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Database: PDB
Entry: 6D0A
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Original site: 6D0A 
HEADER    TRANSFERASE                             10-APR-18   6D0A              
TITLE     CRYSTAL STRUCTURE OF KYNURENINE AMINOTRANSFERASE-II IN APO-FORM, AT   
TITLE    2 1.47 A RESOLUTION                                                    
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;                                                     
COMPND  12 OTHER_DETAILS: THERE IS A HEXAHISTIDINE TAG ON THE N-TERMINAL END.   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AADAT, KAT2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, PLP-DEPENDENT, HEXAHISTIDINE TAG, ALPHA-BETA FOLD        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.JAYAWICKRAMA,G.SUN,A.NEMATOLLAHI,W.B.CHURCH                       
REVDAT   1   02-MAY-18 6D0A    0                                                
JRNL        AUTH   G.S.JAYAWICKRAMA,G.SUN,A.NEMATOLLAHI,W.B.CHURCH              
JRNL        TITL   CRYSTAL STRUCTURE OF KYNURENINE AMINOTRANSFERASE-II IN       
JRNL        TITL 2 APO-FORM                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.384                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 79169                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.526                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 45.9804 -  3.5378    1.00     5858   152  0.1763 0.1817        
REMARK   3     2  3.5378 -  2.8082    1.00     5636   146  0.1743 0.1833        
REMARK   3     3  2.8082 -  2.4532    1.00     5560   144  0.1777 0.2057        
REMARK   3     4  2.4532 -  2.2289    1.00     5545   143  0.1671 0.1762        
REMARK   3     5  2.2289 -  2.0692    1.00     5509   144  0.1655 0.1835        
REMARK   3     6  2.0692 -  1.9472    1.00     5490   142  0.1672 0.2148        
REMARK   3     7  1.9472 -  1.8497    1.00     5504   143  0.1752 0.1908        
REMARK   3     8  1.8497 -  1.7691    1.00     5448   141  0.1711 0.1736        
REMARK   3     9  1.7691 -  1.7010    1.00     5470   141  0.1758 0.1884        
REMARK   3    10  1.7010 -  1.6423    1.00     5463   142  0.1738 0.1894        
REMARK   3    11  1.6423 -  1.5910    1.00     5473   142  0.1758 0.1958        
REMARK   3    12  1.5910 -  1.5455    1.00     5428   140  0.1731 0.1802        
REMARK   3    13  1.5455 -  1.5048    1.00     5476   142  0.1772 0.1912        
REMARK   3    14  1.5048 -  1.4681    0.99     5309   138  0.1848 0.1988        
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)     : 0.107            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.288           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.49                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.03                          
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      :  0.009           3480                                  
REMARK   3   ANGLE     :  0.999           4724                                  
REMARK   3   CHIRALITY :  0.076            521                                  
REMARK   3   PLANARITY :  0.008            611                                  
REMARK   3   DIHEDRAL  : 11.605           1298                                  
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 6D0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233677.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-17                          
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79172                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.468                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.958                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.05847                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 41.0700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26930                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 11.61                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (1.12-2829:2017)                               
REMARK 200 STARTING MODEL: 5EUN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 10 MG/ML WAS MIXED WITH AN       
REMARK 280  EQUAL VOLUME OF A RESERVOIR SOLUTION CONTAINING 200 MM NACL, 0.1    
REMARK 280  M NACITRATE PH 5.6, 24% PEG4K AND EQUILIBRATED AGAINST 1 ML OF A    
REMARK 280  RESERVOIR SOLUTION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
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       43.24900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       51.38250            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       51.38250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.87350            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       51.38250            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       51.38250            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       21.62450            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       51.38250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.38250            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       64.87350            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       51.38250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.38250            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       21.62450            
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       43.24900            
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: 7830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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        0.00000            
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 566  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 767  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 796  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 873  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 979  LIES ON A SPECIAL POSITION.                          
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     ARG A    20                                                      
REMARK 475     THR A    21                                                      
REMARK 475     MET A    22                                                      
REMARK 475     THR A    23                                                      
REMARK 475     ASP A    24                                                      
REMARK 475     ILE A    25                                                      
REMARK 475     LEU A    26                                                      
REMARK 475     SER A    27                                                      
REMARK 475     ARG A    28                                                      
REMARK 475     GLY A    29                                                      
REMARK 475     PRO A    30                                                      
REMARK 475     LYS A    31                                                      
REMARK 475     SER A    32                                                      
REMARK 475     MET A    33                                                      
REMARK 475     LYS A   367                                                      
REMARK 475     GLU A   368                                                      
REMARK 475     LEU A   369                                                      
REMARK 475     ILE A   370                                                      
REMARK 475     GLU A   371                                                      
REMARK 475     GLU A   372                                                      
REMARK 475     LYS A   373                                                      
REMARK 475     ALA A   374                                                      
REMARK 475     VAL A   375                                                      
REMARK 475     LYS A   376                                                      
REMARK 475     MET A   377                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     HIS A   -5   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     HIS A   -4   CG   ND1  CD2  CE1  NE2                             
REMARK 480     HIS A   -3   CG   ND1  CD2  CE1  NE2                             
REMARK 480     HIS A   -2   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     HIS A   -1   CG   ND1  CD2  CE1  NE2                             
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   HE1  TRP A   340     OD1  ASP A   411              1.58            
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    HIS A  -2      151.55    135.87                                   
REMARK 500    SER A  17       54.88   -143.17                                   
REMARK 500    ARG A  20       81.41     50.11                                   
REMARK 500    THR A  21        1.72    -66.13                                   
REMARK 500    ASN A  96       62.47     33.07                                   
REMARK 500    ASP A 162     -156.57   -138.22                                   
REMARK 500    SER A 266      125.35   -173.86                                   
REMARK 500    SER A 291      -99.34   -120.75                                   
REMARK 500    LEU A 293      -49.72     76.80                                   
REMARK 500    MET A 354       18.22   -143.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6D0A A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
SEQADV 6D0A HIS A   -5  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6D0A HIS A   -4  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6D0A HIS A   -3  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6D0A HIS A   -2  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6D0A HIS A   -1  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQADV 6D0A HIS A    0  UNP  Q8N5Z0              EXPRESSION TAG                 
SEQRES   1 A  431  HIS HIS HIS HIS HIS HIS MET ASN TYR ALA ARG PHE ILE          
SEQRES   2 A  431  THR ALA ALA SER ALA ALA ARG ASN PRO SER PRO ILE ARG          
SEQRES   3 A  431  THR MET THR ASP ILE LEU SER ARG GLY PRO LYS SER MET          
SEQRES   4 A  431  ILE SER LEU ALA GLY GLY LEU PRO ASN PRO ASN MET PHE          
SEQRES   5 A  431  PRO PHE LYS THR ALA VAL ILE THR VAL GLU ASN GLY LYS          
SEQRES   6 A  431  THR ILE GLN PHE GLY GLU GLU MET MET LYS ARG ALA LEU          
SEQRES   7 A  431  GLN TYR SER PRO SER ALA GLY ILE PRO GLU LEU LEU SER          
SEQRES   8 A  431  TRP LEU LYS GLN LEU GLN ILE LYS LEU HIS ASN PRO PRO          
SEQRES   9 A  431  THR ILE HIS TYR PRO PRO SER GLN GLY GLN MET ASP LEU          
SEQRES  10 A  431  CYS VAL THR SER GLY SER GLN GLN GLY LEU CYS LYS VAL          
SEQRES  11 A  431  PHE GLU MET ILE ILE ASN PRO GLY ASP ASN VAL LEU LEU          
SEQRES  12 A  431  ASP GLU PRO ALA TYR SER GLY THR LEU GLN SER LEU HIS          
SEQRES  13 A  431  PRO LEU GLY CYS ASN ILE ILE ASN VAL ALA SER ASP GLU          
SEQRES  14 A  431  SER GLY ILE VAL PRO ASP SER LEU ARG ASP ILE LEU SER          
SEQRES  15 A  431  ARG TRP LYS PRO GLU ASP ALA LYS ASN PRO GLN LYS ASN          
SEQRES  16 A  431  THR PRO LYS PHE LEU TYR THR VAL PRO ASN GLY ASN ASN          
SEQRES  17 A  431  PRO THR GLY ASN SER LEU THR SER GLU ARG LYS LYS GLU          
SEQRES  18 A  431  ILE TYR GLU LEU ALA ARG LYS TYR ASP PHE LEU ILE ILE          
SEQRES  19 A  431  GLU ASP ASP PRO TYR TYR PHE LEU GLN PHE ASN LYS PHE          
SEQRES  20 A  431  ARG VAL PRO THR PHE LEU SER MET ASP VAL ASP GLY ARG          
SEQRES  21 A  431  VAL ILE ARG ALA ASP SER PHE SER LYS ILE ILE SER SER          
SEQRES  22 A  431  GLY LEU ARG ILE GLY PHE LEU THR GLY PRO LYS PRO LEU          
SEQRES  23 A  431  ILE GLU ARG VAL ILE LEU HIS ILE GLN VAL SER THR LEU          
SEQRES  24 A  431  HIS PRO SER THR PHE ASN GLN LEU MET ILE SER GLN LEU          
SEQRES  25 A  431  LEU HIS GLU TRP GLY GLU GLU GLY PHE MET ALA HIS VAL          
SEQRES  26 A  431  ASP ARG VAL ILE ASP PHE TYR SER ASN GLN LYS ASP ALA          
SEQRES  27 A  431  ILE LEU ALA ALA ALA ASP LYS TRP LEU THR GLY LEU ALA          
SEQRES  28 A  431  GLU TRP HIS VAL PRO ALA ALA GLY MET PHE LEU TRP ILE          
SEQRES  29 A  431  LYS VAL LYS GLY ILE ASN ASP VAL LYS GLU LEU ILE GLU          
SEQRES  30 A  431  GLU LYS ALA VAL LYS MET GLY VAL LEU MET LEU PRO GLY          
SEQRES  31 A  431  ASN ALA PHE TYR VAL ASP SER SER ALA PRO SER PRO TYR          
SEQRES  32 A  431  LEU ARG ALA SER PHE SER SER ALA SER PRO GLU GLN MET          
SEQRES  33 A  431  ASP VAL ALA PHE GLN VAL LEU ALA GLN LEU ILE LYS GLU          
SEQRES  34 A  431  SER LEU                                                      
FORMUL   2  HOH   *483(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 MET A   22  ARG A   28  1                                   7    
HELIX    4 AA4 ASN A   42  PHE A   46  5                                   5    
HELIX    5 AA5 GLY A   64  LEU A   72  1                                   9    
HELIX    6 AA6 ILE A   80  ASN A   96  1                                  17    
HELIX    7 AA7 PRO A  103  GLY A  107  5                                   5    
HELIX    8 AA8 GLY A  116  ILE A  129  1                                  14    
HELIX    9 AA9 TYR A  142  HIS A  150  1                                   9    
HELIX   10 AB1 PRO A  151  GLY A  153  5                                   3    
HELIX   11 AB2 VAL A  167  SER A  176  1                                  10    
HELIX   12 AB3 ARG A  177  TRP A  178  5                                   2    
HELIX   13 AB4 LYS A  179  ASN A  189  5                                  11    
HELIX   14 AB5 THR A  209  ASP A  224  1                                  16    
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 LYS A  367  GLU A  372  1                                   6    
HELIX   19 AC1 ASN A  385  TYR A  388  5                                   4    
HELIX   20 AC2 SER A  406  GLU A  423  1                                  18    
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  ALA A 258           
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  ALA A 400   N  LEU A 356           
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        -0.04                     
CISPEP   2 ASN A  202    PRO A  203          0        22.37                     
CRYST1  102.765  102.765   86.498  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      0.009731  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009731  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011561        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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