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PDBsum entry 1v0e

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
1v0e
Jmol
Contents
Protein chains
(+ 0 more) 666 a.a.
Ligands
PO4 ×6
Waters ×3075
HEADER    HYDROLASE                               28-MAR-04   1V0E
TITLE     ENDOSIALIDASE OF BACTERIOPHAGE K1F
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ENDO-ALPHA-SIALIDASE;
COMPND   3 CHAIN: A, B, C, D, E, F;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 246-911;
COMPND   5 SYNONYM: ENDOSIALIDASE;
COMPND   6 EC: 3.2.1.129;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: COLIPHAGE K1F;
SOURCE   3 ORGANISM_TAXID: 344021;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ENDOSIALIDASE, POLYSIALIC ACID DEGRADATION, HYDROLASE,
KEYWDS   2 GLYCOSIDASE.
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.STUMMEYER,A.DICKMANNS,M.MUEHLENHOFF,R.GERADY-SCHAHN,
AUTHOR   2 R.FICNER
REVDAT   4   24-FEB-09 1V0E    1       VERSN
REVDAT   3   15-JUN-05 1V0E    1       JRNL
REVDAT   2   22-DEC-04 1V0E    1       JRNL
REVDAT   1   13-DEC-04 1V0E    0
JRNL        AUTH   K.STUMMEYER,A.DICKMANNS,M.MUEHLENHOFF,
JRNL        AUTH 2 R.GERARDY-SCHAHN,R.FICNER
JRNL        TITL   CRYSTAL STRUCTURE OF THE POLYSIALIC ACID-DEGRADING
JRNL        TITL 2 ENDOSIALIDASE OF BACTERIOPHAGE K1F
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  12    90 2005
JRNL        REFN                   ISSN 1545-9993
JRNL        PMID   15608653
JRNL        DOI    10.1038/NSMB874
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.MUHLENHOFF,K.STUMMEYER,M.GROVE,M.SAUERBORN,
REMARK   1  AUTH 2 R.GERARDY-SCHAHN
REMARK   1  TITL   PROTEOLYTIC PROCESSING AND OLIGOMERIZATION OF
REMARK   1  TITL 2 BACTERIOPHAGE-DERIVED ENDOSIALIDASES
REMARK   1  REF    J.BIOL.CHEM.                  V. 278 12634 2003
REMARK   1  REFN                   ISSN 0021-9258
REMARK   1  PMID   12556457
REMARK   1  DOI    10.1074/JBC.M212048200
REMARK   2
REMARK   2 RESOLUTION.    1.9  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.0
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7
REMARK   3   NUMBER OF REFLECTIONS             : 318265
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) : 0.16781
REMARK   3   R VALUE            (WORKING SET) : 0.16597
REMARK   3   FREE R VALUE                     : 0.20228
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 16879
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 31380
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 30
REMARK   3   SOLVENT ATOMS            : 3075
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.374
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.66
REMARK   3    B22 (A**2) : -0.57
REMARK   3    B33 (A**2) : -0.09
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.143
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.131
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.163
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1V0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-04.
REMARK 100 THE PDBE ID CODE IS EBI-14866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : BW7A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8416
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 335241
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : 0.10300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.35200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-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      173.35000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      173.35000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 GENERATING THE BIOMOLECULE
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 BIOMOLECULE:  2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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    VAL A 295   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES
REMARK 500    LEU A 355   CA  -  CB  -  CG  ANGL. DEV. =  19.7 DEGREES
REMARK 500    ARG A 396   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP A 455   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A 478   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 545   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 558   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A 596   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ARG A 596   NE  -  CZ  -  NH2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    LEU A 620   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES
REMARK 500    ASP A 639   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 711   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP A 741   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    LEU B 355   CA  -  CB  -  CG  ANGL. DEV. =  16.0 DEGREES
REMARK 500    ARG B 396   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ASP B 420   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP B 478   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP B 533   CB  -  CG  -  OD2 ANGL. DEV. =   7.6 DEGREES
REMARK 500    ARG B 568   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG B 596   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG B 596   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES
REMARK 500    LEU B 620   CA  -  CB  -  CG  ANGL. DEV. =  19.2 DEGREES
REMARK 500    ARG B 621   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP B 711   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    LEU C 355   CA  -  CB  -  CG  ANGL. DEV. =  19.6 DEGREES
REMARK 500    ASP C 364   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG C 396   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP C 533   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP C 558   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ARG C 596   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG C 596   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES
REMARK 500    LEU C 620   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES
REMARK 500    ASP C 682   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP C 722   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG C 865   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP D 249   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP D 253   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP D 331   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP D 348   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    LEU D 355   CA  -  CB  -  CG  ANGL. DEV. =  20.0 DEGREES
REMARK 500    ASP D 364   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP D 455   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP D 533   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASP D 558   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ARG D 596   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG D 596   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG D 609   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG D 609   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    LEU D 620   CA  -  CB  -  CG  ANGL. DEV. =  19.2 DEGREES
REMARK 500    ARG D 621   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      69 ANGLE DEVIATIONS
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLU A 310       -1.85     70.59
REMARK 500    ASP A 321       76.67   -154.87
REMARK 500    SER A 347     -154.92   -127.90
REMARK 500    SER A 528      159.91     82.16
REMARK 500    HIS A 628       -1.44     72.43
REMARK 500    TYR A 665       78.80   -119.12
REMARK 500    ASP A 711     -125.10     51.44
REMARK 500    GLU A 721     -167.02   -106.77
REMARK 500    SER A 740     -136.67     57.32
REMARK 500    SER A 806      -14.59   -142.41
REMARK 500    SER A 808       73.49     63.01
REMARK 500    SER A 878      -10.82     77.37
REMARK 500    GLU B 310       -6.89     72.58
REMARK 500    ASP B 321       78.74   -156.83
REMARK 500    ASN B 338       -0.33     68.99
REMARK 500    SER B 347     -156.87   -131.53
REMARK 500    SER B 528      158.21     78.56
REMARK 500    ASP B 533     -161.18   -163.91
REMARK 500    HIS B 628       -7.97     73.24
REMARK 500    TRP B 678       54.27     23.49
REMARK 500    ASP B 711     -123.31     47.57
REMARK 500    SER B 740     -127.93     45.42
REMARK 500    SER B 806      -15.68   -145.88
REMARK 500    SER B 808       68.79     61.89
REMARK 500    SER B 878       -5.37     72.65
REMARK 500    THR B 900     -178.80   -170.64
REMARK 500    VAL C 251      -44.88   -132.62
REMARK 500    PRO C 284     -169.31    -79.69
REMARK 500    GLU C 310       -1.94     74.64
REMARK 500    ASP C 321       77.99   -154.27
REMARK 500    SER C 347     -157.06   -133.90
REMARK 500    ARG C 354       16.82     56.93
REMARK 500    SER C 528      160.56     81.35
REMARK 500    ASP C 533     -156.12   -157.87
REMARK 500    HIS C 628       -7.30     67.72
REMARK 500    TYR C 665       78.03   -117.52
REMARK 500    ASP C 711     -124.97     52.55
REMARK 500    SER C 740     -131.45     48.98
REMARK 500    SER C 806      -14.79   -142.22
REMARK 500    SER C 808       72.00     60.34
REMARK 500    SER C 878       -5.85     78.05
REMARK 500    VAL D 251      -42.47   -133.19
REMARK 500    ASP D 321       79.04   -153.29
REMARK 500    ASN D 338       -0.61     73.80
REMARK 500    SER D 347     -155.31   -128.92
REMARK 500    SER D 528      154.94     78.64
REMARK 500    ASP D 533     -156.47   -155.90
REMARK 500    GLU D 581       66.87     39.51
REMARK 500    HIS D 628       -4.26     69.98
REMARK 500    ASN D 679      118.92   -160.46
REMARK 500    ASP D 711     -125.01     49.86
REMARK 500    GLU D 721     -168.92   -104.95
REMARK 500    SER D 740     -131.52     55.04
REMARK 500    SER D 806      -18.05   -145.40
REMARK 500    SER D 808       72.55     62.21
REMARK 500    SER D 878       -6.59     77.81
REMARK 500    VAL E 251      -44.56   -135.70
REMARK 500    ASP E 321       76.15   -157.88
REMARK 500    ASN E 338       -2.40     78.86
REMARK 500    SER E 347     -155.52   -132.59
REMARK 500    ARG E 354       19.77     57.37
REMARK 500    ASP E 478     -165.81   -162.24
REMARK 500    SER E 528      161.37     75.47
REMARK 500    ASP E 533     -158.01   -162.78
REMARK 500    GLU E 581       65.93     36.11
REMARK 500    SER E 605      136.38    -39.62
REMARK 500    HIS E 624       32.45     71.70
REMARK 500    HIS E 628       -7.12     75.28
REMARK 500    TYR E 665       79.15   -117.66
REMARK 500    TRP E 678       61.90     38.83
REMARK 500    ASP E 711     -121.53     53.56
REMARK 500    SER E 740     -131.46     56.16
REMARK 500    SER E 806      -20.79   -144.62
REMARK 500    SER E 808       69.01     65.54
REMARK 500    SER E 878       -7.88     77.25
REMARK 500    VAL F 251      -48.27   -132.83
REMARK 500    ASP F 321       81.17   -153.63
REMARK 500    ASN F 338       -4.60     77.04
REMARK 500    SER F 347     -157.36   -131.99
REMARK 500    ARG F 354       15.07     58.62
REMARK 500    ASP F 478     -163.71   -162.04
REMARK 500    SER F 528      155.65     79.80
REMARK 500    ASP F 533     -162.03   -162.97
REMARK 500    GLU F 581       65.19     38.04
REMARK 500    HIS F 628       -4.15     70.31
REMARK 500    TRP F 678       56.37     36.78
REMARK 500    ASP F 711     -124.30     53.27
REMARK 500    GLU F 721     -168.79   -106.22
REMARK 500    SER F 740     -127.30     54.52
REMARK 500    SER F 806      -19.45   -143.49
REMARK 500    SER F 808       72.84     55.72
REMARK 500    SER F 878      -10.94     78.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 MET B  503     GLY B  504                   53.78
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 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    VAL B 702        24.0      L          L   OUTSIDE RANGE
REMARK 500    VAL C 702        24.6      L          L   OUTSIDE RANGE
REMARK 500    THR D 443        24.7      L          L   OUTSIDE RANGE
REMARK 500    VAL D 702        24.5      L          L   OUTSIDE RANGE
REMARK 500    THR E 505        24.4      L          L   OUTSIDE RANGE
REMARK 500    VAL E 702        23.0      L          L   OUTSIDE RANGE
REMARK 500    VAL F 702        23.4      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 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1686
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D1685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F1685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F1686
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V0F   RELATED DB: PDB
REMARK 900  ENDOSIALIDASE OF BACTERIOPHAGE K1F IN COMPLEX
REMARK 900  WITH OLIGOMERIC ALPHA-2,8-SIALIC ACID
DBREF  1V0E A  245   245  PDB    1V0E     1V0E           245    245
DBREF  1V0E A  246   910  UNP    Q858B1   Q858B1         246    910
DBREF  1V0E B  245   245  PDB    1V0E     1V0E           245    245
DBREF  1V0E B  246   910  UNP    Q858B1   Q858B1         246    910
DBREF  1V0E C  245   245  PDB    1V0E     1V0E           245    245
DBREF  1V0E C  246   910  UNP    Q858B1   Q858B1         246    910
DBREF  1V0E D  245   245  PDB    1V0E     1V0E           245    245
DBREF  1V0E D  246   910  UNP    Q858B1   Q858B1         246    910
DBREF  1V0E E  245   245  PDB    1V0E     1V0E           245    245
DBREF  1V0E E  246   910  UNP    Q858B1   Q858B1         246    910
DBREF  1V0E F  245   245  PDB    1V0E     1V0E           245    245
DBREF  1V0E F  246   910  UNP    Q858B1   Q858B1         246    910
SEQRES   1 A  666  SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES   2 A  666  LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES   3 A  666  ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES   4 A  666  PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES   5 A  666  GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES   6 A  666  GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES   7 A  666  PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES   8 A  666  TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES   9 A  666  ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES  10 A  666  SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES  11 A  666  LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES  12 A  666  HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES  13 A  666  ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES  14 A  666  THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES  15 A  666  LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES  16 A  666  ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES  17 A  666  VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES  18 A  666  GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES  19 A  666  LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES  20 A  666  SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES  21 A  666  THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES  22 A  666  GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES  23 A  666  THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES  24 A  666  GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES  25 A  666  PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES  26 A  666  GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES  27 A  666  CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES  28 A  666  ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES  29 A  666  ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES  30 A  666  PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES  31 A  666  LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES  32 A  666  ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES  33 A  666  TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES  34 A  666  ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES  35 A  666  ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES  36 A  666  SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES  37 A  666  TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES  38 A  666  PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES  39 A  666  LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES  40 A  666  MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES  41 A  666  ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES  42 A  666  PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES  43 A  666  GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES  44 A  666  ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES  45 A  666  MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES  46 A  666  THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES  47 A  666  GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES  48 A  666  LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES  49 A  666  TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES  50 A  666  LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES  51 A  666  SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES  52 A  666  ILE VAL THR
SEQRES   1 B  666  SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES   2 B  666  LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES   3 B  666  ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES   4 B  666  PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES   5 B  666  GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES   6 B  666  GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES   7 B  666  PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES   8 B  666  TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES   9 B  666  ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES  10 B  666  SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES  11 B  666  LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES  12 B  666  HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES  13 B  666  ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES  14 B  666  THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES  15 B  666  LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES  16 B  666  ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES  17 B  666  VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES  18 B  666  GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES  19 B  666  LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES  20 B  666  SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES  21 B  666  THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES  22 B  666  GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES  23 B  666  THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES  24 B  666  GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES  25 B  666  PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES  26 B  666  GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES  27 B  666  CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES  28 B  666  ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES  29 B  666  ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES  30 B  666  PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES  31 B  666  LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES  32 B  666  ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES  33 B  666  TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES  34 B  666  ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES  35 B  666  ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES  36 B  666  SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES  37 B  666  TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES  38 B  666  PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES  39 B  666  LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES  40 B  666  MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES  41 B  666  ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES  42 B  666  PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES  43 B  666  GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES  44 B  666  ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES  45 B  666  MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES  46 B  666  THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES  47 B  666  GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES  48 B  666  LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES  49 B  666  TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES  50 B  666  LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES  51 B  666  SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES  52 B  666  ILE VAL THR
SEQRES   1 C  666  SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES   2 C  666  LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES   3 C  666  ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES   4 C  666  PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES   5 C  666  GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES   6 C  666  GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES   7 C  666  PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES   8 C  666  TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES   9 C  666  ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES  10 C  666  SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES  11 C  666  LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES  12 C  666  HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES  13 C  666  ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES  14 C  666  THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES  15 C  666  LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES  16 C  666  ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES  17 C  666  VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES  18 C  666  GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES  19 C  666  LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES  20 C  666  SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES  21 C  666  THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES  22 C  666  GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES  23 C  666  THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES  24 C  666  GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES  25 C  666  PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES  26 C  666  GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES  27 C  666  CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES  28 C  666  ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES  29 C  666  ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES  30 C  666  PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES  31 C  666  LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES  32 C  666  ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES  33 C  666  TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES  34 C  666  ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES  35 C  666  ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES  36 C  666  SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES  37 C  666  TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES  38 C  666  PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES  39 C  666  LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES  40 C  666  MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES  41 C  666  ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES  42 C  666  PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES  43 C  666  GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES  44 C  666  ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES  45 C  666  MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES  46 C  666  THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES  47 C  666  GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES  48 C  666  LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES  49 C  666  TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES  50 C  666  LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES  51 C  666  SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES  52 C  666  ILE VAL THR
SEQRES   1 D  666  SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES   2 D  666  LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES   3 D  666  ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES   4 D  666  PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES   5 D  666  GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES   6 D  666  GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES   7 D  666  PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES   8 D  666  TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES   9 D  666  ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES  10 D  666  SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES  11 D  666  LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES  12 D  666  HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES  13 D  666  ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES  14 D  666  THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES  15 D  666  LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES  16 D  666  ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES  17 D  666  VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES  18 D  666  GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES  19 D  666  LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES  20 D  666  SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES  21 D  666  THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES  22 D  666  GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES  23 D  666  THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES  24 D  666  GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES  25 D  666  PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES  26 D  666  GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES  27 D  666  CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES  28 D  666  ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES  29 D  666  ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES  30 D  666  PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES  31 D  666  LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES  32 D  666  ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES  33 D  666  TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES  34 D  666  ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES  35 D  666  ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES  36 D  666  SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES  37 D  666  TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES  38 D  666  PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES  39 D  666  LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES  40 D  666  MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES  41 D  666  ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES  42 D  666  PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES  43 D  666  GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES  44 D  666  ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES  45 D  666  MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES  46 D  666  THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES  47 D  666  GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES  48 D  666  LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES  49 D  666  TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES  50 D  666  LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES  51 D  666  SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES  52 D  666  ILE VAL THR
SEQRES   1 E  666  SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES   2 E  666  LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES   3 E  666  ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES   4 E  666  PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES   5 E  666  GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES   6 E  666  GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES   7 E  666  PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES   8 E  666  TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES   9 E  666  ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES  10 E  666  SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES  11 E  666  LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES  12 E  666  HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES  13 E  666  ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES  14 E  666  THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES  15 E  666  LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES  16 E  666  ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES  17 E  666  VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES  18 E  666  GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES  19 E  666  LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES  20 E  666  SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES  21 E  666  THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES  22 E  666  GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES  23 E  666  THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES  24 E  666  GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES  25 E  666  PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES  26 E  666  GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES  27 E  666  CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES  28 E  666  ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES  29 E  666  ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES  30 E  666  PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES  31 E  666  LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES  32 E  666  ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES  33 E  666  TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES  34 E  666  ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES  35 E  666  ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES  36 E  666  SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES  37 E  666  TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES  38 E  666  PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES  39 E  666  LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES  40 E  666  MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES  41 E  666  ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES  42 E  666  PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES  43 E  666  GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES  44 E  666  ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES  45 E  666  MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES  46 E  666  THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES  47 E  666  GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES  48 E  666  LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES  49 E  666  TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES  50 E  666  LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES  51 E  666  SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES  52 E  666  ILE VAL THR
SEQRES   1 F  666  SER ALA LYS GLY ASP GLY VAL THR ASP ASP THR ALA ALA
SEQRES   2 F  666  LEU THR SER ALA LEU ASN ASP THR PRO VAL GLY GLN LYS
SEQRES   3 F  666  ILE ASN GLY ASN GLY LYS THR TYR LYS VAL THR SER LEU
SEQRES   4 F  666  PRO ASP ILE SER ARG PHE ILE ASN THR ARG PHE VAL TYR
SEQRES   5 F  666  GLU ARG ILE PRO GLY GLN PRO LEU TYR TYR ALA SER GLU
SEQRES   6 F  666  GLU PHE VAL GLN GLY GLU LEU PHE LYS ILE THR ASP THR
SEQRES   7 F  666  PRO TYR TYR ASN ALA TRP PRO GLN ASP LYS ALA PHE VAL
SEQRES   8 F  666  TYR GLU ASN VAL ILE TYR ALA PRO TYR MET GLY SER ASP
SEQRES   9 F  666  ARG HIS GLY VAL SER ARG LEU HIS VAL SER TRP VAL LYS
SEQRES  10 F  666  SER GLY ASP ASP GLY GLN THR TRP SER THR PRO GLU TRP
SEQRES  11 F  666  LEU THR ASP LEU HIS PRO ASP TYR PRO THR VAL ASN TYR
SEQRES  12 F  666  HIS CYS MET SER MET GLY VAL CYS ARG ASN ARG LEU PHE
SEQRES  13 F  666  ALA MET ILE GLU THR ARG THR LEU ALA LYS ASN ALA LEU
SEQRES  14 F  666  THR ASN CYS ALA LEU TRP ASP ARG PRO MET SER ARG SER
SEQRES  15 F  666  LEU HIS LEU THR GLY GLY ILE THR LYS ALA ALA ASN GLN
SEQRES  16 F  666  ARG TYR ALA THR ILE HIS VAL PRO ASP HIS GLY LEU PHE
SEQRES  17 F  666  VAL GLY ASP PHE VAL ASN PHE SER ASN SER ALA VAL THR
SEQRES  18 F  666  GLY VAL SER GLY ASP MET THR VAL ALA THR VAL ILE ASP
SEQRES  19 F  666  LYS ASP ASN PHE THR VAL LEU THR PRO ASN GLN GLN THR
SEQRES  20 F  666  SER ASP LEU ASN ASN ALA GLY LYS ASN TRP HIS MET GLY
SEQRES  21 F  666  THR SER PHE HIS LYS SER PRO TRP ARG LYS THR ASP LEU
SEQRES  22 F  666  GLY LEU ILE PRO SER VAL THR GLU VAL HIS SER PHE ALA
SEQRES  23 F  666  THR ILE ASP ASN ASN GLY PHE ALA MET GLY TYR HIS GLN
SEQRES  24 F  666  GLY ASP VAL ALA PRO ARG GLU VAL GLY LEU PHE TYR PHE
SEQRES  25 F  666  PRO ASP ALA PHE ASN SER PRO SER ASN TYR VAL ARG ARG
SEQRES  26 F  666  GLN ILE PRO SER GLU TYR GLU PRO ASP ALA SER GLU PRO
SEQRES  27 F  666  CYS ILE LYS TYR TYR ASP GLY VAL LEU TYR LEU ILE THR
SEQRES  28 F  666  ARG GLY THR ARG GLY ASP ARG LEU GLY SER SER LEU HIS
SEQRES  29 F  666  ARG SER ARG ASP ILE GLY GLN THR TRP GLU SER LEU ARG
SEQRES  30 F  666  PHE PRO HIS ASN VAL HIS HIS THR THR LEU PRO PHE ALA
SEQRES  31 F  666  LYS VAL GLY ASP ASP LEU ILE MET PHE GLY SER GLU ARG
SEQRES  32 F  666  ALA GLU ASN GLU TRP GLU ALA GLY ALA PRO ASP ASP ARG
SEQRES  33 F  666  TYR LYS ALA SER TYR PRO ARG THR PHE TYR ALA ARG LEU
SEQRES  34 F  666  ASN VAL ASN ASN TRP ASN ALA ASP ASP ILE GLU TRP VAL
SEQRES  35 F  666  ASN ILE THR ASP GLN ILE TYR GLN GLY GLY ILE VAL ASN
SEQRES  36 F  666  SER GLY VAL GLY VAL GLY SER VAL VAL VAL LYS ASP ASN
SEQRES  37 F  666  TYR ILE TYR TYR MET PHE GLY GLY GLU ASP HIS PHE ASN
SEQRES  38 F  666  PRO TRP THR TYR GLY ASP ASN SER ALA LYS ASP PRO PHE
SEQRES  39 F  666  LYS SER ASP GLY HIS PRO SER ASP LEU TYR CYS TYR LYS
SEQRES  40 F  666  MET LYS ILE GLY PRO ASP ASN ARG VAL SER ARG ASP PHE
SEQRES  41 F  666  ARG TYR GLY ALA VAL PRO ASN ARG ALA VAL PRO VAL PHE
SEQRES  42 F  666  PHE ASP THR ASN GLY VAL ARG THR VAL PRO ALA PRO MET
SEQRES  43 F  666  GLU PHE THR GLY ASP LEU GLY LEU GLY HIS VAL THR ILE
SEQRES  44 F  666  ARG ALA SER THR SER SER ASN ILE ARG SER GLU VAL LEU
SEQRES  45 F  666  MET GLU GLY GLU TYR GLY PHE ILE GLY LYS SER ILE PRO
SEQRES  46 F  666  THR ASP ASN PRO ALA GLY GLN ARG ILE ILE PHE CYS GLY
SEQRES  47 F  666  GLY GLU GLY THR SER SER THR THR GLY ALA GLN ILE THR
SEQRES  48 F  666  LEU TYR GLY ALA ASN ASN THR ASP SER ARG ARG ILE VAL
SEQRES  49 F  666  TYR ASN GLY ASP GLU HIS LEU PHE GLN SER ALA ASP VAL
SEQRES  50 F  666  LYS PRO TYR ASN ASP ASN VAL THR ALA LEU GLY GLY PRO
SEQRES  51 F  666  SER ASN ARG PHE THR THR ALA TYR LEU GLY SER ASN PRO
SEQRES  52 F  666  ILE VAL THR
HET    PO4  B1685       5
HET    PO4  C1685       5
HET    PO4  C1686       5
HET    PO4  D1685       5
HET    PO4  F1685       5
HET    PO4  F1686       5
HETNAM     PO4 PHOSPHATE ION
FORMUL   7  PO4    6(O4 P 3-)
FORMUL  13  HOH   *3075(H2 O1)
HELIX    1   1 ASP A  254  THR A  265  1                                  12
HELIX    2   2 ASP A  285  SER A  287  5                                   3
HELIX    3   3 PRO A  572  GLU A  576  5                                   5
HELIX    4   4 ASN A  832  GLY A  835  5                                   4
HELIX    5   5 SER A  847  THR A  850  5                                   4
HELIX    6   6 ASP B  254  THR B  265  1                                  12
HELIX    7   7 ASP B  285  SER B  287  5                                   3
HELIX    8   8 PRO B  572  GLU B  576  5                                   5
HELIX    9   9 ASN B  832  GLY B  835  5                                   4
HELIX   10  10 SER B  847  THR B  850  5                                   4
HELIX   11  11 ASP C  254  ASP C  264  1                                  11
HELIX   12  12 ASP C  285  SER C  287  5                                   3
HELIX   13  13 PRO C  572  GLU C  576  5                                   5
HELIX   14  14 ASN C  832  GLY C  835  5                                   4
HELIX   15  15 SER C  847  THR C  850  5                                   4
HELIX   16  16 ASP D  254  THR D  265  1                                  12
HELIX   17  17 ASP D  285  SER D  287  5                                   3
HELIX   18  18 PRO D  572  GLU D  576  5                                   5
HELIX   19  19 ASN D  832  GLY D  835  5                                   4
HELIX   20  20 SER D  847  THR D  850  5                                   4
HELIX   21  21 ASP E  254  THR E  265  1                                  12
HELIX   22  22 ASP E  285  SER E  287  5                                   3
HELIX   23  23 PRO E  572  GLU E  576  5                                   5
HELIX   24  24 ASN E  832  GLY E  835  5                                   4
HELIX   25  25 SER E  847  THR E  850  5                                   4
HELIX   26  26 ASP F  254  THR F  265  1                                  12
HELIX   27  27 ASP F  285  SER F  287  5                                   3
HELIX   28  28 PRO F  572  GLU F  576  5                                   5
HELIX   29  29 ASN F  832  GLY F  835  5                                   4
HELIX   30  30 SER F  847  THR F  850  5                                   4
SHEET    1  AA 8 ASP A 249  ASP A 253  0
SHEET    2  AA 8 THR A 277  LYS A 279  1  O  THR A 277   N  GLY A 250
SHEET    3  AA 8 ARG A 293  TYR A 296  1  O  ARG A 293   N  TYR A 278
SHEET    4  AA 8 LEU A 304  ALA A 307 -1  O  LEU A 304   N  TYR A 296
SHEET    5  AA 8 VAL A 686  ASP A 690  1  O  ASN A 687   N  ALA A 307
SHEET    6  AA 8 ARG A 667  ASN A 674 -1  O  THR A 668   N  ILE A 688
SHEET    7  AA 8 ASP A 639  SER A 645 -1  O  LEU A 640   N  LEU A 673
SHEET    8  AA 8 PHE A 633  VAL A 636 -1  O  ALA A 634   N  ILE A 641
SHEET    1  AB 2 ILE A 271  ASN A 272  0
SHEET    2  AB 2 PHE A 289  ILE A 290  1  N  ILE A 290   O  ILE A 271
SHEET    1  AC 5 GLY A 703  LYS A 710  0
SHEET    2  AC 5 TYR A 713  GLY A 720 -1  O  TYR A 713   N  LYS A 710
SHEET    3  AC 5 ASP A 746  LYS A 753 -1  O  ASP A 746   N  GLY A 720
SHEET    4  AC 5 GLY A 314  LYS A 318 -1  O  GLU A 315   N  LYS A 751
SHEET    5  AC 5 ARG B 765  TYR B 766  1  O  ARG B 765   N  LYS A 318
SHEET    1  AD 3 TYR A 325  ALA A 327  0
SHEET    2  AD 3 VAL A 339  SER A 347 -1  O  MET A 345   N  ALA A 327
SHEET    3  AD 3 PHE A 334  TYR A 336 -1  O  PHE A 334   N  TYR A 341
SHEET    1  AE 4 TYR A 325  ALA A 327  0
SHEET    2  AE 4 VAL A 339  SER A 347 -1  O  MET A 345   N  ALA A 327
SHEET    3  AE 4 HIS A 356  SER A 362 -1  O  HIS A 356   N  GLY A 346
SHEET    4  AE 4 GLU A 373  TRP A 374 -1  O  GLU A 373   N  TRP A 359
SHEET    1  AF 3 VAL A 385  HIS A 388  0
SHEET    2  AF 3 ARG A 398  THR A 407 -1  O  GLU A 404   N  HIS A 388
SHEET    3  AF 3 MET A 392  CYS A 395 -1  O  GLY A 393   N  PHE A 400
SHEET    1  AG 4 VAL A 385  HIS A 388  0
SHEET    2  AG 4 ARG A 398  THR A 407 -1  O  GLU A 404   N  HIS A 388
SHEET    3  AG 4 LEU A 413  PRO A 422 -1  N  THR A 414   O  THR A 405
SHEET    4  AG 4 ARG A 513  ASP A 516 -1  O  ARG A 513   N  ASP A 420
SHEET    1  AH 4 SER A 426  THR A 430  0
SHEET    2  AH 4 ASN A 500  THR A 505 -1  O  TRP A 501   N  LEU A 429
SHEET    3  AH 4 PHE A 456  SER A 460 -1  O  ASN A 458   N  GLY A 504
SHEET    4  AH 4 GLY A 469  THR A 472 -1  O  GLY A 469   N  PHE A 459
SHEET    1  AI 5 THR A 475  ASP A 478  0
SHEET    2  AI 5 ASN A 481  LEU A 485 -1  O  ASN A 481   N  ILE A 477
SHEET    3  AI 5 TYR A 441  HIS A 445 -1  O  ALA A 442   N  VAL A 484
SHEET    4  AI 5 ILE A 433  LYS A 435 -1  O  THR A 434   N  THR A 443
SHEET    5  AI 5 LEU A 494  ASN A 495 -1  O  LEU A 494   N  LYS A 435
SHEET    1  AJ 4 GLU A 525  THR A 531  0
SHEET    2  AJ 4 PHE A 537  GLN A 543 -1  O  ALA A 538   N  ALA A 530
SHEET    3  AJ 4 GLU A 550  PHE A 556 -1  O  GLU A 550   N  GLN A 543
SHEET    4  AJ 4 VAL A 567  GLN A 570 -1  O  VAL A 567   N  TYR A 555
SHEET    1  AK 4 ALA A 579  TYR A 587  0
SHEET    2  AK 4 VAL A 590  GLY A 597 -1  O  VAL A 590   N  TYR A 587
SHEET    3  AK 4 SER A 606  SER A 610 -1  O  SER A 606   N  THR A 595
SHEET    4  AK 4 GLU A 618  ARG A 621 -1  O  GLU A 618   N  ARG A 609
SHEET    1  AL 5 ARG A 765  TYR A 766  0
SHEET    2  AL 5 GLY C 314  LYS C 318  1  O  LEU C 316   N  ARG A 765
SHEET    3  AL 5 ASP C 746  LYS C 753 -1  O  CYS C 749   N  PHE C 317
SHEET    4  AL 5 TYR C 713  GLY C 720 -1  O  ILE C 714   N  MET C 752
SHEET    5  AL 5 GLY C 703  LYS C 710 -1  O  GLY C 703   N  GLY C 719
SHEET    1  AM12 PHE A 777  PHE A 778  0
SHEET    2  AM12 ARG A 784  VAL A 786 -1  O  THR A 785   N  PHE A 777
SHEET    3  AM12 MET C 790  PHE C 792  1  O  GLU C 791   N  VAL A 786
SHEET    4  AM12 LEU B 796  LEU B 798  1  O  GLY B 797   N  PHE C 792
SHEET    5  AM12 VAL A 801  ILE A 803  1  O  THR A 802   N  LEU B 798
SHEET    6  AM12 ARG C 812  MET C 817  1  O  GLU C 814   N  VAL A 801
SHEET    7  AM12 TYR B 821  LYS B 826  1  O  TYR B 821   N  SER C 813
SHEET    8  AM12 ARG A 837  CYS A 841  1  O  ARG A 837   N  GLY B 822
SHEET    9  AM12 GLN A 853  TYR A 857 -1  O  ILE A 854   N  PHE A 840
SHEET   10  AM12 ARG A 866  ASN A 870 -1  O  ARG A 866   N  TYR A 857
SHEET   11  AM12 GLU C 873  GLN C 877  1  O  GLU C 873   N  ILE A 867
SHEET   12  AM12 VAL B 881  PRO B 883  1  O  LYS B 882   N  PHE C 876
SHEET    1  BA12 PHE B 777  PHE B 778  0
SHEET    2  BA12 ARG B 784  VAL B 786 -1  O  THR B 785   N  PHE B 777
SHEET    3  BA12 MET A 790  PHE A 792  1  O  GLU A 791   N  VAL B 786
SHEET    4  BA12 LEU C 796  LEU C 798  1  O  GLY C 797   N  PHE A 792
SHEET    5  BA12 VAL B 801  ILE B 803  1  O  THR B 802   N  LEU C 798
SHEET    6  BA12 ARG A 812  MET A 817  1  O  GLU A 814   N  VAL B 801
SHEET    7  BA12 TYR C 821  LYS C 826  1  O  TYR C 821   N  SER A 813
SHEET    8  BA12 ARG B 837  CYS B 841  1  O  ARG B 837   N  GLY C 822
SHEET    9  BA12 GLN B 853  TYR B 857 -1  O  ILE B 854   N  PHE B 840
SHEET   10  BA12 ARG B 866  ASN B 870 -1  O  ARG B 866   N  TYR B 857
SHEET   11  BA12 GLU A 873  GLN A 877  1  O  GLU A 873   N  ILE B 867
SHEET   12  BA12 VAL C 881  PRO C 883  1  O  LYS C 882   N  PHE A 876
SHEET    1  AN12 VAL A 881  PRO A 883  0
SHEET    2  AN12 GLU B 873  GLN B 877  1  O  HIS B 874   N  LYS A 882
SHEET    3  AN12 ARG C 866  ASN C 870  1  O  ILE C 867   N  LEU B 875
SHEET    4  AN12 GLN C 853  TYR C 857 -1  O  GLN C 853   N  ASN C 870
SHEET    5  AN12 ARG C 837  CYS C 841 -1  O  ILE C 838   N  LEU C 856
SHEET    6  AN12 TYR A 821  LYS A 826  1  O  GLY A 822   N  ILE C 839
SHEET    7  AN12 ARG B 812  MET B 817  1  O  SER B 813   N  PHE A 823
SHEET    8  AN12 VAL C 801  ILE C 803  1  O  VAL C 801   N  LEU B 816
SHEET    9  AN12 LEU A 796  LEU A 798  1  O  LEU A 796   N  THR C 802
SHEET   10  AN12 MET B 790  PHE B 792  1  O  MET B 790   N  GLY A 797
SHEET   11  AN12 ARG C 784  VAL C 786  1  O  ARG C 784   N  GLU B 791
SHEET   12  AN12 PHE C 777  PHE C 778 -1  O  PHE C 777   N  THR C 785
SHEET    1  AO 2 TYR A 902  LEU A 903  0
SHEET    2  AO 2 ILE C 908  VAL C 909  1  O  ILE C 908   N  LEU A 903
SHEET    1  AP 2 ILE A 908  VAL A 909  0
SHEET    2  AP 2 TYR B 902  LEU B 903  1  N  LEU B 903   O  ILE A 908
SHEET    1  BB 8 ASP B 249  ASP B 253  0
SHEET    2  BB 8 THR B 277  LYS B 279  1  O  THR B 277   N  GLY B 250
SHEET    3  BB 8 ARG B 293  TYR B 296  1  O  ARG B 293   N  TYR B 278
SHEET    4  BB 8 LEU B 304  ALA B 307 -1  O  LEU B 304   N  TYR B 296
SHEET    5  BB 8 VAL B 686  ASP B 690  1  O  ASN B 687   N  ALA B 307
SHEET    6  BB 8 ARG B 667  ASN B 674 -1  O  THR B 668   N  ILE B 688
SHEET    7  BB 8 ASP B 639  SER B 645 -1  O  LEU B 640   N  LEU B 673
SHEET    8  BB 8 PHE B 633  VAL B 636 -1  O  ALA B 634   N  ILE B 641
SHEET    1  BC 2 ILE B 271  ASN B 272  0
SHEET    2  BC 2 PHE B 289  ILE B 290  1  N  ILE B 290   O  ILE B 271
SHEET    1  BD 5 GLY B 703  LYS B 710  0
SHEET    2  BD 5 TYR B 713  GLY B 720 -1  O  TYR B 713   N  LYS B 710
SHEET    3  BD 5 ASP B 746  LYS B 753 -1  O  ASP B 746   N  GLY B 720
SHEET    4  BD 5 GLY B 314  LYS B 318 -1  O  GLU B 315   N  LYS B 751
SHEET    5  BD 5 ARG C 765  TYR C 766  1  O  ARG C 765   N  LYS B 318
SHEET    1  BE 3 TYR B 325  ALA B 327  0
SHEET    2  BE 3 VAL B 339  SER B 347 -1  O  MET B 345   N  ALA B 327
SHEET    3  BE 3 PHE B 334  TYR B 336 -1  O  PHE B 334   N  TYR B 341
SHEET    1  BF 4 TYR B 325  ALA B 327  0
SHEET    2  BF 4 VAL B 339  SER B 347 -1  O  MET B 345   N  ALA B 327
SHEET    3  BF 4 HIS B 356  SER B 362 -1  O  HIS B 356   N  GLY B 346
SHEET    4  BF 4 GLU B 373  TRP B 374 -1  O  GLU B 373   N  TRP B 359
SHEET    1  BG 7 VAL B 385  HIS B 388  0
SHEET    2  BG 7 ARG B 398  THR B 407 -1  O  GLU B 404   N  HIS B 388
SHEET    3  BG 7 MET B 392  CYS B 395 -1  O  GLY B 393   N  PHE B 400
SHEET    4  BG 7 ARG B 398  THR B 407 -1  O  ARG B 398   N  CYS B 395
SHEET    5  BG 7 ARG B 513  ASP B 516
SHEET    6  BG 7 LEU B 413  PRO B 422 -1  O  LEU B 418   N  THR B 515
SHEET    7  BG 7 ARG B 398  THR B 407 -1  O  LEU B 399   N  ARG B 421
SHEET    1  BH 8 SER B 426  THR B 430  0
SHEET    2  BH 8 ASN B 500  THR B 505 -1  O  TRP B 501   N  LEU B 429
SHEET    3  BH 8 PHE B 456  SER B 460 -1  O  ASN B 458   N  GLY B 504
SHEET    4  BH 8 GLY B 469  ASP B 478 -1  O  GLY B 469   N  PHE B 459
SHEET    5  BH 8 ASN B 481  LEU B 485 -1  O  ASN B 481   N  ILE B 477
SHEET    6  BH 8 TYR B 441  HIS B 445 -1  O  ALA B 442   N  VAL B 484
SHEET    7  BH 8 ILE B 433  LYS B 435 -1  O  THR B 434   N  THR B 443
SHEET    8  BH 8 LEU B 494  ASN B 495 -1  O  LEU B 494   N  LYS B 435
SHEET    1  BI 4 GLU B 525  THR B 531  0
SHEET    2  BI 4 PHE B 537  GLN B 543 -1  O  ALA B 538   N  ALA B 530
SHEET    3  BI 4 GLU B 550  PHE B 556 -1  O  GLU B 550   N  GLN B 543
SHEET    4  BI 4 VAL B 567  GLN B 570 -1  O  VAL B 567   N  TYR B 555
SHEET    1  BJ 4 ALA B 579  TYR B 587  0
SHEET    2  BJ 4 VAL B 590  GLY B 597 -1  O  VAL B 590   N  TYR B 587
SHEET    3  BJ 4 SER B 606  SER B 610 -1  O  SER B 606   N  THR B 595
SHEET    4  BJ 4 GLU B 618  ARG B 621 -1  O  GLU B 618   N  ARG B 609
SHEET    1  BK 2 ILE B 908  VAL B 909  0
SHEET    2  BK 2 TYR C 902  LEU C 903  1  N  LEU C 903   O  ILE B 908
SHEET    1  CA 8 ASP C 249  ASP C 253  0
SHEET    2  CA 8 THR C 277  LYS C 279  1  O  THR C 277   N  GLY C 250
SHEET    3  CA 8 ARG C 293  TYR C 296  1  O  ARG C 293   N  TYR C 278
SHEET    4  CA 8 LEU C 304  ALA C 307 -1  O  LEU C 304   N  TYR C 296
SHEET    5  CA 8 VAL C 686  ASP C 690  1  O  ASN C 687   N  ALA C 307
SHEET    6  CA 8 ARG C 667  ASN C 674 -1  O  THR C 668   N  ILE C 688
SHEET    7  CA 8 ASP C 639  SER C 645 -1  O  LEU C 640   N  LEU C 673
SHEET    8  CA 8 PHE C 633  VAL C 636 -1  O  ALA C 634   N  ILE C 641
SHEET    1  CB 2 ILE C 271  ASN C 272  0
SHEET    2  CB 2 PHE C 289  ILE C 290  1  N  ILE C 290   O  ILE C 271
SHEET    1  CC 7 TYR C 325  ALA C 327  0
SHEET    2  CC 7 VAL C 339  SER C 347 -1  O  MET C 345   N  ALA C 327
SHEET    3  CC 7 PHE C 334  TYR C 336 -1  O  PHE C 334   N  TYR C 341
SHEET    4  CC 7 VAL C 339  SER C 347 -1  O  VAL C 339   N  TYR C 336
SHEET    5  CC 7 GLU C 373  TRP C 374
SHEET    6  CC 7 HIS C 356  SER C 362 -1  O  TRP C 359   N  GLU C 373
SHEET    7  CC 7 VAL C 339  SER C 347 -1  O  ILE C 340   N  SER C 362
SHEET    1  CD 7 VAL C 385  HIS C 388  0
SHEET    2  CD 7 ARG C 398  THR C 407 -1  O  GLU C 404   N  HIS C 388
SHEET    3  CD 7 MET C 392  CYS C 395 -1  O  GLY C 393   N  PHE C 400
SHEET    4  CD 7 ARG C 398  THR C 407 -1  O  ARG C 398   N  CYS C 395
SHEET    5  CD 7 ARG C 513  GLY C 518
SHEET    6  CD 7 LEU C 413  PRO C 422 -1  O  CYS C 416   N  LEU C 517
SHEET    7  CD 7 ARG C 398  THR C 407 -1  O  LEU C 399   N  ARG C 421
SHEET    1  CE 2 SER C 426  THR C 430  0
SHEET    2  CE 2 ASN C 500  GLY C 504 -1  O  TRP C 501   N  LEU C 429
SHEET    1  CF 6 PHE C 456  PHE C 459  0
SHEET    2  CF 6 GLY C 469  ASP C 478 -1  O  GLY C 469   N  PHE C 459
SHEET    3  CF 6 ASN C 481  LEU C 485 -1  O  ASN C 481   N  ASP C 478
SHEET    4  CF 6 TYR C 441  HIS C 445 -1  O  ALA C 442   N  VAL C 484
SHEET    5  CF 6 ILE C 433  LYS C 435 -1  O  THR C 434   N  THR C 443
SHEET    6  CF 6 LEU C 494  ASN C 495 -1  O  LEU C 494   N  LYS C 435
SHEET    1  CG 4 GLU C 525  THR C 531  0
SHEET    2  CG 4 PHE C 537  GLN C 543 -1  O  ALA C 538   N  ALA C 530
SHEET    3  CG 4 GLU C 550  PHE C 556 -1  O  GLU C 550   N  GLN C 543
SHEET    4  CG 4 VAL C 567  GLN C 570 -1  O  VAL C 567   N  TYR C 555
SHEET    1  CH 4 ALA C 579  TYR C 587  0
SHEET    2  CH 4 VAL C 590  GLY C 597 -1  O  VAL C 590   N  TYR C 587
SHEET    3  CH 4 SER C 606  SER C 610 -1  O  SER C 606   N  THR C 595
SHEET    4  CH 4 GLU C 618  ARG C 621 -1  O  GLU C 618   N  ARG C 609
SHEET    1  DA 8 ASP D 249  ASP D 253  0
SHEET    2  DA 8 THR D 277  LYS D 279  1  O  THR D 277   N  GLY D 250
SHEET    3  DA 8 ARG D 293  TYR D 296  1  O  ARG D 293   N  TYR D 278
SHEET    4  DA 8 LEU D 304  ALA D 307 -1  O  LEU D 304   N  TYR D 296
SHEET    5  DA 8 VAL D 686  ASP D 690  1  O  ASN D 687   N  ALA D 307
SHEET    6  DA 8 ARG D 667  ASN D 674 -1  O  THR D 668   N  ILE D 688
SHEET    7  DA 8 ASP D 639  SER D 645 -1  O  LEU D 640   N  LEU D 673
SHEET    8  DA 8 PHE D 633  VAL D 636 -1  O  ALA D 634   N  ILE D 641
SHEET    1  DB 2 ILE D 271  ASN D 272  0
SHEET    2  DB 2 PHE D 289  ILE D 290  1  N  ILE D 290   O  ILE D 271
SHEET    1  DC 5 GLY D 703  LYS D 710  0
SHEET    2  DC 5 TYR D 713  GLY D 720 -1  O  TYR D 713   N  LYS D 710
SHEET    3  DC 5 ASP D 746  LYS D 753 -1  O  ASP D 746   N  GLY D 720
SHEET    4  DC 5 GLY D 314  LYS D 318 -1  O  GLU D 315   N  LYS D 751
SHEET    5  DC 5 ARG F 765  TYR F 766  1  O  ARG F 765   N  LYS D 318
SHEET    1  DD 7 TYR D 325  ALA D 327  0
SHEET    2  DD 7 VAL D 339  SER D 347 -1  O  MET D 345   N  ALA D 327
SHEET    3  DD 7 PHE D 334  TYR D 336 -1  O  PHE D 334   N  TYR D 341
SHEET    4  DD 7 VAL D 339  SER D 347 -1  O  VAL D 339   N  TYR D 336
SHEET    5  DD 7 GLU D 373  TRP D 374
SHEET    6  DD 7 HIS D 356  SER D 362 -1  O  TRP D 359   N  GLU D 373
SHEET    7  DD 7 VAL D 339  SER D 347 -1  O  ILE D 340   N  SER D 362
SHEET    1  DE 7 VAL D 385  HIS D 388  0
SHEET    2  DE 7 ARG D 398  THR D 407 -1  O  GLU D 404   N  HIS D 388
SHEET    3  DE 7 MET D 392  CYS D 395 -1  O  GLY D 393   N  PHE D 400
SHEET    4  DE 7 ARG D 398  THR D 407 -1  O  ARG D 398   N  CYS D 395
SHEET    5  DE 7 ARG D 513  GLY D 518
SHEET    6  DE 7 LEU D 413  PRO D 422 -1  O  CYS D 416   N  LEU D 517
SHEET    7  DE 7 ARG D 398  THR D 407 -1  O  LEU D 399   N  ARG D 421
SHEET    1  DF 8 SER D 426  THR D 430  0
SHEET    2  DF 8 ASN D 500  THR D 505 -1  O  TRP D 501   N  LEU D 429
SHEET    3  DF 8 PHE D 456  SER D 460 -1  O  ASN D 458   N  GLY D 504
SHEET    4  DF 8 GLY D 469  ASP D 478 -1  O  GLY D 469   N  PHE D 459
SHEET    5  DF 8 ASN D 481  LEU D 485 -1  O  ASN D 481   N  ASP D 478
SHEET    6  DF 8 TYR D 441  HIS D 445 -1  O  ALA D 442   N  VAL D 484
SHEET    7  DF 8 ILE D 433  LYS D 435 -1  O  THR D 434   N  THR D 443
SHEET    8  DF 8 LEU D 494  ASN D 495 -1  O  LEU D 494   N  LYS D 435
SHEET    1  DG 4 GLU D 525  THR D 531  0
SHEET    2  DG 4 PHE D 537  GLN D 543 -1  O  ALA D 538   N  ALA D 530
SHEET    3  DG 4 GLU D 550  PHE D 556 -1  O  GLU D 550   N  GLN D 543
SHEET    4  DG 4 VAL D 567  GLN D 570 -1  O  VAL D 567   N  TYR D 555
SHEET    1  DH 4 ALA D 579  TYR D 587  0
SHEET    2  DH 4 VAL D 590  GLY D 597 -1  O  VAL D 590   N  TYR D 587
SHEET    3  DH 4 SER D 606  SER D 610 -1  O  SER D 606   N  THR D 595
SHEET    4  DH 4 GLU D 618  ARG D 621 -1  O  GLU D 618   N  ARG D 609
SHEET    1  DI 5 ARG D 765  TYR D 766  0
SHEET    2  DI 5 GLY E 314  LYS E 318  1  O  LEU E 316   N  ARG D 765
SHEET    3  DI 5 ASP E 746  LYS E 753 -1  O  CYS E 749   N  PHE E 317
SHEET    4  DI 5 TYR E 713  GLY E 720 -1  O  ILE E 714   N  MET E 752
SHEET    5  DI 5 GLY E 703  LYS E 710 -1  O  GLY E 703   N  GLY E 719
SHEET    1  DJ12 PHE D 777  PHE D 778  0
SHEET    2  DJ12 ARG D 784  VAL D 786 -1  O  THR D 785   N  PHE D 777
SHEET    3  DJ12 MET E 790  PHE E 792  1  O  GLU E 791   N  VAL D 786
SHEET    4  DJ12 LEU F 796  LEU F 798  1  O  GLY F 797   N  PHE E 792
SHEET    5  DJ12 VAL D 801  ILE D 803  1  O  THR D 802   N  LEU F 798
SHEET    6  DJ12 ARG E 812  MET E 817  1  O  GLU E 814   N  VAL D 801
SHEET    7  DJ12 TYR F 821  LYS F 826  1  O  TYR F 821   N  SER E 813
SHEET    8  DJ12 ARG D 837  CYS D 841  1  O  ARG D 837   N  GLY F 822
SHEET    9  DJ12 GLN D 853  TYR D 857 -1  O  ILE D 854   N  PHE D 840
SHEET   10  DJ12 ARG D 866  ASN D 870 -1  O  ARG D 866   N  TYR D 857
SHEET   11  DJ12 GLU E 873  GLN E 877  1  O  GLU E 873   N  ILE D 867
SHEET   12  DJ12 VAL F 881  PRO F 883  1  O  LYS F 882   N  PHE E 876
SHEET    1  EA12 VAL E 881  PRO E 883  0
SHEET    2  EA12 GLU D 873  GLN D 877  1  O  HIS D 874   N  LYS E 882
SHEET    3  EA12 ARG F 866  ASN F 870  1  O  ILE F 867   N  LEU D 875
SHEET    4  EA12 GLN F 853  TYR F 857 -1  O  GLN F 853   N  ASN F 870
SHEET    5  EA12 ARG F 837  CYS F 841 -1  O  ILE F 838   N  LEU F 856
SHEET    6  EA12 TYR E 821  LYS E 826  1  O  GLY E 822   N  ILE F 839
SHEET    7  EA12 ARG D 812  MET D 817  1  O  SER D 813   N  PHE E 823
SHEET    8  EA12 VAL F 801  ILE F 803  1  O  VAL F 801   N  LEU D 816
SHEET    9  EA12 LEU E 796  LEU E 798  1  O  LEU E 796   N  THR F 802
SHEET   10  EA12 MET D 790  PHE D 792  1  O  MET D 790   N  GLY E 797
SHEET   11  EA12 ARG F 784  VAL F 786  1  O  ARG F 784   N  GLU D 791
SHEET   12  EA12 PHE F 777  PHE F 778 -1  O  PHE F 777   N  THR F 785
SHEET    1  DK12 VAL D 881  PRO D 883  0
SHEET    2  DK12 GLU F 873  GLN F 877  1  O  HIS F 874   N  LYS D 882
SHEET    3  DK12 ARG E 866  ASN E 870  1  O  ILE E 867   N  LEU F 875
SHEET    4  DK12 GLN E 853  TYR E 857 -1  O  GLN E 853   N  ASN E 870
SHEET    5  DK12 ARG E 837  CYS E 841 -1  O  ILE E 838   N  LEU E 856
SHEET    6  DK12 TYR D 821  LYS D 826  1  O  GLY D 822   N  ILE E 839
SHEET    7  DK12 ARG F 812  MET F 817  1  O  SER F 813   N  PHE D 823
SHEET    8  DK12 VAL E 801  ILE E 803  1  O  VAL E 801   N  LEU F 816
SHEET    9  DK12 LEU D 796  LEU D 798  1  O  LEU D 796   N  THR E 802
SHEET   10  DK12 MET F 790  PHE F 792  1  O  MET F 790   N  GLY D 797
SHEET   11  DK12 ARG E 784  VAL E 786  1  O  ARG E 784   N  GLU F 791
SHEET   12  DK12 PHE E 777  PHE E 778 -1  O  PHE E 777   N  THR E 785
SHEET    1  DL 2 TYR D 902  LEU D 903  0
SHEET    2  DL 2 ILE E 908  VAL E 909  1  O  ILE E 908   N  LEU D 903
SHEET    1  DM 2 ILE D 908  VAL D 909  0
SHEET    2  DM 2 TYR F 902  LEU F 903  1  N  LEU F 903   O  ILE D 908
SHEET    1  EB 2 ILE E 271  ASN E 272  0
SHEET    2  EB 2 PHE E 289  ILE E 290  1  N  ILE E 290   O  ILE E 271
SHEET    1  EC 7 THR E 277  LYS E 279  0
SHEET    2  EC 7 ARG E 293  TYR E 296  1  O  ARG E 293   N  TYR E 278
SHEET    3  EC 7 LEU E 304  ALA E 307 -1  O  LEU E 304   N  TYR E 296
SHEET    4  EC 7 VAL E 686  ASP E 690  1  O  ASN E 687   N  ALA E 307
SHEET    5  EC 7 ARG E 667  ASN E 674 -1  O  THR E 668   N  ILE E 688
SHEET    6  EC 7 ASP E 639  SER E 645 -1  O  LEU E 640   N  LEU E 673
SHEET    7  EC 7 PHE E 633  VAL E 636 -1  O  ALA E 634   N  ILE E 641
SHEET    1  ED 7 TYR E 325  ALA E 327  0
SHEET    2  ED 7 VAL E 339  SER E 347 -1  O  MET E 345   N  ALA E 327
SHEET    3  ED 7 PHE E 334  TYR E 336 -1  O  PHE E 334   N  TYR E 341
SHEET    4  ED 7 VAL E 339  SER E 347 -1  O  VAL E 339   N  TYR E 336
SHEET    5  ED 7 GLU E 373  TRP E 374
SHEET    6  ED 7 HIS E 356  SER E 362 -1  O  TRP E 359   N  GLU E 373
SHEET    7  ED 7 VAL E 339  SER E 347 -1  O  ILE E 340   N  SER E 362
SHEET    1  EE 7 VAL E 385  HIS E 388  0
SHEET    2  EE 7 ARG E 398  THR E 407 -1  O  GLU E 404   N  HIS E 388
SHEET    3  EE 7 MET E 392  CYS E 395 -1  O  GLY E 393   N  PHE E 400
SHEET    4  EE 7 ARG E 398  THR E 407 -1  O  ARG E 398   N  CYS E 395
SHEET    5  EE 7 ARG E 513  GLY E 518
SHEET    6  EE 7 LEU E 413  PRO E 422 -1  O  CYS E 416   N  LEU E 517
SHEET    7  EE 7 ARG E 398  THR E 407 -1  O  LEU E 399   N  ARG E 421
SHEET    1  EF 8 SER E 426  THR E 430  0
SHEET    2  EF 8 ASN E 500  THR E 505 -1  O  TRP E 501   N  LEU E 429
SHEET    3  EF 8 PHE E 456  SER E 460 -1  O  ASN E 458   N  GLY E 504
SHEET    4  EF 8 GLY E 469  ASP E 478 -1  O  GLY E 469   N  PHE E 459
SHEET    5  EF 8 ASN E 481  LEU E 485 -1  O  ASN E 481   N  ASP E 478
SHEET    6  EF 8 TYR E 441  HIS E 445 -1  O  ALA E 442   N  VAL E 484
SHEET    7  EF 8 ILE E 433  LYS E 435 -1  O  THR E 434   N  THR E 443
SHEET    8  EF 8 LEU E 494  ASN E 495 -1  O  LEU E 494   N  LYS E 435
SHEET    1  EG 4 GLU E 525  THR E 531  0
SHEET    2  EG 4 PHE E 537  GLN E 543 -1  O  ALA E 538   N  ALA E 530
SHEET    3  EG 4 GLU E 550  PHE E 556 -1  O  GLU E 550   N  GLN E 543
SHEET    4  EG 4 VAL E 567  GLN E 570 -1  O  VAL E 567   N  TYR E 555
SHEET    1  EH 4 ALA E 579  TYR E 587  0
SHEET    2  EH 4 VAL E 590  GLY E 597 -1  O  VAL E 590   N  TYR E 587
SHEET    3  EH 4 SER E 606  SER E 610 -1  O  SER E 606   N  THR E 595
SHEET    4  EH 4 GLU E 618  ARG E 621 -1  O  GLU E 618   N  ARG E 609
SHEET    1  EI 5 ARG E 765  TYR E 766  0
SHEET    2  EI 5 GLY F 314  LYS F 318  1  O  LEU F 316   N  ARG E 765
SHEET    3  EI 5 ASP F 746  LYS F 753 -1  O  CYS F 749   N  PHE F 317
SHEET    4  EI 5 TYR F 713  GLY F 720 -1  O  ILE F 714   N  MET F 752
SHEET    5  EI 5 GLY F 703  LYS F 710 -1  O  GLY F 703   N  GLY F 719
SHEET    1  EJ 2 TYR E 902  LEU E 903  0
SHEET    2  EJ 2 ILE F 908  VAL F 909  1  O  ILE F 908   N  LEU E 903
SHEET    1  FA 2 ILE F 271  ASN F 272  0
SHEET    2  FA 2 PHE F 289  ILE F 290  1  N  ILE F 290   O  ILE F 271
SHEET    1  FB 7 THR F 277  LYS F 279  0
SHEET    2  FB 7 ARG F 293  TYR F 296  1  O  ARG F 293   N  TYR F 278
SHEET    3  FB 7 LEU F 304  ALA F 307 -1  O  LEU F 304   N  TYR F 296
SHEET    4  FB 7 VAL F 686  ASP F 690  1  O  ASN F 687   N  ALA F 307
SHEET    5  FB 7 ARG F 667  ASN F 674 -1  O  THR F 668   N  ILE F 688
SHEET    6  FB 7 ASP F 639  SER F 645 -1  O  LEU F 640   N  LEU F 673
SHEET    7  FB 7 PHE F 633  VAL F 636 -1  O  ALA F 634   N  ILE F 641
SHEET    1  FC 7 TYR F 325  ALA F 327  0
SHEET    2  FC 7 VAL F 339  SER F 347 -1  O  MET F 345   N  ALA F 327
SHEET    3  FC 7 PHE F 334  TYR F 336 -1  O  PHE F 334   N  TYR F 341
SHEET    4  FC 7 VAL F 339  SER F 347 -1  O  VAL F 339   N  TYR F 336
SHEET    5  FC 7 GLU F 373  TRP F 374
SHEET    6  FC 7 HIS F 356  SER F 362 -1  O  TRP F 359   N  GLU F 373
SHEET    7  FC 7 VAL F 339  SER F 347 -1  O  ILE F 340   N  SER F 362
SHEET    1  FD 7 VAL F 385  HIS F 388  0
SHEET    2  FD 7 ARG F 398  THR F 407 -1  O  GLU F 404   N  HIS F 388
SHEET    3  FD 7 MET F 392  CYS F 395 -1  O  GLY F 393   N  PHE F 400
SHEET    4  FD 7 ARG F 398  THR F 407 -1  O  ARG F 398   N  CYS F 395
SHEET    5  FD 7 ARG F 513  GLY F 518
SHEET    6  FD 7 LEU F 413  PRO F 422 -1  O  CYS F 416   N  LEU F 517
SHEET    7  FD 7 ARG F 398  THR F 407 -1  O  LEU F 399   N  ARG F 421
SHEET    1  FE 4 SER F 426  THR F 430  0
SHEET    2  FE 4 ASN F 500  THR F 505 -1  O  TRP F 501   N  LEU F 429
SHEET    3  FE 4 PHE F 456  SER F 460 -1  O  ASN F 458   N  GLY F 504
SHEET    4  FE 4 GLY F 469  THR F 472 -1  O  GLY F 469   N  PHE F 459
SHEET    1  FF 5 THR F 475  ASP F 478  0
SHEET    2  FF 5 ASN F 481  LEU F 485 -1  O  ASN F 481   N  ASP F 478
SHEET    3  FF 5 TYR F 441  HIS F 445 -1  O  ALA F 442   N  VAL F 484
SHEET    4  FF 5 ILE F 433  LYS F 435 -1  O  THR F 434   N  THR F 443
SHEET    5  FF 5 LEU F 494  ASN F 495 -1  O  LEU F 494   N  LYS F 435
SHEET    1  FG 4 GLU F 525  THR F 531  0
SHEET    2  FG 4 PHE F 537  GLN F 543 -1  O  ALA F 538   N  ALA F 530
SHEET    3  FG 4 GLU F 550  PHE F 556 -1  O  GLU F 550   N  GLN F 543
SHEET    4  FG 4 VAL F 567  GLN F 570 -1  O  VAL F 567   N  TYR F 555
SHEET    1  FH 4 ALA F 579  TYR F 587  0
SHEET    2  FH 4 VAL F 590  GLY F 597 -1  O  VAL F 590   N  TYR F 587
SHEET    3  FH 4 SER F 606  SER F 610 -1  O  SER F 606   N  THR F 595
SHEET    4  FH 4 GLU F 618  ARG F 621 -1  O  GLU F 618   N  ARG F 609
CISPEP   1 GLN A  330    ASP A  331          0       -25.77
CISPEP   2 TYR A  382    PRO A  383          0         5.71
CISPEP   3 MET A  503    GLY A  504          0         7.70
CISPEP   4 ALA A  547    PRO A  548          0        -4.15
CISPEP   5 GLN B  330    ASP B  331          0       -23.04
CISPEP   6 TYR B  382    PRO B  383          0         2.55
CISPEP   7 ALA B  547    PRO B  548          0        -6.20
CISPEP   8 GLN C  330    ASP C  331          0       -23.60
CISPEP   9 TYR C  382    PRO C  383          0         5.98
CISPEP  10 MET C  503    GLY C  504          0       -11.08
CISPEP  11 ALA C  547    PRO C  548          0        -3.12
CISPEP  12 GLN D  330    ASP D  331          0       -23.61
CISPEP  13 TYR D  382    PRO D  383          0         8.47
CISPEP  14 MET D  503    GLY D  504          0         9.22
CISPEP  15 ALA D  547    PRO D  548          0        -7.20
CISPEP  16 GLN E  330    ASP E  331          0       -26.17
CISPEP  17 TYR E  382    PRO E  383          0         6.12
CISPEP  18 MET E  503    GLY E  504          0        21.22
CISPEP  19 ALA E  547    PRO E  548          0        -4.14
CISPEP  20 GLN F  330    ASP F  331          0       -24.64
CISPEP  21 TYR F  382    PRO F  383          0         8.40
CISPEP  22 MET F  503    GLY F  504          0         3.09
CISPEP  23 ALA F  547    PRO F  548          0        -3.31
SITE     1 AC1  6 PRO A 829  THR A 830  GLU B 818  GLY B 819
SITE     2 AC1  6 HOH B2478  HOH B2534
SITE     1 AC2  7 PRO B 829  THR B 830  HOH B2482  GLU C 818
SITE     2 AC2  7 GLY C 819  HOH C2456  HOH C2515
SITE     1 AC3  5 GLY A 819  HOH A2470  PRO C 829  THR C 830
SITE     2 AC3  5 HOH C2516
SITE     1 AC4  7 GLU D 818  GLY D 819  HOH D2468  HOH D2529
SITE     2 AC4  7 PRO E 829  THR E 830  HOH E2406
SITE     1 AC5  7 ALA D 805  GLU E 818  GLY E 819  HOH E2401
SITE     2 AC5  7 PRO F 829  THR F 830  HOH F2508
SITE     1 AC6  7 PRO D 829  THR D 830  HOH D2471  ALA E 805
SITE     2 AC6  7 GLU F 818  GLY F 819  HOH F2509
CRYST1   99.650  131.250  346.700  90.00  90.00  90.00 P 2 2 21     24
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      0.010035  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007619  0.000000        0.00000
SCALE3      0.000000  0.000000  0.002884        0.00000
MTRIX1   1 -0.499000 -0.449000 -0.741000      108.35400    1
MTRIX2   1  0.461000  0.586000 -0.666000       26.35600    1
MTRIX3   1  0.734000 -0.674000 -0.085000       43.79400    1
MTRIX1   2 -0.505000  0.460000  0.730000       10.29500    1
MTRIX2   2 -0.444000  0.587000 -0.677000       62.35500    1
MTRIX3   2 -0.740000 -0.666000 -0.092000      101.97300    1
MTRIX1   3 -1.000000  0.010000 -0.004000       24.21700    1
MTRIX2   3 -0.009000 -0.957000 -0.291000       21.69900    1
MTRIX3   3 -0.007000 -0.291000  0.957000        3.78700    1
MTRIX1   4  0.504000 -0.453000 -0.735000       14.10200    1
MTRIX2   4  0.648000 -0.365000  0.669000      -68.06600    1
MTRIX3   4 -0.571000 -0.813000  0.109000       82.80800    1
MTRIX1   5  0.499000  0.458000  0.736000      -83.98500    1
MTRIX2   5 -0.653000 -0.360000  0.666000      -16.94700    1
MTRIX3   5  0.570000 -0.813000  0.119000       37.30200    1
      
PROCHECK
Go to PROCHECK summary
 References