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Database: PDB
Entry: 4GDY
LinkDB: 4GDY
Original site: 4GDY 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-AUG-12   4GDY              
TITLE     KYNURENINE AMINOTRANSFERASE II INHIBITORS                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: KAT/AADAT, 2-AMINOADIPATE AMINOTRANSFERASE, 2-AMINOADIPATE  
COMPND   6 TRANSAMINASE, ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT, KYNURENINE 
COMPND   7 AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE AMINOTRANSFERASE II,   
COMPND   8 KYNURENINE--OXOGLUTARATE TRANSAMINASE 2, KYNURENINE--OXOGLUTARATE    
COMPND   9 TRANSAMINASE II;                                                     
COMPND  10 EC: 2.6.1.39, 2.6.1.7;                                               
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AADAT, KAT2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    AMINOTRANSFERASE, PYRIDOXAL PHOSPHATE CO-FACTOR, TRANSFERASE-         
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT                                                              
REVDAT   1   29-AUG-12 4GDY    0                                                
JRNL        AUTH   P.R.VERHOEST,J.L.HENDERSON,A.SAWANT-BASAK,J.B.TUTTLE,        
JRNL        AUTH 2 A.B.DOUNAY,L.A.MCALLISTER,J.PANDIT,S.RONG,X.HOU,B.BECHLE,    
JRNL        AUTH 3 V.PARIKH,E.EVRARD,S.GHOSH,M.A.SALAFIA,B.RAGO,R.OBACH,        
JRNL        AUTH 4 K.R.FONSECA,C.CHANG                                          
JRNL        TITL   DISCOVERY OF HYDROXAMATE BIOISOSTERES AS KATII INHIBITORS    
JRNL        TITL 2 WITH IMPROVED ORAL BIOAVAILABILITY AND PHARMACOKINETICS      
JRNL        REF    MEDCHEMCOMM                                2012              
JRNL        REFN                   ESSN 2040-2511                               
JRNL        DOI    10.1039/C2MD20166F                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.3                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.85                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 20510                          
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)  : 0.174                          
REMARK   3   R VALUE            (WORKING SET)  : 0.171                          
REMARK   3   FREE R VALUE                      : 0.240                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.110                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1049                           
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               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.89                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.05                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.33                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2879                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1936                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2730                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1888                   
REMARK   3   BIN FREE R VALUE                        : 0.2810                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.18                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 149                      
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            : 6589                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 217                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.75860                                              
REMARK   3    B22 (A**2) : 1.75860                                              
REMARK   3    B33 (A**2) : -3.51720                                             
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) : 0.34                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6832   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9287   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2310   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 162    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 990    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6832   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 889    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7498   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.22                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.74                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.70                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|428 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.4331   25.2370    5.1812           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1527 T22:   -0.0121                                    
REMARK   3     T33:   -0.0698 T12:   -0.0462                                    
REMARK   3     T13:   -0.0126 T23:   -0.0317                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5677 L22:    1.5219                                    
REMARK   3     L33:    0.6690 L12:    0.8001                                    
REMARK   3     L13:   -0.1950 L23:    0.2563                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1524 S12:    0.4796 S13:    0.0938                     
REMARK   3     S21:   -0.2978 S22:    0.1306 S23:    0.1079                     
REMARK   3     S31:   -0.0415 S32:   -0.1499 S33:    0.0219                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1 - B|428 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):    3.8939   39.2762   26.6199           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1594 T22:   -0.1331                                    
REMARK   3     T33:    0.0747 T12:    0.0125                                    
REMARK   3     T13:   -0.0297 T23:    0.0089                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1938 L22:    0.9321                                    
REMARK   3     L33:    0.7453 L12:    0.5122                                    
REMARK   3     L13:   -0.0525 L23:    0.1352                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0004 S12:   -0.0162 S13:    0.0547                     
REMARK   3     S21:    0.0296 S22:   -0.0426 S23:   -0.1057                     
REMARK   3     S31:   -0.0544 S32:   -0.0250 S33:    0.0423                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GDY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074062.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20593                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 115.211                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.500                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.49500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3UE8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.80733            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       38.40367            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       38.40367            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       76.80733            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     LYS A   373                                                      
REMARK 465     ALA A   374                                                      
REMARK 465     VAL A   375                                                      
REMARK 465     LYS A   376                                                      
REMARK 465     MET A   377                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     LEU A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     ARG B   429                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     LEU B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
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    ARG A  20       60.89   -151.68                                   
REMARK 500    THR A  21      165.00     44.98                                   
REMARK 500    MET A  22      -65.15     64.44                                   
REMARK 500    SER A  32       40.51   -105.03                                   
REMARK 500    ALA A  37      -78.35    -81.90                                   
REMARK 500    ASN A  96       65.81     32.33                                   
REMARK 500    ASP A 224       71.33     43.34                                   
REMARK 500    ASP A 231       69.90   -112.51                                   
REMARK 500    SER A 240      114.91    -38.57                                   
REMARK 500    SER A 266      134.07   -176.41                                   
REMARK 500    SER A 291      -83.50   -104.26                                   
REMARK 500    LEU A 293      -49.26     65.56                                   
REMARK 500    SER A 296      122.07    -34.59                                   
REMARK 500    VAL A 379      -70.32     76.76                                   
REMARK 500    SER A 404      -35.80   -133.66                                   
REMARK 500    MET B  22      157.38    170.28                                   
REMARK 500    ASP B  24      -70.99    -47.61                                   
REMARK 500    ILE B  25      -41.45     61.78                                   
REMARK 500    ARG B  28      -77.08      6.98                                   
REMARK 500    ALA B  37      -71.35    -95.83                                   
REMARK 500    ASN B  57       31.36     71.37                                   
REMARK 500    ASN B  96       65.09     33.04                                   
REMARK 500    ASP B 224       70.65     43.56                                   
REMARK 500    ASP B 231       69.66   -112.93                                   
REMARK 500    SER B 266      134.20   -174.17                                   
REMARK 500    SER B 291      -81.96   -103.66                                   
REMARK 500    LEU B 293      -53.65     75.43                                   
REMARK 500    SER B 296      121.74    -34.10                                   
REMARK 500    SER B 404      -35.10   -133.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR A  21        23.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 129        24.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 319        24.8      L          L   OUTSIDE RANGE           
REMARK 500    LYS B  49        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 129        24.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 319        22.4      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 367        23.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 613        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH A 614        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH A 633        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A 639        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A 642        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH A 643        DISTANCE =  8.56 ANGSTROMS                       
REMARK 525    HOH A 651        DISTANCE = 11.27 ANGSTROMS                       
REMARK 525    HOH A 657        DISTANCE =  9.45 ANGSTROMS                       
REMARK 525    HOH A 675        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH A 676        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH B 644        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH B 647        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH B 649        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH B 666        DISTANCE =  9.62 ANGSTROMS                       
REMARK 525    HOH B 675        DISTANCE =  8.03 ANGSTROMS                       
REMARK 525    HOH B 679        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH B 681        DISTANCE =  8.27 ANGSTROMS                       
REMARK 525    HOH B 682        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH B 683        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH B 713        DISTANCE = 12.70 ANGSTROMS                       
REMARK 525    HOH B 714        DISTANCE =  8.06 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0X1 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0X1 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GE9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GE4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GE7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GEB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UE8   RELATED DB: PDB                                   
DBREF  4GDY A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  4GDY B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 4GDY SER A  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GDY GLY A  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GDY LEU A  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY VAL A  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY PRO A  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY ARG A  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY GLY A  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY SER A  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY LEU A  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY GLU A  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS A  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS A  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS A  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS A  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS A  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS A  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY SER B  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GDY GLY B  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GDY LEU B  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY VAL B  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY PRO B  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY ARG B  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY GLY B  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY SER B  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY LEU B  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY GLU B  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS B  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS B  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS B  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS B  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS B  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GDY HIS B  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQRES   1 A  439  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 A  439  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 A  439  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 A  439  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 A  439  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 A  439  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 A  439  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 A  439  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 A  439  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 A  439  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 A  439  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 A  439  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 A  439  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 A  439  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 A  439  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 A  439  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 A  439  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 A  439  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 A  439  PHE LEU GLN PHE ASN SER GLY ARG VAL PRO THR PHE LEU          
SEQRES  20 A  439  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 A  439  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 A  439  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 A  439  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 A  439  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 A  439  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 A  439  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 A  439  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 A  439  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 A  439  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 A  439  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 A  439  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 A  439  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 A  439  LEU ALA GLN LEU ILE LYS GLU SER LEU LEU VAL PRO ARG          
SEQRES  34 A  439  GLY SER LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  439  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 B  439  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 B  439  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 B  439  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 B  439  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 B  439  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 B  439  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 B  439  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 B  439  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 B  439  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 B  439  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 B  439  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 B  439  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 B  439  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 B  439  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 B  439  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 B  439  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 B  439  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 B  439  PHE LEU GLN PHE ASN SER GLY ARG VAL PRO THR PHE LEU          
SEQRES  20 B  439  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 B  439  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 B  439  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 B  439  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 B  439  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 B  439  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 B  439  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 B  439  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 B  439  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 B  439  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 B  439  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 B  439  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 B  439  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 B  439  LEU ALA GLN LEU ILE LYS GLU SER LEU LEU VAL PRO ARG          
SEQRES  34 B  439  GLY SER LEU GLU HIS HIS HIS HIS HIS HIS                      
HET    0X1  A 501      37                                                       
HET    0X1  B 501      37                                                       
HETNAM     0X1 (5-HYDROXY-6-METHYL-4-{[(1-OXO-7-PHENOXY-1,2-DIHYDRO[1,          
HETNAM   2 0X1  2,4]TRIAZOLO[4,3-A]QUINOLIN-4-YL)AMINO]METHYL}PYRIDIN-          
HETNAM   3 0X1  3-YL)METHYL DIHYDROGEN PHOSPHATE                                
FORMUL   3  0X1    2(C24 H22 N5 O7 P)                                           
FORMUL   5  HOH   *217(H2 O)                                                    
HELIX    1   1 ASN A    2  PHE A    6  5                                   5    
HELIX    2   2 THR A    8  ARG A   14  1                                   7    
HELIX    3   3 ASN A   42  PHE A   46  5                                   5    
HELIX    4   4 GLY A   64  LEU A   72  1                                   9    
HELIX    5   5 ILE A   80  ASN A   96  1                                  17    
HELIX    6   6 PRO A  103  GLY A  107  5                                   5    
HELIX    7   7 GLY A  116  ILE A  129  1                                  14    
HELIX    8   8 TYR A  142  HIS A  150  1                                   9    
HELIX    9   9 PRO A  151  GLY A  153  5                                   3    
HELIX   10  10 VAL A  167  SER A  176  1                                  10    
HELIX   11  11 ARG A  177  TRP A  178  5                                   2    
HELIX   12  12 LYS A  179  ASN A  189  5                                  11    
HELIX   13  13 THR A  209  TYR A  223  1                                  15    
HELIX   14  14 TYR A  233  GLN A  237  5                                   5    
HELIX   15  15 THR A  245  ASP A  250  5                                   6    
HELIX   16  16 LYS A  278  GLN A  289  1                                  12    
HELIX   17  17 SER A  296  THR A  342  1                                  47    
HELIX   18  18 VAL A  366  GLU A  371  1                                   6    
HELIX   19  19 ASN A  385  TYR A  388  5                                   4    
HELIX   20  20 SER A  406  VAL A  427  1                                  22    
HELIX   21  21 ASN B    2  PHE B    6  5                                   5    
HELIX   22  22 THR B    8  ARG B   14  1                                   7    
HELIX   23  23 ASN B   42  PHE B   46  5                                   5    
HELIX   24  24 GLY B   64  LEU B   72  1                                   9    
HELIX   25  25 ILE B   80  ASN B   96  1                                  17    
HELIX   26  26 PRO B  103  GLY B  107  5                                   5    
HELIX   27  27 GLY B  116  ILE B  129  1                                  14    
HELIX   28  28 TYR B  142  HIS B  150  1                                   9    
HELIX   29  29 PRO B  151  GLY B  153  5                                   3    
HELIX   30  30 VAL B  167  SER B  176  1                                  10    
HELIX   31  31 ARG B  177  TRP B  178  5                                   2    
HELIX   32  32 LYS B  179  ASN B  189  5                                  11    
HELIX   33  33 THR B  209  TYR B  223  1                                  15    
HELIX   34  34 TYR B  233  GLN B  237  5                                   5    
HELIX   35  35 THR B  245  ASP B  250  5                                   6    
HELIX   36  36 LYS B  278  GLN B  289  1                                  12    
HELIX   37  37 SER B  296  THR B  342  1                                  47    
HELIX   38  38 VAL B  366  GLU B  372  1                                   7    
HELIX   39  39 GLU B  372  MET B  377  1                                   6    
HELIX   40  40 ASN B  385  TYR B  388  5                                   4    
HELIX   41  41 SER B  406  VAL B  427  1                                  22    
SHEET    1   A 2 ILE A  34  SER A  35  0                                        
SHEET    2   A 2 VAL B 379  LEU B 380  1  O  LEU B 380   N  ILE A  34           
SHEET    1   B 4 THR A  60  PHE A  63  0                                        
SHEET    2   B 4 PHE A  48  THR A  54 -1  N  ALA A  51   O  PHE A  63           
SHEET    3   B 4 THR B  50  VAL B  55 -1  O  THR B  54   N  LYS A  49           
SHEET    4   B 4 ILE B  61  PHE B  63 -1  O  PHE B  63   N  ALA B  51           
SHEET    1   C 5 MET A 109  THR A 114  0                                        
SHEET    2   C 5 GLY A 272  PRO A 277 -1  O  GLY A 276   N  ASP A 110           
SHEET    3   C 5 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4   C 5 LEU A 226  ASP A 230  1  N  GLU A 229   O  ALA A 258           
SHEET    5   C 5 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    1   D 2 ASN A 134  LEU A 137  0                                        
SHEET    2   D 2 ASN A 155  ASN A 158  1  O  ASN A 155   N  VAL A 135           
SHEET    1   E 2 SER A 161  ASP A 162  0                                        
SHEET    2   E 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1   F 4 ALA A 345  TRP A 347  0                                        
SHEET    2   F 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3   F 4 TYR A 397  SER A 401 -1  O  ALA A 400   N  LEU A 356           
SHEET    4   F 4 MET A 381  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1   G 2 THR B  21  THR B  23  0                                        
SHEET    2   G 2 MET B  33  SER B  35 -1  O  ILE B  34   N  MET B  22           
SHEET    1   H 5 MET B 109  THR B 114  0                                        
SHEET    2   H 5 GLY B 272  PRO B 277 -1  O  GLY B 276   N  ASP B 110           
SHEET    3   H 5 VAL B 255  SER B 260 -1  N  ARG B 257   O  THR B 275           
SHEET    4   H 5 LEU B 226  ASP B 230  1  N  ILE B 227   O  ILE B 256           
SHEET    5   H 5 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    1   I 2 ASN B 134  LEU B 137  0                                        
SHEET    2   I 2 ASN B 155  ASN B 158  1  O  ASN B 155   N  VAL B 135           
SHEET    1   J 2 SER B 161  ASP B 162  0                                        
SHEET    2   J 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1   K 4 ALA B 345  TRP B 347  0                                        
SHEET    2   K 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3   K 4 TYR B 397  SER B 401 -1  O  ALA B 400   N  LEU B 356           
SHEET    4   K 4 LEU B 382  PRO B 383 -1  N  LEU B 382   O  ARG B 399           
CISPEP   1 ARG A   20    THR A   21          0        -6.56                     
CISPEP   2 GLU A   56    ASN A   57          0         0.06                     
CISPEP   3 GLU A  139    PRO A  140          0        -0.15                     
CISPEP   4 ASN A  202    PRO A  203          0        11.22                     
CISPEP   5 ALA B   37    GLY B   38          0        -1.66                     
CISPEP   6 GLU B  139    PRO B  140          0        -0.37                     
CISPEP   7 ASN B  202    PRO B  203          0        11.80                     
SITE     1 AC1 19 GLY A 116  SER A 117  GLN A 118  TYR A 142                    
SITE     2 AC1 19 ASN A 202  ASP A 230  TYR A 233  SER A 260                    
SITE     3 AC1 19 SER A 262  ARG A 270  PHE A 355  ARG A 399                    
SITE     4 AC1 19 ILE B  19  MET B  33  GLY B  39  LEU B  40                    
SITE     5 AC1 19 TYR B  74  SER B  75  SER B  77                               
SITE     1 AC2 21 ILE A  19  ARG A  20  GLY A  39  LEU A  40                    
SITE     2 AC2 21 TYR A  74  SER A  75  SER A  77  LEU A 293                    
SITE     3 AC2 21 GLY B 116  SER B 117  GLN B 118  TYR B 142                    
SITE     4 AC2 21 ASN B 202  ASP B 230  PRO B 232  TYR B 233                    
SITE     5 AC2 21 SER B 260  SER B 262  ARG B 270  PHE B 355                    
SITE     6 AC2 21 ARG B 399                                                     
CRYST1  116.457  116.457  115.211  90.00  90.00 120.00 P 32 2 1     12          
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      0.008587  0.004958  0.000000        0.00000                         
SCALE2      0.000000  0.009915  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008680        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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