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Database: PDB
Entry: 3II0
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HEADER    TRANSFERASE                             31-JUL-09   3II0              
TITLE     CRYSTAL STRUCTURE OF HUMAN GLUTAMATE OXALOACETATE TRANSAMINASE 1      
TITLE    2 (GOT1)                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC;                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 14-412;                                       
COMPND   5 SYNONYM: TRANSAMINASE A, GLUTAMATE OXALOACETATE TRANSAMINASE 1;      
COMPND   6 EC: 2.6.1.1;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GOT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF                                 
KEYWDS    GLUTAMATE OXALOACETATE TRANSAMINASE 1, ASPARTATE AMINOTRANSFERASE 1,  
KEYWDS   2 PYRIDOXAL PHOSPHATE-DEPENDENT ENZYME, AMINO ACID METABOLISM, UREA    
KEYWDS   3 AND TRICARBOXYLIC ACID CYCLES, STRUCTURAL GENOMICS, STRUCTURAL       
KEYWDS   4 GENOMICS CONSORTIUM, SGC, AMINOTRANSFERASE, PHOSPHOPROTEIN,          
KEYWDS   5 PYRIDOXAL PHOSPHATE, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.UGOCHUKWU,E.PILKA,C.COOPER,J.E.BRAY,W.W.YUE,J.MUNIZ,A.CHAIKUAD,     
AUTHOR   2 F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,            
AUTHOR   3 K.L.KAVANAGH,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM (SGC)        
REVDAT   3   01-NOV-17 3II0    1       REMARK                                   
REVDAT   2   13-JUL-11 3II0    1       VERSN                                    
REVDAT   1   11-AUG-09 3II0    0                                                
JRNL        AUTH   E.UGOCHUKWU,E.PILKA,C.COOPER,J.E.BRAY,W.W.YUE,J.MUNIZ,       
JRNL        AUTH 2 A.CHAIKUAD,K.L.KAVANAGH,U.OPPERMANN                          
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN GLUTAMATE OXALOACETATE            
JRNL        TITL 2 TRANSAMINASE 1 (GOT1)                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0089                                      
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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 121312                         
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6417                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8782                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 483                          
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12745                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 156                                     
REMARK   3   SOLVENT ATOMS            : 733                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.62000                                              
REMARK   3    B22 (A**2) : -1.70000                                             
REMARK   3    B33 (A**2) : 0.08000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.171         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.157         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.293         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13312 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  8977 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18105 ; 1.444 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21769 ; 0.937 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1648 ; 5.624 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   623 ;35.614 ;23.756       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2088 ;13.419 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    87 ;18.796 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1965 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14943 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2820 ; 0.001 ; 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):  8133 ; 0.932 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3293 ; 0.330 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13119 ; 1.607 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5179 ; 2.789 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4973 ; 4.002 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  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   NUMBER OF DIFFERENT NCS GROUPS : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     14       A     213      5                      
REMARK   3           1     B     14       B     213      5                      
REMARK   3           2     A    215       A     410      5                      
REMARK   3           2     B    215       B     410      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2321 ; 0.060 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2879 ; 0.160 ; 5.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2321 ; 0.570 ; 2.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   2879 ; 0.690 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     14       C     213      5                      
REMARK   3           1     D     14       D     213      5                      
REMARK   3           2     C    215       C     410      5                      
REMARK   3           2     D    215       D     410      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   2323 ; 0.080 ; 0.500           
REMARK   3   LOOSE POSITIONAL   2    A    (A):   2899 ; 0.160 ; 5.000           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   2323 ; 0.590 ; 2.000           
REMARK   3   LOOSE THERMAL      2    A (A**2):   2899 ; 0.690 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    411       A     417      6                      
REMARK   3           1     B    411       B     417      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   3    A    (A):     84 ; 0.570 ; 5.000           
REMARK   3   LOOSE THERMAL      3    A (A**2):     84 ; 3.230 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    411       C     417      6                      
REMARK   3           1     D    411       D     417      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   4    A    (A):     81 ; 0.220 ; 5.000           
REMARK   3   LOOSE THERMAL      4    A (A**2):     81 ; 1.690 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    15        A   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.2199  -6.0572 -30.2947              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1004 T22:   0.0507                                     
REMARK   3      T33:   0.0153 T12:   0.0622                                     
REMARK   3      T13:  -0.0043 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8685 L22:   1.2868                                     
REMARK   3      L33:   0.2902 L12:  -0.3872                                     
REMARK   3      L13:  -0.2702 L23:   0.1982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0418 S12:  -0.0398 S13:   0.0109                       
REMARK   3      S21:   0.2009 S22:   0.0373 S23:  -0.1169                       
REMARK   3      S31:   0.0369 S32:   0.0374 S33:   0.0045                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   410        A   418                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.9761 -14.0687 -60.7858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1984 T22:   0.2037                                     
REMARK   3      T33:   0.0646 T12:  -0.0137                                     
REMARK   3      T13:   0.0905 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5121 L22:   6.6180                                     
REMARK   3      L33:  10.0031 L12:   2.3339                                     
REMARK   3      L13:  -3.8771 L23:  -7.8300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1556 S12:  -0.5391 S13:  -0.0856                       
REMARK   3      S21:   0.0471 S22:   0.0203 S23:  -0.0939                       
REMARK   3      S31:   0.0395 S32:   0.3439 S33:   0.1353                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    15        B   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0813 -48.9168 -30.7671              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0594 T22:   0.0421                                     
REMARK   3      T33:   0.0313 T12:   0.0453                                     
REMARK   3      T13:   0.0179 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0646 L22:   1.1033                                     
REMARK   3      L33:   0.4445 L12:  -0.3260                                     
REMARK   3      L13:   0.2981 L23:  -0.1709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0763 S12:  -0.0642 S13:   0.0011                       
REMARK   3      S21:   0.1488 S22:   0.0425 S23:   0.1575                       
REMARK   3      S31:  -0.0792 S32:  -0.0725 S33:   0.0338                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   410        B   418                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.4420 -41.9148 -62.0321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1600 T22:   0.1831                                     
REMARK   3      T33:   0.1609 T12:   0.0256                                     
REMARK   3      T13:  -0.0143 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3309 L22:   4.8137                                     
REMARK   3      L33:   9.6771 L12:   2.3989                                     
REMARK   3      L13:   3.5065 L23:   6.7798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0127 S12:  -0.0730 S13:   0.0094                       
REMARK   3      S21:   0.2436 S22:  -0.0747 S23:   0.1207                       
REMARK   3      S31:   0.2367 S32:  -0.1084 S33:   0.0874                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    13        C    17                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0279 -71.3159 -23.6763              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1288 T22:   0.1342                                     
REMARK   3      T33:   0.1548 T12:   0.0583                                     
REMARK   3      T13:   0.0387 T23:   0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4382 L22:   7.9112                                     
REMARK   3      L33:   9.6362 L12:   2.6880                                     
REMARK   3      L13:   6.5231 L23:   3.5286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1034 S12:  -0.0470 S13:  -0.1932                       
REMARK   3      S21:  -0.0725 S22:   0.1303 S23:  -0.0479                       
REMARK   3      S31:   0.1853 S32:  -0.0523 S33:  -0.2336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    18        C   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1005 -62.1761 -38.0092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0185 T22:   0.0456                                     
REMARK   3      T33:   0.0737 T12:   0.0157                                     
REMARK   3      T13:   0.0146 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7324 L22:   1.5090                                     
REMARK   3      L33:   0.6497 L12:  -0.1339                                     
REMARK   3      L13:  -0.0074 L23:   0.3634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0094 S12:  -0.0054 S13:   0.0639                       
REMARK   3      S21:  -0.0444 S22:   0.0132 S23:  -0.3017                       
REMARK   3      S31:  -0.0204 S32:   0.1242 S33:  -0.0038                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   275        C   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.3174 -61.9064 -26.5362              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0539 T22:   0.0989                                     
REMARK   3      T33:   0.1442 T12:   0.0355                                     
REMARK   3      T13:  -0.0553 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1706 L22:   1.3924                                     
REMARK   3      L33:   0.7431 L12:  -0.0303                                     
REMARK   3      L13:   0.2219 L23:  -0.0708                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0295 S12:  -0.0819 S13:   0.0386                       
REMARK   3      S21:   0.1556 S22:  -0.0392 S23:  -0.4451                       
REMARK   3      S31:   0.0535 S32:   0.2120 S33:   0.0097                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   410        C   418                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4318 -87.7292 -16.6056              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3883 T22:   0.3289                                     
REMARK   3      T33:   0.2557 T12:  -0.0074                                     
REMARK   3      T13:  -0.0844 T23:   0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7500 L22:   5.4933                                     
REMARK   3      L33:  10.5400 L12:   4.5195                                     
REMARK   3      L13:   6.2803 L23:   7.5808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2219 S12:  -0.0020 S13:   0.1911                       
REMARK   3      S21:  -0.1203 S22:  -0.0542 S23:   0.1922                       
REMARK   3      S31:  -0.2927 S32:   0.0606 S33:   0.2761                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    13        D    19                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4112  14.9692 -21.3539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1742 T22:   0.0899                                     
REMARK   3      T33:   0.3518 T12:   0.0063                                     
REMARK   3      T13:  -0.0667 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7388 L22:   6.5563                                     
REMARK   3      L33:   9.1446 L12:   0.3695                                     
REMARK   3      L13:  -3.2646 L23:  -4.9488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0005 S12:  -0.1500 S13:   0.1652                       
REMARK   3      S21:   0.1247 S22:   0.0567 S23:   0.0689                       
REMARK   3      S31:  -0.1500 S32:   0.2258 S33:  -0.0572                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    20        D   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5842   6.6543 -36.5784              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0604 T22:   0.0469                                     
REMARK   3      T33:   0.0894 T12:   0.0208                                     
REMARK   3      T13:   0.0192 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9188 L22:   1.3225                                     
REMARK   3      L33:   0.6538 L12:  -0.1715                                     
REMARK   3      L13:  -0.1888 L23:  -0.3030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:   0.0740 S13:  -0.0859                       
REMARK   3      S21:  -0.0162 S22:  -0.0322 S23:   0.3068                       
REMARK   3      S31:   0.0772 S32:  -0.1069 S33:   0.0248                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   275        D   411                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0830   7.3888 -24.3127              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1229 T22:   0.0662                                     
REMARK   3      T33:   0.1291 T12:   0.0371                                     
REMARK   3      T13:   0.0924 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4541 L22:   1.3395                                     
REMARK   3      L33:   0.7446 L12:  -0.1139                                     
REMARK   3      L13:  -0.4228 L23:  -0.0008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0353 S12:  -0.0552 S13:  -0.0580                       
REMARK   3      S21:   0.2196 S22:  -0.0428 S23:   0.4001                       
REMARK   3      S31:  -0.0413 S32:  -0.1477 S33:   0.0076                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   412        D   418                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.3394  35.3822 -19.0069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4735 T22:   0.3211                                     
REMARK   3      T33:   0.4081 T12:   0.0219                                     
REMARK   3      T13:   0.0490 T23:   0.1770                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7992 L22:   1.3970                                     
REMARK   3      L33:   8.9942 L12:  -1.1086                                     
REMARK   3      L13:  -0.2042 L23:   3.2941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0420 S12:  -0.7645 S13:  -1.1689                       
REMARK   3      S21:   0.4541 S22:  -0.1630 S23:   0.2521                       
REMARK   3      S31:   1.1509 S32:  -0.9008 S33:   0.1211                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3II0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054435.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 0                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97630                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 127732                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.78000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.78000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AJS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25M NA_K_TARTRATE; 15W/V PEG_3350,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 0               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       39.26550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      119.99850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.67350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      119.99850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.26550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.67350            
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 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 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 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     MET A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     SER A   420                                                      
REMARK 465     HIS A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     HIS A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     HIS A   426                                                      
REMARK 465     ASP A   427                                                      
REMARK 465     TYR A   428                                                      
REMARK 465     LYS A   429                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     ASP A   431                                                      
REMARK 465     ASP A   432                                                      
REMARK 465     ASP A   433                                                      
REMARK 465     LYS A   434                                                      
REMARK 465     MET B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     SER B   420                                                      
REMARK 465     HIS B   421                                                      
REMARK 465     HIS B   422                                                      
REMARK 465     HIS B   423                                                      
REMARK 465     HIS B   424                                                      
REMARK 465     HIS B   425                                                      
REMARK 465     HIS B   426                                                      
REMARK 465     ASP B   427                                                      
REMARK 465     TYR B   428                                                      
REMARK 465     LYS B   429                                                      
REMARK 465     ASP B   430                                                      
REMARK 465     ASP B   431                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     LYS B   434                                                      
REMARK 465     SER C   420                                                      
REMARK 465     HIS C   421                                                      
REMARK 465     HIS C   422                                                      
REMARK 465     HIS C   423                                                      
REMARK 465     HIS C   424                                                      
REMARK 465     HIS C   425                                                      
REMARK 465     HIS C   426                                                      
REMARK 465     ASP C   427                                                      
REMARK 465     TYR C   428                                                      
REMARK 465     LYS C   429                                                      
REMARK 465     ASP C   430                                                      
REMARK 465     ASP C   431                                                      
REMARK 465     ASP C   432                                                      
REMARK 465     ASP C   433                                                      
REMARK 465     LYS C   434                                                      
REMARK 465     SER D   420                                                      
REMARK 465     HIS D   421                                                      
REMARK 465     HIS D   422                                                      
REMARK 465     HIS D   423                                                      
REMARK 465     HIS D   424                                                      
REMARK 465     HIS D   425                                                      
REMARK 465     HIS D   426                                                      
REMARK 465     ASP D   427                                                      
REMARK 465     TYR D   428                                                      
REMARK 465     LYS D   429                                                      
REMARK 465     ASP D   430                                                      
REMARK 465     ASP D   431                                                      
REMARK 465     ASP D   432                                                      
REMARK 465     ASP D   433                                                      
REMARK 465     LYS D   434                                                      
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     ARG A  26    CZ   NH1  NH2                                       
REMARK 470     GLU A  27    CD   OE1  OE2                                       
REMARK 470     LYS A  99    CD   CE   NZ                                        
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     LYS A 369    CG   CD   CE   NZ                                   
REMARK 470     LYS A 396    CE   NZ                                             
REMARK 470     GLN A 419    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  26    CZ   NH1  NH2                                       
REMARK 470     GLU B  27    CD   OE1  OE2                                       
REMARK 470     GLU B 165    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 166    CG   CD   CE   NZ                                   
REMARK 470     GLU B 179    CD   OE1  OE2                                       
REMARK 470     LYS B 214    CD   CE   NZ                                        
REMARK 470     PHE B 217    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 277    CD   OE1  OE2                                       
REMARK 470     GLU B 279    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 283    CD   OE1  NE2                                       
REMARK 470     LYS B 290    CD   CE   NZ                                        
REMARK 470     LYS B 369    CE   NZ                                             
REMARK 470     LYS B 396    CE   NZ                                             
REMARK 470     GLU B 414    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 419    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  26    CZ   NH1  NH2                                       
REMARK 470     GLU C  27    CD   OE1  OE2                                       
REMARK 470     LYS C  55    CE   NZ                                             
REMARK 470     LYS C  60    CE   NZ                                             
REMARK 470     LYS C  97    CE   NZ                                             
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     LYS C 290    NZ                                                  
REMARK 470     GLU C 315    CD   OE1  OE2                                       
REMARK 470     ASN C 352    OD1  ND2                                            
REMARK 470     LYS C 369    CE   NZ                                             
REMARK 470     LYS C 396    CE   NZ                                             
REMARK 470     GLU C 414    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 415    CG   OD1  ND2                                       
REMARK 470     ARG D  26    CZ   NH1  NH2                                       
REMARK 470     GLU D  27    CD   OE1  OE2                                       
REMARK 470     LYS D  55    CE   NZ                                             
REMARK 470     ASP D  92    OD1  OD2                                            
REMARK 470     LYS D 166    CG   CD   CE   NZ                                   
REMARK 470     ILE D 199    CD1                                                 
REMARK 470     LYS D 214    CD   CE   NZ                                        
REMARK 470     GLU D 277    CD   OE1  OE2                                       
REMARK 470     GLU D 315    CD   OE1  OE2                                       
REMARK 470     LYS D 369    CE   NZ                                             
REMARK 470     GLU D 414    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 415    CG   OD1  ND2                                       
REMARK 470     LEU D 416    CG   CD1  CD2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  122   CA   CB   CG   CD   NE   CZ   NH1                   
REMARK 480     ARG A  122   NH2                                                 
REMARK 480     GLU B   79   CA   CB   CG   CD   OE1  OE2                        
REMARK 480     ARG B  122   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     GLU D   79   CA   CB   CG   CD   OE1  OE2                        
REMARK 480     HIS D  215   CA   CB   CG   ND1  CD2  CE1  NE2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   467     O    HOH C   466              1.97            
REMARK 500   NZ   LYS C   378     O    HOH C   635              2.16            
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    HIS D 215   N     HIS D 215   CA     -0.184                       
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    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 122   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG B 122   N   -  CA  -  CB  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    HIS D 215   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    HIS D 215   N   -  CA  -  C   ANGL. DEV. =  20.7 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    TYR A 161      -68.38   -140.15                                   
REMARK 500    LEU A 263       42.16   -101.51                                   
REMARK 500    SER A 297      -58.48     77.70                                   
REMARK 500    PHE A 418        9.52     83.08                                   
REMARK 500    TYR B 161      -66.98   -146.08                                   
REMARK 500    LEU B 263       39.02    -98.27                                   
REMARK 500    SER B 297      -56.67     79.39                                   
REMARK 500    TYR C 161      -62.60   -152.78                                   
REMARK 500    PHE C 184        0.32     83.14                                   
REMARK 500    ARG C 267       61.18     61.91                                   
REMARK 500    SER C 297      -56.98     72.56                                   
REMARK 500    TYR D 161      -63.82   -149.33                                   
REMARK 500    PHE D 184       -0.50     77.97                                   
REMARK 500    LEU D 263       40.70   -103.82                                   
REMARK 500    THR D 295      -67.64   -107.68                                   
REMARK 500    SER D 297      -58.53     74.40                                   
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 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 436                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR B 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 436                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR C 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 436                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR D 435                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 9                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AJS   RELATED DB: PDB                                   
REMARK 900 REFINEMENT AND COMPARISONS OF THE CRYSTAL STRUCTURES OF PIG          
REMARK 900 CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-         
REMARK 900 METHYLASPARTATE                                                      
DBREF  3II0 A   14   412  UNP    P17174   AATC_HUMAN      14    412             
DBREF  3II0 B   14   412  UNP    P17174   AATC_HUMAN      14    412             
DBREF  3II0 C   14   412  UNP    P17174   AATC_HUMAN      14    412             
DBREF  3II0 D   14   412  UNP    P17174   AATC_HUMAN      14    412             
SEQADV 3II0 MET A   13  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ALA A  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLU A  414  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASN A  415  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LEU A  416  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR A  417  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 PHE A  418  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLN A  419  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 SER A  420  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS A  421  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS A  422  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS A  423  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS A  424  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS A  425  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS A  426  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP A  427  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR A  428  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS A  429  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP A  430  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP A  431  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP A  432  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP A  433  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS A  434  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 MET B   13  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ALA B  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLU B  414  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASN B  415  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LEU B  416  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR B  417  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 PHE B  418  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLN B  419  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 SER B  420  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS B  421  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS B  422  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS B  423  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS B  424  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS B  425  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS B  426  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP B  427  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR B  428  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS B  429  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP B  430  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP B  431  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP B  432  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP B  433  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS B  434  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 MET C   13  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ALA C  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLU C  414  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASN C  415  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LEU C  416  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR C  417  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 PHE C  418  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLN C  419  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 SER C  420  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS C  421  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS C  422  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS C  423  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS C  424  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS C  425  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS C  426  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP C  427  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR C  428  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS C  429  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP C  430  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP C  431  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP C  432  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP C  433  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS C  434  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 MET D   13  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ALA D  413  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLU D  414  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASN D  415  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LEU D  416  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR D  417  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 PHE D  418  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 GLN D  419  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 SER D  420  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS D  421  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS D  422  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS D  423  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS D  424  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS D  425  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 HIS D  426  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP D  427  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 TYR D  428  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS D  429  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP D  430  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP D  431  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP D  432  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 ASP D  433  UNP  P17174              EXPRESSION TAG                 
SEQADV 3II0 LYS D  434  UNP  P17174              EXPRESSION TAG                 
SEQRES   1 A  422  MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE          
SEQRES   2 A  422  ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL          
SEQRES   3 A  422  GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU          
SEQRES   4 A  422  PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP          
SEQRES   5 A  422  ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU          
SEQRES   6 A  422  ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY          
SEQRES   7 A  422  ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY          
SEQRES   8 A  422  VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY          
SEQRES   9 A  422  ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN          
SEQRES  10 A  422  LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU          
SEQRES  11 A  422  ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP          
SEQRES  12 A  422  ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY          
SEQRES  13 A  422  LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA          
SEQRES  14 A  422  PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS          
SEQRES  15 A  422  ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS          
SEQRES  16 A  422  GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO          
SEQRES  17 A  422  PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN          
SEQRES  18 A  422  LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER          
SEQRES  19 A  422  GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS          
SEQRES  20 A  422  ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR          
SEQRES  21 A  422  VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU          
SEQRES  22 A  422  SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN          
SEQRES  23 A  422  PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU          
SEQRES  24 A  422  SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL          
SEQRES  25 A  422  LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU          
SEQRES  26 A  422  LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR          
SEQRES  27 A  422  TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE          
SEQRES  28 A  422  THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN          
SEQRES  29 A  422  GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN          
SEQRES  30 A  422  VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA          
SEQRES  31 A  422  THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN          
SEQRES  32 A  422  LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR          
SEQRES  33 A  422  LYS ASP ASP ASP ASP LYS                                      
SEQRES   1 B  422  MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE          
SEQRES   2 B  422  ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL          
SEQRES   3 B  422  GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU          
SEQRES   4 B  422  PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP          
SEQRES   5 B  422  ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU          
SEQRES   6 B  422  ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY          
SEQRES   7 B  422  ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY          
SEQRES   8 B  422  VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY          
SEQRES   9 B  422  ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN          
SEQRES  10 B  422  LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU          
SEQRES  11 B  422  ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP          
SEQRES  12 B  422  ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY          
SEQRES  13 B  422  LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA          
SEQRES  14 B  422  PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS          
SEQRES  15 B  422  ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS          
SEQRES  16 B  422  GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO          
SEQRES  17 B  422  PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN          
SEQRES  18 B  422  LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER          
SEQRES  19 B  422  GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS          
SEQRES  20 B  422  ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR          
SEQRES  21 B  422  VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU          
SEQRES  22 B  422  SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN          
SEQRES  23 B  422  PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU          
SEQRES  24 B  422  SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL          
SEQRES  25 B  422  LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU          
SEQRES  26 B  422  LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR          
SEQRES  27 B  422  TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE          
SEQRES  28 B  422  THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN          
SEQRES  29 B  422  GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN          
SEQRES  30 B  422  VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA          
SEQRES  31 B  422  THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN          
SEQRES  32 B  422  LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR          
SEQRES  33 B  422  LYS ASP ASP ASP ASP LYS                                      
SEQRES   1 C  422  MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE          
SEQRES   2 C  422  ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL          
SEQRES   3 C  422  GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU          
SEQRES   4 C  422  PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP          
SEQRES   5 C  422  ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU          
SEQRES   6 C  422  ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY          
SEQRES   7 C  422  ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY          
SEQRES   8 C  422  VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY          
SEQRES   9 C  422  ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN          
SEQRES  10 C  422  LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU          
SEQRES  11 C  422  ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP          
SEQRES  12 C  422  ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY          
SEQRES  13 C  422  LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA          
SEQRES  14 C  422  PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS          
SEQRES  15 C  422  ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS          
SEQRES  16 C  422  GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO          
SEQRES  17 C  422  PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN          
SEQRES  18 C  422  LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER          
SEQRES  19 C  422  GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS          
SEQRES  20 C  422  ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR          
SEQRES  21 C  422  VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU          
SEQRES  22 C  422  SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN          
SEQRES  23 C  422  PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU          
SEQRES  24 C  422  SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL          
SEQRES  25 C  422  LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU          
SEQRES  26 C  422  LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR          
SEQRES  27 C  422  TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE          
SEQRES  28 C  422  THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN          
SEQRES  29 C  422  GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN          
SEQRES  30 C  422  VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA          
SEQRES  31 C  422  THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN          
SEQRES  32 C  422  LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR          
SEQRES  33 C  422  LYS ASP ASP ASP ASP LYS                                      
SEQRES   1 D  422  MET GLN PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE          
SEQRES   2 D  422  ARG GLU ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL          
SEQRES   3 D  422  GLY ALA TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU          
SEQRES   4 D  422  PRO VAL VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP          
SEQRES   5 D  422  ASN SER LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU          
SEQRES   6 D  422  ALA GLU PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY          
SEQRES   7 D  422  ASP ASP SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY          
SEQRES   8 D  422  VAL GLN SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY          
SEQRES   9 D  422  ALA ASP PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN          
SEQRES  10 D  422  LYS ASN THR PRO VAL TYR VAL SER SER PRO THR TRP GLU          
SEQRES  11 D  422  ASN HIS ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP          
SEQRES  12 D  422  ILE ARG SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY          
SEQRES  13 D  422  LEU ASP LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA          
SEQRES  14 D  422  PRO GLU PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS          
SEQRES  15 D  422  ASN PRO THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS          
SEQRES  16 D  422  GLN ILE ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO          
SEQRES  17 D  422  PHE PHE ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN          
SEQRES  18 D  422  LEU GLU ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER          
SEQRES  19 D  422  GLU GLY PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS          
SEQRES  20 D  422  ASN PHE GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR          
SEQRES  21 D  422  VAL VAL GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU          
SEQRES  22 D  422  SER GLN MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN          
SEQRES  23 D  422  PRO PRO ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU          
SEQRES  24 D  422  SER ASN PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL          
SEQRES  25 D  422  LYS THR MET ALA ASP ARG ILE LEU THR MET ARG SER GLU          
SEQRES  26 D  422  LEU ARG ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR          
SEQRES  27 D  422  TRP ASN HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE          
SEQRES  28 D  422  THR GLY LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN          
SEQRES  29 D  422  GLU LYS HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN          
SEQRES  30 D  422  VAL SER GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA          
SEQRES  31 D  422  THR SER ILE HIS GLU ALA VAL THR LYS ILE ALA GLU ASN          
SEQRES  32 D  422  LEU TYR PHE GLN SER HIS HIS HIS HIS HIS HIS ASP TYR          
SEQRES  33 D  422  LYS ASP ASP ASP ASP LYS                                      
HET    PLP  A   1      16                                                       
HET    TAR  A 435      10                                                       
HET    EDO  A   3       4                                                       
HET    EDO  A  11       4                                                       
HET    EDO  A 436       4                                                       
HET    PLP  B   2      16                                                       
HET    TAR  B 435      10                                                       
HET    EDO  B   1       4                                                       
HET    EDO  B  10       4                                                       
HET    EDO  B 436       4                                                       
HET    PLP  C   3      16                                                       
HET    TAR  C 435      10                                                       
HET    EDO  C   5       4                                                       
HET    EDO  C   7       4                                                       
HET    EDO  C  12       4                                                       
HET    EDO  C 436       4                                                       
HET    PLP  D   4      16                                                       
HET    TAR  D 435      10                                                       
HET    EDO  D   6       4                                                       
HET    EDO  D   8       4                                                       
HET    EDO  D   9       4                                                       
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     TAR D(-)-TARTARIC ACID                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  PLP    4(C8 H10 N O6 P)                                             
FORMUL   6  TAR    4(C4 H6 O6)                                                  
FORMUL   7  EDO    13(C2 H6 O2)                                                 
FORMUL  26  HOH   *733(H2 O)                                                    
HELIX    1   1 VAL A   16  ASP A   28  1                                  13    
HELIX    2   2 LEU A   51  ASN A   63  1                                  13    
HELIX    3   3 LEU A   77  GLY A   90  1                                  14    
HELIX    4   4 SER A   93  GLU A   98  1                                   6    
HELIX    5   5 GLY A  108  TYR A  124  1                                  17    
HELIX    6   6 GLU A  142  ALA A  151  1                                  10    
HELIX    7   7 ASP A  170  ASN A  180  1                                  11    
HELIX    8   8 THR A  202  PHE A  217  1                                  16    
HELIX    9   9 ASN A  233  ALA A  238  1                                   6    
HELIX   10  10 ALA A  238  GLU A  247  1                                  10    
HELIX   11  11 LEU A  263  GLU A  266  5                                   4    
HELIX   12  12 GLU A  277  ILE A  294  1                                  18    
HELIX   13  13 ALA A  301  SER A  312  1                                  12    
HELIX   14  14 ASN A  313  LEU A  345  1                                  33    
HELIX   15  15 TRP A  351  GLN A  357  1                                   7    
HELIX   16  16 ASN A  367  HIS A  379  1                                  13    
HELIX   17  17 SER A  391  LEU A  393  5                                   3    
HELIX   18  18 ASN A  397  ILE A  412  1                                  16    
HELIX   19  19 VAL B   16  ASP B   28  1                                  13    
HELIX   20  20 LEU B   51  ASP B   64  1                                  14    
HELIX   21  21 LEU B   77  GLY B   90  1                                  14    
HELIX   22  22 SER B   93  GLU B   98  1                                   6    
HELIX   23  23 GLY B  108  TYR B  124  1                                  17    
HELIX   24  24 GLU B  142  ALA B  151  1                                  10    
HELIX   25  25 ASP B  170  ASN B  180  1                                  11    
HELIX   26  26 THR B  202  PHE B  217  1                                  16    
HELIX   27  27 ASN B  233  ALA B  238  1                                   6    
HELIX   28  28 ALA B  238  GLU B  247  1                                  10    
HELIX   29  29 LEU B  263  GLU B  266  5                                   4    
HELIX   30  30 GLU B  277  ILE B  294  1                                  18    
HELIX   31  31 ALA B  301  SER B  312  1                                  12    
HELIX   32  32 ASN B  313  LEU B  345  1                                  33    
HELIX   33  33 TRP B  351  GLN B  357  1                                   7    
HELIX   34  34 ASN B  367  HIS B  379  1                                  13    
HELIX   35  35 SER B  391  LEU B  393  5                                   3    
HELIX   36  36 ASN B  397  ILE B  412  1                                  16    
HELIX   37  37 VAL C   16  ASP C   28  1                                  13    
HELIX   38  38 LEU C   51  ASN C   63  1                                  13    
HELIX   39  39 LEU C   77  GLY C   90  1                                  14    
HELIX   40  40 SER C   93  GLU C   98  1                                   6    
HELIX   41  41 GLY C  108  TYR C  124  1                                  17    
HELIX   42  42 GLU C  142  GLY C  152  1                                  11    
HELIX   43  43 ASP C  170  ASN C  180  1                                  11    
HELIX   44  44 THR C  202  PHE C  217  1                                  16    
HELIX   45  45 ASN C  233  ALA C  238  1                                   6    
HELIX   46  46 ALA C  238  GLU C  247  1                                  10    
HELIX   47  47 LEU C  263  GLU C  266  5                                   4    
HELIX   48  48 GLU C  277  ILE C  294  1                                  18    
HELIX   49  49 ALA C  301  SER C  312  1                                  12    
HELIX   50  50 ASN C  313  LEU C  345  1                                  33    
HELIX   51  51 TRP C  351  GLN C  357  1                                   7    
HELIX   52  52 ASN C  367  HIS C  379  1                                  13    
HELIX   53  53 SER C  391  LEU C  393  5                                   3    
HELIX   54  54 ASN C  397  ILE C  412  1                                  16    
HELIX   55  55 VAL D   16  ASP D   28  1                                  13    
HELIX   56  56 LEU D   51  ASP D   64  1                                  14    
HELIX   57  57 LEU D   77  GLY D   90  1                                  14    
HELIX   58  58 SER D   93  GLU D   98  1                                   6    
HELIX   59  59 GLY D  108  TYR D  124  1                                  17    
HELIX   60  60 GLU D  142  GLY D  152  1                                  11    
HELIX   61  61 ASP D  170  ASN D  180  1                                  11    
HELIX   62  62 THR D  202  ARG D  216  1                                  15    
HELIX   63  63 ASN D  233  ALA D  238  1                                   6    
HELIX   64  64 ALA D  238  GLU D  247  1                                  10    
HELIX   65  65 LEU D  263  GLU D  266  5                                   4    
HELIX   66  66 GLU D  277  ILE D  294  1                                  18    
HELIX   67  67 ALA D  301  ASN D  313  1                                  13    
HELIX   68  68 ASN D  313  LEU D  345  1                                  33    
HELIX   69  69 TRP D  351  GLN D  357  1                                   7    
HELIX   70  70 ASN D  367  GLU D  377  1                                  11    
HELIX   71  71 SER D  391  LEU D  393  5                                   3    
HELIX   72  72 ASN D  397  ILE D  412  1                                  16    
SHEET    1   A 2 VAL A  34  ASN A  35  0                                        
SHEET    2   A 2 ILE A 380  TYR A 381  1  O  TYR A 381   N  VAL A  34           
SHEET    1   B 7 VAL A 101  LEU A 107  0                                        
SHEET    2   B 7 VAL A 268  VAL A 274 -1  O  LEU A 271   N  VAL A 104           
SHEET    3   B 7 PHE A 251  SER A 256 -1  N  GLN A 255   O  ASN A 270           
SHEET    4   B 7 PHE A 219  SER A 224  1  N  SER A 224   O  ALA A 254           
SHEET    5   B 7 ILE A 186  HIS A 190  1  N  VAL A 187   O  PHE A 219           
SHEET    6   B 7 VAL A 134  SER A 138  1  N  TYR A 135   O  ILE A 186           
SHEET    7   B 7 ILE A 156  ARG A 160  1  O  ARG A 157   N  VAL A 134           
SHEET    1   C 2 TRP A 162  ASP A 163  0                                        
SHEET    2   C 2 GLY A 168  LEU A 169 -1  O  GLY A 168   N  ASP A 163           
SHEET    1   D 2 PHE A 361  PHE A 363  0                                        
SHEET    2   D 2 ARG A 387  ASN A 389 -1  O  ILE A 388   N  SER A 362           
SHEET    1   E 2 VAL B  34  ASN B  35  0                                        
SHEET    2   E 2 ILE B 380  TYR B 381  1  O  TYR B 381   N  VAL B  34           
SHEET    1   F 7 VAL B 101  LEU B 107  0                                        
SHEET    2   F 7 VAL B 268  VAL B 274 -1  O  LEU B 271   N  VAL B 104           
SHEET    3   F 7 PHE B 251  SER B 256 -1  N  GLN B 255   O  ASN B 270           
SHEET    4   F 7 PHE B 219  SER B 224  1  N  SER B 224   O  ALA B 254           
SHEET    5   F 7 ILE B 186  HIS B 190  1  N  VAL B 187   O  PHE B 219           
SHEET    6   F 7 VAL B 134  SER B 138  1  N  TYR B 135   O  ILE B 186           
SHEET    7   F 7 ILE B 156  ARG B 160  1  O  ARG B 157   N  VAL B 134           
SHEET    1   G 2 TRP B 162  ASP B 163  0                                        
SHEET    2   G 2 GLY B 168  LEU B 169 -1  O  GLY B 168   N  ASP B 163           
SHEET    1   H 2 PHE B 361  PHE B 363  0                                        
SHEET    2   H 2 ARG B 387  ASN B 389 -1  O  ILE B 388   N  SER B 362           
SHEET    1   I 2 VAL C  34  ASN C  35  0                                        
SHEET    2   I 2 ILE C 380  TYR C 381  1  O  TYR C 381   N  VAL C  34           
SHEET    1   J 7 VAL C 101  LEU C 107  0                                        
SHEET    2   J 7 VAL C 268  VAL C 274 -1  O  VAL C 273   N  GLY C 102           
SHEET    3   J 7 PHE C 251  SER C 256 -1  N  GLN C 255   O  ASN C 270           
SHEET    4   J 7 PHE C 219  SER C 224  1  N  SER C 224   O  ALA C 254           
SHEET    5   J 7 ILE C 186  HIS C 190  1  N  VAL C 187   O  PHE C 219           
SHEET    6   J 7 VAL C 134  SER C 138  1  N  TYR C 135   O  VAL C 188           
SHEET    7   J 7 ILE C 156  ARG C 160  1  O  ARG C 157   N  VAL C 134           
SHEET    1   K 2 TRP C 162  ASP C 163  0                                        
SHEET    2   K 2 GLY C 168  LEU C 169 -1  O  GLY C 168   N  ASP C 163           
SHEET    1   L 2 PHE C 361  PHE C 363  0                                        
SHEET    2   L 2 ARG C 387  ASN C 389 -1  O  ILE C 388   N  SER C 362           
SHEET    1   M 2 VAL D  34  ASN D  35  0                                        
SHEET    2   M 2 ILE D 380  TYR D 381  1  O  TYR D 381   N  VAL D  34           
SHEET    1   N 7 VAL D 101  LEU D 107  0                                        
SHEET    2   N 7 VAL D 268  VAL D 274 -1  O  VAL D 273   N  GLY D 102           
SHEET    3   N 7 PHE D 251  SER D 256 -1  N  GLN D 255   O  ASN D 270           
SHEET    4   N 7 PHE D 219  SER D 224  1  N  PHE D 222   O  ALA D 254           
SHEET    5   N 7 ILE D 186  HIS D 190  1  N  VAL D 187   O  PHE D 219           
SHEET    6   N 7 VAL D 134  SER D 138  1  N  TYR D 135   O  VAL D 188           
SHEET    7   N 7 ILE D 156  ARG D 160  1  O  ARG D 157   N  VAL D 134           
SHEET    1   O 2 TRP D 162  ASP D 163  0                                        
SHEET    2   O 2 GLY D 168  LEU D 169 -1  O  GLY D 168   N  ASP D 163           
SHEET    1   P 2 PHE D 361  PHE D 363  0                                        
SHEET    2   P 2 ARG D 387  ASN D 389 -1  O  ILE D 388   N  SER D 362           
CISPEP   1 SER A  138    PRO A  139          0        -6.80                     
CISPEP   2 ASN A  195    PRO A  196          0        14.51                     
CISPEP   3 SER B  138    PRO B  139          0        -2.70                     
CISPEP   4 ASN B  195    PRO B  196          0        15.36                     
CISPEP   5 GLN C   14    PRO C   15          0         6.67                     
CISPEP   6 SER C  138    PRO C  139          0        -5.18                     
CISPEP   7 ASN C  195    PRO C  196          0        14.75                     
CISPEP   8 GLN D   14    PRO D   15          0         8.16                     
CISPEP   9 SER D  138    PRO D  139          0        -4.30                     
CISPEP  10 ASN D  195    PRO D  196          0        16.94                     
SITE     1 AC1 15 GLY A 108  GLY A 109  THR A 110  TRP A 141                    
SITE     2 AC1 15 ASN A 195  ASP A 223  ALA A 225  TYR A 226                    
SITE     3 AC1 15 SER A 256  SER A 258  LYS A 259  ARG A 267                    
SITE     4 AC1 15 TAR A 435  HOH A 445  TYR D  71                               
SITE     1 AC2 15 PLP A   1  VAL A  18  PHE A  19  VAL A  38                    
SITE     2 AC2 15 GLY A  39  TRP A 141  ASN A 195  TYR A 226                    
SITE     3 AC2 15 LYS A 259  PHE A 361  ARG A 387  HOH A 445                    
SITE     4 AC2 15 HOH A 548  TYR D  71  ARG D 293                               
SITE     1 AC3  4 ASN A 128  LYS A 130  HOH A 438  EDO C   7                    
SITE     1 AC4  5 TYR A  41  THR A  43  TRP A  49  HOH A 455                    
SITE     2 AC4  5 HOH A 500                                                     
SITE     1 AC5  7 ALA A  78  ARG A  81  SER A  82  SER A  85                    
SITE     2 AC5  7 GLY A 102  GLY A 103  HOH A 475                               
SITE     1 AC6 15 GLY B 108  GLY B 109  THR B 110  TRP B 141                    
SITE     2 AC6 15 ASN B 195  ASP B 223  ALA B 225  TYR B 226                    
SITE     3 AC6 15 SER B 256  SER B 258  LYS B 259  ARG B 267                    
SITE     4 AC6 15 TAR B 435  HOH B 483  TYR C  71                               
SITE     1 AC7 14 PLP B   2  VAL B  18  PHE B  19  VAL B  38                    
SITE     2 AC7 14 GLY B  39  TRP B 141  ASN B 195  TYR B 226                    
SITE     3 AC7 14 LYS B 259  ARG B 387  HOH B 483  HOH B 576                    
SITE     4 AC7 14 TYR C  71  ARG C 293                                          
SITE     1 AC8  4 TYR B  41  THR B  43  TRP B  49  HOH B 551                    
SITE     1 AC9  4 ASN B 128  LYS B 130  HOH B 470  EDO D   6                    
SITE     1 BC1  6 ALA B  78  ARG B  81  SER B  82  GLY B 103                    
SITE     2 BC1  6 HOH B 510  HOH B 696                                          
SITE     1 BC2 14 TYR B  71  HOH B 462  GLY C 108  GLY C 109                    
SITE     2 BC2 14 THR C 110  TRP C 141  ASN C 195  ASP C 223                    
SITE     3 BC2 14 TYR C 226  SER C 256  SER C 258  LYS C 259                    
SITE     4 BC2 14 ARG C 267  TAR C 435                                          
SITE     1 BC3 15 TYR B  71  ARG B 293  HOH B 462  PLP C   3                    
SITE     2 BC3 15 VAL C  18  PHE C  19  VAL C  38  GLY C  39                    
SITE     3 BC3 15 TRP C 141  ASN C 195  TYR C 226  LYS C 259                    
SITE     4 BC3 15 PHE C 361  ARG C 387  HOH C 527                               
SITE     1 BC4  3 LEU A 416  TYR C 124  ASN C 125                               
SITE     1 BC5  3 EDO A   3  ARG C 157  SER C 158                               
SITE     1 BC6  3 TYR C  41  THR C 326  HOH C 704                               
SITE     1 BC7  4 ARG C  81  GLY C 103  HOH C 467  HOH C 468                    
SITE     1 BC8 14 TYR A  71  HOH A 458  GLY D 108  GLY D 109                    
SITE     2 BC8 14 THR D 110  TRP D 141  ASN D 195  ASP D 223                    
SITE     3 BC8 14 TYR D 226  SER D 256  SER D 258  LYS D 259                    
SITE     4 BC8 14 ARG D 267  TAR D 435                                          
SITE     1 BC9 14 TYR A  71  ARG A 293  HOH A 458  PLP D   4                    
SITE     2 BC9 14 VAL D  18  PHE D  19  GLY D  39  TRP D 141                    
SITE     3 BC9 14 ASN D 195  TYR D 226  LYS D 259  PHE D 361                    
SITE     4 BC9 14 ARG D 387  HOH D 521                                          
SITE     1 CC1  3 EDO B  10  ARG D 157  SER D 158                               
SITE     1 CC2  4 TYR D  41  THR D  43  TRP D  49  HOH D 497                    
SITE     1 CC3  5 ARG D  81  SER D  85  VAL D 101  HOH D 535                    
SITE     2 CC3  5 HOH D 551                                                     
CRYST1   78.531  107.347  239.997  90.00  90.00  90.00 P 21 21 21   16          
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      0.012734  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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