longtext: 2ECF-pdb

content
HEADER    HYDROLASE                               13-FEB-07   2ECF
TITLE     CRYSTAL STRUCTURE OF DIPEPTIDYL AMINOPEPTIDASE IV FROM
TITLE    2 STENOTROPHOMONAS MALTOPHILIA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE IV;
COMPND   5 EC: 3.4.14.5;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STENOTROPHOMONAS MALTOPHILIA;
SOURCE   3 ORGANISM_COMMON: PSEUDOMONAS MALTOPHILIA;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS    PROLYL OLIGOPEPTIDASE FAMILY, PEPTIDASE FAMILY S9,
KEYWDS   2 DIPEPTIDYL PEPTIDASE IV, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.NAKAJIMA,K.ITO,T.YOSHIMOTO
REVDAT   1   26-FEB-08 2ECF    0
JRNL        AUTH   Y.NAKAJIMA,T.TOSHIMA,K.ITO,T.EGAWA,K.KYONO,
JRNL        AUTH 2 F.MATSUBARA,H.OYAMA,T.YOSHIMOTO
JRNL        TITL   CRYSTAL STRUCTURE OF DIPEPTIDYL AMINOPEPTIDASE IV
JRNL        TITL 2 FROM STENOTROPHOMONAS MALTOPHILIA EXHIBITED AN
JRNL        TITL 3 ACTIVITY AGAINST SUBSTRATE CONTAING
JRNL        TITL 4 4-HYDROXYPROLINE RESIDUE
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 2.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9
REMARK   3   NUMBER OF REFLECTIONS             : 23264
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.185
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1197
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.90
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710
REMARK   3   BIN FREE R VALUE                    : 0.3370
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 120
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5445
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 66
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 56.80
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31
REMARK   3   ESD FROM SIGMAA              (A) : 0.37
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : 1.31
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.60
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2ECF COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB026495.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-2003; 03-JUL-2003; 03-
REMARK 200                                   JUL-2003
REMARK 200  TEMPERATURE           (KELVIN) : 298; 298; 298
REMARK 200  PH                             : 8.00
REMARK 200  NUMBER OF CRYSTALS USED        : 3
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N; N; N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE; ROTATING
REMARK 200                                   ANODE; ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200; RIGAKU RU200;
REMARK 200                                   RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418; 1.5418; 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE; OSMIC MIRROR;
REMARK 200                                   GRAPHITE
REMARK 200  OPTICS                         : MONOCHROMETOR; OSMIC MIRROR;
REMARK 200                                   MONOCHROMETOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE;
REMARK 200                                   IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV; RIGAKU RAXIS
REMARK 200                                   IV; RIGAKU RAXIS IV
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23396
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 7.700
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07700
REMARK 200   FOR THE DATA SET  : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.33300
REMARK 200   FOR SHELL         : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH;
REMARK 200                       SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.2M MAGNESIUM
REMARK 280  CHLORIDE, 0.1M TRIS-HCL, PH 8.0, VAPOR DIFFUSION, TEMPERATURE
REMARK 280  293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,1/2+Z
REMARK 290       3555   1/2-Y,1/2+X,3/4+Z
REMARK 290       4555   1/2+Y,1/2-X,1/4+Z
REMARK 290       5555   1/2-X,1/2+Y,3/4-Z
REMARK 290       6555   1/2+X,1/2-Y,1/4-Z
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,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       80.94750
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       52.93850
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       52.93850
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      121.42125
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       52.93850
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       52.93850
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       40.47375
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       52.93850
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.93850
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      121.42125
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       52.93850
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.93850
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       40.47375
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       80.94750
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: DIMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      105.87700
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      105.87700
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      242.84250
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C  SSEQI
REMARK 465     MET A     1
REMARK 465     ARG A     2
REMARK 465     HIS A     3
REMARK 465     LEU A     4
REMARK 465     PHE A     5
REMARK 465     ALA A     6
REMARK 465     SER A     7
REMARK 465     LEU A     8
REMARK 465     ALA A     9
REMARK 465     PHE A    10
REMARK 465     MET A    11
REMARK 465     LEU A    12
REMARK 465     ALA A    13
REMARK 465     THR A    14
REMARK 465     SER A    15
REMARK 465     THR A    16
REMARK 465     VAL A    17
REMARK 465     ALA A    18
REMARK 465     HIS A    19
REMARK 465     ALA A    20
REMARK 465     GLU A    21
REMARK 465     PRO A    87
REMARK 465     GLY A    88
REMARK 465     THR A    89
REMARK 465     GLU A    90
REMARK 465     THR A    91
REMARK 465     LEU A    92
REMARK 465     SER A    93
REMARK 465     ASP A    94
REMARK 465     GLU A    95
REMARK 465     GLU A    96
REMARK 465     LYS A    97
REMARK 465     ALA A    98
REMARK 465     ARG A    99
REMARK 465     ARG A   100
REMARK 465     GLU A   101
REMARK 465     ARG A   102
REMARK 465     GLN A   103
REMARK 465     ARG A   104
REMARK 465     ILE A   105
REMARK 465     ALA A   106
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  61    CG    CD    NE    CZ    NH1   NH2
REMARK 470     LYS A 137    CG    CD    CE    NZ
REMARK 470     GLN A 138    CG    CD    OE1   NE2
REMARK 470     GLU A 139    CG    CD    OE1   OE2
REMARK 470     LYS A 141    CG    CD    CE    NZ
REMARK 470     LYS A 368    CG    CD    CE    NZ
REMARK 470     LYS A 370    CG    CD    CE    NZ
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    PRO A  37      176.86    -59.97
REMARK 500    THR A  38     -172.86   -171.89
REMARK 500    ILE A 111       90.37    -67.66
REMARK 500    GLN A 115      146.01   -170.54
REMARK 500    ALA A 120       27.58     43.77
REMARK 500    LYS A 137      -78.64    -43.61
REMARK 500    ASP A 190       21.88    -73.32
REMARK 500    ASP A 220        0.33     94.94
REMARK 500    PRO A 270       49.57    -78.32
REMARK 500    PRO A 297       -2.48    -52.66
REMARK 500    THR A 334      -88.21   -111.79
REMARK 500    SER A 367       -5.93    -56.87
REMARK 500    LYS A 368      -72.04   -102.78
REMARK 500    ASN A 378       46.52    -94.27
REMARK 500    ALA A 386      177.29    177.79
REMARK 500    SER A 406      108.81   -160.88
REMARK 500    ALA A 436       11.76     86.12
REMARK 500    SER A 444      163.33    179.15
REMARK 500    ASN A 446       -9.42    -53.89
REMARK 500    ALA A 463     -176.40   -175.88
REMARK 500    PRO A 476       -8.52    -44.55
REMARK 500    LYS A 498      -29.77   -155.92
REMARK 500    TYR A 524      -66.75   -127.63
REMARK 500    LYS A 577       63.72   -153.30
REMARK 500    THR A 580      -81.23   -128.77
REMARK 500    SER A 610     -115.45     57.02
REMARK 500    ALA A 623       53.89   -159.35
REMARK 500    ALA A 634       62.11     30.08
REMARK 500    ASP A 652      179.38     66.85
REMARK 500    ASN A 657       54.62   -148.05
REMARK 500    MET A 710      106.10   -172.49
REMARK 500    LYS A 716     -145.87   -100.85
REMARK 500    LYS A 740       81.14     53.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2ECF A    1   741  UNP    P95782   P95782_XANMA     1    741
SEQRES   1 A  741  MET ARG HIS LEU PHE ALA SER LEU ALA PHE MET LEU ALA
SEQRES   2 A  741  THR SER THR VAL ALA HIS ALA GLU LYS LEU THR LEU GLU
SEQRES   3 A  741  ALA ILE THR GLY PRO LEU PRO LEU SER GLY PRO THR LEU
SEQRES   4 A  741  MET LYS PRO LYS VAL ALA PRO ASP GLY SER ARG VAL THR
SEQRES   5 A  741  PHE LEU ARG GLY LYS ASP SER ASP ARG ASN GLN LEU ASP
SEQRES   6 A  741  LEU TRP SER TYR ASP ILE GLY SER GLY GLN THR ARG LEU
SEQRES   7 A  741  LEU VAL ASP SER LYS VAL VAL LEU PRO GLY THR GLU THR
SEQRES   8 A  741  LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG GLN ARG
SEQRES   9 A  741  ILE ALA ALA MET THR GLY ILE VAL ASP TYR GLN TRP SER
SEQRES  10 A  741  PRO ASP ALA GLN ARG LEU LEU PHE PRO LEU GLY GLY GLU
SEQRES  11 A  741  LEU TYR LEU TYR ASP LEU LYS GLN GLU GLY LYS ALA ALA
SEQRES  12 A  741  VAL ARG GLN LEU THR HIS GLY GLU GLY PHE ALA THR ASP
SEQRES  13 A  741  ALA LYS LEU SER PRO LYS GLY GLY PHE VAL SER PHE ILE
SEQRES  14 A  741  ARG GLY ARG ASN LEU TRP VAL ILE ASP LEU ALA SER GLY
SEQRES  15 A  741  ARG GLN MET GLN LEU THR ALA ASP GLY SER THR THR ILE
SEQRES  16 A  741  GLY ASN GLY ILE ALA GLU PHE VAL ALA ASP GLU GLU MET
SEQRES  17 A  741  ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP ASP SER
SEQRES  18 A  741  ALA ILE ALA TYR ALA ARG ILE ASP GLU SER PRO VAL PRO
SEQRES  19 A  741  VAL GLN LYS ARG TYR GLU VAL TYR ALA ASP ARG THR ASP
SEQRES  20 A  741  VAL ILE GLU GLN ARG TYR PRO ALA ALA GLY ASP ALA ASN
SEQRES  21 A  741  VAL GLN VAL LYS LEU GLY VAL ILE SER PRO ALA GLU GLN
SEQRES  22 A  741  ALA GLN THR GLN TRP ILE ASP LEU GLY LYS GLU GLN ASP
SEQRES  23 A  741  ILE TYR LEU ALA ARG VAL ASN TRP ARG ASP PRO GLN HIS
SEQRES  24 A  741  LEU SER PHE GLN ARG GLN SER ARG ASP GLN LYS LYS LEU
SEQRES  25 A  741  ASP LEU VAL GLU VAL THR LEU ALA SER ASN GLN GLN ARG
SEQRES  26 A  741  VAL LEU ALA HIS GLU THR SER PRO THR TRP VAL PRO LEU
SEQRES  27 A  741  HIS ASN SER LEU ARG PHE LEU ASP ASP GLY SER ILE LEU
SEQRES  28 A  741  TRP SER SER GLU ARG THR GLY PHE GLN HIS LEU TYR ARG
SEQRES  29 A  741  ILE ASP SER LYS GLY LYS ALA ALA ALA LEU THR HIS GLY
SEQRES  30 A  741  ASN TRP SER VAL ASP GLU LEU LEU ALA VAL ASP GLU LYS
SEQRES  31 A  741  ALA GLY LEU ALA TYR PHE ARG ALA GLY ILE GLU SER ALA
SEQRES  32 A  741  ARG GLU SER GLN ILE TYR ALA VAL PRO LEU GLN GLY GLY
SEQRES  33 A  741  GLN PRO GLN ARG LEU SER LYS ALA PRO GLY MET HIS SER
SEQRES  34 A  741  ALA SER PHE ALA ARG ASN ALA SER VAL TYR VAL ASP SER
SEQRES  35 A  741  TRP SER ASN ASN SER THR PRO PRO GLN ILE GLU LEU PHE
SEQRES  36 A  741  ARG ALA ASN GLY GLU LYS ILE ALA THR LEU VAL GLU ASN
SEQRES  37 A  741  ASP LEU ALA ASP PRO LYS HIS PRO TYR ALA ARG TYR ARG
SEQRES  38 A  741  GLU ALA GLN ARG PRO VAL GLU PHE GLY THR LEU THR ALA
SEQRES  39 A  741  ALA ASP GLY LYS THR PRO LEU ASN TYR SER VAL ILE LYS
SEQRES  40 A  741  PRO ALA GLY PHE ASP PRO ALA LYS ARG TYR PRO VAL ALA
SEQRES  41 A  741  VAL TYR VAL TYR GLY GLY PRO ALA SER GLN THR VAL THR
SEQRES  42 A  741  ASP SER TRP PRO GLY ARG GLY ASP HIS LEU PHE ASN GLN
SEQRES  43 A  741  TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE SER LEU ASP
SEQRES  44 A  741  ASN ARG GLY THR PRO ARG ARG GLY ARG ASP PHE GLY GLY
SEQRES  45 A  741  ALA LEU TYR GLY LYS GLN GLY THR VAL GLU VAL ALA ASP
SEQRES  46 A  741  GLN LEU ARG GLY VAL ALA TRP LEU LYS GLN GLN PRO TRP
SEQRES  47 A  741  VAL ASP PRO ALA ARG ILE GLY VAL GLN GLY TRP SER ASN
SEQRES  48 A  741  GLY GLY TYR MET THR LEU MET LEU LEU ALA LYS ALA SER
SEQRES  49 A  741  ASP SER TYR ALA CYS GLY VAL ALA GLY ALA PRO VAL THR
SEQRES  50 A  741  ASP TRP GLY LEU TYR ASP SER HIS TYR THR GLU ARG TYR
SEQRES  51 A  741  MET ASP LEU PRO ALA ARG ASN ASP ALA GLY TYR ARG GLU
SEQRES  52 A  741  ALA ARG VAL LEU THR HIS ILE GLU GLY LEU ARG SER PRO
SEQRES  53 A  741  LEU LEU LEU ILE HIS GLY MET ALA ASP ASP ASN VAL LEU
SEQRES  54 A  741  PHE THR ASN SER THR SER LEU MET SER ALA LEU GLN LYS
SEQRES  55 A  741  ARG GLY GLN PRO PHE GLU LEU MET THR TYR PRO GLY ALA
SEQRES  56 A  741  LYS HIS GLY LEU SER GLY ALA ASP ALA LEU HIS ARG TYR
SEQRES  57 A  741  ARG VAL ALA GLU ALA PHE LEU GLY ARG CYS LEU LYS PRO
FORMUL   2  HOH   *66(H2 O)
HELIX    1   1 THR A   24  THR A   29  1                                   6
HELIX    2   2 ASP A   81  VAL A   85  5                                   5
HELIX    3   3 GLU A  201  MET A  208  1                                   8
HELIX    4   4 TYR A  477  GLU A  482  1                                   6
HELIX    5   5 ARG A  539  GLN A  551  1                                  13
HELIX    6   6 GLY A  567  ALA A  573  1                                   7
HELIX    7   7 THR A  580  GLN A  595  1                                  16
HELIX    8   8 SER A  610  ALA A  623  1                                  14
HELIX    9   9 ASP A  638  TYR A  642  5                                   5
HELIX   10  10 ASP A  643  ASP A  652  1                                  10
HELIX   11  11 PRO A  654  ARG A  656  5                                   3
HELIX   12  12 ASN A  657  ARG A  665  1                                   9
HELIX   13  13 VAL A  666  LEU A  673  5                                   8
HELIX   14  14 PHE A  690  ARG A  703  1                                  14
HELIX   15  15 SER A  720  LYS A  740  1                                  21
SHEET    1   A 4 MET A  40  VAL A  44  0
SHEET    2   A 4 ARG A  50  ARG A  55 -1  O  LEU A  54   N  MET A  40
SHEET    3   A 4 GLN A  63  ASP A  70 -1  O  ASP A  65   N  ARG A  55
SHEET    4   A 4 THR A  76  VAL A  80 -1  O  VAL A  80   N  LEU A  66
SHEET    1   B 4 MET A  40  VAL A  44  0
SHEET    2   B 4 ARG A  50  ARG A  55 -1  O  LEU A  54   N  MET A  40
SHEET    3   B 4 GLN A  63  ASP A  70 -1  O  ASP A  65   N  ARG A  55
SHEET    4   B 4 THR A 109  GLY A 110  1  O  THR A 109   N  LEU A  64
SHEET    1   C 3 GLN A 115  TRP A 116  0
SHEET    2   C 3 ARG A 122  LEU A 127 -1  O  LEU A 124   N  GLN A 115
SHEET    3   C 3 GLU A 130  ASP A 135 -1  O  TYR A 132   N  PHE A 125
SHEET    1   D 4 ALA A 154  LEU A 159  0
SHEET    2   D 4 PHE A 165  ARG A 170 -1  O  ILE A 169   N  THR A 155
SHEET    3   D 4 ASN A 173  ASP A 178 -1  O  TRP A 175   N  PHE A 168
SHEET    4   D 4 ARG A 183  GLN A 186 -1  O  MET A 185   N  VAL A 176
SHEET    1   E 3 ILE A 195  ASN A 197  0
SHEET    2   E 3 ILE A 223  ASP A 229 -1  O  ILE A 228   N  GLY A 196
SHEET    3   E 3 TYR A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224
SHEET    1   F 4 ILE A 195  ASN A 197  0
SHEET    2   F 4 ILE A 223  ASP A 229 -1  O  ILE A 228   N  GLY A 196
SHEET    3   F 4 GLN A 262  ILE A 268 -1  O  GLY A 266   N  TYR A 225
SHEET    4   F 4 GLN A 277  ILE A 279 -1  O  ILE A 279   N  LEU A 265
SHEET    1   G 2 VAL A 235  VAL A 241  0
SHEET    2   G 2 THR A 246  ARG A 252 -1  O  ILE A 249   N  ARG A 238
SHEET    1   H 4 ILE A 287  ASP A 296  0
SHEET    2   H 4 HIS A 299  SER A 306 -1  O  SER A 301   N  ASN A 293
SHEET    3   H 4 LYS A 311  THR A 318 -1  O  ASP A 313   N  ARG A 304
SHEET    4   H 4 GLN A 324  THR A 331 -1  O  ARG A 325   N  GLU A 316
SHEET    1   I 4 ARG A 343  PHE A 344  0
SHEET    2   I 4 ILE A 350  SER A 354 -1  O  LEU A 351   N  ARG A 343
SHEET    3   I 4 HIS A 361  ILE A 365 -1  O  TYR A 363   N  TRP A 352
SHEET    4   I 4 ALA A 371  ALA A 373 -1  O  ALA A 372   N  ARG A 364
SHEET    1   J 4 VAL A 381  ASP A 388  0
SHEET    2   J 4 LEU A 393  ALA A 398 -1  O  ARG A 397   N  GLU A 383
SHEET    3   J 4 GLN A 407  PRO A 412 -1  O  GLN A 407   N  ALA A 398
SHEET    4   J 4 GLN A 419  ARG A 420 -1  O  GLN A 419   N  ALA A 410
SHEET    1   K 4 MET A 427  PHE A 432  0
SHEET    2   K 4 VAL A 438  ASN A 445 -1  O  SER A 442   N  SER A 429
SHEET    3   K 4 THR A 448  ARG A 456 -1  O  GLU A 453   N  ASP A 441
SHEET    4   K 4 LYS A 461  ALA A 463 -1  O  ILE A 462   N  LEU A 454
SHEET    1   L 8 VAL A 487  THR A 493  0
SHEET    2   L 8 PRO A 500  ILE A 506 -1  O  LEU A 501   N  LEU A 492
SHEET    3   L 8 VAL A 554  LEU A 558 -1  O  SER A 557   N  SER A 504
SHEET    4   L 8 TYR A 517  TYR A 522  1  N  ALA A 520   O  VAL A 554
SHEET    5   L 8 VAL A 599  TRP A 609  1  O  GLY A 605   N  VAL A 519
SHEET    6   L 8 CYS A 629  GLY A 633  1  O  GLY A 633   N  GLY A 608
SHEET    7   L 8 LEU A 677  GLY A 682  1  O  ILE A 680   N  ALA A 632
SHEET    8   L 8 GLU A 708  TYR A 712  1  O  GLU A 708   N  LEU A 679
SSBOND   1 CYS A  629    CYS A  738                        1555   1555    2.02
CRYST1  105.877  105.877  161.895  90.00  90.00  90.00 P 43 21 2     8
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      0.009445  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009445  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006177        0.00000
TER    5446      PRO A 741
MASTER      348    0    0   15   48    0    0    6 5511    1    2   57
END