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Database: PDB
Entry: 4GE9
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Original site: 4GE9 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-AUG-12   4GE9              
TITLE     KYNURENINE AMINOTRANSFERASE II INHIBITORS                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A, B, C, D;                                                   
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, IRREVERSIBLE INHIBITOR, TRANSFERASE-TRANSFERASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT                                                              
REVDAT   2   16-JUL-14 4GE9    1       JRNL                                     
REVDAT   1   07-NOV-12 4GE9    0                                                
JRNL        AUTH   J.B.TUTTLE,M.ANDERSON,B.M.BECHLE,B.M.CAMPBELL,C.CHANG,       
JRNL        AUTH 2 A.B.DOUNAY,E.EVRARD,K.R.FONSECA,X.GAN,S.GHOSH,W.HORNER,      
JRNL        AUTH 3 L.C.JAMES,J.Y.KIM,L.A.MCALLISTER,J.PANDIT,V.D.PARIKH,        
JRNL        AUTH 4 B.J.RAGO,M.A.SALAFIA,C.A.STRICK,L.E.ZAWADZKE,P.R.VERHOEST    
JRNL        TITL   STRUCTURE-BASED DESIGN OF IRREVERSIBLE HUMAN KAT II          
JRNL        TITL 2 INHIBITORS: DISCOVERY OF NEW POTENCY-ENHANCING INTERACTIONS. 
JRNL        REF    ACS MED CHEM LETT             V.   4    37 2013              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900560                                                     
JRNL        DOI    10.1021/ML300237V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 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) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 62628                          
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)  : 0.178                          
REMARK   3   R VALUE            (WORKING SET)  : 0.175                          
REMARK   3   FREE R VALUE                      : 0.230                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3193                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.43                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.49                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.08                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4594                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1951                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4365                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1917                   
REMARK   3   BIN FREE R VALUE                        : 0.2573                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.98                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 229                      
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            : 13376                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 148                                     
REMARK   3   SOLVENT ATOMS            : 745                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.02                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.47290                                              
REMARK   3    B22 (A**2) : 7.48680                                              
REMARK   3    B33 (A**2) : -10.95970                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.70840                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.360               
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) : 0.686               
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      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 13864  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 18844  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4704   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 328    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1980   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 13864  ; 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   : 1804   ; 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   : 16500  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.24                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.33                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|428 A|4000 - A|4000 }                        
REMARK   3    ORIGIN FOR THE GROUP (A):    9.0217   -2.8054  -49.6560           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2466 T22:   -0.1528                                    
REMARK   3     T33:    0.0375 T12:   -0.0087                                    
REMARK   3     T13:    0.0581 T23:   -0.0033                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2697 L22:    3.0985                                    
REMARK   3     L33:    0.1159 L12:    0.7336                                    
REMARK   3     L13:   -0.0923 L23:   -0.0035                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0739 S12:   -0.1195 S13:   -0.0484                     
REMARK   3     S21:    0.4011 S22:   -0.0364 S23:    0.2305                     
REMARK   3     S31:    0.0303 S32:   -0.0138 S33:   -0.0374                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1 - B|428 B|4000 - B|4000 }                        
REMARK   3    ORIGIN FOR THE GROUP (A):   34.7469   13.3271  -49.7295           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3151 T22:   -0.1814                                    
REMARK   3     T33:    0.2542 T12:   -0.0019                                    
REMARK   3     T13:    0.0483 T23:   -0.0029                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1294 L22:    3.0217                                    
REMARK   3     L33:    0.1262 L12:    0.6598                                    
REMARK   3     L13:    0.2025 L23:   -0.0283                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0525 S12:   -0.1030 S13:   -0.1090                     
REMARK   3     S21:    0.4030 S22:   -0.0306 S23:   -0.5141                     
REMARK   3     S31:   -0.0169 S32:    0.0186 S33:   -0.0219                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|1 - C|428 C|4000 - C|4000 }                        
REMARK   3    ORIGIN FOR THE GROUP (A):    4.5024  -14.4415    8.4425           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3260 T22:   -0.3040                                    
REMARK   3     T33:   -0.0152 T12:    0.0032                                    
REMARK   3     T13:   -0.1268 T23:   -0.0489                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6939 L22:    3.2203                                    
REMARK   3     L33:    0.3329 L12:    1.2482                                    
REMARK   3     L13:    0.2794 L23:   -0.2737                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1525 S12:   -0.0745 S13:    0.2224                     
REMARK   3     S21:    0.3186 S22:   -0.1799 S23:    0.5711                     
REMARK   3     S31:   -0.0285 S32:    0.0212 S33:    0.0274                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|1 - D|428 D|4000 - D|4000 }                        
REMARK   3    ORIGIN FOR THE GROUP (A):   30.1552    1.8736    8.3538           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3241 T22:   -0.2650                                    
REMARK   3     T33:   -0.3241 T12:   -0.0458                                    
REMARK   3     T13:   -0.1023 T23:    0.0085                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1154 L22:    3.8073                                    
REMARK   3     L33:    0.7202 L12:    1.2668                                    
REMARK   3     L13:    0.6025 L23:   -0.0713                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1731 S12:   -0.0848 S13:   -0.0604                     
REMARK   3     S21:    0.2860 S22:   -0.1665 S23:   -0.1187                     
REMARK   3     S31:    0.0153 S32:    0.0379 S33:   -0.0066                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GE9 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 RCSB074073.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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) : 1.00                               
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   : 63063                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.425                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 116.237                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48900                            
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       53.52500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: 9240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30220 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 9310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     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 465     ARG C   429                                                      
REMARK 465     GLY C   430                                                      
REMARK 465     SER C   431                                                      
REMARK 465     LEU C   432                                                      
REMARK 465     GLU C   433                                                      
REMARK 465     HIS C   434                                                      
REMARK 465     HIS C   435                                                      
REMARK 465     HIS C   436                                                      
REMARK 465     HIS C   437                                                      
REMARK 465     HIS C   438                                                      
REMARK 465     HIS C   439                                                      
REMARK 465     ARG D   429                                                      
REMARK 465     GLY D   430                                                      
REMARK 465     SER D   431                                                      
REMARK 465     LEU D   432                                                      
REMARK 465     GLU D   433                                                      
REMARK 465     HIS D   434                                                      
REMARK 465     HIS D   435                                                      
REMARK 465     HIS D   436                                                      
REMARK 465     HIS D   437                                                      
REMARK 465     HIS D   438                                                      
REMARK 465     HIS D   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    ASN A 189       50.01     39.46                                   
REMARK 500    ASP A 231       66.94   -114.67                                   
REMARK 500    ASN A 239       54.51     32.44                                   
REMARK 500    SER A 240      -50.82   -136.91                                   
REMARK 500    ARG A 242      102.75     62.72                                   
REMARK 500    SER A 266      127.99    179.76                                   
REMARK 500    SER A 291      -78.75   -108.14                                   
REMARK 500    LEU A 293      -60.54     69.82                                   
REMARK 500    SER A 296      122.02    -38.83                                   
REMARK 500    GLU A 372      -68.22   -103.40                                   
REMARK 500    ASN B  57       76.59     57.16                                   
REMARK 500    ASN B  96       59.69     39.63                                   
REMARK 500    ASP B 162     -160.87   -128.03                                   
REMARK 500    ASP B 231       67.45   -116.81                                   
REMARK 500    ASN B 239       46.48     37.77                                   
REMARK 500    SER B 266      130.25   -178.69                                   
REMARK 500    SER B 291      -79.93   -105.55                                   
REMARK 500    LEU B 293      -57.82     71.29                                   
REMARK 500    GLU B 372      -69.29   -103.86                                   
REMARK 500    ASP C 162     -161.74   -122.66                                   
REMARK 500    ASP C 224       68.77     38.41                                   
REMARK 500    ASP C 231       66.76   -115.48                                   
REMARK 500    SER C 266      130.04    179.27                                   
REMARK 500    SER C 291      -79.25   -107.04                                   
REMARK 500    LEU C 293      -60.25     71.79                                   
REMARK 500    GLU C 372      -68.60   -103.92                                   
REMARK 500    ASN D  57       80.10     55.77                                   
REMARK 500    ASP D 162     -151.73   -112.59                                   
REMARK 500    ASP D 224       64.61     39.30                                   
REMARK 500    ASP D 231       66.62   -115.61                                   
REMARK 500    SER D 240      -42.35   -139.77                                   
REMARK 500    ARG D 242      107.06     17.19                                   
REMARK 500    SER D 266      129.14    179.98                                   
REMARK 500    SER D 291      -79.79   -108.09                                   
REMARK 500    LEU D 293      -60.38     72.24                                   
REMARK 500    GLU D 312      -16.62    -48.58                                   
REMARK 500    GLU D 372      -68.56   -102.97                                   
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    ILE A 129        23.6      L          L   OUTSIDE RANGE           
REMARK 500    THR A 145        22.3      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 147        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 242        24.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 361        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE B   7        24.9      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 101        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 361        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 129        24.1      L          L   OUTSIDE RANGE           
REMARK 500    THR C 145        24.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS C 361        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE D  25        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG D  28        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE D 129        23.9      L          L   OUTSIDE RANGE           
REMARK 500    GLN D 147        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG D 242        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LYS D 361        23.7      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 A4115        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A4148        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH A4157        DISTANCE =  8.92 ANGSTROMS                       
REMARK 525    HOH A4167        DISTANCE =  9.66 ANGSTROMS                       
REMARK 525    HOH A4187        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A4188        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A4255        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A4260        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH A4261        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A4264        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A4269        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A4278        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH A4282        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH A4284        DISTANCE =  7.53 ANGSTROMS                       
REMARK 525    HOH A4289        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH A4294        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH A4330        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH A4348        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A4363        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A4364        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A4365        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A4385        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH A4390        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH B4149        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH B4183        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH B4190        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH B4196        DISTANCE =  9.57 ANGSTROMS                       
REMARK 525    HOH B4198        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH B4222        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH B4237        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH B4249        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B4293        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH B4295        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH B4299        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B4304        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH B4324        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH B4326        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH B4328        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH C4128        DISTANCE = 13.93 ANGSTROMS                       
REMARK 525    HOH C4131        DISTANCE =  9.43 ANGSTROMS                       
REMARK 525    HOH C4135        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH C4144        DISTANCE = 10.85 ANGSTROMS                       
REMARK 525    HOH C4152        DISTANCE = 16.75 ANGSTROMS                       
REMARK 525    HOH C4153        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH C4158        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH C4159        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH C4183        DISTANCE = 11.33 ANGSTROMS                       
REMARK 525    HOH C4185        DISTANCE = 12.95 ANGSTROMS                       
REMARK 525    HOH C4188        DISTANCE = 14.65 ANGSTROMS                       
REMARK 525    HOH C4191        DISTANCE = 14.40 ANGSTROMS                       
REMARK 525    HOH C4194        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH D4112        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH D4119        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH D4129        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH D4145        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH D4147        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH D4156        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH D4157        DISTANCE = 10.20 ANGSTROMS                       
REMARK 525    HOH D4159        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH D4167        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH D4168        DISTANCE =  9.30 ANGSTROMS                       
REMARK 525    HOH D4172        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH D4177        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH D4178        DISTANCE =  9.77 ANGSTROMS                       
REMARK 525    HOH D4183        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH D4192        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH D4194        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH D4196        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH D4197        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH D4200        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH D4210        DISTANCE =  5.12 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0L0 A 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0L0 B 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0L0 C 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0L0 D 4000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GDY   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  4GE9 A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  4GE9 B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  4GE9 C    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  4GE9 D    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 4GE9 SER A  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GE9 GLY A  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GE9 LEU A  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 VAL A  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 PRO A  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 ARG A  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLY A  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER A  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 LEU A  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLU A  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS A  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS A  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS A  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS A  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS A  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS A  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER B  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GE9 GLY B  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GE9 LEU B  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 VAL B  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 PRO B  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 ARG B  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLY B  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER B  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 LEU B  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLU B  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS B  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS B  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS B  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS B  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS B  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS B  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER C  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GE9 GLY C  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GE9 LEU C  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 VAL C  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 PRO C  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 ARG C  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLY C  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER C  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 LEU C  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLU C  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS C  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS C  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS C  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS C  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS C  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS C  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER D  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GE9 GLY D  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GE9 LEU D  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 VAL D  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 PRO D  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 ARG D  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLY D  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 SER D  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 LEU D  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 GLU D  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS D  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS D  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS D  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS D  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS D  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GE9 HIS D  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                      
SEQRES   1 C  439  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 C  439  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 C  439  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 C  439  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 C  439  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 C  439  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 C  439  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 C  439  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 C  439  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 C  439  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 C  439  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 C  439  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 C  439  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 C  439  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 C  439  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 C  439  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 C  439  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 C  439  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 C  439  PHE LEU GLN PHE ASN SER GLY ARG VAL PRO THR PHE LEU          
SEQRES  20 C  439  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 C  439  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 C  439  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 C  439  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 C  439  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 C  439  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 C  439  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 C  439  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 C  439  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 C  439  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 C  439  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 C  439  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 C  439  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 C  439  LEU ALA GLN LEU ILE LYS GLU SER LEU LEU VAL PRO ARG          
SEQRES  34 C  439  GLY SER LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D  439  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 D  439  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 D  439  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 D  439  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 D  439  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 D  439  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 D  439  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 D  439  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 D  439  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 D  439  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 D  439  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 D  439  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 D  439  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 D  439  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 D  439  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 D  439  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 D  439  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 D  439  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 D  439  PHE LEU GLN PHE ASN SER GLY ARG VAL PRO THR PHE LEU          
SEQRES  20 D  439  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 D  439  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 D  439  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 D  439  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 D  439  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 D  439  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 D  439  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 D  439  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 D  439  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 D  439  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 D  439  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 D  439  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 D  439  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 D  439  LEU ALA GLN LEU ILE LYS GLU SER LEU LEU VAL PRO ARG          
SEQRES  34 D  439  GLY SER LEU GLU HIS HIS HIS HIS HIS HIS                      
HET    0L0  A4000      37                                                       
HET    0L0  B4000      37                                                       
HET    0L0  C4000      37                                                       
HET    0L0  D4000      37                                                       
HETNAM     0L0 (4-{[(6-BENZYL-1-HYDROXY-7-METHOXY-2-OXO-1,2-                    
HETNAM   2 0L0  DIHYDROQUINOLIN-3-YL)AMINO]METHYL}-5-HYDROXY-6-                 
HETNAM   3 0L0  METHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE                  
FORMUL   5  0L0    4(C25 H26 N3 O8 P)                                           
FORMUL   9  HOH   *745(H2 O)                                                    
HELIX    1   1 ASN A    2  ILE A    7  5                                   6    
HELIX    2   2 THR A    8  ALA A   13  1                                   6    
HELIX    3   3 SER A   17  LEU A   26  1                                  10    
HELIX    4   4 ASN A   42  PHE A   46  5                                   5    
HELIX    5   5 GLY A   64  LEU A   72  1                                   9    
HELIX    6   6 ILE A   80  ASN A   96  1                                  17    
HELIX    7   7 PRO A  103  GLY A  107  5                                   5    
HELIX    8   8 SER A  115  ILE A  129  1                                  15    
HELIX    9   9 TYR A  142  HIS A  150  1                                   9    
HELIX   10  10 PRO A  151  GLY A  153  5                                   3    
HELIX   11  11 VAL A  167  SER A  176  1                                  10    
HELIX   12  12 ARG A  177  TRP A  178  5                                   2    
HELIX   13  13 LYS A  179  ASN A  185  5                                   7    
HELIX   14  14 THR A  209  TYR A  223  1                                  15    
HELIX   15  15 LYS A  278  SER A  291  1                                  14    
HELIX   16  16 SER A  296  THR A  342  1                                  47    
HELIX   17  17 VAL A  366  GLU A  372  1                                   7    
HELIX   18  18 ALA A  374  MET A  377  5                                   4    
HELIX   19  19 ASN A  385  TYR A  388  5                                   4    
HELIX   20  20 SER A  406  LEU A  426  1                                  21    
HELIX   21  21 ASN B    2  ILE B    7  5                                   6    
HELIX   22  22 THR B    8  ALA B   13  1                                   6    
HELIX   23  23 SER B   17  ARG B   28  1                                  12    
HELIX   24  24 ASN B   42  PHE B   46  5                                   5    
HELIX   25  25 GLY B   64  LEU B   72  1                                   9    
HELIX   26  26 ILE B   80  ASN B   96  1                                  17    
HELIX   27  27 PRO B  103  GLY B  107  5                                   5    
HELIX   28  28 SER B  115  ILE B  129  1                                  15    
HELIX   29  29 TYR B  142  HIS B  150  1                                   9    
HELIX   30  30 PRO B  151  GLY B  153  5                                   3    
HELIX   31  31 VAL B  167  SER B  176  1                                  10    
HELIX   32  32 ARG B  177  TRP B  178  5                                   2    
HELIX   33  33 LYS B  179  LYS B  184  5                                   6    
HELIX   34  34 THR B  209  TYR B  223  1                                  15    
HELIX   35  35 LYS B  278  SER B  291  1                                  14    
HELIX   36  36 SER B  296  THR B  342  1                                  47    
HELIX   37  37 VAL B  366  GLU B  372  1                                   7    
HELIX   38  38 ALA B  374  MET B  377  5                                   4    
HELIX   39  39 ASN B  385  TYR B  388  5                                   4    
HELIX   40  40 SER B  406  LEU B  426  1                                  21    
HELIX   41  41 ASN C    2  ILE C    7  5                                   6    
HELIX   42  42 THR C    8  ALA C   13  1                                   6    
HELIX   43  43 SER C   17  ARG C   28  1                                  12    
HELIX   44  44 ASN C   42  PHE C   46  5                                   5    
HELIX   45  45 GLY C   64  LEU C   72  1                                   9    
HELIX   46  46 ILE C   80  ASN C   96  1                                  17    
HELIX   47  47 PRO C  103  GLY C  107  5                                   5    
HELIX   48  48 SER C  115  ILE C  129  1                                  15    
HELIX   49  49 TYR C  142  HIS C  150  1                                   9    
HELIX   50  50 PRO C  151  GLY C  153  5                                   3    
HELIX   51  51 VAL C  167  SER C  176  1                                  10    
HELIX   52  52 ARG C  177  TRP C  178  5                                   2    
HELIX   53  53 LYS C  179  LYS C  184  5                                   6    
HELIX   54  54 THR C  209  TYR C  223  1                                  15    
HELIX   55  55 LYS C  278  SER C  291  1                                  14    
HELIX   56  56 SER C  296  THR C  342  1                                  47    
HELIX   57  57 VAL C  366  GLU C  372  1                                   7    
HELIX   58  58 ALA C  374  MET C  377  5                                   4    
HELIX   59  59 ASN C  385  TYR C  388  5                                   4    
HELIX   60  60 SER C  406  LEU C  426  1                                  21    
HELIX   61  61 ASN D    2  PHE D    6  5                                   5    
HELIX   62  62 THR D    8  ALA D   13  1                                   6    
HELIX   63  63 SER D   17  SER D   27  1                                  11    
HELIX   64  64 ASN D   42  PHE D   46  5                                   5    
HELIX   65  65 GLY D   64  LEU D   72  1                                   9    
HELIX   66  66 ILE D   80  ASN D   96  1                                  17    
HELIX   67  67 PRO D  103  GLY D  107  5                                   5    
HELIX   68  68 SER D  115  ILE D  129  1                                  15    
HELIX   69  69 TYR D  142  HIS D  150  1                                   9    
HELIX   70  70 PRO D  151  GLY D  153  5                                   3    
HELIX   71  71 VAL D  167  SER D  176  1                                  10    
HELIX   72  72 GLU D  181  ASN D  185  5                                   5    
HELIX   73  73 THR D  209  TYR D  223  1                                  15    
HELIX   74  74 LYS D  278  SER D  291  1                                  14    
HELIX   75  75 SER D  296  LEU D  341  1                                  46    
HELIX   76  76 VAL D  366  GLU D  372  1                                   7    
HELIX   77  77 ALA D  374  MET D  377  5                                   4    
HELIX   78  78 ASN D  385  TYR D  388  5                                   4    
HELIX   79  79 SER D  406  LEU D  425  1                                  20    
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 ILE A  61  PHE A  63  0                                        
SHEET    2   B 4 PHE A  48  VAL A  55 -1  N  ALA A  51   O  PHE A  63           
SHEET    3   B 4 PHE B  48  VAL B  55 -1  O  LYS B  49   N  THR A  54           
SHEET    4   B 4 GLY B  58  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  LEU A 274   N  CYS A 112           
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  ILE A 256           
SHEET    5   C 5 PHE A 193  THR A 196  1  N  THR A 196   O  ASP A 230           
SHEET    1   D 2 ASN A 134  LEU A 137  0                                        
SHEET    2   D 2 ASN A 155  ASN A 158  1  O  ILE A 157   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 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1   G 2 VAL A 379  LEU A 380  0                                        
SHEET    2   G 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1   H 5 MET B 109  THR B 114  0                                        
SHEET    2   H 5 GLY B 272  PRO B 277 -1  O  LEU B 274   N  CYS B 112           
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  GLU B 229   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  ILE B 157   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           
SHEET    1   L 2 ILE C  34  SER C  35  0                                        
SHEET    2   L 2 VAL D 379  LEU D 380  1  O  LEU D 380   N  ILE C  34           
SHEET    1   M 4 ILE C  61  PHE C  63  0                                        
SHEET    2   M 4 PHE C  48  VAL C  55 -1  N  ALA C  51   O  PHE C  63           
SHEET    3   M 4 PHE D  48  VAL D  55 -1  O  THR D  54   N  LYS C  49           
SHEET    4   M 4 ILE D  61  PHE D  63 -1  O  PHE D  63   N  ALA D  51           
SHEET    1   N 5 MET C 109  THR C 114  0                                        
SHEET    2   N 5 GLY C 272  PRO C 277 -1  O  LEU C 274   N  CYS C 112           
SHEET    3   N 5 VAL C 255  SER C 260 -1  N  ARG C 257   O  THR C 275           
SHEET    4   N 5 LEU C 226  ASP C 230  1  N  ILE C 227   O  ILE C 256           
SHEET    5   N 5 PHE C 193  THR C 196  1  N  THR C 196   O  ILE C 228           
SHEET    1   O 2 ASN C 134  LEU C 137  0                                        
SHEET    2   O 2 ASN C 155  ASN C 158  1  O  ILE C 157   N  VAL C 135           
SHEET    1   P 2 SER C 161  ASP C 162  0                                        
SHEET    2   P 2 GLY C 165  ILE C 166 -1  O  GLY C 165   N  ASP C 162           
SHEET    1   Q 4 ALA C 345  TRP C 347  0                                        
SHEET    2   Q 4 PHE C 355  VAL C 360 -1  O  LYS C 359   N  GLU C 346           
SHEET    3   Q 4 TYR C 397  SER C 401 -1  O  ALA C 400   N  LEU C 356           
SHEET    4   Q 4 LEU C 382  PRO C 383 -1  N  LEU C 382   O  ARG C 399           
SHEET    1   R 2 VAL C 379  LEU C 380  0                                        
SHEET    2   R 2 ILE D  34  SER D  35  1  O  ILE D  34   N  LEU C 380           
SHEET    1   S 7 MET D 109  THR D 114  0                                        
SHEET    2   S 7 GLY D 272  PRO D 277 -1  O  LEU D 274   N  CYS D 112           
SHEET    3   S 7 VAL D 255  SER D 260 -1  N  ARG D 257   O  THR D 275           
SHEET    4   S 7 LEU D 226  ASP D 230  1  N  GLU D 229   O  ILE D 256           
SHEET    5   S 7 PHE D 193  THR D 196  1  N  THR D 196   O  ILE D 228           
SHEET    6   S 7 ASN D 134  LEU D 137  1  N  LEU D 136   O  TYR D 195           
SHEET    7   S 7 ASN D 155  ASN D 158  1  O  ILE D 157   N  VAL D 135           
SHEET    1   T 2 SER D 161  ASP D 162  0                                        
SHEET    2   T 2 GLY D 165  ILE D 166 -1  O  GLY D 165   N  ASP D 162           
SHEET    1   U 4 ALA D 345  TRP D 347  0                                        
SHEET    2   U 4 PHE D 355  VAL D 360 -1  O  LYS D 359   N  GLU D 346           
SHEET    3   U 4 TYR D 397  SER D 401 -1  O  ALA D 400   N  LEU D 356           
SHEET    4   U 4 LEU D 382  PRO D 383 -1  N  LEU D 382   O  ARG D 399           
CISPEP   1 ARG A   28    GLY A   29          0        -1.06                     
CISPEP   2 GLU A  139    PRO A  140          0         0.30                     
CISPEP   3 ASN A  202    PRO A  203          0        13.65                     
CISPEP   4 GLU B  139    PRO B  140          0         2.28                     
CISPEP   5 ASN B  202    PRO B  203          0        13.99                     
CISPEP   6 GLU C  139    PRO C  140          0         1.02                     
CISPEP   7 ASN C  202    PRO C  203          0        13.30                     
CISPEP   8 ARG D   28    GLY D   29          0        -8.50                     
CISPEP   9 GLU D  139    PRO D  140          0         1.09                     
CISPEP  10 ASN D  202    PRO D  203          0        12.62                     
SITE     1 AC1 22 SER A 117  GLN A 118  TYR A 142  VAL A 197                    
SITE     2 AC1 22 ASN A 202  ASP A 230  PRO A 232  TYR A 233                    
SITE     3 AC1 22 SER A 260  SER A 262  LYS A 263  ARG A 270                    
SITE     4 AC1 22 PHE A 355  ARG A 399  HOH A4387  ILE B  19                    
SITE     5 AC1 22 ARG B  20  THR B  23  GLY B  39  TYR B  74                    
SITE     6 AC1 22 SER B  75  SER B  77                                          
SITE     1 AC2 25 ILE A  19  ARG A  20  THR A  23  GLY A  39                    
SITE     2 AC2 25 LEU A  40  TYR A  74  SER A  75  SER A  77                    
SITE     3 AC2 25 LEU A 293  SER B 117  GLN B 118  TYR B 142                    
SITE     4 AC2 25 VAL B 197  ASN B 202  ASP B 230  PRO B 232                    
SITE     5 AC2 25 TYR B 233  SER B 260  SER B 262  LYS B 263                    
SITE     6 AC2 25 ARG B 270  PHE B 355  ARG B 399  HOH B4113                    
SITE     7 AC2 25 HOH B4260                                                     
SITE     1 AC3 24 SER C 117  GLN C 118  TYR C 142  VAL C 197                    
SITE     2 AC3 24 ASN C 202  ASP C 230  PRO C 232  TYR C 233                    
SITE     3 AC3 24 SER C 260  SER C 262  LYS C 263  ARG C 270                    
SITE     4 AC3 24 PHE C 355  ARG C 399  HOH C4163  ILE D  19                    
SITE     5 AC3 24 ARG D  20  THR D  23  GLY D  39  LEU D  40                    
SITE     6 AC3 24 TYR D  74  SER D  75  SER D  77  LEU D 293                    
SITE     1 AC4 22 ILE C  19  ARG C  20  THR C  23  GLY C  39                    
SITE     2 AC4 22 TYR C  74  SER C  75  SER C  77  LEU C 293                    
SITE     3 AC4 22 SER D 117  GLN D 118  TYR D 142  VAL D 197                    
SITE     4 AC4 22 ASN D 202  ASP D 230  PRO D 232  TYR D 233                    
SITE     5 AC4 22 SER D 260  SER D 262  LYS D 263  ARG D 270                    
SITE     6 AC4 22 PHE D 355  ARG D 399                                          
CRYST1   69.155  107.050  116.599  90.00  94.52  90.00 P 1 21 1      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      0.014460  0.000000  0.001143        0.00000                         
SCALE2      0.000000  0.009341  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008603        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system