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Database: PDB
Entry: 3UE8
LinkDB: 3UE8
Original site: 3UE8 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       28-OCT-11   3UE8              
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: 2-AMINOADIPATE AMINOTRANSFERASE, 2-AMINOADIPATE             
COMPND   6 TRANSAMINASE, ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT, KAT/AADAT, 
COMPND   7 KYNURENINE AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE             
COMPND   8 AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE TRANSAMINASE II;       
COMPND   9 EC: 2.6.1.39, 2.6.1.7;                                               
COMPND  10 ENGINEERED: 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KAT II, KYNURENINE AMINOTRANSFERASE, TRANSFERASE-TRANSFERASE          
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.DOUNAY,M.ANDERSON,B.M.BECHLE,B.M.CAMPBELL,M.M.CLAFFEY,            
AUTHOR   2 A.EVDOKIMOV,E.EDELWEISS,K.R.FONSECA,X.GAN,S.GHOSH,M.M.HAYWARD,       
AUTHOR   3 W.HORNER,J.Y.KIM,L.A.MCALLISTER,J.PANDIT,V.PARADIS,V.D.PARIKH,       
AUTHOR   4 M.R.REESE,S.B.RONG,M.A.SALAFIA,K.SCHUYTEN,C.A.STRICK,J.B.TUTTLE,     
AUTHOR   5 J.VALENTINE,H.WANG,L.E.ZAWADZKE,P.R.VERHOEST                         
REVDAT   2   18-APR-18 3UE8    1       JRNL                                     
REVDAT   1   01-FEB-12 3UE8    0                                                
JRNL        AUTH   A.B.DOUNAY,M.ANDERSON,B.M.BECHLE,B.M.CAMPBELL,M.M.CLAFFEY,   
JRNL        AUTH 2 A.EVDOKIMOV,E.EVRARD,K.R.FONSECA,X.GAN,S.GHOSH,M.M.HAYWARD,  
JRNL        AUTH 3 W.HORNER,J.Y.KIM,L.A.MCALLISTER,J.PANDIT,V.PARADIS,          
JRNL        AUTH 4 V.D.PARIKH,M.R.REESE,S.RONG,M.A.SALAFIA,K.SCHUYTEN,          
JRNL        AUTH 5 C.A.STRICK,J.B.TUTTLE,J.VALENTINE,H.WANG,L.E.ZAWADZKE,       
JRNL        AUTH 6 P.R.VERHOEST                                                 
JRNL        TITL   DISCOVERY OF BRAIN-PENETRANT, IRREVERSIBLE KYNURENINE        
JRNL        TITL 2 AMINOTRANSFERASE II INHIBITORS FOR SCHIZOPHRENIA.            
JRNL        REF    ACS MED CHEM LETT             V.   3   187 2012              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900455                                                     
JRNL        DOI    10.1021/ML200204M                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
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) : 3.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15793                          
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)  : 0.204                          
REMARK   3   R VALUE            (WORKING SET)  : 0.200                          
REMARK   3   FREE R VALUE                      : 0.275                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 790                            
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               : 8                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.31                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.77                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2814                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2149                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2667                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2090                   
REMARK   3   BIN FREE R VALUE                        : 0.3250                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.22                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 147                      
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            : 6427                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 21.73390                                             
REMARK   3    B22 (A**2) : -10.45460                                            
REMARK   3    B33 (A**2) : -11.27930                                            
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) : 0.547               
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      : 0.900                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.833                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6647   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9038   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2249   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 161    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 995    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6647   ; 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   : 864    ; 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   : 8129   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.33                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.89                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 24.39                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   18.9415   21.1206   31.6026           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1745 T22:   -0.2077                                    
REMARK   3     T33:   -0.1173 T12:    0.0346                                    
REMARK   3     T13:   -0.0372 T23:    0.0672                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3155 L22:    1.6944                                    
REMARK   3     L33:    1.4523 L12:    0.5742                                    
REMARK   3     L13:   -0.1638 L23:   -0.5295                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0771 S12:    0.1915 S13:    0.2113                     
REMARK   3     S21:   -0.2191 S22:    0.2567 S23:    0.1984                     
REMARK   3     S31:   -0.1126 S32:   -0.3456 S33:   -0.1796                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   18.3204    2.9265   57.8121           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0651 T22:   -0.2070                                    
REMARK   3     T33:   -0.3326 T12:    0.0853                                    
REMARK   3     T13:    0.0105 T23:    0.0161                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4443 L22:    1.9876                                    
REMARK   3     L33:    3.0648 L12:    0.2264                                    
REMARK   3     L13:   -0.4400 L23:   -1.1349                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0080 S12:   -0.2715 S13:   -0.0690                     
REMARK   3     S21:    0.1380 S22:   -0.0486 S23:   -0.0565                     
REMARK   3     S31:    0.2773 S32:    0.1765 S33:    0.0566                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068643.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : RIGAKU VARIMAX MIRRORS             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16095                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.80800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.63350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.29850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.63350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.80800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.29850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 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     SER A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     THR A    23                                                      
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     LYS A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     MET A    33                                                      
REMARK 465     PRO A   428                                                      
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     PRO B    18                                                      
REMARK 465     ILE B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     ILE B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     LEU B   426                                                      
REMARK 465     VAL B   427                                                      
REMARK 465     PRO B   428                                                      
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 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     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     GLU A 163    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     GLU A 313    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 373    CG   CD   CE   NZ                                   
REMARK 470     LYS A 376    CG   CD   CE   NZ                                   
REMARK 470     LYS B  93    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR B    74     O7   09M A   440              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  59     -153.81    -75.38                                   
REMARK 500    PRO A  76      -31.69    -31.02                                   
REMARK 500    SER A  77      -45.97    101.81                                   
REMARK 500    ASN A  96       60.29     30.70                                   
REMARK 500    ASP A 162     -177.90   -177.67                                   
REMARK 500    SER A 176       -4.11    -58.75                                   
REMARK 500    GLN A 187      -11.01    126.58                                   
REMARK 500    ASP A 231       68.12   -118.17                                   
REMARK 500    TYR A 233       35.73    -98.81                                   
REMARK 500    LEU A 236       50.38    -90.97                                   
REMARK 500    LYS A 240      -99.38     86.09                                   
REMARK 500    SER A 266      120.21   -178.11                                   
REMARK 500    SER A 291      -77.39   -104.10                                   
REMARK 500    LEU A 293      -60.22     73.48                                   
REMARK 500    SER A 296      110.25    -33.60                                   
REMARK 500    THR A 342      -60.46     -4.54                                   
REMARK 500    LEU A 369       34.70    -70.92                                   
REMARK 500    ILE A 370      -72.33   -134.77                                   
REMARK 500    GLU A 372      -32.92   -144.05                                   
REMARK 500    THR B   8      153.16    -48.85                                   
REMARK 500    ARG B  14      140.66    -24.91                                   
REMARK 500    PRO B  30     -159.74    -84.56                                   
REMARK 500    LYS B  31      -56.12     64.95                                   
REMARK 500    SER B  32        3.54    -63.57                                   
REMARK 500    ALA B  37      -85.17    -79.53                                   
REMARK 500    HIS B  95       59.93   -152.11                                   
REMARK 500    ASN B  96      101.50    -21.36                                   
REMARK 500    GLN B 106     -103.97    -77.94                                   
REMARK 500    GLN B 108      142.23    -37.66                                   
REMARK 500    SER B 115       85.37    -69.67                                   
REMARK 500    TYR B 142      109.94    -48.02                                   
REMARK 500    LEU B 152       -0.86    -55.95                                   
REMARK 500    ASN B 189       74.30   -101.64                                   
REMARK 500    LYS B 222      -71.93    -61.67                                   
REMARK 500    ASP B 224       93.30    -10.89                                   
REMARK 500    GLU B 229       83.53    -69.50                                   
REMARK 500    ASP B 231       60.51   -115.15                                   
REMARK 500    ASP B 250       70.01    -53.88                                   
REMARK 500    ILE B 265      -51.17   -125.02                                   
REMARK 500    SER B 266      134.79   -179.02                                   
REMARK 500    ARG B 270       62.00     64.89                                   
REMARK 500    SER B 291      -90.38    -92.47                                   
REMARK 500    LEU B 293      -57.17     68.34                                   
REMARK 500    SER B 296      109.44    -43.12                                   
REMARK 500    LYS B 339      -73.12    -63.82                                   
REMARK 500    GLU B 372      -95.34    -89.53                                   
REMARK 500    LYS B 376       43.33    -87.89                                   
REMARK 500    ASN B 385      -35.46    -38.22                                   
REMARK 500    PRO B 396       34.15    -91.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 09M A 440                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 09M B 440                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 441                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 441                  
DBREF  3UE8 A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  3UE8 B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 3UE8 LEU A  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 VAL A  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 PRO A  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 ARG A  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 GLY A  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 SER A  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 LEU A  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 GLU A  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS A  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS A  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS A  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS A  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS A  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS A  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 LEU B  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 VAL B  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 PRO B  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 ARG B  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 GLY B  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 SER B  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 LEU B  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 GLU B  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS B  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS B  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS B  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS B  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 HIS B  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 3UE8 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 LYS PHE 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 LYS PHE 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    09M  A 440      28                                                       
HET     CL  A 441       1                                                       
HET    09M  B 440      28                                                       
HET     CL  B 441       1                                                       
HETNAM     09M (5-HYDROXY-4-{[(1-HYDROXY-2-OXO-1,2-DIHYDROQUINOLIN-3-           
HETNAM   2 09M  YL)AMINO]METHYL}-6-METHYLPYRIDIN-3-YL)METHYL                    
HETNAM   3 09M  DIHYDROGEN PHOSPHATE                                            
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  09M    2(C17 H18 N3 O7 P)                                           
FORMUL   4   CL    2(CL 1-)                                                     
HELIX    1   1 THR A    8  ALA A   13  1                                   6    
HELIX    2   2 ASN A   42  PHE A   46  5                                   5    
HELIX    3   3 GLY A   64  GLN A   73  1                                  10    
HELIX    4   4 ILE A   80  ASN A   96  1                                  17    
HELIX    5   5 PRO A   97  TYR A  102  5                                   6    
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 VAL A  167  SER A  176  1                                  10    
HELIX   10  10 ARG A  177  TRP A  178  5                                   2    
HELIX   11  11 LYS A  179  LYS A  184  5                                   6    
HELIX   12  12 THR A  209  TYR A  223  1                                  15    
HELIX   13  13 LYS A  278  THR A  292  1                                  15    
HELIX   14  14 SER A  296  LEU A  341  1                                  46    
HELIX   15  15 LYS A  367  GLU A  372  1                                   6    
HELIX   16  16 ALA A  374  MET A  377  5                                   4    
HELIX   17  17 ASN A  385  TYR A  388  5                                   4    
HELIX   18  18 SER A  406  LEU A  426  1                                  21    
HELIX   19  19 TYR B    3  ILE B    7  5                                   5    
HELIX   20  20 THR B    8  ARG B   14  1                                   7    
HELIX   21  21 ASN B   42  PHE B   46  5                                   5    
HELIX   22  22 GLY B   64  GLN B   73  1                                  10    
HELIX   23  23 ILE B   80  ASN B   96  1                                  17    
HELIX   24  24 PRO B   97  TYR B  102  5                                   6    
HELIX   25  25 SER B  115  ILE B  129  1                                  15    
HELIX   26  26 TYR B  142  HIS B  150  1                                   9    
HELIX   27  27 VAL B  167  SER B  176  1                                  10    
HELIX   28  28 THR B  209  TYR B  223  1                                  15    
HELIX   29  29 THR B  245  ASP B  250  1                                   6    
HELIX   30  30 LYS B  278  THR B  292  1                                  15    
HELIX   31  31 SER B  296  LEU B  341  1                                  46    
HELIX   32  32 VAL B  366  GLU B  372  1                                   7    
HELIX   33  33 ALA B  374  GLY B  378  5                                   5    
HELIX   34  34 PRO B  383  TYR B  388  5                                   6    
HELIX   35  35 SER B  406  LEU B  425  1                                  20    
SHEET    1   A 4 THR A  60  PHE A  63  0                                        
SHEET    2   A 4 PHE A  48  VAL A  55 -1  N  ALA A  51   O  PHE A  63           
SHEET    3   A 4 PHE B  48  VAL B  55 -1  O  THR B  54   N  THR A  50           
SHEET    4   A 4 GLY B  58  PHE B  63 -1  O  PHE B  63   N  ALA B  51           
SHEET    1   B 7 MET A 109  THR A 114  0                                        
SHEET    2   B 7 GLY A 272  PRO A 277 -1  O  GLY A 272   N  THR A 114           
SHEET    3   B 7 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4   B 7 LEU A 226  ASP A 230  1  N  GLU A 229   O  ALA A 258           
SHEET    5   B 7 PHE A 193  THR A 196  1  N  THR A 196   O  ASP A 230           
SHEET    6   B 7 ASN A 134  LEU A 137  1  N  LEU A 136   O  PHE A 193           
SHEET    7   B 7 ASN A 155  ASN A 158  1  O  ASN A 155   N  VAL A 135           
SHEET    1   C 4 ALA A 345  TRP A 347  0                                        
SHEET    2   C 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3   C 4 TYR A 397  SER A 401 -1  O  ALA A 400   N  LEU A 356           
SHEET    4   C 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1   D 2 VAL A 379  LEU A 380  0                                        
SHEET    2   D 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1   E 7 MET B 109  THR B 114  0                                        
SHEET    2   E 7 GLY B 272  PRO B 277 -1  O  GLY B 272   N  THR B 114           
SHEET    3   E 7 VAL B 255  SER B 260 -1  N  ARG B 257   O  THR B 275           
SHEET    4   E 7 LEU B 226  ASP B 230  1  N  GLU B 229   O  ALA B 258           
SHEET    5   E 7 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    6   E 7 ASN B 134  LEU B 137  1  N  LEU B 136   O  TYR B 195           
SHEET    7   E 7 ASN B 155  ASN B 158  1  O  ASN B 155   N  VAL B 135           
SHEET    1   F 2 SER B 161  ASP B 162  0                                        
SHEET    2   F 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1   G 3 ALA B 345  TRP B 347  0                                        
SHEET    2   G 3 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3   G 3 TYR B 397  SER B 401 -1  O  LEU B 398   N  ILE B 358           
CISPEP   1 GLU A  139    PRO A  140          0         1.80                     
CISPEP   2 ASN A  202    PRO A  203          0        16.26                     
CISPEP   3 GLU B  139    PRO B  140          0        -0.95                     
CISPEP   4 ASN B  202    PRO B  203          0        10.24                     
SITE     1 AC1 15 GLY A 116  SER A 117  GLN A 118  TYR A 142                    
SITE     2 AC1 15 ASN A 202  ASP A 230  PRO A 232  TYR A 233                    
SITE     3 AC1 15 SER A 260  SER A 262  LYS A 263  ARG A 270                    
SITE     4 AC1 15 PHE A 355  ARG A 399  TYR B  74                               
SITE     1 AC2 15 GLY A  39  TYR A  74  GLY B 116  SER B 117                    
SITE     2 AC2 15 GLN B 118  TYR B 142  ASN B 202  ASP B 230                    
SITE     3 AC2 15 PRO B 232  TYR B 233  SER B 260  SER B 262                    
SITE     4 AC2 15 LYS B 263  ARG B 270  ARG B 399                               
SITE     1 AC3  2 TRP A 178  ASN A 189                                          
SITE     1 AC4  2 TRP B 178  ASN B 189                                          
CRYST1   63.616  116.597  129.267  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      0.015719  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008577  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007736        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system