longtext: 2P8S-pdb

content
HEADER    HYDROLASE                               23-MAR-07   2P8S
TITLE     HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN COMPLEX WITH A
TITLE    2 CYCLOHEXALAMINE INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND   5 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,
COMPND   6 ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;
COMPND   7 EC: 3.4.14.5;
COMPND   8 ENGINEERED: YES;
COMPND   9 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 GENE: DPP4, ADCP2, CD26;
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: HI5;
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HI5;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PBLUEBAC4.5;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBLUEBAC4.5
KEYWDS    ALPHA/BETA, BETA-PROPELLER, DIMER, STRUCTURE-BASED DESIGN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.SCAPIN,T.BIFTU
REVDAT   2   20-NOV-07 2P8S    1       JRNL
REVDAT   1   22-MAY-07 2P8S    0
JRNL        AUTH   T.BIFTU,G.SCAPIN,S.SINGH,D.FENG,J.W.BECKER,
JRNL        AUTH 2 G.EIERMANN,H.HE,K.LYONS,S.PATEL,A.PETROV,
JRNL        AUTH 3 R.SINHA-ROY,B.ZHANG,J.WU,X.ZHANG,G.A.DOSS,
JRNL        AUTH 4 N.A.THORNBERRY,A.E.WEBER
JRNL        TITL   RATIONAL DESIGN OF A NOVEL, POTENT, AND ORALLY
JRNL        TITL 2 BIOAVAILABLE CYCLOHEXYLAMINE DPP-4 INHIBITOR BY
JRNL        TITL 3 APPLICATION OF MOLECULAR MODELING AND X-RAY
JRNL        TITL 4 CRYSTALLOGRAPHY OF SITAGLIPTIN
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17  3384 2007
JRNL        REFN   ASTM BMCLE8  UK ISSN 0960-894X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION. 2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNX
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  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
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)   (%) : 98.9
REMARK   3   NUMBER OF REFLECTIONS             : 103343
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) : 0.189
REMARK   3   R VALUE            (WORKING SET) : 0.186
REMARK   3   FREE R VALUE                     : 0.227
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5220
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 104509
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.90
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9372
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280
REMARK   3   BIN FREE R VALUE                    : 0.2870
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 542
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            : 11994
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 453
REMARK   3   SOLVENT ATOMS            : 995
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 31.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.40
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 7.28000
REMARK   3    B22 (A**2) : -3.62000
REMARK   3    B33 (A**2) : -3.66000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24
REMARK   3   ESD FROM SIGMAA              (A) : 0.19
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) : 0.29
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.43
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.57
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.980 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.600 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.580 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.360 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : MASK
REMARK   3   KSOL        : 0.34
REMARK   3   BSOL        : 28.80
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2P8S COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006
REMARK   4
REMARK   4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.
REMARK   4 REMEDIATED DATA FILE REVISION 3.100 (2007-05-18)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB042109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-2004
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 8.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 103521
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 7.040
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.49300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: 1X70
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 59.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM ACETATE, TRIS, PH
REMARK 280  8.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   1/2-X,-Y,1/2+Z
REMARK 290       3555   -X,1/2+Y,1/2-Z
REMARK 290       4555   1/2+X,1/2-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       59.06950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.67000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.08700
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.67000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.06950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.08700
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 APPLY THE FOLLOWING TO CHAINS: A, B, S
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI
REMARK 500   O    HOH      79     O    HOH     957              2.12
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    MET A 503   SD    MET A 503   CE     0.055
REMARK 500    MET A 689   SD    MET A 689   CE     0.057
REMARK 500    ILE A 719   CG1   ILE A 719   CD1    0.062
REMARK 500    PRO B 257   CB    PRO B 257   CG     0.058
REMARK 500    MET B 689   CG    MET B 689   SD     0.055
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASN A  80   N   -  CA  -  C   ANGL. DEV. = -8.9 DEGREES
REMARK 500    SER A 158   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES
REMARK 500    GLU A 206   N   -  CA  -  C   ANGL. DEV. = 10.3 DEGREES
REMARK 500    ILE A 236   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES
REMARK 500    PHE A 240   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES
REMARK 500    LEU A 300   N   -  CA  -  C   ANGL. DEV. =-13.7 DEGREES
REMARK 500    ILE A 319   N   -  CA  -  C   ANGL. DEV. =-15.8 DEGREES
REMARK 500    GLN A 320   N   -  CA  -  C   ANGL. DEV. = 11.0 DEGREES
REMARK 500    GLN A 388   N   -  CA  -  C   ANGL. DEV. =-13.1 DEGREES
REMARK 500    TRP A 402   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES
REMARK 500    LEU A 415   N   -  CA  -  C   ANGL. DEV. =-10.1 DEGREES
REMARK 500    SER A 458   N   -  CA  -  C   ANGL. DEV. =-12.3 DEGREES
REMARK 500    SER A 458   N   -  CA  -  C   ANGL. DEV. =-13.6 DEGREES
REMARK 500    ILE A 529   N   -  CA  -  C   ANGL. DEV. =-10.9 DEGREES
REMARK 500    TYR A 547   N   -  CA  -  C   ANGL. DEV. =-10.1 DEGREES
REMARK 500    ALA A 548   N   -  CA  -  C   ANGL. DEV. =  8.7 DEGREES
REMARK 500    VAL A 656   N   -  CA  -  C   ANGL. DEV. =-11.8 DEGREES
REMARK 500    VAL A 711   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES
REMARK 500    ASP B 200   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES
REMARK 500    GLU B 206   N   -  CA  -  C   ANGL. DEV. =  8.8 DEGREES
REMARK 500    ILE B 236   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES
REMARK 500    PHE B 240   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES
REMARK 500    LEU B 300   N   -  CA  -  C   ANGL. DEV. =-13.7 DEGREES
REMARK 500    ILE B 319   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES
REMARK 500    GLN B 320   N   -  CA  -  C   ANGL. DEV. = 11.9 DEGREES
REMARK 500    GLN B 388   N   -  CA  -  C   ANGL. DEV. =-14.4 DEGREES
REMARK 500    SER B 458   N   -  CA  -  C   ANGL. DEV. =-12.4 DEGREES
REMARK 500    ILE B 517   N   -  CA  -  C   ANGL. DEV. = -9.8 DEGREES
REMARK 500    ILE B 529   N   -  CA  -  C   ANGL. DEV. =-11.2 DEGREES
REMARK 500    TYR B 547   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES
REMARK 500    ALA B 548   N   -  CA  -  C   ANGL. DEV. =  9.7 DEGREES
REMARK 500    LEU B 561   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES
REMARK 500    GLY B 617   N   -  CA  -  C   ANGL. DEV. =  9.2 DEGREES
REMARK 500    VAL B 656   N   -  CA  -  C   ANGL. DEV. =-11.5 DEGREES
REMARK 500    VAL B 711   N   -  CA  -  C   ANGL. DEV. =-11.4 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X70   RELATED DB: PDB
REMARK 900 STRUCTURE OD DPP-IV IN COMPLEX WITH SITAGLIPTIN
DBREF  2P8S A   40   766  UNP    P27487   DPP4_HUMAN      40    766
DBREF  2P8S B   40   766  UNP    P27487   DPP4_HUMAN      40    766
SEQADV 2P8S THR A   39  UNP  P27487    SER    39 CLONING ARTIFACT
SEQADV 2P8S THR B   39  UNP  P27487    SER    39 CLONING ARTIFACT
SEQRES   1 A  728  THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES   2 A  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES   3 A  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES   4 A  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES   5 A  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES   6 A  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES   7 A  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES   8 A  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES   9 A  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES  10 A  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES  11 A  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES  12 A  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES  13 A  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES  14 A  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES  15 A  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES  16 A  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES  17 A  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES  18 A  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES  19 A  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES  20 A  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES  21 A  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES  22 A  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES  23 A  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES  24 A  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES  25 A  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES  26 A  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES  27 A  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES  28 A  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES  29 A  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES  30 A  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES  31 A  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES  32 A  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES  33 A  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES  34 A  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES  35 A  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES  36 A  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES  37 A  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES  38 A  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES  39 A  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES  40 A  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES  41 A  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES  42 A  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES  43 A  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES  44 A  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES  45 A  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES  46 A  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES  47 A  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES  48 A  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES  49 A  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES  50 A  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES  51 A  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES  52 A  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES  53 A  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES  54 A  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES  55 A  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES  56 A  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES   1 B  728  THR ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES   2 B  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES   3 B  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES   4 B  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES   5 B  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES   6 B  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES   7 B  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES   8 B  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES   9 B  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES  10 B  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES  11 B  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES  12 B  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES  13 B  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES  14 B  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES  15 B  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES  16 B  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES  17 B  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES  18 B  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES  19 B  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES  20 B  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES  21 B  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES  22 B  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES  23 B  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES  24 B  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES  25 B  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES  26 B  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES  27 B  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES  28 B  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES  29 B  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES  30 B  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES  31 B  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES  32 B  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES  33 B  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES  34 B  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES  35 B  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES  36 B  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES  37 B  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES  38 B  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES  39 B  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES  40 B  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES  41 B  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES  42 B  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES  43 B  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES  44 B  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES  45 B  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES  46 B  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES  47 B  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES  48 B  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES  49 B  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES  50 B  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES  51 B  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES  52 B  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES  53 B  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES  54 B  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES  55 B  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES  56 B  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
MODRES 2P8S ASN A   85  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A   92  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A  150  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A  219  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A  229  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A  281  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A  321  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN A  520  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B   85  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B   92  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B  150  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B  219  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B  229  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B  281  ASN  GLYCOSYLATION SITE
MODRES 2P8S ASN B  321  ASN  GLYCOSYLATION SITE
HET    NAG  S1085      14
HET    NAG  S1086      14
HET    NAG  S1092      14
HET    NAG  S1150      14
HET    NAG  S1151      14
HET    NAG  S1219      14
HET    NAG  S1220      14
HET    NAG  S1229      14
HET    NAG  S1230      14
HET    NAG  S1281      14
HET    NAG  S1321      14
HET    NAG  S1322      14
HET    NAG  S1520      14
HET    NAG  S2085      14
HET    NAG  S2086      14
HET    NAG  S2092      14
HET    NAG  S2150      14
HET    NAG  S2219      14
HET    NAG  S2220      14
HET    NAG  S2229      14
HET    NAG  S2230      14
HET    NAG  S2281      14
HET    NAG  S2282      14
HET    NAG  S2321      14
HET     NA   9001       1
HET    417   1001      58
HET    417   1002      58
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM      NA SODIUM ION
HETNAM     417 (1S,2R,5S)-5-[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,
HETNAM   2 417  4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]-2-(2,4,5-
HETNAM   3 417  TRIFLUOROPHENYL)CYCLOHEXANAMINE
HETSYN     NAG NAG
FORMUL   3  NAG    24(C8 H15 N O6)
FORMUL  18   NA    NA 1+
FORMUL  19  417    2(C18 H19 F6 N5)
FORMUL  21  HOH   *995(H2 O)
HELIX    1   1 THR A   44  ASN A   51  1                                   8
HELIX    2   2 ASN A   92  ASP A   96  5                                   5
HELIX    3   3 ASP A  200  VAL A  207  1                                   8
HELIX    4   4 ASP A  274  LEU A  276  5                                   3
HELIX    5   5 PRO A  290  ILE A  295  1                                   6
HELIX    6   6 VAL A  341  GLN A  344  5                                   4
HELIX    7   7 GLU A  421  MET A  425  5                                   5
HELIX    8   8 ASN A  497  GLN A  505  1                                   9
HELIX    9   9 ASN A  562  THR A  570  1                                   9
HELIX   10  10 GLY A  587  HIS A  592  1                                   6
HELIX   11  11 ALA A  593  ASN A  595  5                                   3
HELIX   12  12 THR A  600  SER A  614  1                                  15
HELIX   13  13 SER A  630  GLY A  641  1                                  12
HELIX   14  14 ARG A  658  TYR A  662  5                                   5
HELIX   15  15 ASP A  663  GLY A  672  1                                  10
HELIX   16  16 ASN A  679  SER A  686  1                                   8
HELIX   17  17 VAL A  688  VAL A  698  5                                  11
HELIX   18  18 HIS A  712  VAL A  726  1                                  15
HELIX   19  19 SER A  744  SER A  764  1                                  21
HELIX   20  20 THR B   44  ASN B   51  1                                   8
HELIX   21  21 ASP B  200  VAL B  207  1                                   8
HELIX   22  22 ASP B  274  LEU B  276  5                                   3
HELIX   23  23 PRO B  290  ILE B  295  1                                   6
HELIX   24  24 VAL B  341  GLN B  344  5                                   4
HELIX   25  25 GLU B  421  MET B  425  5                                   5
HELIX   26  26 ASN B  497  LEU B  504  1                                   8
HELIX   27  27 ASN B  562  THR B  570  1                                   9
HELIX   28  28 GLY B  587  HIS B  592  1                                   6
HELIX   29  29 ALA B  593  ASN B  595  5                                   3
HELIX   30  30 THR B  600  MET B  616  1                                  17
HELIX   31  31 SER B  630  GLY B  641  1                                  12
HELIX   32  32 ARG B  658  TYR B  662  5                                   5
HELIX   33  33 ASP B  663  GLY B  672  1                                  10
HELIX   34  34 ASN B  679  SER B  686  1                                   8
HELIX   35  35 VAL B  688  VAL B  698  5                                  11
HELIX   36  36 HIS B  712  VAL B  726  1                                  15
HELIX   37  37 SER B  744  PHE B  763  1                                  20
SHEET    1   A 2 LYS A  41  THR A  42  0
SHEET    2   A 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41
SHEET    1   B 4 ARG A  61  TRP A  62  0
SHEET    2   B 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61
SHEET    3   B 4 ASN A  75  ASN A  80 -1  O  ASN A  75   N  GLN A  72
SHEET    4   B 4 SER A  86  LEU A  90 -1  O  PHE A  89   N  ILE A  76
SHEET    1   C 4 ILE A 102  ILE A 107  0
SHEET    2   C 4 PHE A 113  LYS A 122 -1  O  GLU A 117   N  ASN A 103
SHEET    3   C 4 TYR A 128  ASP A 136 -1  O  ASP A 133   N  LEU A 116
SHEET    4   C 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136
SHEET    1   D 4 TRP A 154  TRP A 157  0
SHEET    2   D 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154
SHEET    3   D 4 ASP A 171  LYS A 175 -1  O  TYR A 173   N  TYR A 166
SHEET    4   D 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174
SHEET    1   E 3 ILE A 194  ASN A 196  0
SHEET    2   E 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195
SHEET    3   E 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224
SHEET    1   F 4 ILE A 194  ASN A 196  0
SHEET    2   F 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195
SHEET    3   F 4 THR A 265  ASN A 272 -1  O  PHE A 269   N  TYR A 225
SHEET    4   F 4 ILE A 285  GLN A 286 -1  O  ILE A 285   N  VAL A 270
SHEET    1   G 2 LEU A 235  PHE A 240  0
SHEET    2   G 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240
SHEET    1   H 4 HIS A 298  THR A 307  0
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299
SHEET    3   H 4 TYR A 322  ASP A 331 -1  O  CYS A 328   N  ILE A 311
SHEET    4   H 4 ARG A 336  CYS A 339 -1  O  ARG A 336   N  ASP A 331
SHEET    1   I 4 HIS A 298  THR A 307  0
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299
SHEET    3   I 4 TYR A 322  ASP A 331 -1  O  CYS A 328   N  ILE A 311
SHEET    4   I 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323
SHEET    1   J 4 HIS A 363  PHE A 364  0
SHEET    2   J 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363
SHEET    3   J 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371
SHEET    4   J 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386
SHEET    1   K 4 VAL A 404  LEU A 410  0
SHEET    2   K 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409
SHEET    3   K 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417
SHEET    4   K 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433
SHEET    1   L 4 TYR A 457  PHE A 461  0
SHEET    2   L 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460
SHEET    3   L 4 LEU A 479  SER A 484 -1  N  LEU A 479   O  CYS A 472
SHEET    4   L 4 LYS A 489  GLU A 495 -1  O  GLU A 495   N  TYR A 480
SHEET    1   M 8 SER A 511  LEU A 519  0
SHEET    2   M 8 THR A 522  LEU A 530 -1  O  THR A 522   N  LEU A 519
SHEET    3   M 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529
SHEET    4   M 8 TYR A 540  VAL A 546  1  N  ASP A 545   O  ALA A 576
SHEET    5   M 8 VAL A 619  TRP A 629  1  O  TRP A 627   N  VAL A 546
SHEET    6   M 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628
SHEET    7   M 8 GLU A 699  GLY A 705  1  O  LEU A 701   N  ALA A 652
SHEET    8   M 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700
SHEET    1   N 2 LYS B  41  THR B  42  0
SHEET    2   N 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41
SHEET    1   O 4 ARG B  61  TRP B  62  0
SHEET    2   O 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61
SHEET    3   O 4 ASN B  75  ASN B  80 -1  O  ASN B  75   N  GLN B  72
SHEET    4   O 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78
SHEET    1   P 4 ASP B 104  ILE B 107  0
SHEET    2   P 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106
SHEET    3   P 4 TYR B 128  ASP B 136 -1  O  THR B 129   N  VAL B 121
SHEET    4   P 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136
SHEET    1   Q 4 THR B 152  TRP B 157  0
SHEET    2   Q 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154
SHEET    3   Q 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164
SHEET    4   Q 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174
SHEET    1   R 3 ILE B 194  ASN B 196  0
SHEET    2   R 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195
SHEET    3   R 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224
SHEET    1   S 4 ILE B 194  ASN B 196  0
SHEET    2   S 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195
SHEET    3   S 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225
SHEET    4   S 4 ILE B 285  GLN B 286 -1  O  ILE B 285   N  VAL B 270
SHEET    1   T 2 LEU B 235  PHE B 240  0
SHEET    2   T 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238
SHEET    1   U 4 HIS B 298  THR B 307  0
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306
SHEET    3   U 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311
SHEET    4   U 4 ARG B 336  CYS B 339 -1  O  ARG B 336   N  ASP B 331
SHEET    1   V 4 HIS B 298  THR B 307  0
SHEET    2   V 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306
SHEET    3   V 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311
SHEET    4   V 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325
SHEET    1   W 4 HIS B 363  PHE B 364  0
SHEET    2   W 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363
SHEET    3   W 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371
SHEET    4   W 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386
SHEET    1   X 4 VAL B 404  LEU B 410  0
SHEET    2   X 4 TYR B 414  SER B 419 -1  O  ILE B 418   N  ILE B 405
SHEET    3   X 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417
SHEET    4   X 4 VAL B 442  CYS B 444 -1  O  THR B 443   N  LYS B 433
SHEET    1   Y 4 TYR B 457  PHE B 461  0
SHEET    2   Y 4 TYR B 467  CYS B 472 -1  O  ARG B 471   N  SER B 458
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470
SHEET    4   Y 4 LYS B 489  GLU B 495 -1  O  LEU B 491   N  LEU B 482
SHEET    1   Z 8 SER B 511  LEU B 519  0
SHEET    2   Z 8 THR B 522  LEU B 530 -1  O  LEU B 530   N  SER B 511
SHEET    3   Z 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529
SHEET    4   Z 8 TYR B 540  VAL B 546  1  N  ASP B 545   O  ALA B 576
SHEET    5   Z 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 542
SHEET    6   Z 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628
SHEET    7   Z 8 GLU B 699  GLY B 705  1  O  GLU B 699   N  GLY B 650
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700
SSBOND   1 CYS A  328    CYS A  339
SSBOND   2 CYS A  385    CYS A  394
SSBOND   3 CYS A  444    CYS A  447
SSBOND   4 CYS A  454    CYS A  472
SSBOND   5 CYS A  649    CYS A  762
SSBOND   6 CYS B  328    CYS B  339
SSBOND   7 CYS B  385    CYS B  394
SSBOND   8 CYS B  444    CYS B  447
SSBOND   9 CYS B  454    CYS B  472
SSBOND  10 CYS B  649    CYS B  762
LINK         ND2 ASN A  85                 C1  NAG S1085
LINK         ND2 ASN A  92                 C1  NAG S1092
LINK         ND2 ASN A 150                 C1  NAG S1150
LINK         ND2 ASN A 219                 C1  NAG S1219
LINK         ND2 ASN A 229                 C1  NAG S1229
LINK         ND2 ASN A 281                 C1  NAG S1281
LINK         ND2 ASN A 321                 C1  NAG S1321
LINK         ND2 ASN A 520                 C1  NAG S1520
LINK         ND2 ASN B  85                 C1  NAG S2085
LINK         ND2 ASN B  92                 C1  NAG S2092
LINK         ND2 ASN B 150                 C1  NAG S2150
LINK         ND2 ASN B 219                 C1  NAG S2219
LINK         ND2 ASN B 229                 C1  NAG S2229
LINK         ND2 ASN B 281                 C1  NAG S2281
LINK         ND2 ASN B 321                 C1  NAG S2321
LINK         O4  NAG S1085                 C1  NAG S1086
LINK         O4  NAG S1150                 C1  NAG S1151
LINK         O4  NAG S1219                 C1  NAG S1220
LINK         O4  NAG S1229                 C1  NAG S1230
LINK         O4  NAG S1321                 C1  NAG S1322
LINK         O4  NAG S2085                 C1  NAG S2086
LINK         O4  NAG S2219                 C1  NAG S2220
LINK         O4  NAG S2229                 C1  NAG S2230
LINK         O4  NAG S2281                 C1  NAG S2282
CISPEP   1 GLY A  474    PRO A  475          0         0.50
CISPEP   2 GLY B  474    PRO B  475          0         5.40
CRYST1  118.139  126.174  137.340  90.00  90.00  90.00 P 21 21 21    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      0.008465  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007926  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007281        0.00000
TER    6001      PRO A 766
TER   11996      PRO B 766
MASTER      302    0   27   37  102    0    0    613442    2  487  112
END