 11 LYS D 146  HIS D 147  MET D 190  TYR D 193
SITE     3 AC4 11 ASP D 225  TRP D 226  GLU D 590
CRYST1  245.847  148.412  119.642  90.00 112.84  90.00 C 1 2 1      16
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      0.004068  0.000000  0.001713        0.00000
SCALE2      0.000000  0.006738  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009069        0.00000
      
PROCHECK
Go to PROCHECK summary
 References