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Database: PDB
Entry: 6DNA
LinkDB: 6DNA
Original site: 6DNA 
HEADER    TRANSFERASE                             06-JUN-18   6DNA              
TITLE     CRYSTAL STRUCTURE OF T110A MUTANT HUMAN GLUTAMATE OXALOACETATE        
TITLE    2 TRANSAMINASE 1 (GOT1)                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC;                   
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: CASPAT,CYSTEINE AMINOTRANSFERASE,CYTOPLASMIC,CYSTEINE       
COMPND   5 TRANSAMINASE,CCAT,GLUTAMATE OXALOACETATE TRANSAMINASE 1,TRANSAMINASE 
COMPND   6 A;                                                                   
COMPND   7 EC: 2.6.1.1,2.6.1.3;                                                 
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GOT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ASPARTATE AMINOTRANSFERASE, GLUTAMATE OXALOACETATE TRANSAMINASE 1,    
KEYWDS   2 GOT1, PLP, TRANSFERASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.ASSAR,M.C.HOLT,A.J.STEIN,L.LAIRSON,C.A.LYSSIOTIS                    
REVDAT   3   05-DEC-18 6DNA    1       JRNL                                     
REVDAT   2   21-NOV-18 6DNA    1       JRNL                                     
REVDAT   1   14-NOV-18 6DNA    0                                                
JRNL        AUTH   M.C.HOLT,Z.ASSAR,R.BEHESHTI ZAVAREH,L.LIN,J.ANGLIN,          
JRNL        AUTH 2 O.MASHADOVA,D.HALDAR,E.MULLARKY,D.M.KREMER,L.C.CANTLEY,      
JRNL        AUTH 3 A.C.KIMMELMAN,A.J.STEIN,L.L.LAIRSON,C.A.LYSSIOTIS            
JRNL        TITL   BIOCHEMICAL CHARACTERIZATION AND STRUCTURE-BASED MUTATIONAL  
JRNL        TITL 2 ANALYSIS PROVIDE INSIGHT INTO THE BINDING AND MECHANISM OF   
JRNL        TITL 3 ACTION OF NOVEL ASPARTATE AMINOTRANSFERASE INHIBITORS.       
JRNL        REF    BIOCHEMISTRY                  V.  57  6604 2018              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   30365304                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.8B00914                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 59473                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3047                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4364                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 219                          
REMARK   3   BIN FREE R VALUE                    : 0.2890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18277                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 132                                     
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.38000                                             
REMARK   3    B22 (A**2) : 0.43000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.19000                                              
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): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.267         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.869        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18990 ; 0.010 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A): 16549 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 25850 ; 1.465 ; 1.658       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 38674 ; 0.888 ; 1.637       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2372 ; 7.953 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1012 ;33.806 ;22.125       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2930 ;18.584 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   125 ;18.175 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2425 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 21657 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3707 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  9431 ; 8.010 ; 7.682       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  9430 ; 8.010 ; 7.682       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11783 ;12.314 ;11.508       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 11784 ;12.313 ;11.508       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9559 ; 6.831 ; 7.772       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  9560 ; 6.830 ; 7.772       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 14055 ;10.366 ;11.610       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 79196 ;20.407 ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 79197 ;20.407 ;  NULL       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 15                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    16    410       B    16    410   11623  0.13  0.05     
REMARK   3    2     A    16    402       C    16    402   11501  0.13  0.05     
REMARK   3    3     A    16    410       D    16    410   11596  0.14  0.05     
REMARK   3    4     A    17    409       E    17    409   11526  0.14  0.05     
REMARK   3    5     A    16    398       F    16    398   11303  0.14  0.05     
REMARK   3    6     B    15    402       C    15    402   11650  0.13  0.05     
REMARK   3    7     B    15    410       D    15    410   11686  0.14  0.05     
REMARK   3    8     B    17    408       E    17    408   11822  0.13  0.05     
REMARK   3    9     B    16    398       F    16    398   11552  0.14  0.05     
REMARK   3   10     C    14    402       D    14    402   11793  0.13  0.05     
REMARK   3   11     C    17    402       E    17    402   11844  0.13  0.05     
REMARK   3   12     C    16    398       F    16    398   11741  0.13  0.05     
REMARK   3   13     D    17    408       E    17    408   11693  0.14  0.05     
REMARK   3   14     D    16    398       F    16    398   11710  0.13  0.05     
REMARK   3   15     E    17    398       F    17    398   11481  0.14  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6DNA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234841.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-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               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 4281                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3II0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V PEG 3,350, 0.1 M HEPES PH 7.5,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      128.85000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.31300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      128.85000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       74.31300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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     VAL A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     ALA A   230                                                      
REMARK 465     VAL A   375                                                      
REMARK 465     ASN A   376                                                      
REMARK 465     GLU A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     LYS A   411                                                      
REMARK 465     ILE A   412                                                      
REMARK 465     GLN A   413                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     PHE B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     VAL B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     LEU B   366                                                      
REMARK 465     LYS B   411                                                      
REMARK 465     ILE B   412                                                      
REMARK 465     GLN B   413                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     PHE C     7                                                      
REMARK 465     ALA C     8                                                      
REMARK 465     GLU C     9                                                      
REMARK 465     VAL C    10                                                      
REMARK 465     PRO C    11                                                      
REMARK 465     TYR C   381                                                      
REMARK 465     SER C   404                                                      
REMARK 465     ILE C   405                                                      
REMARK 465     HIS C   406                                                      
REMARK 465     GLU C   407                                                      
REMARK 465     ALA C   408                                                      
REMARK 465     VAL C   409                                                      
REMARK 465     THR C   410                                                      
REMARK 465     LYS C   411                                                      
REMARK 465     ILE C   412                                                      
REMARK 465     GLN C   413                                                      
REMARK 465     VAL D     6                                                      
REMARK 465     PHE D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     GLU D     9                                                      
REMARK 465     VAL D    10                                                      
REMARK 465     PRO D    11                                                      
REMARK 465     GLN D    12                                                      
REMARK 465     ALA D    13                                                      
REMARK 465     VAL D   375                                                      
REMARK 465     LYS D   411                                                      
REMARK 465     ILE D   412                                                      
REMARK 465     GLN D   413                                                      
REMARK 465     VAL E     6                                                      
REMARK 465     PHE E     7                                                      
REMARK 465     ALA E     8                                                      
REMARK 465     GLU E     9                                                      
REMARK 465     VAL E    10                                                      
REMARK 465     PRO E    11                                                      
REMARK 465     GLN E    12                                                      
REMARK 465     ALA E    13                                                      
REMARK 465     GLN E    14                                                      
REMARK 465     PRO E    15                                                      
REMARK 465     VAL E    16                                                      
REMARK 465     THR E   410                                                      
REMARK 465     LYS E   411                                                      
REMARK 465     ILE E   412                                                      
REMARK 465     GLN E   413                                                      
REMARK 465     VAL F     6                                                      
REMARK 465     PHE F     7                                                      
REMARK 465     ALA F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     VAL F    10                                                      
REMARK 465     PRO F    11                                                      
REMARK 465     GLN F    12                                                      
REMARK 465     ALA F    13                                                      
REMARK 465     GLN F    14                                                      
REMARK 465     PRO F    15                                                      
REMARK 465     TYR F   381                                                      
REMARK 465     TYR F   400                                                      
REMARK 465     VAL F   401                                                      
REMARK 465     ALA F   402                                                      
REMARK 465     THR F   403                                                      
REMARK 465     SER F   404                                                      
REMARK 465     ILE F   405                                                      
REMARK 465     HIS F   406                                                      
REMARK 465     GLU F   407                                                      
REMARK 465     ALA F   408                                                      
REMARK 465     VAL F   409                                                      
REMARK 465     THR F   410                                                      
REMARK 465     LYS F   411                                                      
REMARK 465     ILE F   412                                                      
REMARK 465     GLN F   413                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A  26    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  27    CD   OE1  OE2                                       
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  99    CD   CE   NZ                                        
REMARK 470     TYR A 135    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 166    CE   NZ                                             
REMARK 470     LYS A 214    CD   CE   NZ                                        
REMARK 470     GLU A 277    CD   OE1  OE2                                       
REMARK 470     GLU A 279    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 290    CD   CE   NZ                                        
REMARK 470     GLU A 315    CD   OE1  OE2                                       
REMARK 470     LEU A 345    CG   CD1  CD2                                       
REMARK 470     LYS A 346    CG   CD   CE   NZ                                   
REMARK 470     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     LEU A 382    CG   CD1  CD2                                       
REMARK 470     ILE A 388    CG1  CG2  CD1                                       
REMARK 470     LYS A 396    CE   NZ                                             
REMARK 470     LYS B  20    CG   CD   CE   NZ                                   
REMARK 470     ARG B  26    CZ   NH1  NH2                                       
REMARK 470     GLU B  27    CD   OE1  OE2                                       
REMARK 470     ASP B  28    CG   OD1  OD2                                       
REMARK 470     LYS B  99    CD   CE   NZ                                        
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 166    CE   NZ                                             
REMARK 470     LYS B 214    CD   CE   NZ                                        
REMARK 470     GLU B 277    CD   OE1  OE2                                       
REMARK 470     GLU B 279    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 290    CD   CE   NZ                                        
REMARK 470     GLU B 315    CD   OE1  OE2                                       
REMARK 470     LYS B 369    CG   CD   CE   NZ                                   
REMARK 470     HIS B 379    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 396    CE   NZ                                             
REMARK 470     ARG C  26    CZ   NH1  NH2                                       
REMARK 470     GLU C  27    CD   OE1  OE2                                       
REMARK 470     LYS C  33    CG   CD   CE   NZ                                   
REMARK 470     LYS C  99    CD   CE   NZ                                        
REMARK 470     GLU C 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 166    CE   NZ                                             
REMARK 470     LYS C 214    CD   CE   NZ                                        
REMARK 470     GLU C 277    CD   OE1  OE2                                       
REMARK 470     GLU C 279    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 290    CD   CE   NZ                                        
REMARK 470     GLU C 315    CD   OE1  OE2                                       
REMARK 470     GLU C 337    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 341    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 346    CG   CD   CE   NZ                                   
REMARK 470     LYS C 369    CG   CD   CE   NZ                                   
REMARK 470     LYS C 396    CE   NZ                                             
REMARK 470     TYR C 400    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE D  19    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE D  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG D  26    CZ   NH1  NH2                                       
REMARK 470     GLU D  27    CD   OE1  OE2                                       
REMARK 470     GLU D  79    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  99    CD   CE   NZ                                        
REMARK 470     GLU D 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 166    CE   NZ                                             
REMARK 470     LYS D 214    CD   CE   NZ                                        
REMARK 470     GLU D 277    CD   OE1  OE2                                       
REMARK 470     LYS D 290    CD   CE   NZ                                        
REMARK 470     GLU D 315    CD   OE1  OE2                                       
REMARK 470     LYS D 369    CG   CD   CE   NZ                                   
REMARK 470     GLU D 372    CG   CD   OE1  OE2                                  
REMARK 470     TYR D 381    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS D 396    CE   NZ                                             
REMARK 470     TYR D 400    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG E  26    CZ   NH1  NH2                                       
REMARK 470     GLU E  27    CD   OE1  OE2                                       
REMARK 470     LYS E  99    CD   CE   NZ                                        
REMARK 470     GLU E 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 166    CE   NZ                                             
REMARK 470     LYS E 214    CD   CE   NZ                                        
REMARK 470     GLU E 277    CD   OE1  OE2                                       
REMARK 470     GLU E 279    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 290    CD   CE   NZ                                        
REMARK 470     GLU E 315    CD   OE1  OE2                                       
REMARK 470     LYS E 369    CG   CD   CE   NZ                                   
REMARK 470     LYS E 396    CE   NZ                                             
REMARK 470     HIS E 406    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG F  26    CZ   NH1  NH2                                       
REMARK 470     GLU F  27    CD   OE1  OE2                                       
REMARK 470     LYS F  99    CD   CE   NZ                                        
REMARK 470     GLU F 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 166    CE   NZ                                             
REMARK 470     LYS F 214    CD   CE   NZ                                        
REMARK 470     GLU F 277    CD   OE1  OE2                                       
REMARK 470     GLU F 279    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 290    CD   CE   NZ                                        
REMARK 470     GLU F 315    CD   OE1  OE2                                       
REMARK 470     LYS F 369    CG   CD   CE   NZ                                   
REMARK 470     LYS F 378    CG   CD   CE   NZ                                   
REMARK 470     HIS F 379    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS F 396    CE   NZ                                             
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   N    GLN B   370     CE1  TYR B   373              0.61            
REMARK 500   CA   GLN B   370     CD1  TYR B   373              0.90            
REMARK 500   NH2  ARG B    32     CD   GLU B   377              1.00            
REMARK 500   CA   GLN B   370     CE1  TYR B   373              1.07            
REMARK 500   N    GLN B   370     CZ   TYR B   373              1.22            
REMARK 500   C    LYS B   369     CZ   TYR B   373              1.25            
REMARK 500   O    PRO B   368     OH   TYR B   373              1.27            
REMARK 500   N    LEU B   374     OH   TYR B   381              1.34            
REMARK 500   CA   ALA B   340     OE1  GLU B   343              1.37            
REMARK 500   NH2  ARG B    32     OE2  GLU B   377              1.37            
REMARK 500   CZ   ARG B    32     CD   GLU B   377              1.37            
REMARK 500   C    PRO B   368     OH   TYR B   373              1.37            
REMARK 500   NH2  ARG B    32     CG   GLU B   377              1.46            
REMARK 500   C    ALA B   340     OE1  GLU B   343              1.46            
REMARK 500   N    LYS B   369     OH   TYR B   373              1.48            
REMARK 500   CZ   ARG B    32     OE1  GLU B   377              1.50            
REMARK 500   OD1  ASN E   367     O    GLU E   372              1.51            
REMARK 500   C    LYS B   369     CE2  TYR B   373              1.53            
REMARK 500   O    ALA B   340     OE2  GLU B   343              1.55            
REMARK 500   N    LYS F    20     OD2  ASP F    24              1.63            
REMARK 500   O    TYR B   381     O    LEU B   382              1.64            
REMARK 500   O    VAL E    34     O    ILE E   380              1.67            
REMARK 500   CA   LYS B   369     CZ   TYR B   373              1.68            
REMARK 500   O    GLU A   337     OD1  ASP A   399              1.69            
REMARK 500   OD1  ASP B    30     OE2  GLU B   377              1.69            
REMARK 500   CA   LYS B   369     OH   TYR B   373              1.70            
REMARK 500   NE   ARG B    32     OE1  GLU B   377              1.70            
REMARK 500   N    LEU B   374     CZ   TYR B   381              1.74            
REMARK 500   O    LEU F    17     CE   LYS F    20              1.74            
REMARK 500   C    LYS B   369     CE1  TYR B   373              1.75            
REMARK 500   O    LEU F    17     CD   LYS F    20              1.76            
REMARK 500   O    ARG B   339     OE1  GLU B   343              1.76            
REMARK 500   OH   TYR D   373     OE1  GLU D   407              1.77            
REMARK 500   N    ALA B   340     OE1  GLU B   343              1.77            
REMARK 500   CA   LYS B   369     CE2  TYR B   373              1.78            
REMARK 500   N    LEU F    21     OD2  ASP F    24              1.79            
REMARK 500   N    GLN B   370     CD1  TYR B   373              1.79            
REMARK 500   OG1  THR C    22     ND2  ASN C    35              1.81            
REMARK 500   O    ALA B   340     CD   GLU B   343              1.81            
REMARK 500   O    ASN D   352     OD1  ASP D   356              1.81            
REMARK 500   CZ   ARG B    32     OE2  GLU B   377              1.84            
REMARK 500   O    LYS B   369     CD2  TYR B   373              1.85            
REMARK 500   O    LEU F   342     N    ALA F   344              1.86            
REMARK 500   N    LEU B   374     CE1  TYR B   381              1.86            
REMARK 500   C    TYR B   373     CE1  TYR B   381              1.88            
REMARK 500   O    LYS F    20     CE2  PHE F    25              1.89            
REMARK 500   O    ASP F    44     CG2  THR F   394              1.90            
REMARK 500   CA   LEU B   374     OH   TYR B   381              1.91            
REMARK 500   NE   ARG B    32     OE2  GLU B   377              1.92            
REMARK 500   OD1  ASN D   389     OG   SER D   391              1.92            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      90 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 B  15   CA  -  N   -  CD  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    TYR B 373   CB  -  CG  -  CD2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    TYR B 373   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 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    LEU A  17      -62.76     16.75                                   
REMARK 500    PHE A  25       83.12    -57.93                                   
REMARK 500    ARG A  26      -38.98    163.79                                   
REMARK 500    PRO A  29     -104.23    -69.13                                   
REMARK 500    PRO A  31       50.22    -50.88                                   
REMARK 500    LYS A  33     -166.37    -57.56                                   
REMARK 500    VAL A  34      124.53   -174.44                                   
REMARK 500    THR A  43     -179.08    -69.69                                   
REMARK 500    GLN A 105      136.46    -39.76                                   
REMARK 500    TYR A 161      -61.05   -153.48                                   
REMARK 500    PHE A 184       -7.93     81.72                                   
REMARK 500    LEU A 263       44.83   -102.04                                   
REMARK 500    THR A 295      -61.73   -105.01                                   
REMARK 500    SER A 297      -54.65     72.22                                   
REMARK 500    LEU A 338      -36.87   -179.10                                   
REMARK 500    LEU A 342       75.25   -107.42                                   
REMARK 500    GLU A 343      -47.76   -145.83                                   
REMARK 500    THR A 347      -75.62   -167.64                                   
REMARK 500    THR A 350     -115.61   -151.17                                   
REMARK 500    TRP A 351      137.92    133.02                                   
REMARK 500    THR A 364      -73.93    -76.50                                   
REMARK 500    ILE A 380       86.13    -42.88                                   
REMARK 500    LEU A 382       67.90    -52.98                                   
REMARK 500    LEU A 398      100.62     51.97                                   
REMARK 500    ASP A 399      -27.53    -33.41                                   
REMARK 500    THR A 403      -84.85     75.44                                   
REMARK 500    ILE A 405      -47.71    108.58                                   
REMARK 500    VAL A 409      -56.50   -121.32                                   
REMARK 500    VAL B  16      -91.19   -141.08                                   
REMARK 500    LEU B  17      -71.41   -163.48                                   
REMARK 500    LYS B  20      -20.92   -155.04                                   
REMARK 500    ASP B  28       58.32     77.65                                   
REMARK 500    TYR B 161      -59.01   -150.80                                   
REMARK 500    PHE B 184       -0.95     81.82                                   
REMARK 500    LEU B 263       43.70   -103.28                                   
REMARK 500    THR B 295      -60.50   -104.85                                   
REMARK 500    SER B 297      -55.03     73.44                                   
REMARK 500    LEU B 342       64.78   -116.73                                   
REMARK 500    ALA B 344      -96.59   -163.97                                   
REMARK 500    LYS B 346      -77.64    -93.95                                   
REMARK 500    TRP B 351       28.89   -143.86                                   
REMARK 500    THR B 364      -79.80    -77.86                                   
REMARK 500    PRO B 368     -103.05    -77.17                                   
REMARK 500    LYS B 369       42.93    -89.44                                   
REMARK 500    GLN B 370       51.22   -112.87                                   
REMARK 500    TYR B 373     -143.30     -1.80                                   
REMARK 500    VAL B 375       10.41    169.65                                   
REMARK 500    LYS B 378     -151.61    -87.94                                   
REMARK 500    ILE B 380       97.28    -52.26                                   
REMARK 500    TYR B 381      105.03    -48.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     153 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 THR A  350     TRP A  351                  141.19                    
REMARK 500 GLY A  365     LEU A  366                 -147.67                    
REMARK 500 VAL B   16     LEU B   17                  147.03                    
REMARK 500 LYS B  369     GLN B  370                  148.62                    
REMARK 500 ALA C  340     ARG C  341                  149.25                    
REMARK 500 ASP D   28     PRO D   29                  142.27                    
REMARK 500 GLU E   27     ASP E   28                 -146.21                    
REMARK 500 GLU F  343     ALA F  344                 -149.39                    
REMARK 500 PRO F  348     GLY F  349                 -143.89                    
REMARK 500 LEU F  366     ASN F  367                 -132.82                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  86         0.09    SIDE CHAIN                              
REMARK 500    ARG A 167         0.11    SIDE CHAIN                              
REMARK 500    ARG A 216         0.08    SIDE CHAIN                              
REMARK 500    ARG A 236         0.08    SIDE CHAIN                              
REMARK 500    ARG B 167         0.08    SIDE CHAIN                              
REMARK 500    ARG B 236         0.08    SIDE CHAIN                              
REMARK 500    ARG C 339         0.08    SIDE CHAIN                              
REMARK 500    ARG E  32         0.09    SIDE CHAIN                              
REMARK 500    ARG E  42         0.11    SIDE CHAIN                              
REMARK 500    ARG E 100         0.09    SIDE CHAIN                              
REMARK 500    ARG E 293         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    SER E 256         10.96                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 B  501                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP F 501                 
DBREF  6DNA A    6   410  UNP    P17174   AATC_HUMAN       6    410             
DBREF  6DNA B    6   410  UNP    P17174   AATC_HUMAN       6    410             
DBREF  6DNA C    6   410  UNP    P17174   AATC_HUMAN       6    410             
DBREF  6DNA D    6   410  UNP    P17174   AATC_HUMAN       6    410             
DBREF  6DNA E    6   410  UNP    P17174   AATC_HUMAN       6    410             
DBREF  6DNA F    6   410  UNP    P17174   AATC_HUMAN       6    410             
SEQADV 6DNA ALA A  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNA LYS A  411  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ILE A  412  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA GLN A  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ALA B  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNA LYS B  411  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ILE B  412  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA GLN B  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ALA C  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNA LYS C  411  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ILE C  412  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA GLN C  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ALA D  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNA LYS D  411  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ILE D  412  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA GLN D  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ALA E  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNA LYS E  411  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ILE E  412  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA GLN E  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ALA F  110  UNP  P17174    THR   110 ENGINEERED MUTATION            
SEQADV 6DNA LYS F  411  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA ILE F  412  UNP  P17174              EXPRESSION TAG                 
SEQADV 6DNA GLN F  413  UNP  P17174              EXPRESSION TAG                 
SEQRES   1 A  408  VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO VAL LEU VAL          
SEQRES   2 A  408  PHE LYS LEU THR ALA ASP PHE ARG GLU ASP PRO ASP PRO          
SEQRES   3 A  408  ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR ARG THR ASP          
SEQRES   4 A  408  ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL LYS LYS VAL          
SEQRES   5 A  408  GLU GLN LYS ILE ALA ASN ASP ASN SER LEU ASN HIS GLU          
SEQRES   6 A  408  TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE ARG SER CYS          
SEQRES   7 A  408  ALA SER ARG LEU ALA LEU GLY ASP ASP SER PRO ALA LEU          
SEQRES   8 A  408  LYS GLU LYS ARG VAL GLY GLY VAL GLN SER LEU GLY GLY          
SEQRES   9 A  408  ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE LEU ALA ARG          
SEQRES  10 A  408  TRP TYR ASN GLY THR ASN ASN LYS ASN THR PRO VAL TYR          
SEQRES  11 A  408  VAL SER SER PRO THR TRP GLU ASN HIS ASN ALA VAL PHE          
SEQRES  12 A  408  SER ALA ALA GLY PHE LYS ASP ILE ARG SER TYR ARG TYR          
SEQRES  13 A  408  TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU GLN GLY PHE          
SEQRES  14 A  408  LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE SER ILE VAL          
SEQRES  15 A  408  VAL LEU HIS ALA CYS ALA HIS ASN PRO THR GLY ILE ASP          
SEQRES  16 A  408  PRO THR PRO GLU GLN TRP LYS GLN ILE ALA SER VAL MET          
SEQRES  17 A  408  LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP SER ALA TYR          
SEQRES  18 A  408  GLN GLY PHE ALA SER GLY ASN LEU GLU ARG ASP ALA TRP          
SEQRES  19 A  408  ALA ILE ARG TYR PHE VAL SER GLU GLY PHE GLU PHE PHE          
SEQRES  20 A  408  CYS ALA GLN SER PHE SER LYS ASN PHE GLY LEU TYR ASN          
SEQRES  21 A  408  GLU ARG VAL GLY ASN LEU THR VAL VAL GLY LYS GLU PRO          
SEQRES  22 A  408  GLU SER ILE LEU GLN VAL LEU SER GLN MET GLU LYS ILE          
SEQRES  23 A  408  VAL ARG ILE THR TRP SER ASN PRO PRO ALA GLN GLY ALA          
SEQRES  24 A  408  ARG ILE VAL ALA SER THR LEU SER ASN PRO GLU LEU PHE          
SEQRES  25 A  408  GLU GLU TRP THR GLY ASN VAL LYS THR MET ALA ASP ARG          
SEQRES  26 A  408  ILE LEU THR MET ARG SER GLU LEU ARG ALA ARG LEU GLU          
SEQRES  27 A  408  ALA LEU LYS THR PRO GLY THR TRP ASN HIS ILE THR ASP          
SEQRES  28 A  408  GLN ILE GLY MET PHE SER PHE THR GLY LEU ASN PRO LYS          
SEQRES  29 A  408  GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS ILE TYR LEU          
SEQRES  30 A  408  LEU PRO SER GLY ARG ILE ASN VAL SER GLY LEU THR THR          
SEQRES  31 A  408  LYS ASN LEU ASP TYR VAL ALA THR SER ILE HIS GLU ALA          
SEQRES  32 A  408  VAL THR LYS ILE GLN                                          
SEQRES   1 B  408  VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO VAL LEU VAL          
SEQRES   2 B  408  PHE LYS LEU THR ALA ASP PHE ARG GLU ASP PRO ASP PRO          
SEQRES   3 B  408  ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR ARG THR ASP          
SEQRES   4 B  408  ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL LYS LYS VAL          
SEQRES   5 B  408  GLU GLN LYS ILE ALA ASN ASP ASN SER LEU ASN HIS GLU          
SEQRES   6 B  408  TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE ARG SER CYS          
SEQRES   7 B  408  ALA SER ARG LEU ALA LEU GLY ASP ASP SER PRO ALA LEU          
SEQRES   8 B  408  LYS GLU LYS ARG VAL GLY GLY VAL GLN SER LEU GLY GLY          
SEQRES   9 B  408  ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE LEU ALA ARG          
SEQRES  10 B  408  TRP TYR ASN GLY THR ASN ASN LYS ASN THR PRO VAL TYR          
SEQRES  11 B  408  VAL SER SER PRO THR TRP GLU ASN HIS ASN ALA VAL PHE          
SEQRES  12 B  408  SER ALA ALA GLY PHE LYS ASP ILE ARG SER TYR ARG TYR          
SEQRES  13 B  408  TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU GLN GLY PHE          
SEQRES  14 B  408  LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE SER ILE VAL          
SEQRES  15 B  408  VAL LEU HIS ALA CYS ALA HIS ASN PRO THR GLY ILE ASP          
SEQRES  16 B  408  PRO THR PRO GLU GLN TRP LYS GLN ILE ALA SER VAL MET          
SEQRES  17 B  408  LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP SER ALA TYR          
SEQRES  18 B  408  GLN GLY PHE ALA SER GLY ASN LEU GLU ARG ASP ALA TRP          
SEQRES  19 B  408  ALA ILE ARG TYR PHE VAL SER GLU GLY PHE GLU PHE PHE          
SEQRES  20 B  408  CYS ALA GLN SER PHE SER LYS ASN PHE GLY LEU TYR ASN          
SEQRES  21 B  408  GLU ARG VAL GLY ASN LEU THR VAL VAL GLY LYS GLU PRO          
SEQRES  22 B  408  GLU SER ILE LEU GLN VAL LEU SER GLN MET GLU LYS ILE          
SEQRES  23 B  408  VAL ARG ILE THR TRP SER ASN PRO PRO ALA GLN GLY ALA          
SEQRES  24 B  408  ARG ILE VAL ALA SER THR LEU SER ASN PRO GLU LEU PHE          
SEQRES  25 B  408  GLU GLU TRP THR GLY ASN VAL LYS THR MET ALA ASP ARG          
SEQRES  26 B  408  ILE LEU THR MET ARG SER GLU LEU ARG ALA ARG LEU GLU          
SEQRES  27 B  408  ALA LEU LYS THR PRO GLY THR TRP ASN HIS ILE THR ASP          
SEQRES  28 B  408  GLN ILE GLY MET PHE SER PHE THR GLY LEU ASN PRO LYS          
SEQRES  29 B  408  GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS ILE TYR LEU          
SEQRES  30 B  408  LEU PRO SER GLY ARG ILE ASN VAL SER GLY LEU THR THR          
SEQRES  31 B  408  LYS ASN LEU ASP TYR VAL ALA THR SER ILE HIS GLU ALA          
SEQRES  32 B  408  VAL THR LYS ILE GLN                                          
SEQRES   1 C  408  VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO VAL LEU VAL          
SEQRES   2 C  408  PHE LYS LEU THR ALA ASP PHE ARG GLU ASP PRO ASP PRO          
SEQRES   3 C  408  ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR ARG THR ASP          
SEQRES   4 C  408  ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL LYS LYS VAL          
SEQRES   5 C  408  GLU GLN LYS ILE ALA ASN ASP ASN SER LEU ASN HIS GLU          
SEQRES   6 C  408  TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE ARG SER CYS          
SEQRES   7 C  408  ALA SER ARG LEU ALA LEU GLY ASP ASP SER PRO ALA LEU          
SEQRES   8 C  408  LYS GLU LYS ARG VAL GLY GLY VAL GLN SER LEU GLY GLY          
SEQRES   9 C  408  ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE LEU ALA ARG          
SEQRES  10 C  408  TRP TYR ASN GLY THR ASN ASN LYS ASN THR PRO VAL TYR          
SEQRES  11 C  408  VAL SER SER PRO THR TRP GLU ASN HIS ASN ALA VAL PHE          
SEQRES  12 C  408  SER ALA ALA GLY PHE LYS ASP ILE ARG SER TYR ARG TYR          
SEQRES  13 C  408  TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU GLN GLY PHE          
SEQRES  14 C  408  LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE SER ILE VAL          
SEQRES  15 C  408  VAL LEU HIS ALA CYS ALA HIS ASN PRO THR GLY ILE ASP          
SEQRES  16 C  408  PRO THR PRO GLU GLN TRP LYS GLN ILE ALA SER VAL MET          
SEQRES  17 C  408  LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP SER ALA TYR          
SEQRES  18 C  408  GLN GLY PHE ALA SER GLY ASN LEU GLU ARG ASP ALA TRP          
SEQRES  19 C  408  ALA ILE ARG TYR PHE VAL SER GLU GLY PHE GLU PHE PHE          
SEQRES  20 C  408  CYS ALA GLN SER PHE SER LYS ASN PHE GLY LEU TYR ASN          
SEQRES  21 C  408  GLU ARG VAL GLY ASN LEU THR VAL VAL GLY LYS GLU PRO          
SEQRES  22 C  408  GLU SER ILE LEU GLN VAL LEU SER GLN MET GLU LYS ILE          
SEQRES  23 C  408  VAL ARG ILE THR TRP SER ASN PRO PRO ALA GLN GLY ALA          
SEQRES  24 C  408  ARG ILE VAL ALA SER THR LEU SER ASN PRO GLU LEU PHE          
SEQRES  25 C  408  GLU GLU TRP THR GLY ASN VAL LYS THR MET ALA ASP ARG          
SEQRES  26 C  408  ILE LEU THR MET ARG SER GLU LEU ARG ALA ARG LEU GLU          
SEQRES  27 C  408  ALA LEU LYS THR PRO GLY THR TRP ASN HIS ILE THR ASP          
SEQRES  28 C  408  GLN ILE GLY MET PHE SER PHE THR GLY LEU ASN PRO LYS          
SEQRES  29 C  408  GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS ILE TYR LEU          
SEQRES  30 C  408  LEU PRO SER GLY ARG ILE ASN VAL SER GLY LEU THR THR          
SEQRES  31 C  408  LYS ASN LEU ASP TYR VAL ALA THR SER ILE HIS GLU ALA          
SEQRES  32 C  408  VAL THR LYS ILE GLN                                          
SEQRES   1 D  408  VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO VAL LEU VAL          
SEQRES   2 D  408  PHE LYS LEU THR ALA ASP PHE ARG GLU ASP PRO ASP PRO          
SEQRES   3 D  408  ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR ARG THR ASP          
SEQRES   4 D  408  ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL LYS LYS VAL          
SEQRES   5 D  408  GLU GLN LYS ILE ALA ASN ASP ASN SER LEU ASN HIS GLU          
SEQRES   6 D  408  TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE ARG SER CYS          
SEQRES   7 D  408  ALA SER ARG LEU ALA LEU GLY ASP ASP SER PRO ALA LEU          
SEQRES   8 D  408  LYS GLU LYS ARG VAL GLY GLY VAL GLN SER LEU GLY GLY          
SEQRES   9 D  408  ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE LEU ALA ARG          
SEQRES  10 D  408  TRP TYR ASN GLY THR ASN ASN LYS ASN THR PRO VAL TYR          
SEQRES  11 D  408  VAL SER SER PRO THR TRP GLU ASN HIS ASN ALA VAL PHE          
SEQRES  12 D  408  SER ALA ALA GLY PHE LYS ASP ILE ARG SER TYR ARG TYR          
SEQRES  13 D  408  TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU GLN GLY PHE          
SEQRES  14 D  408  LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE SER ILE VAL          
SEQRES  15 D  408  VAL LEU HIS ALA CYS ALA HIS ASN PRO THR GLY ILE ASP          
SEQRES  16 D  408  PRO THR PRO GLU GLN TRP LYS GLN ILE ALA SER VAL MET          
SEQRES  17 D  408  LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP SER ALA TYR          
SEQRES  18 D  408  GLN GLY PHE ALA SER GLY ASN LEU GLU ARG ASP ALA TRP          
SEQRES  19 D  408  ALA ILE ARG TYR PHE VAL SER GLU GLY PHE GLU PHE PHE          
SEQRES  20 D  408  CYS ALA GLN SER PHE SER LYS ASN PHE GLY LEU TYR ASN          
SEQRES  21 D  408  GLU ARG VAL GLY ASN LEU THR VAL VAL GLY LYS GLU PRO          
SEQRES  22 D  408  GLU SER ILE LEU GLN VAL LEU SER GLN MET GLU LYS ILE          
SEQRES  23 D  408  VAL ARG ILE THR TRP SER ASN PRO PRO ALA GLN GLY ALA          
SEQRES  24 D  408  ARG ILE VAL ALA SER THR LEU SER ASN PRO GLU LEU PHE          
SEQRES  25 D  408  GLU GLU TRP THR GLY ASN VAL LYS THR MET ALA ASP ARG          
SEQRES  26 D  408  ILE LEU THR MET ARG SER GLU LEU ARG ALA ARG LEU GLU          
SEQRES  27 D  408  ALA LEU LYS THR PRO GLY THR TRP ASN HIS ILE THR ASP          
SEQRES  28 D  408  GLN ILE GLY MET PHE SER PHE THR GLY LEU ASN PRO LYS          
SEQRES  29 D  408  GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS ILE TYR LEU          
SEQRES  30 D  408  LEU PRO SER GLY ARG ILE ASN VAL SER GLY LEU THR THR          
SEQRES  31 D  408  LYS ASN LEU ASP TYR VAL ALA THR SER ILE HIS GLU ALA          
SEQRES  32 D  408  VAL THR LYS ILE GLN                                          
SEQRES   1 E  408  VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO VAL LEU VAL          
SEQRES   2 E  408  PHE LYS LEU THR ALA ASP PHE ARG GLU ASP PRO ASP PRO          
SEQRES   3 E  408  ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR ARG THR ASP          
SEQRES   4 E  408  ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL LYS LYS VAL          
SEQRES   5 E  408  GLU GLN LYS ILE ALA ASN ASP ASN SER LEU ASN HIS GLU          
SEQRES   6 E  408  TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE ARG SER CYS          
SEQRES   7 E  408  ALA SER ARG LEU ALA LEU GLY ASP ASP SER PRO ALA LEU          
SEQRES   8 E  408  LYS GLU LYS ARG VAL GLY GLY VAL GLN SER LEU GLY GLY          
SEQRES   9 E  408  ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE LEU ALA ARG          
SEQRES  10 E  408  TRP TYR ASN GLY THR ASN ASN LYS ASN THR PRO VAL TYR          
SEQRES  11 E  408  VAL SER SER PRO THR TRP GLU ASN HIS ASN ALA VAL PHE          
SEQRES  12 E  408  SER ALA ALA GLY PHE LYS ASP ILE ARG SER TYR ARG TYR          
SEQRES  13 E  408  TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU GLN GLY PHE          
SEQRES  14 E  408  LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE SER ILE VAL          
SEQRES  15 E  408  VAL LEU HIS ALA CYS ALA HIS ASN PRO THR GLY ILE ASP          
SEQRES  16 E  408  PRO THR PRO GLU GLN TRP LYS GLN ILE ALA SER VAL MET          
SEQRES  17 E  408  LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP SER ALA TYR          
SEQRES  18 E  408  GLN GLY PHE ALA SER GLY ASN LEU GLU ARG ASP ALA TRP          
SEQRES  19 E  408  ALA ILE ARG TYR PHE VAL SER GLU GLY PHE GLU PHE PHE          
SEQRES  20 E  408  CYS ALA GLN SER PHE SER LYS ASN PHE GLY LEU TYR ASN          
SEQRES  21 E  408  GLU ARG VAL GLY ASN LEU THR VAL VAL GLY LYS GLU PRO          
SEQRES  22 E  408  GLU SER ILE LEU GLN VAL LEU SER GLN MET GLU LYS ILE          
SEQRES  23 E  408  VAL ARG ILE THR TRP SER ASN PRO PRO ALA GLN GLY ALA          
SEQRES  24 E  408  ARG ILE VAL ALA SER THR LEU SER ASN PRO GLU LEU PHE          
SEQRES  25 E  408  GLU GLU TRP THR GLY ASN VAL LYS THR MET ALA ASP ARG          
SEQRES  26 E  408  ILE LEU THR MET ARG SER GLU LEU ARG ALA ARG LEU GLU          
SEQRES  27 E  408  ALA LEU LYS THR PRO GLY THR TRP ASN HIS ILE THR ASP          
SEQRES  28 E  408  GLN ILE GLY MET PHE SER PHE THR GLY LEU ASN PRO LYS          
SEQRES  29 E  408  GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS ILE TYR LEU          
SEQRES  30 E  408  LEU PRO SER GLY ARG ILE ASN VAL SER GLY LEU THR THR          
SEQRES  31 E  408  LYS ASN LEU ASP TYR VAL ALA THR SER ILE HIS GLU ALA          
SEQRES  32 E  408  VAL THR LYS ILE GLN                                          
SEQRES   1 F  408  VAL PHE ALA GLU VAL PRO GLN ALA GLN PRO VAL LEU VAL          
SEQRES   2 F  408  PHE LYS LEU THR ALA ASP PHE ARG GLU ASP PRO ASP PRO          
SEQRES   3 F  408  ARG LYS VAL ASN LEU GLY VAL GLY ALA TYR ARG THR ASP          
SEQRES   4 F  408  ASP CYS HIS PRO TRP VAL LEU PRO VAL VAL LYS LYS VAL          
SEQRES   5 F  408  GLU GLN LYS ILE ALA ASN ASP ASN SER LEU ASN HIS GLU          
SEQRES   6 F  408  TYR LEU PRO ILE LEU GLY LEU ALA GLU PHE ARG SER CYS          
SEQRES   7 F  408  ALA SER ARG LEU ALA LEU GLY ASP ASP SER PRO ALA LEU          
SEQRES   8 F  408  LYS GLU LYS ARG VAL GLY GLY VAL GLN SER LEU GLY GLY          
SEQRES   9 F  408  ALA GLY ALA LEU ARG ILE GLY ALA ASP PHE LEU ALA ARG          
SEQRES  10 F  408  TRP TYR ASN GLY THR ASN ASN LYS ASN THR PRO VAL TYR          
SEQRES  11 F  408  VAL SER SER PRO THR TRP GLU ASN HIS ASN ALA VAL PHE          
SEQRES  12 F  408  SER ALA ALA GLY PHE LYS ASP ILE ARG SER TYR ARG TYR          
SEQRES  13 F  408  TRP ASP ALA GLU LYS ARG GLY LEU ASP LEU GLN GLY PHE          
SEQRES  14 F  408  LEU ASN ASP LEU GLU ASN ALA PRO GLU PHE SER ILE VAL          
SEQRES  15 F  408  VAL LEU HIS ALA CYS ALA HIS ASN PRO THR GLY ILE ASP          
SEQRES  16 F  408  PRO THR PRO GLU GLN TRP LYS GLN ILE ALA SER VAL MET          
SEQRES  17 F  408  LYS HIS ARG PHE LEU PHE PRO PHE PHE ASP SER ALA TYR          
SEQRES  18 F  408  GLN GLY PHE ALA SER GLY ASN LEU GLU ARG ASP ALA TRP          
SEQRES  19 F  408  ALA ILE ARG TYR PHE VAL SER GLU GLY PHE GLU PHE PHE          
SEQRES  20 F  408  CYS ALA GLN SER PHE SER LYS ASN PHE GLY LEU TYR ASN          
SEQRES  21 F  408  GLU ARG VAL GLY ASN LEU THR VAL VAL GLY LYS GLU PRO          
SEQRES  22 F  408  GLU SER ILE LEU GLN VAL LEU SER GLN MET GLU LYS ILE          
SEQRES  23 F  408  VAL ARG ILE THR TRP SER ASN PRO PRO ALA GLN GLY ALA          
SEQRES  24 F  408  ARG ILE VAL ALA SER THR LEU SER ASN PRO GLU LEU PHE          
SEQRES  25 F  408  GLU GLU TRP THR GLY ASN VAL LYS THR MET ALA ASP ARG          
SEQRES  26 F  408  ILE LEU THR MET ARG SER GLU LEU ARG ALA ARG LEU GLU          
SEQRES  27 F  408  ALA LEU LYS THR PRO GLY THR TRP ASN HIS ILE THR ASP          
SEQRES  28 F  408  GLN ILE GLY MET PHE SER PHE THR GLY LEU ASN PRO LYS          
SEQRES  29 F  408  GLN VAL GLU TYR LEU VAL ASN GLU LYS HIS ILE TYR LEU          
SEQRES  30 F  408  LEU PRO SER GLY ARG ILE ASN VAL SER GLY LEU THR THR          
SEQRES  31 F  408  LYS ASN LEU ASP TYR VAL ALA THR SER ILE HIS GLU ALA          
SEQRES  32 F  408  VAL THR LYS ILE GLN                                          
HET    PG4  A 501      13                                                       
HET    PLP  A 502      16                                                       
HET    PG4  B 501      10                                                       
HET    PLP  B 502      16                                                       
HET    PLP  C 501      16                                                       
HET    PG4  D 501      13                                                       
HET    PLP  D 502      16                                                       
HET    PLP  E 501      16                                                       
HET    PLP  F 501      16                                                       
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   7  PG4    3(C8 H18 O5)                                                 
FORMUL   8  PLP    6(C8 H10 N O6 P)                                             
FORMUL  16  HOH   *9(H2 O)                                                      
HELIX    1 AA1 VAL A   16  PHE A   19  5                                   4    
HELIX    2 AA2 LYS A   20  PHE A   25  1                                   6    
HELIX    3 AA3 LEU A   51  ASN A   63  1                                  13    
HELIX    4 AA4 LEU A   77  GLY A   90  1                                  14    
HELIX    5 AA5 SER A   93  GLU A   98  1                                   6    
HELIX    6 AA6 GLY A  108  TYR A  124  1                                  17    
HELIX    7 AA7 GLU A  142  ALA A  151  1                                  10    
HELIX    8 AA8 ASP A  170  ALA A  181  1                                  12    
HELIX    9 AA9 THR A  202  ARG A  216  1                                  15    
HELIX   10 AB1 ASN A  233  ALA A  238  1                                   6    
HELIX   11 AB2 ALA A  238  GLY A  248  1                                  11    
HELIX   12 AB3 LEU A  263  GLU A  266  5                                   4    
HELIX   13 AB4 GLU A  277  ILE A  294  1                                  18    
HELIX   14 AB5 PRO A  300  ASN A  313  1                                  14    
HELIX   15 AB6 ASN A  313  ALA A  340  1                                  28    
HELIX   16 AB7 ASN A  367  LEU A  374  1                                   8    
HELIX   17 AB8 SER A  391  LEU A  393  5                                   3    
HELIX   18 AB9 LEU B   51  ASN B   63  1                                  13    
HELIX   19 AC1 LEU B   77  GLY B   90  1                                  14    
HELIX   20 AC2 SER B   93  GLU B   98  1                                   6    
HELIX   21 AC3 GLY B  108  TYR B  124  1                                  17    
HELIX   22 AC4 GLU B  142  ALA B  151  1                                  10    
HELIX   23 AC5 ASP B  170  ASN B  180  1                                  11    
HELIX   24 AC6 THR B  202  ARG B  216  1                                  15    
HELIX   25 AC7 ASN B  233  ALA B  238  1                                   6    
HELIX   26 AC8 ALA B  238  GLU B  247  1                                  10    
HELIX   27 AC9 LEU B  263  GLU B  266  5                                   4    
HELIX   28 AD1 GLU B  277  ILE B  294  1                                  18    
HELIX   29 AD2 PRO B  300  ASN B  313  1                                  14    
HELIX   30 AD3 ASN B  313  LEU B  342  1                                  30    
HELIX   31 AD4 TRP B  351  THR B  355  5                                   5    
HELIX   32 AD5 SER B  391  LEU B  393  5                                   3    
HELIX   33 AD6 ASN B  397  VAL B  409  1                                  13    
HELIX   34 AD7 LEU C   17  GLU C   27  1                                  11    
HELIX   35 AD8 LEU C   51  ASN C   63  1                                  13    
HELIX   36 AD9 LEU C   77  GLY C   90  1                                  14    
HELIX   37 AE1 SER C   93  GLU C   98  1                                   6    
HELIX   38 AE2 GLY C  108  TYR C  124  1                                  17    
HELIX   39 AE3 GLU C  142  GLY C  152  1                                  11    
HELIX   40 AE4 ASP C  170  ALA C  181  1                                  12    
HELIX   41 AE5 THR C  202  ARG C  216  1                                  15    
HELIX   42 AE6 ALA C  238  GLU C  247  1                                  10    
HELIX   43 AE7 LEU C  263  GLU C  266  5                                   4    
HELIX   44 AE8 GLU C  277  ILE C  294  1                                  18    
HELIX   45 AE9 PRO C  300  ASN C  313  1                                  14    
HELIX   46 AF1 ASN C  313  ALA C  340  1                                  28    
HELIX   47 AF2 TRP C  351  THR C  355  5                                   5    
HELIX   48 AF3 ASN C  367  GLU C  377  1                                  11    
HELIX   49 AF4 SER C  391  LEU C  393  5                                   3    
HELIX   50 AF5 THR C  394  LEU C  398  5                                   5    
HELIX   51 AF6 LYS D   20  ARG D   26  1                                   7    
HELIX   52 AF7 LEU D   51  ASP D   64  1                                  14    
HELIX   53 AF8 LEU D   77  GLY D   90  1                                  14    
HELIX   54 AF9 SER D   93  GLU D   98  1                                   6    
HELIX   55 AG1 GLY D  108  TYR D  124  1                                  17    
HELIX   56 AG2 ASN D  143  ALA D  151  1                                   9    
HELIX   57 AG3 ASP D  170  ALA D  181  1                                  12    
HELIX   58 AG4 THR D  202  ARG D  216  1                                  15    
HELIX   59 AG5 ASN D  233  ALA D  238  1                                   6    
HELIX   60 AG6 ALA D  238  GLU D  247  1                                  10    
HELIX   61 AG7 LEU D  263  GLU D  266  5                                   4    
HELIX   62 AG8 GLU D  277  ILE D  294  1                                  18    
HELIX   63 AG9 PRO D  300  ASN D  313  1                                  14    
HELIX   64 AH1 ASN D  313  GLU D  337  1                                  25    
HELIX   65 AH2 SER D  391  LEU D  393  5                                   3    
HELIX   66 AH3 ASN D  397  SER D  404  1                                   8    
HELIX   67 AH4 ILE D  405  GLU D  407  5                                   3    
HELIX   68 AH5 VAL E   18  THR E   22  1                                   5    
HELIX   69 AH6 LEU E   51  ASN E   63  1                                  13    
HELIX   70 AH7 LEU E   77  GLY E   90  1                                  14    
HELIX   71 AH8 SER E   93  GLU E   98  1                                   6    
HELIX   72 AH9 GLY E  108  TYR E  124  1                                  17    
HELIX   73 AI1 ASN E  143  GLY E  152  1                                  10    
HELIX   74 AI2 ASP E  170  ASN E  180  1                                  11    
HELIX   75 AI3 THR E  202  ARG E  216  1                                  15    
HELIX   76 AI4 ASN E  233  ALA E  238  1                                   6    
HELIX   77 AI5 ALA E  238  GLU E  247  1                                  10    
HELIX   78 AI6 LEU E  263  GLU E  266  5                                   4    
HELIX   79 AI7 GLU E  277  ILE E  294  1                                  18    
HELIX   80 AI8 ALA E  301  ASN E  313  1                                  13    
HELIX   81 AI9 ASN E  313  SER E  336  1                                  24    
HELIX   82 AJ1 SER E  391  LEU E  393  5                                   3    
HELIX   83 AJ2 LEU F   51  ASP F   64  1                                  14    
HELIX   84 AJ3 LEU F   77  GLY F   90  1                                  14    
HELIX   85 AJ4 SER F   93  GLU F   98  1                                   6    
HELIX   86 AJ5 GLY F  108  TYR F  124  1                                  17    
HELIX   87 AJ6 ASN F  143  GLY F  152  1                                  10    
HELIX   88 AJ7 ASP F  170  ALA F  181  1                                  12    
HELIX   89 AJ8 THR F  202  ARG F  216  1                                  15    
HELIX   90 AJ9 ASN F  233  ALA F  238  1                                   6    
HELIX   91 AK1 ALA F  238  GLY F  248  1                                  11    
HELIX   92 AK2 LEU F  263  GLU F  266  5                                   4    
HELIX   93 AK3 GLU F  277  ILE F  294  1                                  18    
HELIX   94 AK4 PRO F  300  ASN F  313  1                                  14    
HELIX   95 AK5 ASN F  313  ARG F  341  1                                  29    
HELIX   96 AK6 TRP F  351  THR F  355  5                                   5    
HELIX   97 AK7 ASN F  367  GLU F  377  1                                  11    
HELIX   98 AK8 SER F  391  LEU F  393  5                                   3    
SHEET    1 AA1 7 VAL A 101  LEU A 107  0                                        
SHEET    2 AA1 7 VAL A 268  VAL A 274 -1  O  VAL A 273   N  GLY A 102           
SHEET    3 AA1 7 PHE A 251  SER A 256 -1  N  GLN A 255   O  ASN A 270           
SHEET    4 AA1 7 PHE A 219  SER A 224  1  N  PHE A 222   O  PHE A 252           
SHEET    5 AA1 7 ILE A 186  HIS A 190  1  N  VAL A 187   O  PHE A 221           
SHEET    6 AA1 7 VAL A 134  SER A 138  1  N  TYR A 135   O  VAL A 188           
SHEET    7 AA1 7 ILE A 156  ARG A 160  1  O  ARG A 157   N  VAL A 134           
SHEET    1 AA2 2 TRP A 162  ASP A 163  0                                        
SHEET    2 AA2 2 GLY A 168  LEU A 169 -1  O  GLY A 168   N  ASP A 163           
SHEET    1 AA3 2 PHE A 361  PHE A 363  0                                        
SHEET    2 AA3 2 ARG A 387  ASN A 389 -1  O  ILE A 388   N  SER A 362           
SHEET    1 AA4 7 VAL B 101  LEU B 107  0                                        
SHEET    2 AA4 7 VAL B 268  VAL B 274 -1  O  VAL B 273   N  GLY B 102           
SHEET    3 AA4 7 PHE B 251  SER B 256 -1  N  GLN B 255   O  ASN B 270           
SHEET    4 AA4 7 PHE B 219  SER B 224  1  N  PHE B 222   O  PHE B 252           
SHEET    5 AA4 7 ILE B 186  HIS B 190  1  N  VAL B 187   O  PHE B 221           
SHEET    6 AA4 7 VAL B 134  SER B 138  1  N  TYR B 135   O  VAL B 188           
SHEET    7 AA4 7 ILE B 156  ARG B 160  1  O  ARG B 157   N  VAL B 134           
SHEET    1 AA5 2 TRP B 162  ASP B 163  0                                        
SHEET    2 AA5 2 GLY B 168  LEU B 169 -1  O  GLY B 168   N  ASP B 163           
SHEET    1 AA6 2 PHE B 361  PHE B 363  0                                        
SHEET    2 AA6 2 ARG B 387  ASN B 389 -1  O  ILE B 388   N  SER B 362           
SHEET    1 AA7 7 VAL C 101  LEU C 107  0                                        
SHEET    2 AA7 7 VAL C 268  VAL C 274 -1  O  VAL C 273   N  GLY C 102           
SHEET    3 AA7 7 PHE C 251  SER C 256 -1  N  GLN C 255   O  ASN C 270           
SHEET    4 AA7 7 PHE C 219  SER C 224  1  N  PHE C 222   O  ALA C 254           
SHEET    5 AA7 7 ILE C 186  HIS C 190  1  N  VAL C 187   O  PHE C 221           
SHEET    6 AA7 7 VAL C 134  SER C 138  1  N  TYR C 135   O  VAL C 188           
SHEET    7 AA7 7 ILE C 156  ARG C 160  1  O  ARG C 157   N  VAL C 134           
SHEET    1 AA8 2 TRP C 162  ASP C 163  0                                        
SHEET    2 AA8 2 GLY C 168  LEU C 169 -1  O  GLY C 168   N  ASP C 163           
SHEET    1 AA9 2 PHE C 361  PHE C 363  0                                        
SHEET    2 AA9 2 ARG C 387  ASN C 389 -1  O  ILE C 388   N  SER C 362           
SHEET    1 AB1 7 VAL D 101  LEU D 107  0                                        
SHEET    2 AB1 7 VAL D 268  VAL D 274 -1  O  VAL D 273   N  GLY D 102           
SHEET    3 AB1 7 PHE D 251  SER D 256 -1  N  GLN D 255   O  ASN D 270           
SHEET    4 AB1 7 PHE D 219  SER D 224  1  N  PHE D 222   O  ALA D 254           
SHEET    5 AB1 7 ILE D 186  HIS D 190  1  N  VAL D 187   O  PHE D 221           
SHEET    6 AB1 7 VAL D 134  SER D 138  1  N  TYR D 135   O  VAL D 188           
SHEET    7 AB1 7 ILE D 156  ARG D 160  1  O  ARG D 157   N  VAL D 134           
SHEET    1 AB2 2 TRP D 162  ASP D 163  0                                        
SHEET    2 AB2 2 GLY D 168  LEU D 169 -1  O  GLY D 168   N  ASP D 163           
SHEET    1 AB3 2 PHE D 361  PHE D 363  0                                        
SHEET    2 AB3 2 ARG D 387  ASN D 389 -1  O  ILE D 388   N  SER D 362           
SHEET    1 AB4 7 VAL E 101  LEU E 107  0                                        
SHEET    2 AB4 7 VAL E 268  VAL E 274 -1  O  VAL E 273   N  GLY E 102           
SHEET    3 AB4 7 PHE E 251  SER E 256 -1  N  GLN E 255   O  ASN E 270           
SHEET    4 AB4 7 PHE E 219  SER E 224  1  N  PHE E 222   O  ALA E 254           
SHEET    5 AB4 7 ILE E 186  HIS E 190  1  N  VAL E 187   O  PHE E 221           
SHEET    6 AB4 7 VAL E 134  SER E 138  1  N  TYR E 135   O  VAL E 188           
SHEET    7 AB4 7 ILE E 156  ARG E 160  1  O  ARG E 157   N  VAL E 134           
SHEET    1 AB5 2 TRP E 162  ASP E 163  0                                        
SHEET    2 AB5 2 GLY E 168  LEU E 169 -1  O  GLY E 168   N  ASP E 163           
SHEET    1 AB6 2 PHE E 361  PHE E 363  0                                        
SHEET    2 AB6 2 ARG E 387  ASN E 389 -1  O  ILE E 388   N  SER E 362           
SHEET    1 AB7 7 VAL F 101  LEU F 107  0                                        
SHEET    2 AB7 7 VAL F 268  VAL F 274 -1  O  VAL F 273   N  GLY F 102           
SHEET    3 AB7 7 PHE F 251  SER F 256 -1  N  GLN F 255   O  ASN F 270           
SHEET    4 AB7 7 PHE F 219  SER F 224  1  N  PHE F 222   O  ALA F 254           
SHEET    5 AB7 7 ILE F 186  HIS F 190  1  N  VAL F 187   O  PHE F 221           
SHEET    6 AB7 7 VAL F 134  SER F 138  1  N  TYR F 135   O  VAL F 188           
SHEET    7 AB7 7 ILE F 156  ARG F 160  1  O  ARG F 157   N  VAL F 134           
SHEET    1 AB8 2 TRP F 162  ASP F 163  0                                        
SHEET    2 AB8 2 GLY F 168  LEU F 169 -1  O  GLY F 168   N  ASP F 163           
SHEET    1 AB9 2 PHE F 361  PHE F 363  0                                        
SHEET    2 AB9 2 ARG F 387  ASN F 389 -1  O  ILE F 388   N  SER F 362           
CISPEP   1 SER A  138    PRO A  139          0        -6.27                     
CISPEP   2 ASN A  195    PRO A  196          0        21.06                     
CISPEP   3 SER B  138    PRO B  139          0        -4.37                     
CISPEP   4 ASN B  195    PRO B  196          0        19.96                     
CISPEP   5 SER C  138    PRO C  139          0        -4.02                     
CISPEP   6 ASN C  195    PRO C  196          0        19.62                     
CISPEP   7 SER D  138    PRO D  139          0        -6.74                     
CISPEP   8 ASN D  195    PRO D  196          0        20.45                     
CISPEP   9 SER E  138    PRO E  139          0        -4.07                     
CISPEP  10 ASN E  195    PRO E  196          0        20.77                     
CISPEP  11 SER F  138    PRO F  139          0        -5.82                     
CISPEP  12 ASN F  195    PRO F  196          0        21.12                     
SITE     1 AC1  1 GLU A 250                                                     
SITE     1 AC2 11 GLY A 108  GLY A 109  ALA A 110  TRP A 141                    
SITE     2 AC2 11 ASN A 195  ASP A 223  ALA A 225  SER A 256                    
SITE     3 AC2 11 SER A 258  LYS A 259  ARG A 267                               
SITE     1 AC3  2 GLU B 250  LYS B 276                                          
SITE     1 AC4 10 GLY B 109  TRP B 141  ASN B 195  ASP B 223                    
SITE     2 AC4 10 ALA B 225  SER B 256  SER B 258  LYS B 259                    
SITE     3 AC4 10 ARG B 267  HOH B 601                                          
SITE     1 AC5 10 GLY C 109  ALA C 110  TRP C 141  ASN C 195                    
SITE     2 AC5 10 ASP C 223  ALA C 225  SER C 256  SER C 258                    
SITE     3 AC5 10 LYS C 259  ARG C 267                                          
SITE     1 AC6  3 GLU D 250  GLN D 283  VAL D 284                               
SITE     1 AC7 11 GLY D 108  GLY D 109  ALA D 110  TRP D 141                    
SITE     2 AC7 11 HIS D 144  ASN D 195  ASP D 223  SER D 256                    
SITE     3 AC7 11 SER D 258  LYS D 259  ARG D 267                               
SITE     1 AC8 11 GLY E 108  GLY E 109  ALA E 110  TRP E 141                    
SITE     2 AC8 11 ASN E 195  ASP E 223  ALA E 225  SER E 256                    
SITE     3 AC8 11 SER E 258  LYS E 259  ARG E 267                               
SITE     1 AC9 10 GLY F 108  GLY F 109  ALA F 110  TRP F 141                    
SITE     2 AC9 10 ASN F 195  ASP F 223  SER F 256  SER F 258                    
SITE     3 AC9 10 LYS F 259  ARG F 267                                          
CRYST1  257.700  148.626   83.183  90.00  89.98  90.00 C 1 2 1      24          
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      0.003880  0.000000 -0.000001        0.00000                         
SCALE2      0.000000  0.006728  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012022        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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