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Database: PDB
Entry: 2VGZ
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HEADER    TRANSFERASE                             16-NOV-07   2VGZ              
TITLE     CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KYNURENINE/ALPHA-AMINOADIPATE AMINOTRANSFERASE;            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-425;                                            
COMPND   5 SYNONYM: KYNURENINE AMINOTRANSFERASE II, KAT/AADAT,                  
COMPND   6  KYNURENINE--OXOGLUTARATE TRANSAMINASE II, KYNURENINE--OXOGLUTARATE  
COMPND   7  AMINOTRANSFERASE II, 2-AMINOADIPATE TRANSAMINASE, 2-AMINOADIPATE    
COMPND   8  AMINOTRANSFERASE, ALPHA-AMINOADIPATE AMINOTRANSFERASE, AADAT;       
COMPND   9 EC: 2.6.1.39, 2.6.1.7;                                               
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET16B                                    
KEYWDS    MULTIFUNCTIONAL ENZYME, TRANSIT PEPTIDE, AMINOTRANSFERASE, PYRIDOXAL  
KEYWDS   2 PHOSPHATE, PLP ENZYME, KYNURENINE, TRANSFERASE, MITOCHONDRION        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.ROSSI,S.GARAVAGLIA,V.MONTALBANO,M.A.WALSH,M.RIZZI                   
REVDAT   5   09-DEC-15 2VGZ    1       COMPND KEYWDS JRNL   REMARK              
REVDAT   5 2                           VERSN  SEQRES HET    MODRES              
REVDAT   5 3                           HETNAM HETSYN FORMUL LINK                
REVDAT   5 4                           SITE   ATOM   TER    HETATM              
REVDAT   5 5                           CONECT MASTER                            
REVDAT   4   24-FEB-09 2VGZ    1       VERSN                                    
REVDAT   3   01-APR-08 2VGZ    1       REMARK HETATM                            
REVDAT   2   19-FEB-08 2VGZ    1       JRNL                                     
REVDAT   1   04-DEC-07 2VGZ    0                                                
JRNL        AUTH   F.ROSSI,S.GARAVAGLIA,V.MONTALBANO,M.A.WALSH,M.RIZZI          
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II,   
JRNL        TITL 2 A DRUG TARGET FOR THE TREATMENT OF SCHIZOPHRENIA.            
JRNL        REF    J.BIOL.CHEM.                  V. 283  3559 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18056996                                                     
JRNL        DOI    10.1074/JBC.M707925200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 40255                          
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) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2161                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2914                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6475                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 49                                      
REMARK   3   SOLVENT ATOMS            : 403                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.317         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.237         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.159         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.355         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6683 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9072 ; 1.675 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   822 ; 6.565 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   284 ;42.077 ;24.789       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1144 ;16.615 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;17.978 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1002 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5028 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3045 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4546 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   457 ; 0.179 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    33 ; 0.282 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4196 ; 1.019 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6714 ; 1.811 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2757 ; 2.858 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2358 ; 4.584 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. RESIDUES FROM -3 TO -1 AT THE N-TERMINI IN        
REMARK   3  BOTH MONOMERS BELONGS TO THE HISTIDINE TAG                          
REMARK   4                                                                      
REMARK   4 2VGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-34442.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41797                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.18                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX-SHARP                                           
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 49.11                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       49.81550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.47800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.81550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       77.47800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 8550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     MET A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     ARG A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     ILE B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     MET B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     ASP B    24                                                      
REMARK 465     ILE B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     ARG B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     PRO B    30                                                      
REMARK 465     LYS B    31                                                      
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     VAL A 284    O                                                   
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   NE2  GLN A    62     O    HOH A  2039              1.66            
REMARK 500   C    GLU B    -1     N    ASN B     2              1.98            
REMARK 500   O    PRO B    18     O    HOH B  2018              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2204     O    HOH B  2204     2665     1.29            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  -1   C     ASN A   2   N       1.136                       
REMARK 500    CYS A 112   CB    CYS A 112   SG     -0.131                       
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    ASN A   2   C   -  N   -  CA  ANGL. DEV. = -46.6 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B 399   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  -1      -29.35    -39.57                                   
REMARK 500    TYR A  74      150.24    -44.78                                   
REMARK 500    ASN A  96       64.07     35.28                                   
REMARK 500    ASP A 162     -153.44   -140.86                                   
REMARK 500    ASN A 189       59.09   -112.45                                   
REMARK 500    SER A 266      124.22    175.83                                   
REMARK 500    SER A 291      -93.65   -127.50                                   
REMARK 500    LEU A 293      -46.15     71.59                                   
REMARK 500    GLU A 372      -50.42   -138.76                                   
REMARK 500    GLU A 423        7.17    -59.13                                   
REMARK 500    SER A 424       64.64   -163.53                                   
REMARK 500    SER B  17       52.31   -142.05                                   
REMARK 500    GLU B  56      -81.69    -22.05                                   
REMARK 500    ASN B  96       62.82     36.67                                   
REMARK 500    GLU B 163       -8.79    -59.87                                   
REMARK 500    SER B 176       -9.92    -59.29                                   
REMARK 500    SER B 266      135.38   -172.60                                   
REMARK 500    SER B 291      -93.51   -122.53                                   
REMARK 500    LEU B 293      -46.03     72.49                                   
REMARK 500    SER B 296      121.67    -36.84                                   
REMARK 500    GLU B 372      -74.58    -72.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A  -2        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A1263                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B1263                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A1426                 
DBREF  2VGZ A   -3    -1  PDB    2VGZ     2VGZ            -3     -1             
DBREF  2VGZ A    2   425  UNP    Q8N5Z0   AADAT_HUMAN      2    425             
DBREF  2VGZ B   -3    -1  PDB    2VGZ     2VGZ            -3     -1             
DBREF  2VGZ B    2   425  UNP    Q8N5Z0   AADAT_HUMAN      2    425             
SEQRES   1 A  427  MET LEU GLU ASN TYR ALA ARG PHE ILE THR ALA ALA SER          
SEQRES   2 A  427  ALA ALA ARG ASN PRO SER PRO ILE ARG THR MET THR ASP          
SEQRES   3 A  427  ILE LEU SER ARG GLY PRO LYS SER MET ILE SER LEU ALA          
SEQRES   4 A  427  GLY GLY LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR          
SEQRES   5 A  427  ALA VAL ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE          
SEQRES   6 A  427  GLY GLU GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO          
SEQRES   7 A  427  SER ALA GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN          
SEQRES   8 A  427  LEU GLN ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR          
SEQRES   9 A  427  PRO PRO SER GLN GLY GLN MET ASP LEU CYS VAL THR SER          
SEQRES  10 A  427  GLY SER GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE          
SEQRES  11 A  427  ILE ASN PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA          
SEQRES  12 A  427  TYR SER GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS          
SEQRES  13 A  427  ASN ILE ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL          
SEQRES  14 A  427  PRO ASP SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO          
SEQRES  15 A  427  GLU ASP ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE          
SEQRES  16 A  427  LEU TYR THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN          
SEQRES  17 A  427  SER LEU THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU          
SEQRES  18 A  427  ALA ARG LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO          
SEQRES  19 A  427  TYR TYR PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR          
SEQRES  20 A  427  PHE LEU SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA          
SEQRES  21 A  427  ASP SER PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE          
SEQRES  22 A  427  GLY PHE LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL          
SEQRES  23 A  427  ILE LEU HIS ILE GLN VAL SER THR LEU HIS PRO SER THR          
SEQRES  24 A  427  PHE ASN GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP          
SEQRES  25 A  427  GLY GLU GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE          
SEQRES  26 A  427  ASP PHE TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA          
SEQRES  27 A  427  ALA ASP LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL          
SEQRES  28 A  427  PRO ALA ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY          
SEQRES  29 A  427  ILE ASN ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL          
SEQRES  30 A  427  LYS MET GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR          
SEQRES  31 A  427  VAL ASP SER SER ALA PRO SER PRO TYR LEU ARG ALA SER          
SEQRES  32 A  427  PHE SER SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE          
SEQRES  33 A  427  GLN VAL LEU ALA GLN LEU ILE LYS GLU SER LEU                  
SEQRES   1 B  427  MET LEU GLU ASN TYR ALA ARG PHE ILE THR ALA ALA SER          
SEQRES   2 B  427  ALA ALA ARG ASN PRO SER PRO ILE ARG THR MET THR ASP          
SEQRES   3 B  427  ILE LEU SER ARG GLY PRO LYS SER MET ILE SER LEU ALA          
SEQRES   4 B  427  GLY GLY LEU PRO ASN PRO ASN MET PHE PRO PHE LYS THR          
SEQRES   5 B  427  ALA VAL ILE THR VAL GLU ASN GLY LYS THR ILE GLN PHE          
SEQRES   6 B  427  GLY GLU GLU MET MET LYS ARG ALA LEU GLN TYR SER PRO          
SEQRES   7 B  427  SER ALA GLY ILE PRO GLU LEU LEU SER TRP LEU LYS GLN          
SEQRES   8 B  427  LEU GLN ILE LYS LEU HIS ASN PRO PRO THR ILE HIS TYR          
SEQRES   9 B  427  PRO PRO SER GLN GLY GLN MET ASP LEU CYS VAL THR SER          
SEQRES  10 B  427  GLY SER GLN GLN GLY LEU CYS LYS VAL PHE GLU MET ILE          
SEQRES  11 B  427  ILE ASN PRO GLY ASP ASN VAL LEU LEU ASP GLU PRO ALA          
SEQRES  12 B  427  TYR SER GLY THR LEU GLN SER LEU HIS PRO LEU GLY CYS          
SEQRES  13 B  427  ASN ILE ILE ASN VAL ALA SER ASP GLU SER GLY ILE VAL          
SEQRES  14 B  427  PRO ASP SER LEU ARG ASP ILE LEU SER ARG TRP LYS PRO          
SEQRES  15 B  427  GLU ASP ALA LYS ASN PRO GLN LYS ASN THR PRO LYS PHE          
SEQRES  16 B  427  LEU TYR THR VAL PRO ASN GLY ASN ASN PRO THR GLY ASN          
SEQRES  17 B  427  SER LEU THR SER GLU ARG LYS LYS GLU ILE TYR GLU LEU          
SEQRES  18 B  427  ALA ARG LYS TYR ASP PHE LEU ILE ILE GLU ASP ASP PRO          
SEQRES  19 B  427  TYR TYR PHE LEU GLN PHE ASN LYS PHE ARG VAL PRO THR          
SEQRES  20 B  427  PHE LEU SER MET ASP VAL ASP GLY ARG VAL ILE ARG ALA          
SEQRES  21 B  427  ASP SER PHE SER LYS ILE ILE SER SER GLY LEU ARG ILE          
SEQRES  22 B  427  GLY PHE LEU THR GLY PRO LYS PRO LEU ILE GLU ARG VAL          
SEQRES  23 B  427  ILE LEU HIS ILE GLN VAL SER THR LEU HIS PRO SER THR          
SEQRES  24 B  427  PHE ASN GLN LEU MET ILE SER GLN LEU LEU HIS GLU TRP          
SEQRES  25 B  427  GLY GLU GLU GLY PHE MET ALA HIS VAL ASP ARG VAL ILE          
SEQRES  26 B  427  ASP PHE TYR SER ASN GLN LYS ASP ALA ILE LEU ALA ALA          
SEQRES  27 B  427  ALA ASP LYS TRP LEU THR GLY LEU ALA GLU TRP HIS VAL          
SEQRES  28 B  427  PRO ALA ALA GLY MET PHE LEU TRP ILE LYS VAL LYS GLY          
SEQRES  29 B  427  ILE ASN ASP VAL LYS GLU LEU ILE GLU GLU LYS ALA VAL          
SEQRES  30 B  427  LYS MET GLY VAL LEU MET LEU PRO GLY ASN ALA PHE TYR          
SEQRES  31 B  427  VAL ASP SER SER ALA PRO SER PRO TYR LEU ARG ALA SER          
SEQRES  32 B  427  PHE SER SER ALA SER PRO GLU GLN MET ASP VAL ALA PHE          
SEQRES  33 B  427  GLN VAL LEU ALA GLN LEU ILE LYS GLU SER LEU                  
HET    PLP  A1263      15                                                       
HET    PLP  B1263      15                                                       
HET    IOD  A1426       1                                                       
HETNAM     IOD IODIDE ION                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
FORMUL   3  IOD    I 1-                                                         
FORMUL   4  PLP    2(C8 H10 N O6 P)                                             
FORMUL   5  HOH   *403(H2 O)                                                    
HELIX    1   1 TYR A    3  ILE A    7  5                                   5    
HELIX    2   2 THR A    8  ARG A   14  1                                   7    
HELIX    3   3 ASN A   42  PHE A   46  5                                   5    
HELIX    4   4 GLY A   64  LEU A   72  1                                   9    
HELIX    5   5 ILE A   80  ASN A   96  1                                  17    
HELIX    6   6 PRO A   97  TYR A  102  5                                   6    
HELIX    7   7 GLY A  116  ILE A  129  1                                  14    
HELIX    8   8 TYR A  142  HIS A  150  1                                   9    
HELIX    9   9 PRO A  151  GLY A  153  5                                   3    
HELIX   10  10 VAL A  167  SER A  176  1                                  10    
HELIX   11  11 LYS A  179  ALA A  183  5                                   5    
HELIX   12  12 THR A  209  TYR A  223  1                                  15    
HELIX   13  13 PHE A  246  ASP A  250  5                                   5    
HELIX   14  14 LYS A  278  ARG A  283  1                                   6    
HELIX   15  15 HIS A  287  SER A  291  5                                   5    
HELIX   16  16 SER A  296  THR A  342  1                                  47    
HELIX   17  17 VAL A  366  GLU A  372  1                                   7    
HELIX   18  18 GLU A  372  MET A  377  1                                   6    
HELIX   19  19 ASN A  385  TYR A  388  5                                   4    
HELIX   20  20 SER A  406  GLU A  423  1                                  18    
HELIX   21  21 LEU B   -2  ILE B    7  5                                   8    
HELIX   22  22 THR B    8  ARG B   14  1                                   7    
HELIX   23  23 ASN B   42  PHE B   46  5                                   5    
HELIX   24  24 GLY B   64  LEU B   72  1                                   9    
HELIX   25  25 ILE B   80  ASN B   96  1                                  17    
HELIX   26  26 PRO B   97  TYR B  102  5                                   6    
HELIX   27  27 GLY B  116  ILE B  129  1                                  14    
HELIX   28  28 TYR B  142  HIS B  150  1                                   9    
HELIX   29  29 PRO B  151  GLY B  153  5                                   3    
HELIX   30  30 VAL B  167  SER B  176  1                                  10    
HELIX   31  31 LYS B  179  ALA B  183  5                                   5    
HELIX   32  32 THR B  209  TYR B  223  1                                  15    
HELIX   33  33 TYR B  233  LEU B  236  5                                   4    
HELIX   34  34 THR B  245  ASP B  250  5                                   6    
HELIX   35  35 LYS B  278  GLN B  289  1                                  12    
HELIX   36  36 SER B  296  THR B  342  1                                  47    
HELIX   37  37 VAL B  366  GLU B  372  1                                   7    
HELIX   38  38 GLU B  372  MET B  377  1                                   6    
HELIX   39  39 ASN B  385  TYR B  388  5                                   4    
HELIX   40  40 SER B  406  SER B  424  1                                  19    
SHEET    1  AA 2 ILE A  34  SER A  35  0                                        
SHEET    2  AA 2 VAL B 379  LEU B 380  1  N  LEU B 380   O  ILE A  34           
SHEET    1  AB 4 ILE A  61  PHE A  63  0                                        
SHEET    2  AB 4 PHE A  48  VAL A  55 -1  O  ALA A  51   N  PHE A  63           
SHEET    3  AB 4 PHE B  48  VAL B  55 -1  N  LYS B  49   O  THR A  54           
SHEET    4  AB 4 ILE B  61  PHE B  63 -1  O  ILE B  61   N  ILE B  53           
SHEET    1  AC 5 MET A 109  THR A 114  0                                        
SHEET    2  AC 5 GLY A 272  PRO A 277 -1  O  GLY A 272   N  THR A 114           
SHEET    3  AC 5 VAL A 255  SER A 260 -1  O  ARG A 257   N  THR A 275           
SHEET    4  AC 5 LEU A 226  ASP A 230  1  O  ILE A 227   N  ILE A 256           
SHEET    5  AC 5 PHE A 193  THR A 196  1  O  LEU A 194   N  ILE A 228           
SHEET    1  AD 2 ASN A 134  ASP A 138  0                                        
SHEET    2  AD 2 ASN A 155  VAL A 159  1  O  ASN A 155   N  VAL A 135           
SHEET    1  AE 2 SER A 161  ASP A 162  0                                        
SHEET    2  AE 2 GLY A 165  ILE A 166 -1  O  GLY A 165   N  ASP A 162           
SHEET    1  AF 4 ALA A 345  TRP A 347  0                                        
SHEET    2  AF 4 PHE A 355  VAL A 360 -1  O  LYS A 359   N  GLU A 346           
SHEET    3  AF 4 TYR A 397  SER A 401 -1  O  LEU A 398   N  ILE A 358           
SHEET    4  AF 4 LEU A 382  PRO A 383 -1  O  LEU A 382   N  ARG A 399           
SHEET    1  AG 2 VAL A 379  LEU A 380  0                                        
SHEET    2  AG 2 ILE B  34  SER B  35  1  O  ILE B  34   N  LEU A 380           
SHEET    1  BA 7 MET B 109  THR B 114  0                                        
SHEET    2  BA 7 GLY B 272  PRO B 277 -1  O  GLY B 272   N  THR B 114           
SHEET    3  BA 7 VAL B 255  SER B 260 -1  O  ARG B 257   N  THR B 275           
SHEET    4  BA 7 LEU B 226  ASP B 230  1  O  ILE B 227   N  ILE B 256           
SHEET    5  BA 7 PHE B 193  THR B 196  1  O  LEU B 194   N  ILE B 228           
SHEET    6  BA 7 ASN B 134  LEU B 137  1  O  LEU B 136   N  TYR B 195           
SHEET    7  BA 7 ASN B 155  ASN B 158  1  O  ASN B 155   N  VAL B 135           
SHEET    1  BB 2 SER B 161  ASP B 162  0                                        
SHEET    2  BB 2 GLY B 165  ILE B 166 -1  O  GLY B 165   N  ASP B 162           
SHEET    1  BC 4 ALA B 345  GLU B 346  0                                        
SHEET    2  BC 4 PHE B 355  VAL B 360 -1  O  LYS B 359   N  GLU B 346           
SHEET    3  BC 4 TYR B 397  SER B 401 -1  O  LEU B 398   N  ILE B 358           
SHEET    4  BC 4 LEU B 382  PRO B 383 -1  O  LEU B 382   N  ARG B 399           
LINK         NZ  LYS A 263                 C4A PLP A1263     1555   1555  1.34  
LINK         NZ  LYS B 263                 C4A PLP B1263     1555   1555  1.32  
CISPEP   1 GLU A  139    PRO A  140          0        -1.51                     
CISPEP   2 ASN A  202    PRO A  203          0        16.35                     
CISPEP   3 GLU B  139    PRO B  140          0        -3.43                     
CISPEP   4 ASN B  202    PRO B  203          0        10.87                     
SITE     1 AC1 12 GLY A 116  SER A 117  GLN A 118  TYR A 142                    
SITE     2 AC1 12 ASN A 202  TYR A 233  SER A 260  SER A 262                    
SITE     3 AC1 12 LYS A 263  ARG A 270  HOH A2154  TYR B  74                    
SITE     1 AC2 12 TYR A  74  GLY B 116  SER B 117  GLN B 118                    
SITE     2 AC2 12 TYR B 142  ASN B 202  PRO B 232  TYR B 233                    
SITE     3 AC2 12 SER B 260  SER B 262  LYS B 263  ARG B 270                    
SITE     1 AC3  4 GLN A 119  LYS A 123  GLN B 119  LYS B 123                    
CRYST1   99.631  154.956   61.201  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010037  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006453  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016340        0.00000                         
MTRIX1   1 -0.999830 -0.008270  0.016510       63.88042    1                    
MTRIX2   1 -0.000980 -0.869090 -0.494660       87.19806    1                    
MTRIX3   1  0.018440 -0.494590  0.868930       22.46176    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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