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Database: PDB
Entry: 5TF5
LinkDB: 5TF5
Original site: 5TF5 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-SEP-16   5TF5              
TITLE     CRYSTAL STRUCTURE OF HUMAN KAT-2 IN COMPLEX WITH A REVERSIBLE         
TITLE    2 INHIBITOR                                                            
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                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AADAT, KAT2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    NS-1502, REVERSIBLE KAT-2 INHIBITOR, LLP, TRANSFERASE-TRANSFERASE     
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.NEMATOLLAHI,G.SUN,W.B.CHURCH                                        
REVDAT   2   12-JUL-17 5TF5    1       JRNL   REMARK                            
REVDAT   1   05-OCT-16 5TF5    0                                                
JRNL        AUTH   A.NEMATOLLAHI,G.SUN,G.JAYAWICKRAMA,J.R.HANRAHAN,W.B.CHURCH   
JRNL        TITL   CRYSTAL STRUCTURE AND MECHANISTIC ANALYSIS OF A NOVEL HUMAN  
JRNL        TITL 2 KYNURENINE AMINOTRANSFERASE-2 REVERSIBLE INHIBITOR           
JRNL        REF    MED.CHEM.RES.                              2017              
JRNL        REFN                   ISSN 1054-2523                               
JRNL        DOI    10.1007/S00044-017-1950-6                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: 2015)                           
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 86456                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1986                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.1414 -  4.3544    1.00     6457   151  0.1921 0.2097        
REMARK   3     2  4.3544 -  3.4566    1.00     6217   148  0.1917 0.2128        
REMARK   3     3  3.4566 -  3.0197    1.00     6174   141  0.1985 0.2127        
REMARK   3     4  3.0197 -  2.7437    1.00     6150   144  0.2030 0.2560        
REMARK   3     5  2.7437 -  2.5470    1.00     6114   147  0.2006 0.1939        
REMARK   3     6  2.5470 -  2.3969    1.00     6106   143  0.1940 0.2332        
REMARK   3     7  2.3969 -  2.2768    1.00     6130   148  0.2053 0.2396        
REMARK   3     8  2.2768 -  2.1777    0.98     5960   126  0.2861 0.3189        
REMARK   3     9  2.1777 -  2.0939    1.00     6076   156  0.2223 0.2852        
REMARK   3    10  2.0939 -  2.0216    0.98     5960   125  0.2643 0.2954        
REMARK   3    11  2.0216 -  1.9584    1.00     6075   143  0.2370 0.2773        
REMARK   3    12  1.9584 -  1.9024    0.92     5536   141  0.4122 0.4317        
REMARK   3    13  1.9024 -  1.8524    0.98     5944   134  0.3340 0.3636        
REMARK   3    14  1.8524 -  1.8072    0.92     5571   139  0.2594 0.2711        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           6886                                  
REMARK   3   ANGLE     :  0.843           9354                                  
REMARK   3   CHIRALITY :  0.049           1030                                  
REMARK   3   PLANARITY :  0.005           1203                                  
REMARK   3   DIHEDRAL  : 15.268           4174                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222794.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-16                          
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               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87159                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.807                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.126                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.05748                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.460                              
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: 5EUN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (1 UL) AT A CONCENTRATION OF 7   
REMARK 280  MG/ML WERE MIXED WITH AN EQUAL VOLUME OF A RESERVOIR SOLUTION       
REMARK 280  CONTAINING 200 MM NACL, 0.1M NACITRATE PH 5.6, 24% PEG4K, 1.5MM     
REMARK 280  DDT AND EQUILIBRATED AGAINST 1 ML OF A RESERVOIR SOLUTION AT 293    
REMARK 280  K., VAPOR DIFFUSION, HANGING DROP                                   
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       44.44150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.96150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.63750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.96150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.44150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.63750            
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: 8120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 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   HE   ARG A   172     O    HOH A   515              1.58            
REMARK 500   OE1  GLN A   118     HH   TYR A   142              1.59            
REMARK 500   H    ASN B    57     O    HOH B   612              1.59            
REMARK 500   O    HOH A   521     O    HOH A   748              2.03            
REMARK 500   O    HOH A   548     O    HOH A   697              2.03            
REMARK 500   O    HOH B   805     O    HOH B   878              2.04            
REMARK 500   O    HOH B   868     O    HOH B   871              2.07            
REMARK 500   O    HOH B   851     O    HOH B   855              2.07            
REMARK 500   O    HOH B   681     O    HOH B   858              2.07            
REMARK 500   O    HOH A   816     O    HOH A   819              2.15            
REMARK 500   O    HOH B   937     O    HOH B   948              2.17            
REMARK 500   O    PRO A    16     O    HOH A   501              2.17            
REMARK 500   O    HOH A   773     O    HOH A   774              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN A   106     HZ2  LYS B   240     2655     1.48            
REMARK 500   O    HOH A   786     O    HOH B   922     1655     2.00            
REMARK 500   O    HOH A   738     O    HOH B   920     3745     2.04            
REMARK 500   O    HOH A   531     O    HOH B   879     3745     2.09            
REMARK 500   O    HOH A   810     O    HOH B   951     2655     2.15            
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    PRO A  18     -170.64    -63.58                                   
REMARK 500    ARG A  20     -113.46   -100.38                                   
REMARK 500    MET A  22      -46.39   -132.51                                   
REMARK 500    ASN A  96       61.13     32.11                                   
REMARK 500    ARG A 270       70.32     50.25                                   
REMARK 500    SER A 291     -101.88   -123.72                                   
REMARK 500    LEU A 293      -51.84     78.28                                   
REMARK 500    THR A 342       42.43   -107.64                                   
REMARK 500    ILE A 370      -61.09    -99.72                                   
REMARK 500    GLU A 372      -63.63   -109.11                                   
REMARK 500    PRO B  18     -171.47    -68.92                                   
REMARK 500    ARG B  20     -114.55   -100.36                                   
REMARK 500    THR B  21       63.74    -69.84                                   
REMARK 500    MET B  22      -45.56   -135.36                                   
REMARK 500    ASN B  96       62.06     29.06                                   
REMARK 500    ASP B 162     -154.00   -138.04                                   
REMARK 500    PRO B 186        4.97    -66.80                                   
REMARK 500    ASN B 189       60.67     60.99                                   
REMARK 500    SER B 266      129.14   -175.42                                   
REMARK 500    ARG B 270       71.92     53.87                                   
REMARK 500    SER B 291     -105.62   -121.86                                   
REMARK 500    LEU B 293      -50.85     74.71                                   
REMARK 500    THR B 342       41.65   -106.10                                   
REMARK 500    MET B 354       21.12   -142.22                                   
REMARK 500    ILE B 370      -64.25    -98.77                                   
REMARK 500    SER B 404      -34.78   -131.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A   17     PRO A   18                 -146.51                    
REMARK 500 LYS A  188     ASN A  189                  138.58                    
REMARK 500 SER B   17     PRO B   18                 -144.52                    
REMARK 500 LYS B  188     ASN B  189                  140.52                    
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 822        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 823        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A 824        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A 825        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A 826        DISTANCE =  8.96 ANGSTROMS                       
REMARK 525    HOH B 953        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B 954        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH B 955        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH B 956        DISTANCE =  9.19 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7AR B 501                 
DBREF  5TF5 A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  5TF5 B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQRES   1 A  425  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 A  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 A  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 A  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 A  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 A  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 A  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 A  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 A  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 A  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 A  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 A  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 A  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 A  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 A  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 A  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 A  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 A  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 A  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 A  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 A  425  PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 A  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 A  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 A  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 A  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 A  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 A  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 A  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 A  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 A  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 A  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 A  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 A  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
SEQRES   1 B  425  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 B  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 B  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 B  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 B  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 B  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 B  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 B  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 B  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 B  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 B  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 B  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 B  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 B  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 B  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 B  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 B  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 B  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 B  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 B  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 B  425  PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 B  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 B  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 B  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 B  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 B  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 B  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 B  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 B  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 B  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 B  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 B  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 B  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
MODRES 5TF5 LLP A  263  LYS  MODIFIED RESIDUE                                   
MODRES 5TF5 LLP B  263  LYS  MODIFIED RESIDUE                                   
HET    LLP  A 263      24                                                       
HET    LLP  B 263      24                                                       
HET    7AR  B 501      24                                                       
HETNAM     LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-                           
HETNAM   2 LLP  (PHOSPHONOOXYMETHYL)PYRIDIN-4-                                  
HETNAM   3 LLP  YL]METHYLIDENEAMINO]HEXANOIC ACID                               
HETNAM     7AR (2R)-2-(5,6-DICHLORO-1,3-DIOXO-1,3-DIHYDRO-2H-ISOINDOL-          
HETNAM   2 7AR  2-YL)-3-PHENYLPROPANOIC ACID                                    
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
FORMUL   1  LLP    2(C14 H22 N3 O7 P)                                           
FORMUL   3  7AR    C17 H11 CL2 N O4                                             
FORMUL   4  HOH   *682(H2 O)                                                    
HELIX    1 AA1 ASN A    2  ILE A    7  5                                   6    
HELIX    2 AA2 THR A    8  ARG A   14  1                                   7    
HELIX    3 AA3 ASN A   42  PHE A   46  5                                   5    
HELIX    4 AA4 GLY A   64  LEU A   72  1                                   9    
HELIX    5 AA5 ILE A   80  ASN A   96  1                                  17    
HELIX    6 AA6 PRO A  103  GLY A  107  5                                   5    
HELIX    7 AA7 GLY A  116  ILE A  129  1                                  14    
HELIX    8 AA8 TYR A  142  HIS A  150  1                                   9    
HELIX    9 AA9 PRO A  151  GLY A  153  5                                   3    
HELIX   10 AB1 VAL A  167  SER A  176  1                                  10    
HELIX   11 AB2 ARG A  177  TRP A  178  5                                   2    
HELIX   12 AB3 LYS A  179  ASN A  189  5                                  11    
HELIX   13 AB4 THR A  209  TYR A  223  1                                  15    
HELIX   14 AB5 TYR A  233  GLN A  237  5                                   5    
HELIX   15 AB6 PHE A  246  ASP A  250  5                                   5    
HELIX   16 AB7 LYS A  278  VAL A  290  1                                  13    
HELIX   17 AB8 SER A  296  LEU A  341  1                                  46    
HELIX   18 AB9 VAL A  366  GLU A  372  1                                   7    
HELIX   19 AC1 GLU A  372  MET A  377  1                                   6    
HELIX   20 AC2 ASN A  385  TYR A  388  5                                   4    
HELIX   21 AC3 SER A  406  SER A  424  1                                  19    
HELIX   22 AC4 ASN B    2  ILE B    7  5                                   6    
HELIX   23 AC5 THR B    8  ARG B   14  1                                   7    
HELIX   24 AC6 ASN B   42  PHE B   46  5                                   5    
HELIX   25 AC7 GLY B   64  LEU B   72  1                                   9    
HELIX   26 AC8 ILE B   80  ASN B   96  1                                  17    
HELIX   27 AC9 PRO B  103  GLY B  107  5                                   5    
HELIX   28 AD1 GLY B  116  ILE B  129  1                                  14    
HELIX   29 AD2 TYR B  142  HIS B  150  1                                   9    
HELIX   30 AD3 PRO B  151  GLY B  153  5                                   3    
HELIX   31 AD4 VAL B  167  SER B  176  1                                  10    
HELIX   32 AD5 ARG B  177  TRP B  178  5                                   2    
HELIX   33 AD6 LYS B  179  ASN B  189  5                                  11    
HELIX   34 AD7 THR B  209  TYR B  223  1                                  15    
HELIX   35 AD8 TYR B  233  GLN B  237  5                                   5    
HELIX   36 AD9 PHE B  246  ASP B  250  5                                   5    
HELIX   37 AE1 LYS B  278  VAL B  290  1                                  13    
HELIX   38 AE2 SER B  296  LEU B  341  1                                  46    
HELIX   39 AE3 VAL B  366  GLU B  372  1                                   7    
HELIX   40 AE4 GLU B  372  MET B  377  1                                   6    
HELIX   41 AE5 ASN B  385  TYR B  388  5                                   4    
HELIX   42 AE6 SER B  406  GLU B  423  1                                  18    
SHEET    1 AA1 2 ILE A  34  SER A  35  0                                        
SHEET    2 AA1 2 VAL B 379  LEU B 380  1  O  LEU B 380   N  ILE A  34           
SHEET    1 AA2 4 ILE A  61  PHE A  63  0                                        
SHEET    2 AA2 4 PHE A  48  VAL A  55 -1  N  ILE A  53   O  ILE A  61           
SHEET    3 AA2 4 PHE B  48  VAL B  55 -1  O  THR B  54   N  LYS A  49           
SHEET    4 AA2 4 ILE B  61  PHE B  63 -1  O  ILE B  61   N  ILE B  53           
SHEET    1 AA3 7 MET A 109  THR A 114  0                                        
SHEET    2 AA3 7 GLY A 272  PRO A 277 -1  O  LEU A 274   N  CYS A 112           
SHEET    3 AA3 7 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4 AA3 7 LEU A 226  ASP A 230  1  N  ILE A 227   O  ILE A 256           
SHEET    5 AA3 7 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    6 AA3 7 ASN A 134  LEU A 137  1  N  LEU A 136   O  TYR A 195           
SHEET    7 AA3 7 ASN A 155  ASN A 158  1  O  ILE A 157   N  VAL A 135           
SHEET    1 AA4 2 SER A 161  ASP A 162  0                                        
SHEET    2 AA4 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1 AA5 4 ALA A 345  TRP A 347  0                                        
SHEET    2 AA5 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3 AA5 4 TYR A 397  SER A 401 -1  O  LEU A 398   N  ILE A 358           
SHEET    4 AA5 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1 AA6 2 VAL A 379  LEU A 380  0                                        
SHEET    2 AA6 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1 AA7 7 MET B 109  THR B 114  0                                        
SHEET    2 AA7 7 GLY B 272  PRO B 277 -1  O  LEU B 274   N  CYS B 112           
SHEET    3 AA7 7 VAL B 255  SER B 260 -1  N  ARG B 257   O  THR B 275           
SHEET    4 AA7 7 LEU B 226  ASP B 230  1  N  GLU B 229   O  ALA B 258           
SHEET    5 AA7 7 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    6 AA7 7 ASN B 134  LEU B 137  1  N  LEU B 136   O  TYR B 195           
SHEET    7 AA7 7 ASN B 155  ASN B 158  1  O  ILE B 157   N  VAL B 135           
SHEET    1 AA8 2 SER B 161  ASP B 162  0                                        
SHEET    2 AA8 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1 AA9 4 ALA B 345  TRP B 347  0                                        
SHEET    2 AA9 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3 AA9 4 TYR B 397  SER B 401 -1  O  ALA B 400   N  LEU B 356           
SHEET    4 AA9 4 LEU B 382  PRO B 383 -1  N  LEU B 382   O  ARG B 399           
LINK         C   SER A 262                 N   LLP A 263     1555   1555  1.33  
LINK         C   LLP A 263                 N   ILE A 264     1555   1555  1.41  
LINK         C   SER B 262                 N   LLP B 263     1555   1555  1.35  
LINK         C   LLP B 263                 N   ILE B 264     1555   1555  1.43  
CISPEP   1 GLU A  139    PRO A  140          0        -3.52                     
CISPEP   2 ASN A  202    PRO A  203          0        14.57                     
CISPEP   3 GLU B  139    PRO B  140          0        -0.06                     
CISPEP   4 ASN B  202    PRO B  203          0        17.05                     
SITE     1 AC1 17 ILE A  19  MET A  22  GLY A  39  PRO A  41                    
SITE     2 AC1 17 TYR A  74  HOH A 783  GLN B 118  TYR B 142                    
SITE     3 AC1 17 SER B 143  ASN B 202  TYR B 233  LLP B 263                    
SITE     4 AC1 17 MET B 354  PHE B 355  LEU B 382  PHE B 387                    
SITE     5 AC1 17 ARG B 399                                                     
CRYST1   88.883   99.275  107.923  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      0.011251  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010073  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009266        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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