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Database: PDB
Entry: 5EFS
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HEADER    TRANSFERASE                             26-OCT-15   5EFS              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
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    KYNURENINE AMINOTRANSFERASE II, TRANSFERASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.NEMATOLLAHI,G.SUN,A.KWAN,S.J.HARROP,J.R.HANRAHAN,N.A.NADVI,         
AUTHOR   2 W.B.CHURCH                                                           
REVDAT   1   11-NOV-15 5EFS    0                                                
JRNL        AUTH   A.NEMATOLLAHI,G.SUN,A.KWAN,C.M.JEFFRIES,S.J.HARROP,          
JRNL        AUTH 2 J.R.HANRAHAN,N.A.NADVI,W.B.CHURCH                            
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE   
JRNL        TITL 2 II                                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 39646                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1942                            
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 40.4724 -  4.3975    1.00     3032   152  0.1749 0.2007        
REMARK   3     2  4.3975 -  3.4910    1.00     2867   148  0.1537 0.1617        
REMARK   3     3  3.4910 -  3.0499    1.00     2835   147  0.1647 0.2068        
REMARK   3     4  3.0499 -  2.7711    1.00     2800   145  0.1697 0.1995        
REMARK   3     5  2.7711 -  2.5725    0.99     2771   143  0.1749 0.2091        
REMARK   3     6  2.5725 -  2.4209    0.99     2769   143  0.1646 0.1684        
REMARK   3     7  2.4209 -  2.2997    0.98     2740   140  0.1604 0.1630        
REMARK   3     8  2.2997 -  2.1996    0.98     2720   140  0.1629 0.2303        
REMARK   3     9  2.1996 -  2.1149    0.97     2699   142  0.1683 0.1751        
REMARK   3    10  2.1149 -  2.0419    0.97     2672   141  0.1709 0.1928        
REMARK   3    11  2.0419 -  1.9781    0.95     2632   135  0.1733 0.1845        
REMARK   3    12  1.9781 -  1.9215    0.95     2622   133  0.1867 0.2242        
REMARK   3    13  1.9215 -  1.8709    0.93     2553   129  0.2023 0.2162        
REMARK   3    14  1.8709 -  1.8253    0.72     1992   104  0.2111 0.2266        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.070           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.44                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.28                          
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      :  0.004           3415                                  
REMARK   3   ANGLE     :  0.709           4636                                  
REMARK   3   CHIRALITY :  0.046            515                                  
REMARK   3   PLANARITY :  0.004            600                                  
REMARK   3   DIHEDRAL  : 21.667           2079                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  16.7643  26.9686  29.4014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0252 T22:   0.0001                                     
REMARK   3      T33:   0.0188 T12:  -0.0001                                     
REMARK   3      T13:   0.0125 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3625 L22:   0.4967                                     
REMARK   3      L33:   0.3287 L12:   0.0345                                     
REMARK   3      L13:   0.0100 L23:  -0.2610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0412 S12:   0.0009 S13:  -0.0190                       
REMARK   3      S21:  -0.1097 S22:   0.0044 S23:  -0.0147                       
REMARK   3      S31:   0.0060 S32:  -0.0318 S33:  -0.0089                       
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 5EFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214799.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40804                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.825                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.30                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.80500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER PHASER MODULE: 2.6.0                           
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM NACL, 0.1M NACITRATE PH 5.6,      
REMARK 280  24% PEG4K, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  300K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.11800            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       51.22750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       51.22750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.67700            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       51.22750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       51.22750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       21.55900            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       51.22750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.22750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       64.67700            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       51.22750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.22750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       21.55900            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       43.11800            
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: 8210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       86.23600            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 602  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 730  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 783  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 856  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 954  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 958  LIES ON A SPECIAL POSITION.                          
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   H    ASN A    57     O    HOH A   508              1.56            
REMARK 500   O    HOH A   571     O    HOH A   707              1.98            
REMARK 500   O    HOH A   698     O    HOH A   914              2.06            
REMARK 500   O    HOH A   580     O    HOH A   899              2.07            
REMARK 500   O    HOH A   655     O    HOH A   884              2.07            
REMARK 500   O    HOH A   808     O    HOH A   909              2.11            
REMARK 500   O    HOH A   501     O    HOH A   877              2.11            
REMARK 500   O    HOH A   543     O    HOH A   560              2.13            
REMARK 500   O    HOH A   868     O    HOH A   889              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A  17   C     PRO A  18   N       0.198                       
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    ASN A  96       62.34     32.97                                   
REMARK 500    ASP A 162     -157.65   -136.16                                   
REMARK 500    SER A 266      129.17   -177.28                                   
REMARK 500    SER A 291      -97.71   -123.59                                   
REMARK 500    LEU A 293      -49.89     76.58                                   
REMARK 500    LYS A 373       52.00    -94.34                                   
REMARK 500    ALA A 374      -79.31   -103.41                                   
REMARK 500    LYS A 376      -73.05    -58.39                                   
REMARK 500    SER A 404      -31.59   -133.52                                   
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 LYS A  240     PHE A  241                  135.64                    
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 954        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A 955        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 956        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 957        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 958        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A 959        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH A 960        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A 961        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH A 962        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH A 963        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH A 964        DISTANCE =  8.51 ANGSTROMS                       
REMARK 525    HOH A 965        DISTANCE =  9.56 ANGSTROMS                       
REMARK 525    HOH A 966        DISTANCE = 11.04 ANGSTROMS                       
DBREF  5EFS A    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 LYS 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                          
FORMUL   2  HOH   *466(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  185  5                                   7    
HELIX   13 AB4 THR A  209  TYR A  223  1                                  15    
HELIX   14 AB5 PHE A  246  ASP A  250  5                                   5    
HELIX   15 AB6 LYS A  278  VAL A  290  1                                  13    
HELIX   16 AB7 SER A  296  LEU A  341  1                                  46    
HELIX   17 AB8 ASP A  365  GLU A  372  1                                   8    
HELIX   18 AB9 ASN A  385  TYR A  388  5                                   4    
HELIX   19 AC1 SER A  406  LEU A  425  1                                  20    
SHEET    1 AA1 2 ALA A  51  ILE A  53  0                                        
SHEET    2 AA1 2 ILE A  61  PHE A  63 -1  O  ILE A  61   N  ILE A  53           
SHEET    1 AA2 7 MET A 109  THR A 114  0                                        
SHEET    2 AA2 7 GLY A 272  PRO A 277 -1  O  LEU A 274   N  CYS A 112           
SHEET    3 AA2 7 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4 AA2 7 LEU A 226  ASP A 230  1  N  GLU A 229   O  ILE A 256           
SHEET    5 AA2 7 PHE A 193  THR A 196  1  N  LEU A 194   O  ILE A 228           
SHEET    6 AA2 7 ASN A 134  LEU A 137  1  N  LEU A 136   O  TYR A 195           
SHEET    7 AA2 7 ASN A 155  ASN A 158  1  O  ILE A 157   N  VAL A 135           
SHEET    1 AA3 2 SER A 161  ASP A 162  0                                        
SHEET    2 AA3 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1 AA4 4 ALA A 345  TRP A 347  0                                        
SHEET    2 AA4 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3 AA4 4 TYR A 397  SER A 401 -1  O  LEU A 398   N  ILE A 358           
SHEET    4 AA4 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
CISPEP   1 GLU A  139    PRO A  140          0        -0.97                     
CISPEP   2 ASN A  202    PRO A  203          0        16.95                     
CRYST1  102.455  102.455   86.236  90.00  90.00  90.00 P 43 21 2     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      0.009760  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009760  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011596        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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