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Database: PDB
Entry: 4GEB
LinkDB: 4GEB
Original site: 4GEB 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-AUG-12   4GEB              
TITLE     KYNURENINE AMINOTRANSFERASE II INHIBITORS                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: KAT/AADAT, 2-AMINOADIPATE AMINOTRANSFERASE, 2-AMINOADIPATE  
COMPND   6 TRANSAMINASE, ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT, KYNURENINE 
COMPND   7 AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE AMINOTRANSFERASE II,   
COMPND   8 KYNURENINE--OXOGLUTARATE TRANSAMINASE 2, KYNURENINE--OXOGLUTARATE    
COMPND   9 TRANSAMINASE II;                                                     
COMPND  10 EC: 2.6.1.39, 2.6.1.7;                                               
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AADAT, KAT2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    AMINOTRANSFERASE, IRREVERSIBLE INHIBITOR, TRANSFERASE-TRANSFERASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PANDIT                                                              
REVDAT   2   22-MAY-13 4GEB    1       JRNL                                     
REVDAT   1   20-MAR-13 4GEB    0                                                
JRNL        AUTH   A.B.DOUNAY,M.ANDERSON,B.M.BECHLE,E.EVRARD,X.GAN,J.Y.KIM,     
JRNL        AUTH 2 L.A.MCALLISTER,J.PANDIT,S.RONG,M.A.SALAFIA,J.B.TUTTLE,       
JRNL        AUTH 3 L.E.ZAWADZKE,P.R.VERHOEST                                    
JRNL        TITL   PF-04859989 AS A TEMPLATE FOR STRUCTURE-BASED DRUG DESIGN:   
JRNL        TITL 2 IDENTIFICATION OF NEW PYRAZOLE SERIES OF IRREVERSIBLE KAT II 
JRNL        TITL 3 INHIBITORS WITH IMPROVED LIPOPHILIC EFFICIENCY.              
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  1961 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23466229                                                     
JRNL        DOI    10.1016/J.BMCL.2013.02.039                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 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) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.34                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 62237                          
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)  : 0.166                          
REMARK   3   R VALUE            (WORKING SET)  : 0.165                          
REMARK   3   FREE R VALUE                      : 0.192                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3152                           
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) : 2.15                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.21                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.71                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3925                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2089                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3715                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2069                   
REMARK   3   BIN FREE R VALUE                        : 0.2478                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.35                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 210                      
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            : 6688                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 86                                      
REMARK   3   SOLVENT ATOMS            : 805                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.07670                                             
REMARK   3    B22 (A**2) : 1.60070                                              
REMARK   3    B33 (A**2) : 0.47600                                              
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) : 0.22                
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) : 0.17                
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      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6940   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9436   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2352   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 164    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1002   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6940   ; 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   : 902    ; 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   : 8436   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.40                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.36                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|1 - A|428 A|999 - A|999 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):    2.5778   14.0130  -49.8078           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1295 T22:   -0.0838                                    
REMARK   3     T33:   -0.0650 T12:    0.0047                                    
REMARK   3     T13:    0.0013 T23:   -0.0135                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7317 L22:    0.7215                                    
REMARK   3     L33:    0.7000 L12:    0.0103                                    
REMARK   3     L13:    0.1571 L23:   -0.1776                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0237 S12:    0.0649 S13:   -0.0555                     
REMARK   3     S21:   -0.0448 S22:   -0.0165 S23:   -0.1086                     
REMARK   3     S31:    0.0486 S32:    0.0670 S33:   -0.0072                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|1 - B|428 B|999 - B|999 }                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.2507   -7.3397  -33.6429           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0681 T22:   -0.0561                                    
REMARK   3     T33:   -0.0744 T12:    0.0000                                    
REMARK   3     T13:   -0.0078 T23:    0.0122                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3778 L22:    0.5828                                    
REMARK   3     L33:    0.5581 L12:    0.0616                                    
REMARK   3     L13:   -0.1713 L23:   -0.2251                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0017 S12:   -0.0083 S13:   -0.0596                     
REMARK   3     S21:    0.0014 S22:    0.0036 S23:   -0.0096                     
REMARK   3     S31:    0.1008 S32:   -0.0409 S33:   -0.0053                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GEB 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 RCSB074075.                                      
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   : 62519                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.147                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 116.523                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3UE8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92                     
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       42.80800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.26150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.34100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.26150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.80800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.34100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 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: 10000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -126.0 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     ARG A   429                                                      
REMARK 465     GLY A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     LEU A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     ARG B   429                                                      
REMARK 465     GLY B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     LEU B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: 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   O    HOH B   638     O    HOH B   658              2.19            
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    GLU A  56      102.98    -56.38                                   
REMARK 500    ASN A  96       60.54     36.84                                   
REMARK 500    ASP A 162     -157.64   -142.41                                   
REMARK 500    ASN A 189       59.16   -113.49                                   
REMARK 500    ASP A 231       61.14   -118.92                                   
REMARK 500    SER A 266      131.05   -179.65                                   
REMARK 500    SER A 291      -88.32   -118.96                                   
REMARK 500    LEU A 293      -54.42     76.58                                   
REMARK 500    SER A 296      122.22    -39.73                                   
REMARK 500    LYS A 361      -79.63    -53.80                                   
REMARK 500    GLU A 372      -65.46   -126.79                                   
REMARK 500    LEU A 426       47.09    -90.81                                   
REMARK 500    ASN B  96       61.04     36.17                                   
REMARK 500    ASN B 189       57.80   -111.19                                   
REMARK 500    ASP B 231       61.43   -119.93                                   
REMARK 500    SER B 266      130.79   -178.47                                   
REMARK 500    SER B 291      -89.16   -118.46                                   
REMARK 500    LEU B 293      -54.08     76.32                                   
REMARK 500    SER B 296      122.73    -38.97                                   
REMARK 500    GLU B 372      -63.45   -128.53                                   
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  19        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 129        23.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 319        22.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 361        21.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 129        23.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 319        22.7      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 A 739        DISTANCE =  7.64 ANGSTROMS                       
REMARK 525    HOH A 834        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH A 840        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 876        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 879        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A 882        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH A 884        DISTANCE = 11.23 ANGSTROMS                       
REMARK 525    HOH A 895        DISTANCE = 14.09 ANGSTROMS                       
REMARK 525    HOH A 928        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A 950        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A 962        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH A 963        DISTANCE =  7.97 ANGSTROMS                       
REMARK 525    HOH B 736        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 868        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH B 901        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH B 908        DISTANCE =  8.37 ANGSTROMS                       
REMARK 525    HOH B 924        DISTANCE =  9.75 ANGSTROMS                       
REMARK 525    HOH B 939        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH B 967        DISTANCE = 10.07 ANGSTROMS                       
REMARK 525    HOH B 970        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH B 978        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH B 983        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH B 984        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH B1009        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B1015        DISTANCE =  6.24 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0LD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0LD B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 504                 
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: 4GE9   RELATED DB: PDB                                   
DBREF  4GEB A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  4GEB B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 4GEB SER A  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GEB GLY A  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GEB LEU A  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB VAL A  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB PRO A  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB ARG A  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB GLY A  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB SER A  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB LEU A  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB GLU A  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS A  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS A  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS A  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS A  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS A  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS A  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB SER B  240  UNP  Q8N5Z0    LYS   240 ENGINEERED MUTATION            
SEQADV 4GEB GLY B  241  UNP  Q8N5Z0    PHE   241 ENGINEERED MUTATION            
SEQADV 4GEB LEU B  426  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB VAL B  427  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB PRO B  428  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB ARG B  429  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB GLY B  430  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB SER B  431  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB LEU B  432  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB GLU B  433  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS B  434  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS B  435  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS B  436  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS B  437  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS B  438  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 4GEB HIS B  439  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQRES   1 A  439  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 A  439  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 A  439  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 A  439  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 A  439  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 A  439  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 A  439  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 A  439  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 A  439  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 A  439  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 A  439  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 A  439  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 A  439  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 A  439  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 A  439  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 A  439  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 A  439  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 A  439  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 A  439  PHE LEU GLN PHE ASN SER GLY ARG VAL PRO THR PHE LEU          
SEQRES  20 A  439  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 A  439  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 A  439  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 A  439  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 A  439  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 A  439  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 A  439  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 A  439  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 A  439  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 A  439  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 A  439  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 A  439  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 A  439  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 A  439  LEU ALA GLN LEU ILE LYS GLU SER LEU LEU VAL PRO ARG          
SEQRES  34 A  439  GLY SER LEU GLU HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  439  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 B  439  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 B  439  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 B  439  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 B  439  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 B  439  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 B  439  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 B  439  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 B  439  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 B  439  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 B  439  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 B  439  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 B  439  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 B  439  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 B  439  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 B  439  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 B  439  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 B  439  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 B  439  PHE LEU GLN PHE ASN SER GLY ARG VAL PRO THR PHE LEU          
SEQRES  20 B  439  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 B  439  PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 B  439  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 B  439  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 B  439  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 B  439  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 B  439  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 B  439  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 B  439  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 B  439  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 B  439  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 B  439  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 B  439  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 B  439  LEU ALA GLN LEU ILE LYS GLU SER LEU LEU VAL PRO ARG          
SEQRES  34 B  439  GLY SER LEU GLU HIS HIS HIS HIS HIS HIS                      
HET    0LD  A 501      33                                                       
HET    SO4  A 502       5                                                       
HET    0LD  B 501      33                                                       
HET    SO4  B 502       5                                                       
HET    SO4  B 503       5                                                       
HET    SO4  B 504       5                                                       
HETNAM     0LD (5-HYDROXY-4-{[(7-HYDROXY-6-OXO-2-PHENYL-6,7-DIHYDRO-            
HETNAM   2 0LD  2H-PYRAZOLO[3,4-B]PYRIDIN-5-YL)AMINO]METHYL}-6-                 
HETNAM   3 0LD  METHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  0LD    2(C20 H20 N5 O7 P)                                           
FORMUL   4  SO4    4(O4 S 2-)                                                   
FORMUL   9  HOH   *805(H2 O)                                                    
HELIX    1   1 ASN A    2  ILE A    7  5                                   6    
HELIX    2   2 THR A    8  ARG A   14  1                                   7    
HELIX    3   3 SER A   17  SER A   27  1                                  11    
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 GLY A  116  ILE A  129  1                                  14    
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 TYR A  233  GLN A  237  5                                   5    
HELIX   16  16 PHE A  246  ASP A  250  5                                   5    
HELIX   17  17 LYS A  278  VAL A  290  1                                  13    
HELIX   18  18 SER A  296  THR A  342  1                                  47    
HELIX   19  19 VAL A  366  GLU A  372  1                                   7    
HELIX   20  20 GLU A  372  MET A  377  1                                   6    
HELIX   21  21 ASN A  385  TYR A  388  5                                   4    
HELIX   22  22 SER A  406  LEU A  426  1                                  21    
HELIX   23  23 ASN B    2  PHE B    6  5                                   5    
HELIX   24  24 THR B    8  ARG B   14  1                                   7    
HELIX   25  25 SER B   17  SER B   27  1                                  11    
HELIX   26  26 ASN B   42  PHE B   46  5                                   5    
HELIX   27  27 GLY B   64  LEU B   72  1                                   9    
HELIX   28  28 ILE B   80  ASN B   96  1                                  17    
HELIX   29  29 PRO B  103  GLY B  107  5                                   5    
HELIX   30  30 GLY B  116  ILE B  129  1                                  14    
HELIX   31  31 TYR B  142  HIS B  150  1                                   9    
HELIX   32  32 PRO B  151  GLY B  153  5                                   3    
HELIX   33  33 VAL B  167  SER B  176  1                                  10    
HELIX   34  34 ARG B  177  TRP B  178  5                                   2    
HELIX   35  35 LYS B  179  ASN B  185  5                                   7    
HELIX   36  36 THR B  209  TYR B  223  1                                  15    
HELIX   37  37 TYR B  233  GLN B  237  5                                   5    
HELIX   38  38 PHE B  246  ASP B  250  5                                   5    
HELIX   39  39 LYS B  278  VAL B  290  1                                  13    
HELIX   40  40 SER B  296  THR B  342  1                                  47    
HELIX   41  41 VAL B  366  GLU B  372  1                                   7    
HELIX   42  42 GLU B  372  MET B  377  1                                   6    
HELIX   43  43 ASN B  385  TYR B  388  5                                   4    
HELIX   44  44 SER B  406  VAL B  427  1                                  22    
SHEET    1   A 2 ILE A  34  SER A  35  0                                        
SHEET    2   A 2 VAL B 379  LEU B 380  1  O  LEU B 380   N  ILE A  34           
SHEET    1   B 4 LYS A  59  PHE A  63  0                                        
SHEET    2   B 4 PHE A  48  VAL A  55 -1  N  ILE A  53   O  ILE A  61           
SHEET    3   B 4 PHE B  48  VAL B  55 -1  O  THR B  54   N  LYS A  49           
SHEET    4   B 4 LYS B  59  PHE B  63 -1  O  ILE B  61   N  ILE B  53           
SHEET    1   C 7 MET A 109  THR A 114  0                                        
SHEET    2   C 7 GLY A 272  PRO A 277 -1  O  LEU A 274   N  CYS A 112           
SHEET    3   C 7 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4   C 7 LEU A 226  ASP A 230  1  N  GLU A 229   O  ALA A 258           
SHEET    5   C 7 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    6   C 7 ASN A 134  LEU A 137  1  N  LEU A 136   O  TYR A 195           
SHEET    7   C 7 ASN A 155  ASN A 158  1  O  ILE A 157   N  VAL A 135           
SHEET    1   D 2 SER A 161  ASP A 162  0                                        
SHEET    2   D 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1   E 4 ALA A 345  TRP A 347  0                                        
SHEET    2   E 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3   E 4 TYR A 397  SER A 401 -1  O  LEU A 398   N  ILE A 358           
SHEET    4   E 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1   F 2 VAL A 379  LEU A 380  0                                        
SHEET    2   F 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1   G 7 MET B 109  THR B 114  0                                        
SHEET    2   G 7 GLY B 272  PRO B 277 -1  O  GLY B 272   N  THR B 114           
SHEET    3   G 7 VAL B 255  SER B 260 -1  N  ARG B 257   O  THR B 275           
SHEET    4   G 7 LEU B 226  ASP B 230  1  N  GLU B 229   O  ILE B 256           
SHEET    5   G 7 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    6   G 7 ASN B 134  LEU B 137  1  N  LEU B 136   O  TYR B 195           
SHEET    7   G 7 ASN B 155  ASN B 158  1  O  ILE B 157   N  VAL B 135           
SHEET    1   H 2 SER B 161  ASP B 162  0                                        
SHEET    2   H 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1   I 4 ALA B 345  TRP B 347  0                                        
SHEET    2   I 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3   I 4 TYR B 397  SER B 401 -1  O  LEU B 398   N  ILE B 358           
SHEET    4   I 4 LEU B 382  PRO B 383 -1  N  LEU B 382   O  ARG B 399           
CISPEP   1 GLU A   56    ASN A   57          0        -8.04                     
CISPEP   2 GLU A  139    PRO A  140          0        -2.31                     
CISPEP   3 ASN A  202    PRO A  203          0        18.91                     
CISPEP   4 GLU B   56    ASN B   57          0       -12.54                     
CISPEP   5 GLU B  139    PRO B  140          0        -2.65                     
CISPEP   6 ASN B  202    PRO B  203          0        18.22                     
SITE     1 AC1 20 GLY A 116  SER A 117  GLN A 118  TYR A 142                    
SITE     2 AC1 20 ASN A 202  ASP A 230  PRO A 232  TYR A 233                    
SITE     3 AC1 20 SER A 260  SER A 262  LYS A 263  ARG A 270                    
SITE     4 AC1 20 ARG A 399  HOH A 807  HOH A 856  ILE B  19                    
SITE     5 AC1 20 GLY B  39  LEU B  40  TYR B  74  SER B  75                    
SITE     1 AC2  6 ARG A 177  TRP A 178  LYS A 188  ASN A 189                    
SITE     2 AC2  6 HOH A 703  HOH A 714                                          
SITE     1 AC3 19 GLY A  39  LEU A  40  TYR A  74  SER A  75                    
SITE     2 AC3 19 GLY B 116  SER B 117  GLN B 118  TYR B 142                    
SITE     3 AC3 19 ASN B 202  ASP B 230  PRO B 232  TYR B 233                    
SITE     4 AC3 19 SER B 260  SER B 262  LYS B 263  ARG B 270                    
SITE     5 AC3 19 ARG B 399  HOH B 792  HOH B 802                               
SITE     1 AC4 10 GLN A 119  LYS A 123  SER A 291  THR A 292                    
SITE     2 AC4 10 GLN B 119  LYS B 123  SER B 291  THR B 292                    
SITE     3 AC4 10 HOH B 789  HOH B1010                                          
SITE     1 AC5  5 ARG B 177  TRP B 178  LYS B 188  ASN B 189                    
SITE     2 AC5  5 HOH B 753                                                     
SITE     1 AC6  3 HIS A 101  HOH A 742  ARG B 242                               
CRYST1   85.616  114.682  116.523  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      0.011680  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008582        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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