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Entry: 3DC1
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HEADER    TRANSFERASE                             03-JUN-08   3DC1              
TITLE     CRYSTAL STRUCTURE OF KYNURENINE AMINOTRANSFERASE II COMPLEX WITH      
TITLE    2 ALPHA-KETOGLUTARATE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE             
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: KAT/AADAT, KYNURENINE--OXOGLUTARATE TRANSAMINASE II,        
COMPND   6 KYNURENINE AMINOTRANSFERASE II, KYNURENINE--OXOGLUTARATE             
COMPND   7 AMINOTRANSFERASE II, 2-AMINOADIPATE TRANSAMINASE, 2-AMINOADIPATE     
COMPND   8 AMINOTRANSFERASE, ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT;        
COMPND   9 EC: 2.6.1.7, 2.6.1.39;                                               
COMPND  10 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTYB                                      
KEYWDS    ALPHA & BETA PROTEIN, PLP-DEPENDENT TRANSFERASE, AMINOTRANSFERASE,    
KEYWDS   2 MULTIFUNCTIONAL ENZYME, PYRIDOXAL PHOSPHATE, MITOCHONDRION,          
KEYWDS   3 TRANSFERASE, TRANSIT PEPTIDE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.HAN,T.CAI,D.A.TAGLE,H.ROBINSON,J.LI                                 
REVDAT   5   13-JUL-11 3DC1    1       VERSN                                    
REVDAT   4   08-DEC-09 3DC1    1       HETNAM                                   
REVDAT   3   24-FEB-09 3DC1    1       VERSN                                    
REVDAT   2   09-SEP-08 3DC1    1       JRNL                                     
REVDAT   1   29-JUL-08 3DC1    0                                                
JRNL        AUTH   Q.HAN,T.CAI,D.A.TAGLE,H.ROBINSON,J.LI                        
JRNL        TITL   SUBSTRATE SPECIFICITY AND STRUCTURE OF HUMAN AMINOADIPATE    
JRNL        TITL 2 AMINOTRANSFERASE/KYNURENINE AMINOTRANSFERASE II              
JRNL        REF    BIOSCI.REP.                   V.  28   205 2008              
JRNL        REFN                   ISSN 0144-8463                               
JRNL        PMID   18620547                                                     
JRNL        DOI    10.1042/BSR20080085                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 54268                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2890                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2281                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 49.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 123                          
REMARK   3   BIN FREE R VALUE                    : 0.2060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13193                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 828                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.327         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13561 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18402 ; 1.857 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1668 ; 9.279 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   570 ;40.794 ;24.632       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2320 ;20.368 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    61 ;18.221 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2022 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10209 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7421 ; 0.261 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9169 ; 0.325 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   940 ; 0.213 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    66 ; 0.259 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.317 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8390 ; 0.983 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13609 ; 1.730 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5171 ; 2.757 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4793 ; 3.965 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DC1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047849.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08090                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63835                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 89.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 15.700                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2R2N                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 15% PEG 10000, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     THR B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     ILE B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     THR D    21                                                      
REMARK 465     MET D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     ASP D    24                                                      
REMARK 465     ILE D    25                                                      
REMARK 465     LEU D    26                                                      
REMARK 465     SER D    27                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    PRO C 350   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO D  30   C   -  N   -  CD  ANGL. DEV. = -15.3 DEGREES          
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    LYS A  31     -171.49     65.23                                   
REMARK 500    SER A  32       71.55     33.68                                   
REMARK 500    PRO A  98       -3.06    -58.97                                   
REMARK 500    ASP A 162     -160.12   -160.07                                   
REMARK 500    ASN A 201      131.29    -24.85                                   
REMARK 500    SER A 266      131.69   -170.01                                   
REMARK 500    ARG A 270       77.76     51.72                                   
REMARK 500    SER A 291      -87.77    -96.91                                   
REMARK 500    LEU A 293      -65.88     63.00                                   
REMARK 500    SER A 296      122.77    -37.70                                   
REMARK 500    ILE B  19       63.95   -101.18                                   
REMARK 500    PRO B  30     -169.89    -64.06                                   
REMARK 500    MET B  33      128.52   -174.82                                   
REMARK 500    ASN B  96       70.34     31.61                                   
REMARK 500    ASP B 162     -156.17   -123.43                                   
REMARK 500    ILE B 166      127.29    -35.40                                   
REMARK 500    ASN B 189       39.72     36.12                                   
REMARK 500    THR B 190      144.23    -35.75                                   
REMARK 500    ASP B 224       56.18     32.70                                   
REMARK 500    SER B 291      -93.02   -122.01                                   
REMARK 500    LEU B 293      -57.80     82.22                                   
REMARK 500    SER B 296      125.64    -29.86                                   
REMARK 500    PRO C  16      131.20    -33.85                                   
REMARK 500    THR C  21      -74.24   -118.87                                   
REMARK 500    HIS C  95      -30.88   -141.20                                   
REMARK 500    ASN C  96       45.93     39.00                                   
REMARK 500    PRO C  97      124.00    -37.54                                   
REMARK 500    ASP C 162     -154.59   -146.65                                   
REMARK 500    ARG C 177      -31.23    -38.69                                   
REMARK 500    ASN C 189       26.28     84.32                                   
REMARK 500    SER C 266      141.50   -179.23                                   
REMARK 500    ARG C 270       63.02     63.00                                   
REMARK 500    SER C 291      -94.02   -116.11                                   
REMARK 500    LEU C 293      -65.38     61.85                                   
REMARK 500    SER C 296      121.27    -37.30                                   
REMARK 500    LYS C 373      -48.70   -132.59                                   
REMARK 500    SER C 404      -52.39   -135.80                                   
REMARK 500    PRO D  16      118.25    -37.41                                   
REMARK 500    SER D  17       73.77   -113.55                                   
REMARK 500    HIS D  95       -7.90   -145.12                                   
REMARK 500    ASN D  96       81.56     11.55                                   
REMARK 500    GLN D 106       26.37    -72.23                                   
REMARK 500    ASP D 162     -158.60   -160.02                                   
REMARK 500    GLU D 163      -24.51    -39.97                                   
REMARK 500    PRO D 180       11.58    -67.93                                   
REMARK 500    ASN D 185       86.37   -162.24                                   
REMARK 500    ASN D 201      119.52    -31.75                                   
REMARK 500    ASN D 202       97.42    -67.06                                   
REMARK 500    PRO D 244      129.72    -39.44                                   
REMARK 500    ASP D 250       76.61   -109.39                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
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   31     SER A   32                  -96.86                    
REMARK 500 PRO B   18     ILE B   19                  139.61                    
REMARK 500 ILE B   19     ARG B   20                   94.81                    
REMARK 500 PRO B   30     LYS B   31                 -129.84                    
REMARK 500 LYS B   31     SER B   32                  144.50                    
REMARK 500 SER B   32     MET B   33                 -139.04                    
REMARK 500 ASN B  202     PRO B  203                   39.67                    
REMARK 500 SER C  403     SER C  404                 -147.80                    
REMARK 500 ARG D   28     GLY D   29                  143.18                    
REMARK 500 GLY D   29     PRO D   30                 -131.70                    
REMARK 500 LYS D  184     ASN D  185                 -138.41                    
REMARK 500 ASN D  201     ASN D  202                  148.47                    
REMARK 500 ASN D  202     PRO D  203                   41.06                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE C 265        22.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 322        23.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 557        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH B 620        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH D 572        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH D 596        DISTANCE =  5.59 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A 426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 426                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 427                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 426                 
DBREF  3DC1 A    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  3DC1 B    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  3DC1 C    1   425  UNP    Q8N5Z0   AADAT_HUMAN      1    425             
DBREF  3DC1 D    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                          
SEQRES   1 C  425  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 C  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 C  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 C  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 C  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 C  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 C  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 C  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 C  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 C  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 C  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 C  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 C  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 C  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 C  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 C  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 C  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 C  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 C  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 C  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 C  425  PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 C  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 C  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 C  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 C  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 C  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 C  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 C  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 C  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 C  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 C  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 C  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 C  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
SEQRES   1 D  425  MET ASN TYR ALA ARG PHE ILE THR ALA ALA SER ALA ALA          
SEQRES   2 D  425  ARG ASN PRO SER PRO ILE ARG THR MET THR ASP ILE LEU          
SEQRES   3 D  425  SER ARG GLY PRO LYS SER MET ILE SER LEU ALA GLY GLY          
SEQRES   4 D  425  LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR ALA VAL          
SEQRES   5 D  425  ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE GLY GLU          
SEQRES   6 D  425  GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO SER ALA          
SEQRES   7 D  425  GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN LEU GLN          
SEQRES   8 D  425  ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR PRO PRO          
SEQRES   9 D  425  SER GLN GLY GLN MET ASP LEU CYS VAL THR SER GLY SER          
SEQRES  10 D  425  GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE ILE ASN          
SEQRES  11 D  425  PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA TYR SER          
SEQRES  12 D  425  GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS ASN ILE          
SEQRES  13 D  425  ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL PRO ASP          
SEQRES  14 D  425  SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO GLU ASP          
SEQRES  15 D  425  ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE LEU TYR          
SEQRES  16 D  425  THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN SER LEU          
SEQRES  17 D  425  THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU ALA ARG          
SEQRES  18 D  425  LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO TYR TYR          
SEQRES  19 D  425  PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR PHE LEU          
SEQRES  20 D  425  SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA ASP SER          
SEQRES  21 D  425  PHE SER LLP ILE ILE SER SER GLY LEU ARG ILE GLY PHE          
SEQRES  22 D  425  LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL ILE LEU          
SEQRES  23 D  425  HIS ILE GLN VAL SER THR LEU HIS PRO SER THR PHE ASN          
SEQRES  24 D  425  GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP GLY GLU          
SEQRES  25 D  425  GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE ASP PHE          
SEQRES  26 D  425  TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA ALA ASP          
SEQRES  27 D  425  LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL PRO ALA          
SEQRES  28 D  425  ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY ILE ASN          
SEQRES  29 D  425  ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL LYS MET          
SEQRES  30 D  425  GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR VAL ASP          
SEQRES  31 D  425  SER SER ALA PRO SER PRO TYR LEU ARG ALA SER PHE SER          
SEQRES  32 D  425  SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE GLN VAL          
SEQRES  33 D  425  LEU ALA GLN LEU ILE LYS GLU SER LEU                          
MODRES 3DC1 LLP A  263  LYS                                                     
MODRES 3DC1 LLP B  263  LYS                                                     
MODRES 3DC1 LLP C  263  LYS                                                     
MODRES 3DC1 LLP D  263  LYS                                                     
HET    LLP  A 263      24                                                       
HET    LLP  B 263      24                                                       
HET    LLP  C 263      24                                                       
HET    LLP  D 263      24                                                       
HET    AKG  A 426      10                                                       
HET    GOL  A 427       6                                                       
HET    GOL  A 428       6                                                       
HET    GOL  A 429       6                                                       
HET    GOL  C 426       6                                                       
HET    GOL  C 427       6                                                       
HET    GOL  D 426       6                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM     AKG 2-OXOGLUTARIC ACID                                               
HETNAM     GOL GLYCEROL                                                         
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  LLP    4(C14 H24 N3 O7 P)                                           
FORMUL   5  AKG    C5 H6 O5                                                     
FORMUL   6  GOL    6(C3 H8 O3)                                                  
FORMUL  12  HOH   *828(H2 O)                                                    
HELIX    1   1 TYR A    3  ILE A    7  5                                   5    
HELIX    2   2 THR A    8  ARG A   14  1                                   7    
HELIX    3   3 ASN A   42  PHE A   46  5                                   5    
HELIX    4   4 GLY A   64  LEU A   72  1                                   9    
HELIX    5   5 ILE A   80  HIS A   95  1                                  16    
HELIX    6   6 PRO A  103  GLY A  107  5                                   5    
HELIX    7   7 GLY A  116  ILE A  129  1                                  14    
HELIX    8   8 TYR A  142  HIS A  150  1                                   9    
HELIX    9   9 PRO A  151  GLY A  153  5                                   3    
HELIX   10  10 VAL A  167  SER A  176  1                                  10    
HELIX   11  11 ARG A  177  TRP A  178  5                                   2    
HELIX   12  12 LYS A  179  LYS A  184  5                                   6    
HELIX   13  13 ASN A  185  ASN A  189  5                                   5    
HELIX   14  14 THR A  209  ASP A  224  1                                  16    
HELIX   15  15 PHE A  246  ASP A  250  5                                   5    
HELIX   16  16 LYS A  278  GLN A  289  1                                  12    
HELIX   17  17 SER A  296  GLY A  311  1                                  16    
HELIX   18  18 GLY A  311  THR A  342  1                                  32    
HELIX   19  19 VAL A  366  GLU A  372  1                                   7    
HELIX   20  20 GLU A  372  MET A  377  1                                   6    
HELIX   21  21 ASN A  385  TYR A  388  5                                   4    
HELIX   22  22 SER A  406  LEU A  425  1                                  20    
HELIX   23  23 TYR B    3  ILE B    7  5                                   5    
HELIX   24  24 THR B    8  ALA B   13  1                                   6    
HELIX   25  25 ASN B   42  PHE B   46  5                                   5    
HELIX   26  26 GLY B   64  LEU B   72  1                                   9    
HELIX   27  27 ILE B   80  ASN B   96  1                                  17    
HELIX   28  28 GLY B  116  ILE B  129  1                                  14    
HELIX   29  29 TYR B  142  HIS B  150  1                                   9    
HELIX   30  30 PRO B  151  GLY B  153  5                                   3    
HELIX   31  31 VAL B  167  SER B  176  1                                  10    
HELIX   32  32 ARG B  177  TRP B  178  5                                   2    
HELIX   33  33 LYS B  179  ASN B  189  5                                  11    
HELIX   34  34 THR B  209  TYR B  223  1                                  15    
HELIX   35  35 TYR B  233  GLN B  237  5                                   5    
HELIX   36  36 PHE B  246  ASP B  250  5                                   5    
HELIX   37  37 LYS B  278  GLN B  289  1                                  12    
HELIX   38  38 SER B  296  LEU B  341  1                                  46    
HELIX   39  39 ASP B  365  GLU B  372  1                                   8    
HELIX   40  40 GLU B  372  MET B  377  1                                   6    
HELIX   41  41 ASN B  385  TYR B  388  5                                   4    
HELIX   42  42 SER B  406  GLU B  423  1                                  18    
HELIX   43  43 THR C    8  ALA C   13  1                                   6    
HELIX   44  44 ASN C   42  PHE C   46  5                                   5    
HELIX   45  45 GLY C   64  LEU C   72  1                                   9    
HELIX   46  46 ILE C   80  ASN C   96  1                                  17    
HELIX   47  47 PRO C  103  GLY C  107  5                                   5    
HELIX   48  48 GLY C  116  ILE C  129  1                                  14    
HELIX   49  49 TYR C  142  HIS C  150  1                                   9    
HELIX   50  50 PRO C  151  GLY C  153  5                                   3    
HELIX   51  51 VAL C  167  SER C  176  1                                  10    
HELIX   52  52 ARG C  177  TRP C  178  5                                   2    
HELIX   53  53 LYS C  179  ASN C  189  5                                  11    
HELIX   54  54 THR C  209  TYR C  223  1                                  15    
HELIX   55  55 PHE C  246  ASP C  250  5                                   5    
HELIX   56  56 LYS C  278  GLN C  289  1                                  12    
HELIX   57  57 SER C  296  LEU C  341  1                                  46    
HELIX   58  58 VAL C  366  GLU C  372  1                                   7    
HELIX   59  59 LYS C  373  GLY C  378  1                                   6    
HELIX   60  60 ASN C  385  TYR C  388  5                                   4    
HELIX   61  61 SER C  406  SER C  424  1                                  19    
HELIX   62  62 ASN D    2  ILE D    7  5                                   6    
HELIX   63  63 THR D    8  ALA D   13  1                                   6    
HELIX   64  64 ASN D   42  PHE D   46  5                                   5    
HELIX   65  65 GLY D   64  LEU D   72  1                                   9    
HELIX   66  66 ILE D   80  HIS D   95  1                                  16    
HELIX   67  67 GLY D  116  ILE D  129  1                                  14    
HELIX   68  68 TYR D  142  HIS D  150  1                                   9    
HELIX   69  69 PRO D  151  GLY D  153  5                                   3    
HELIX   70  70 VAL D  167  SER D  176  1                                  10    
HELIX   71  71 GLU D  181  ASN D  189  5                                   9    
HELIX   72  72 THR D  209  TYR D  223  1                                  15    
HELIX   73  73 TYR D  233  GLN D  237  5                                   5    
HELIX   74  74 PHE D  246  ASP D  250  5                                   5    
HELIX   75  75 LYS D  278  GLN D  289  1                                  12    
HELIX   76  76 SER D  296  LEU D  341  1                                  46    
HELIX   77  77 VAL D  366  LYS D  373  1                                   8    
HELIX   78  78 ASN D  385  TYR D  388  5                                   4    
HELIX   79  79 SER D  406  LEU D  425  1                                  20    
SHEET    1   A 2 ILE A  34  SER A  35  0                                        
SHEET    2   A 2 VAL B 379  LEU B 380  1  O  LEU B 380   N  ILE A  34           
SHEET    1   B 4 ILE A  61  PHE A  63  0                                        
SHEET    2   B 4 PHE A  48  VAL A  55 -1  N  ALA A  51   O  PHE A  63           
SHEET    3   B 4 PHE B  48  VAL B  55 -1  O  LYS B  49   N  THR A  54           
SHEET    4   B 4 ILE B  61  PHE B  63 -1  O  ILE B  61   N  ILE B  53           
SHEET    1   C 7 MET A 109  THR A 114  0                                        
SHEET    2   C 7 GLY A 272  PRO A 277 -1  O  GLY A 272   N  THR A 114           
SHEET    3   C 7 VAL A 255  SER A 260 -1  N  ARG A 257   O  THR A 275           
SHEET    4   C 7 LEU A 226  ASP A 230  1  N  ILE A 227   O  ILE A 256           
SHEET    5   C 7 PHE A 193  THR A 196  1  N  LEU A 194   O  LEU A 226           
SHEET    6   C 7 ASN A 134  ASP A 138  1  N  LEU A 136   O  TYR A 195           
SHEET    7   C 7 ASN A 155  VAL A 159  1  O  ILE A 157   N  VAL A 135           
SHEET    1   D 2 SER A 161  ASP A 162  0                                        
SHEET    2   D 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1   E 4 ALA A 345  TRP A 347  0                                        
SHEET    2   E 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3   E 4 TYR A 397  SER A 401 -1  O  ALA A 400   N  LEU A 356           
SHEET    4   E 4 LEU A 382  PRO A 383 -1  N  LEU A 382   O  ARG A 399           
SHEET    1   F 2 VAL A 379  LEU A 380  0                                        
SHEET    2   F 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1   G 7 MET B 109  THR B 114  0                                        
SHEET    2   G 7 GLY B 272  PRO B 277 -1  O  GLY B 272   N  THR B 114           
SHEET    3   G 7 VAL B 255  SER B 260 -1  N  ASP B 259   O  PHE B 273           
SHEET    4   G 7 LEU B 226  ASP B 230  1  N  GLU B 229   O  ALA B 258           
SHEET    5   G 7 PHE B 193  THR B 196  1  N  LEU B 194   O  ILE B 228           
SHEET    6   G 7 ASN B 134  ASP B 138  1  N  LEU B 136   O  TYR B 195           
SHEET    7   G 7 ASN B 155  VAL B 159  1  O  ILE B 157   N  VAL B 135           
SHEET    1   H 2 SER B 161  ASP B 162  0                                        
SHEET    2   H 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1   I 4 ALA B 345  TRP B 347  0                                        
SHEET    2   I 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3   I 4 TYR B 397  SER B 401 -1  O  LEU B 398   N  ILE B 358           
SHEET    4   I 4 LEU B 382  PRO B 383 -1  N  LEU B 382   O  ARG B 399           
SHEET    1   J 2 ILE C  34  SER C  35  0                                        
SHEET    2   J 2 VAL D 379  LEU D 380  1  O  LEU D 380   N  ILE C  34           
SHEET    1   K 4 ILE C  61  PHE C  63  0                                        
SHEET    2   K 4 PHE C  48  VAL C  55 -1  N  ALA C  51   O  PHE C  63           
SHEET    3   K 4 PHE D  48  VAL D  55 -1  O  LYS D  49   N  THR C  54           
SHEET    4   K 4 ILE D  61  PHE D  63 -1  O  ILE D  61   N  ILE D  53           
SHEET    1   L 7 MET C 109  THR C 114  0                                        
SHEET    2   L 7 GLY C 272  PRO C 277 -1  O  GLY C 272   N  THR C 114           
SHEET    3   L 7 VAL C 255  ASP C 259 -1  N  ARG C 257   O  THR C 275           
SHEET    4   L 7 LEU C 226  ASP C 231  1  N  ILE C 227   O  ILE C 256           
SHEET    5   L 7 PHE C 193  THR C 196  1  N  THR C 196   O  ASP C 230           
SHEET    6   L 7 ASN C 134  LEU C 137  1  N  LEU C 136   O  TYR C 195           
SHEET    7   L 7 ASN C 155  ASN C 158  1  O  ILE C 157   N  VAL C 135           
SHEET    1   M 2 SER C 161  ASP C 162  0                                        
SHEET    2   M 2 GLY C 165  ILE C 166 -1  O  GLY C 165   N  ASP C 162           
SHEET    1   N 4 ALA C 345  TRP C 347  0                                        
SHEET    2   N 4 PHE C 355  VAL C 360 -1  O  LYS C 359   N  GLU C 346           
SHEET    3   N 4 TYR C 397  SER C 401 -1  O  ALA C 400   N  LEU C 356           
SHEET    4   N 4 LEU C 382  PRO C 383 -1  N  LEU C 382   O  ARG C 399           
SHEET    1   O 2 VAL C 379  LEU C 380  0                                        
SHEET    2   O 2 ILE D  34  SER D  35  1  O  ILE D  34   N  LEU C 380           
SHEET    1   P 7 MET D 109  THR D 114  0                                        
SHEET    2   P 7 GLY D 272  PRO D 277 -1  O  GLY D 272   N  THR D 114           
SHEET    3   P 7 VAL D 255  ASP D 259 -1  N  ARG D 257   O  THR D 275           
SHEET    4   P 7 LEU D 226  ASP D 231  1  N  ILE D 227   O  ILE D 256           
SHEET    5   P 7 PHE D 193  THR D 196  1  N  THR D 196   O  ASP D 230           
SHEET    6   P 7 ASN D 134  ASP D 138  1  N  LEU D 136   O  TYR D 195           
SHEET    7   P 7 ASN D 155  VAL D 159  1  O  ILE D 157   N  VAL D 135           
SHEET    1   Q 2 SER D 161  ASP D 162  0                                        
SHEET    2   Q 2 GLY D 165  ILE D 166 -1  O  GLY D 165   N  ASP D 162           
SHEET    1   R 4 ALA D 345  GLU D 346  0                                        
SHEET    2   R 4 PHE D 355  VAL D 360 -1  O  LYS D 359   N  GLU D 346           
SHEET    3   R 4 TYR D 397  SER D 401 -1  O  ALA D 400   N  LEU D 356           
SHEET    4   R 4 LEU D 382  PRO D 383 -1  N  LEU D 382   O  ARG D 399           
LINK         C   SER A 262                 N   LLP A 263     1555   1555  1.32  
LINK         C   LLP A 263                 N   ILE A 264     1555   1555  1.32  
LINK         C   SER B 262                 N   LLP B 263     1555   1555  1.33  
LINK         C   LLP B 263                 N   ILE B 264     1555   1555  1.33  
LINK         C   SER C 262                 N   LLP C 263     1555   1555  1.32  
LINK         C   LLP C 263                 N   ILE C 264     1555   1555  1.32  
LINK         C   SER D 262                 N   LLP D 263     1555   1555  1.32  
LINK         C   LLP D 263                 N   ILE D 264     1555   1555  1.33  
CISPEP   1 GLU A  139    PRO A  140          0         5.44                     
CISPEP   2 ASN A  202    PRO A  203          0        15.45                     
CISPEP   3 GLU B  139    PRO B  140          0        13.60                     
CISPEP   4 GLU C  139    PRO C  140          0        -4.72                     
CISPEP   5 ASN C  202    PRO C  203          0        11.78                     
CISPEP   6 GLU D  139    PRO D  140          0         4.86                     
SITE     1 AC1  5 PRO A  18  GLY A  39  LEU A 293  TYR B 142                    
SITE     2 AC1  5 LLP B 263                                                     
SITE     1 AC2  6 GLN A 118  TYR A 142  LLP A 263  ILE B  19                    
SITE     2 AC2  6 TYR B  74  LEU B 293                                          
SITE     1 AC3  3 PRO A  16  PRO A  18  HOH A 653                               
SITE     1 AC4  5 ILE C  19  GLY C  39  TYR C  74  GLN D 118                    
SITE     2 AC4  5 LLP D 263                                                     
SITE     1 AC5  3 GLY C  29  PRO C  30  VAL D 375                               
SITE     1 AC6  7 TYR C 142  TYR C 233  LLP C 263  MET C 354                    
SITE     2 AC6  7 ILE D  19  GLY D  39  TYR D  74                               
CRYST1   60.930   72.090  109.079  89.97 100.65  93.88 P 1           4          
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      0.016412  0.001114  0.003099        0.00000                         
SCALE2      0.000000  0.013903  0.000169        0.00000                         
SCALE3      0.000000  0.000000  0.009329        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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