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Database: PDB
Entry: 3BG3
LinkDB: 3BG3
Original site: 3BG3 
HEADER    LIGASE                                  26-NOV-07   3BG3              
TITLE     CRYSTAL STRUCTURE OF HUMAN PYRUVATE CARBOXYLASE (MISSING THE BIOTIN   
TITLE    2 CARBOXYLASE DOMAIN AT THE N-TERMINUS)                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRUVATE CARBOXYLASE, MITOCHONDRIAL;                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CT+PT+BCCP DOMAIN;                                         
COMPND   5 SYNONYM: PYRUVIC CARBOXYLASE, PCB;                                   
COMPND   6 EC: 6.4.1.1;                                                         
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: PC;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) STAR;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    TIM BARREL, ATP-BINDING, BIOTIN, DISEASE MUTATION, GLUCONEOGENESIS,   
KEYWDS   2 LIGASE, LIPID SYNTHESIS, MANGANESE, MITOCHONDRION, MULTIFUNCTIONAL   
KEYWDS   3 ENZYME, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, TRANSIT PEPTIDE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XIANG,L.TONG                                                        
REVDAT   4   25-OCT-17 3BG3    1       REMARK                                   
REVDAT   3   24-FEB-09 3BG3    1       VERSN                                    
REVDAT   2   29-APR-08 3BG3    1       JRNL                                     
REVDAT   1   26-FEB-08 3BG3    0                                                
JRNL        AUTH   S.XIANG,L.TONG                                               
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN AND STAPHYLOCOCCUS AUREUS        
JRNL        TITL 2 PYRUVATE CARBOXYLASE AND MOLECULAR INSIGHTS INTO THE         
JRNL        TITL 3 CARBOXYLTRANSFER REACTION.                                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  15   295 2008              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   18297087                                                     
JRNL        DOI    10.1038/NSMB.1393                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 71717                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3915                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3693                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 228                          
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19770                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.52000                                              
REMARK   3    B22 (A**2) : -2.62000                                             
REMARK   3    B33 (A**2) : -2.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.79000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.414         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.357         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.363        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20255 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27466 ; 1.228 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2562 ; 5.949 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   880 ;36.415 ;23.977       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3370 ;19.909 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   130 ;17.810 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3047 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15486 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  9634 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 13681 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   609 ; 0.153 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.204 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.144 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 13100 ; 0.375 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20594 ; 0.661 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7906 ; 0.725 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6872 ; 1.182 ; 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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    520       A     860      6                      
REMARK   3           1     B    520       B     860      6                      
REMARK   3           1     C    520       C     860      6                      
REMARK   3           1     D    520       D     860      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   2602 ;  0.49 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   2602 ;  0.48 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   2602 ;  0.50 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   2602 ;  0.46 ;  5.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   2602 ;  1.30 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   2602 ;  1.51 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   2602 ;  1.60 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   2602 ;  1.35 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A   1103       A    1178      6                      
REMARK   3           1     D   1103       D    1178      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   2    A    (A):    559 ;  0.87 ;  5.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    559 ;  0.80 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    494       A     519      6                      
REMARK   3           1     D    494       D     519      6                      
REMARK   3           2     A    861       A    1097      6                      
REMARK   3           2     D    861       D    1097      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   3    A    (A):   2062 ;  0.66 ;  5.00           
REMARK   3   LOOSE THERMAL      3    A (A**2):   2062 ;  1.87 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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   494        A  1097                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.4815 -74.0557 -52.2826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4066 T22:  -0.1127                                     
REMARK   3      T33:  -0.1365 T12:  -0.0349                                     
REMARK   3      T13:  -0.0630 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2969 L22:   2.6367                                     
REMARK   3      L33:   2.2279 L12:   0.2521                                     
REMARK   3      L13:   0.2622 L23:   0.5704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0092 S12:  -0.3770 S13:   0.3116                       
REMARK   3      S21:   0.0883 S22:  -0.0775 S23:   0.5404                       
REMARK   3      S31:  -0.0772 S32:  -0.5547 S33:   0.0683                       
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 :   B   494        B  1097                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7925 -55.2484  17.7594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0932 T22:  -0.2122                                     
REMARK   3      T33:  -0.3411 T12:  -0.0579                                     
REMARK   3      T13:   0.0229 T23:   0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6952 L22:   3.1681                                     
REMARK   3      L33:   2.7440 L12:   1.0245                                     
REMARK   3      L13:   0.0527 L23:   0.8194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1212 S12:  -0.1684 S13:  -0.0613                       
REMARK   3      S21:   0.3328 S22:  -0.1682 S23:   0.3477                       
REMARK   3      S31:   0.2664 S32:  -0.4588 S33:   0.0470                       
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 :   C   494        C  1097                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.9685 -29.1610  -9.8040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1418 T22:  -0.1496                                     
REMARK   3      T33:  -0.0324 T12:  -0.1833                                     
REMARK   3      T13:  -0.0213 T23:   0.1521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6820 L22:   1.3949                                     
REMARK   3      L33:   2.9854 L12:   0.9344                                     
REMARK   3      L13:   1.4911 L23:   0.1403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2734 S12:   0.7020 S13:   0.3539                       
REMARK   3      S21:  -0.3456 S22:   0.2300 S23:  -0.1694                       
REMARK   3      S31:  -0.3601 S32:   0.5229 S33:   0.0434                       
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 :   D   494        D  1097                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0026 -97.2982 -53.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1148 T22:  -0.2718                                     
REMARK   3      T33:  -0.2870 T12:   0.1768                                     
REMARK   3      T13:   0.0631 T23:  -0.0611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9583 L22:   0.9573                                     
REMARK   3      L33:   4.3512 L12:  -0.1359                                     
REMARK   3      L13:   0.1931 L23:   0.1303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:  -0.1620 S13:  -0.1113                       
REMARK   3      S21:  -0.0708 S22:   0.1593 S23:  -0.2969                       
REMARK   3      S31:   0.5983 S32:   0.7275 S33:  -0.1399                       
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 :   A  1103        A  1178                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6246 -56.0674  10.1344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3791 T22:   0.3983                                     
REMARK   3      T33:   0.2699 T12:  -0.1564                                     
REMARK   3      T13:  -0.0828 T23:  -0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  50.8417 L22:  12.5271                                     
REMARK   3      L33:  17.1283 L12:   0.1383                                     
REMARK   3      L13:  -1.4661 L23:   0.8513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1745 S12:  -0.8198 S13:  -0.4104                       
REMARK   3      S21:  -0.4742 S22:  -0.0548 S23:   0.2704                       
REMARK   3      S31:   0.5666 S32:  -1.3265 S33:   0.2294                       
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 :   D  1103        D  1178                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.2825 -63.8438 -23.7063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4121 T22:   0.5180                                     
REMARK   3      T33:   0.3074 T12:  -0.0574                                     
REMARK   3      T13:   0.1758 T23:  -0.1754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  21.1252 L22:  27.9499                                     
REMARK   3      L33:   9.9622 L12:  -8.7726                                     
REMARK   3      L13:  -1.5734 L23:  -0.2657                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6509 S12:  -0.2728 S13:   0.8596                       
REMARK   3      S21:   1.3679 S22:   0.8897 S23:   0.1537                       
REMARK   3      S31:  -0.1778 S32:   0.0401 S33:  -0.2388                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3BG3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045476.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0809                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76525                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 90 MM MNCL2, 0.8%(V/V)PEG3350, PH 7.5,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       86.66050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12070 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3930 ANGSTROM**2                          
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3550 ANGSTROM**2                          
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   461                                                      
REMARK 465     GLY A   462                                                      
REMARK 465     SER A   463                                                      
REMARK 465     SER A   464                                                      
REMARK 465     HIS A   465                                                      
REMARK 465     HIS A   466                                                      
REMARK 465     HIS A   467                                                      
REMARK 465     HIS A   468                                                      
REMARK 465     HIS A   469                                                      
REMARK 465     HIS A   470                                                      
REMARK 465     SER A   471                                                      
REMARK 465     SER A   472                                                      
REMARK 465     GLY A   473                                                      
REMARK 465     LEU A   474                                                      
REMARK 465     VAL A   475                                                      
REMARK 465     PRO A   476                                                      
REMARK 465     ARG A   477                                                      
REMARK 465     GLY A   478                                                      
REMARK 465     SER A   479                                                      
REMARK 465     HIS A   480                                                      
REMARK 465     MET A   481                                                      
REMARK 465     ASP A   482                                                      
REMARK 465     GLU A   483                                                      
REMARK 465     ASN A   484                                                      
REMARK 465     PRO A   485                                                      
REMARK 465     GLU A   486                                                      
REMARK 465     LEU A   487                                                      
REMARK 465     PHE A   488                                                      
REMARK 465     GLN A   489                                                      
REMARK 465     LEU A   490                                                      
REMARK 465     ARG A   491                                                      
REMARK 465     PRO A   492                                                      
REMARK 465     ALA A   493                                                      
REMARK 465     MET A  1098                                                      
REMARK 465     HIS A  1099                                                      
REMARK 465     PHE A  1100                                                      
REMARK 465     HIS A  1101                                                      
REMARK 465     PRO A  1102                                                      
REMARK 465     MET B   461                                                      
REMARK 465     GLY B   462                                                      
REMARK 465     SER B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     HIS B   465                                                      
REMARK 465     HIS B   466                                                      
REMARK 465     HIS B   467                                                      
REMARK 465     HIS B   468                                                      
REMARK 465     HIS B   469                                                      
REMARK 465     HIS B   470                                                      
REMARK 465     SER B   471                                                      
REMARK 465     SER B   472                                                      
REMARK 465     GLY B   473                                                      
REMARK 465     LEU B   474                                                      
REMARK 465     VAL B   475                                                      
REMARK 465     PRO B   476                                                      
REMARK 465     ARG B   477                                                      
REMARK 465     GLY B   478                                                      
REMARK 465     SER B   479                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     MET B   481                                                      
REMARK 465     ASP B   482                                                      
REMARK 465     GLU B   483                                                      
REMARK 465     ASN B   484                                                      
REMARK 465     PRO B   485                                                      
REMARK 465     GLU B   486                                                      
REMARK 465     LEU B   487                                                      
REMARK 465     PHE B   488                                                      
REMARK 465     GLN B   489                                                      
REMARK 465     LEU B   490                                                      
REMARK 465     ARG B   491                                                      
REMARK 465     PRO B   492                                                      
REMARK 465     ALA B   493                                                      
REMARK 465     MET B  1098                                                      
REMARK 465     HIS B  1099                                                      
REMARK 465     PHE B  1100                                                      
REMARK 465     HIS B  1101                                                      
REMARK 465     PRO B  1102                                                      
REMARK 465     LYS B  1103                                                      
REMARK 465     ALA B  1104                                                      
REMARK 465     LEU B  1105                                                      
REMARK 465     LYS B  1106                                                      
REMARK 465     ASP B  1107                                                      
REMARK 465     VAL B  1108                                                      
REMARK 465     LYS B  1109                                                      
REMARK 465     GLY B  1110                                                      
REMARK 465     GLN B  1111                                                      
REMARK 465     ILE B  1112                                                      
REMARK 465     GLY B  1113                                                      
REMARK 465     ALA B  1114                                                      
REMARK 465     PRO B  1115                                                      
REMARK 465     MET B  1116                                                      
REMARK 465     PRO B  1117                                                      
REMARK 465     GLY B  1118                                                      
REMARK 465     LYS B  1119                                                      
REMARK 465     VAL B  1120                                                      
REMARK 465     ILE B  1121                                                      
REMARK 465     ASP B  1122                                                      
REMARK 465     ILE B  1123                                                      
REMARK 465     LYS B  1124                                                      
REMARK 465     VAL B  1125                                                      
REMARK 465     VAL B  1126                                                      
REMARK 465     ALA B  1127                                                      
REMARK 465     GLY B  1128                                                      
REMARK 465     ALA B  1129                                                      
REMARK 465     LYS B  1130                                                      
REMARK 465     VAL B  1131                                                      
REMARK 465     ALA B  1132                                                      
REMARK 465     LYS B  1133                                                      
REMARK 465     GLY B  1134                                                      
REMARK 465     GLN B  1135                                                      
REMARK 465     PRO B  1136                                                      
REMARK 465     LEU B  1137                                                      
REMARK 465     CYS B  1138                                                      
REMARK 465     VAL B  1139                                                      
REMARK 465     LEU B  1140                                                      
REMARK 465     SER B  1141                                                      
REMARK 465     ALA B  1142                                                      
REMARK 465     MET B  1143                                                      
REMARK 465     LYS B  1144                                                      
REMARK 465     MET B  1145                                                      
REMARK 465     GLU B  1146                                                      
REMARK 465     THR B  1147                                                      
REMARK 465     VAL B  1148                                                      
REMARK 465     VAL B  1149                                                      
REMARK 465     THR B  1150                                                      
REMARK 465     SER B  1151                                                      
REMARK 465     PRO B  1152                                                      
REMARK 465     MET B  1153                                                      
REMARK 465     GLU B  1154                                                      
REMARK 465     GLY B  1155                                                      
REMARK 465     THR B  1156                                                      
REMARK 465     VAL B  1157                                                      
REMARK 465     ARG B  1158                                                      
REMARK 465     LYS B  1159                                                      
REMARK 465     VAL B  1160                                                      
REMARK 465     HIS B  1161                                                      
REMARK 465     VAL B  1162                                                      
REMARK 465     THR B  1163                                                      
REMARK 465     LYS B  1164                                                      
REMARK 465     ASP B  1165                                                      
REMARK 465     MET B  1166                                                      
REMARK 465     THR B  1167                                                      
REMARK 465     LEU B  1168                                                      
REMARK 465     GLU B  1169                                                      
REMARK 465     GLY B  1170                                                      
REMARK 465     ASP B  1171                                                      
REMARK 465     ASP B  1172                                                      
REMARK 465     LEU B  1173                                                      
REMARK 465     ILE B  1174                                                      
REMARK 465     LEU B  1175                                                      
REMARK 465     GLU B  1176                                                      
REMARK 465     ILE B  1177                                                      
REMARK 465     GLU B  1178                                                      
REMARK 465     MET C   461                                                      
REMARK 465     GLY C   462                                                      
REMARK 465     SER C   463                                                      
REMARK 465     SER C   464                                                      
REMARK 465     HIS C   465                                                      
REMARK 465     HIS C   466                                                      
REMARK 465     HIS C   467                                                      
REMARK 465     HIS C   468                                                      
REMARK 465     HIS C   469                                                      
REMARK 465     HIS C   470                                                      
REMARK 465     SER C   471                                                      
REMARK 465     SER C   472                                                      
REMARK 465     GLY C   473                                                      
REMARK 465     LEU C   474                                                      
REMARK 465     VAL C   475                                                      
REMARK 465     PRO C   476                                                      
REMARK 465     ARG C   477                                                      
REMARK 465     GLY C   478                                                      
REMARK 465     SER C   479                                                      
REMARK 465     HIS C   480                                                      
REMARK 465     MET C   481                                                      
REMARK 465     ASP C   482                                                      
REMARK 465     GLU C   483                                                      
REMARK 465     ASN C   484                                                      
REMARK 465     PRO C   485                                                      
REMARK 465     GLU C   486                                                      
REMARK 465     LEU C   487                                                      
REMARK 465     PHE C   488                                                      
REMARK 465     GLN C   489                                                      
REMARK 465     LEU C   490                                                      
REMARK 465     ARG C   491                                                      
REMARK 465     PRO C   492                                                      
REMARK 465     ALA C   493                                                      
REMARK 465     MET C  1098                                                      
REMARK 465     HIS C  1099                                                      
REMARK 465     PHE C  1100                                                      
REMARK 465     HIS C  1101                                                      
REMARK 465     PRO C  1102                                                      
REMARK 465     LYS C  1103                                                      
REMARK 465     ALA C  1104                                                      
REMARK 465     LEU C  1105                                                      
REMARK 465     LYS C  1106                                                      
REMARK 465     ASP C  1107                                                      
REMARK 465     VAL C  1108                                                      
REMARK 465     LYS C  1109                                                      
REMARK 465     GLY C  1110                                                      
REMARK 465     GLN C  1111                                                      
REMARK 465     ILE C  1112                                                      
REMARK 465     GLY C  1113                                                      
REMARK 465     ALA C  1114                                                      
REMARK 465     PRO C  1115                                                      
REMARK 465     MET C  1116                                                      
REMARK 465     PRO C  1117                                                      
REMARK 465     GLY C  1118                                                      
REMARK 465     LYS C  1119                                                      
REMARK 465     VAL C  1120                                                      
REMARK 465     ILE C  1121                                                      
REMARK 465     ASP C  1122                                                      
REMARK 465     ILE C  1123                                                      
REMARK 465     LYS C  1124                                                      
REMARK 465     VAL C  1125                                                      
REMARK 465     VAL C  1126                                                      
REMARK 465     ALA C  1127                                                      
REMARK 465     GLY C  1128                                                      
REMARK 465     ALA C  1129                                                      
REMARK 465     LYS C  1130                                                      
REMARK 465     VAL C  1131                                                      
REMARK 465     ALA C  1132                                                      
REMARK 465     LYS C  1133                                                      
REMARK 465     GLY C  1134                                                      
REMARK 465     GLN C  1135                                                      
REMARK 465     PRO C  1136                                                      
REMARK 465     LEU C  1137                                                      
REMARK 465     CYS C  1138                                                      
REMARK 465     VAL C  1139                                                      
REMARK 465     LEU C  1140                                                      
REMARK 465     SER C  1141                                                      
REMARK 465     ALA C  1142                                                      
REMARK 465     MET C  1143                                                      
REMARK 465     LYS C  1144                                                      
REMARK 465     MET C  1145                                                      
REMARK 465     GLU C  1146                                                      
REMARK 465     THR C  1147                                                      
REMARK 465     VAL C  1148                                                      
REMARK 465     VAL C  1149                                                      
REMARK 465     THR C  1150                                                      
REMARK 465     SER C  1151                                                      
REMARK 465     PRO C  1152                                                      
REMARK 465     MET C  1153                                                      
REMARK 465     GLU C  1154                                                      
REMARK 465     GLY C  1155                                                      
REMARK 465     THR C  1156                                                      
REMARK 465     VAL C  1157                                                      
REMARK 465     ARG C  1158                                                      
REMARK 465     LYS C  1159                                                      
REMARK 465     VAL C  1160                                                      
REMARK 465     HIS C  1161                                                      
REMARK 465     VAL C  1162                                                      
REMARK 465     THR C  1163                                                      
REMARK 465     LYS C  1164                                                      
REMARK 465     ASP C  1165                                                      
REMARK 465     MET C  1166                                                      
REMARK 465     THR C  1167                                                      
REMARK 465     LEU C  1168                                                      
REMARK 465     GLU C  1169                                                      
REMARK 465     GLY C  1170                                                      
REMARK 465     ASP C  1171                                                      
REMARK 465     ASP C  1172                                                      
REMARK 465     LEU C  1173                                                      
REMARK 465     ILE C  1174                                                      
REMARK 465     LEU C  1175                                                      
REMARK 465     GLU C  1176                                                      
REMARK 465     ILE C  1177                                                      
REMARK 465     GLU C  1178                                                      
REMARK 465     MET D   461                                                      
REMARK 465     GLY D   462                                                      
REMARK 465     SER D   463                                                      
REMARK 465     SER D   464                                                      
REMARK 465     HIS D   465                                                      
REMARK 465     HIS D   466                                                      
REMARK 465     HIS D   467                                                      
REMARK 465     HIS D   468                                                      
REMARK 465     HIS D   469                                                      
REMARK 465     HIS D   470                                                      
REMARK 465     SER D   471                                                      
REMARK 465     SER D   472                                                      
REMARK 465     GLY D   473                                                      
REMARK 465     LEU D   474                                                      
REMARK 465     VAL D   475                                                      
REMARK 465     PRO D   476                                                      
REMARK 465     ARG D   477                                                      
REMARK 465     GLY D   478                                                      
REMARK 465     SER D   479                                                      
REMARK 465     HIS D   480                                                      
REMARK 465     MET D   481                                                      
REMARK 465     ASP D   482                                                      
REMARK 465     GLU D   483                                                      
REMARK 465     ASN D   484                                                      
REMARK 465     PRO D   485                                                      
REMARK 465     GLU D   486                                                      
REMARK 465     LEU D   487                                                      
REMARK 465     PHE D   488                                                      
REMARK 465     GLN D   489                                                      
REMARK 465     LEU D   490                                                      
REMARK 465     ARG D   491                                                      
REMARK 465     PRO D   492                                                      
REMARK 465     ALA D   493                                                      
REMARK 465     MET D  1098                                                      
REMARK 465     HIS D  1099                                                      
REMARK 465     PHE D  1100                                                      
REMARK 465     HIS D  1101                                                      
REMARK 465     PRO D  1102                                                      
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    SER D   523     NH1  ARG D  1036              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 937   CD    GLU A 937   OE1     0.069                       
REMARK 500    GLU A 937   CD    GLU A 937   OE2     0.098                       
REMARK 500    ARG A 973   CD    ARG A 973   NE      0.121                       
REMARK 500    ARG A 973   CZ    ARG A 973   NH2     0.087                       
REMARK 500    ARG B 973   CZ    ARG B 973   NH1     0.153                       
REMARK 500    SER B1066   CB    SER B1066   OG      0.227                       
REMARK 500    GLU D 664   CD    GLU D 664   OE1     0.091                       
REMARK 500    GLU D 664   CD    GLU D 664   OE2     0.097                       
REMARK 500    GLU D 991   CD    GLU D 991   OE2     0.125                       
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    ASP A 543   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 567   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 672   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 795   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 860   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 903   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 973   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A1091   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP A1172   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 572   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B 799   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 973   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASP B1067   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP C 761   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C 774   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C 833   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP C 849   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP C 860   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP C1006   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D 613   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP D 742   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP D 774   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP D 860   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP D 970   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 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    PRO A 512      107.32    -43.75                                   
REMARK 500    LYS A 519       31.33    -67.93                                   
REMARK 500    ARG A 571      -87.96   -139.37                                   
REMARK 500    ALA A 579       44.34     37.00                                   
REMARK 500    THR A 580       19.83     56.73                                   
REMARK 500    ASN A 606       16.28   -148.98                                   
REMARK 500    ASN A 647        8.25    -66.67                                   
REMARK 500    ALA A 648      -91.63     43.84                                   
REMARK 500    ASP A 656      -55.16    -26.07                                   
REMARK 500    ASN A 681       72.21    -65.26                                   
REMARK 500    ASP A 765       72.42   -112.62                                   
REMARK 500    MET A 804     -133.14     49.38                                   
REMARK 500    PRO A 821      -18.45    -49.49                                   
REMARK 500    ASP A 823      125.96    -23.97                                   
REMARK 500    ASN A 873       32.20    -90.76                                   
REMARK 500    LEU A 874      -35.12   -149.32                                   
REMARK 500    SER A 880      -65.32   -106.44                                   
REMARK 500    ASP A 903       90.36     56.50                                   
REMARK 500    ASN A 924       36.05   -153.18                                   
REMARK 500    SER A 939       87.46     63.23                                   
REMARK 500    PRO A 960      106.02    -55.67                                   
REMARK 500    LYS A 969      -30.56     56.21                                   
REMARK 500    ASP A 970       23.74   -155.17                                   
REMARK 500    ASP A1031        2.07    -69.27                                   
REMARK 500    ALA A1045      -12.49     66.41                                   
REMARK 500    GLU A1053       92.23      9.11                                   
REMARK 500    ARG A1054      -14.26     83.51                                   
REMARK 500    ALA A1071        1.22    -62.58                                   
REMARK 500    LEU A1080     -102.67    -80.97                                   
REMARK 500    ASP A1107      -82.27    -98.02                                   
REMARK 500    ALA A1127       93.67    -51.74                                   
REMARK 500    ALA A1142      -90.96    -80.12                                   
REMARK 500    LYS A1144       -8.73     62.11                                   
REMARK 500    ARG A1158     -139.13    -72.65                                   
REMARK 500    THR A1163      -90.39   -104.15                                   
REMARK 500    ASP A1165      -95.58     94.15                                   
REMARK 500    MET A1166      149.63    -39.62                                   
REMARK 500    ILE A1174      -73.66   -124.78                                   
REMARK 500    ARG B 571      -77.18   -134.13                                   
REMARK 500    ARG B 644       34.64    -83.03                                   
REMARK 500    ALA B 648     -113.33     51.24                                   
REMARK 500    ASN B 681       13.53     54.30                                   
REMARK 500    LYS B 717      -48.12   -152.32                                   
REMARK 500    TYR B 718       59.01   -117.17                                   
REMARK 500    MET B 804     -122.60     45.81                                   
REMARK 500    PRO B 821      -31.00    -39.06                                   
REMARK 500    ASP B 823      124.60    -33.01                                   
REMARK 500    GLU B 825       12.31     57.49                                   
REMARK 500    ASN B 873       39.89    -75.02                                   
REMARK 500    LEU B 874      -42.70   -136.87                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     137 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 572   OD1                                                    
REMARK 620 2 KCX A 741   OQ1  90.0                                              
REMARK 620 3 KCX A 741   OQ2 143.3  56.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 572   OD1                                                    
REMARK 620 2 KCX B 741   OQ1  95.6                                              
REMARK 620 3 KCX B 741   OQ2 150.1  55.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 572   OD1                                                    
REMARK 620 2 KCX C 741   OQ1  82.2                                              
REMARK 620 3 KCX C 741   OQ2 132.5  50.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 572   OD1                                                    
REMARK 620 2 KCX D 741   OQ1  88.0                                              
REMARK 620 3 KCX D 741   OQ2 139.9  52.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 2000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTI A 2100                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 2000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR C 2000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR D 2000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RQH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BG5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3BG9   RELATED DB: PDB                                   
DBREF  3BG3 A  482  1178  UNP    P11498   PYC_HUMAN      482   1178             
DBREF  3BG3 B  482  1178  UNP    P11498   PYC_HUMAN      482   1178             
DBREF  3BG3 C  482  1178  UNP    P11498   PYC_HUMAN      482   1178             
DBREF  3BG3 D  482  1178  UNP    P11498   PYC_HUMAN      482   1178             
SEQADV 3BG3 MET A  461  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY A  462  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER A  463  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER A  464  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  465  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  466  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  467  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  468  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  469  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  470  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER A  471  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER A  472  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY A  473  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 LEU A  474  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 VAL A  475  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 PRO A  476  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 ARG A  477  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY A  478  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER A  479  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS A  480  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET A  481  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET B  461  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY B  462  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER B  463  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER B  464  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  465  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  466  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  467  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  468  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  469  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  470  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER B  471  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER B  472  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY B  473  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 LEU B  474  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 VAL B  475  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 PRO B  476  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 ARG B  477  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY B  478  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER B  479  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS B  480  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET B  481  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET C  461  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY C  462  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER C  463  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER C  464  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  465  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  466  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  467  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  468  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  469  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  470  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER C  471  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER C  472  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY C  473  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 LEU C  474  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 VAL C  475  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 PRO C  476  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 ARG C  477  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY C  478  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER C  479  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS C  480  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET C  481  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET D  461  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY D  462  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER D  463  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER D  464  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  465  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  466  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  467  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  468  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  469  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  470  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER D  471  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER D  472  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY D  473  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 LEU D  474  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 VAL D  475  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 PRO D  476  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 ARG D  477  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 GLY D  478  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 SER D  479  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 HIS D  480  UNP  P11498              EXPRESSION TAG                 
SEQADV 3BG3 MET D  481  UNP  P11498              EXPRESSION TAG                 
SEQRES   1 A  718  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  718  LEU VAL PRO ARG GLY SER HIS MET ASP GLU ASN PRO GLU          
SEQRES   3 A  718  LEU PHE GLN LEU ARG PRO ALA GLN ASN ARG ALA GLN LYS          
SEQRES   4 A  718  LEU LEU HIS TYR LEU GLY HIS VAL MET VAL ASN GLY PRO          
SEQRES   5 A  718  THR THR PRO ILE PRO VAL LYS ALA SER PRO SER PRO THR          
SEQRES   6 A  718  ASP PRO VAL VAL PRO ALA VAL PRO ILE GLY PRO PRO PRO          
SEQRES   7 A  718  ALA GLY PHE ARG ASP ILE LEU LEU ARG GLU GLY PRO GLU          
SEQRES   8 A  718  GLY PHE ALA ARG ALA VAL ARG ASN HIS PRO GLY LEU LEU          
SEQRES   9 A  718  LEU MET ASP THR THR PHE ARG ASP ALA HIS GLN SER LEU          
SEQRES  10 A  718  LEU ALA THR ARG VAL ARG THR HIS ASP LEU LYS LYS ILE          
SEQRES  11 A  718  ALA PRO TYR VAL ALA HIS ASN PHE SER LYS LEU PHE SER          
SEQRES  12 A  718  MET GLU ASN TRP GLY GLY ALA THR PHE ASP VAL ALA MET          
SEQRES  13 A  718  ARG PHE LEU TYR GLU CYS PRO TRP ARG ARG LEU GLN GLU          
SEQRES  14 A  718  LEU ARG GLU LEU ILE PRO ASN ILE PRO PHE GLN MET LEU          
SEQRES  15 A  718  LEU ARG GLY ALA ASN ALA VAL GLY TYR THR ASN TYR PRO          
SEQRES  16 A  718  ASP ASN VAL VAL PHE LYS PHE CYS GLU VAL ALA LYS GLU          
SEQRES  17 A  718  ASN GLY MET ASP VAL PHE ARG VAL PHE ASP SER LEU ASN          
SEQRES  18 A  718  TYR LEU PRO ASN MET LEU LEU GLY MET GLU ALA ALA GLY          
SEQRES  19 A  718  SER ALA GLY GLY VAL VAL GLU ALA ALA ILE SER TYR THR          
SEQRES  20 A  718  GLY ASP VAL ALA ASP PRO SER ARG THR LYS TYR SER LEU          
SEQRES  21 A  718  GLN TYR TYR MET GLY LEU ALA GLU GLU LEU VAL ARG ALA          
SEQRES  22 A  718  GLY THR HIS ILE LEU CYS ILE KCX ASP MET ALA GLY LEU          
SEQRES  23 A  718  LEU LYS PRO THR ALA CYS THR MET LEU VAL SER SER LEU          
SEQRES  24 A  718  ARG ASP ARG PHE PRO ASP LEU PRO LEU HIS ILE HIS THR          
SEQRES  25 A  718  HIS ASP THR SER GLY ALA GLY VAL ALA ALA MET LEU ALA          
SEQRES  26 A  718  CYS ALA GLN ALA GLY ALA ASP VAL VAL ASP VAL ALA ALA          
SEQRES  27 A  718  ASP SER MET SER GLY MET THR SER GLN PRO SER MET GLY          
SEQRES  28 A  718  ALA LEU VAL ALA CYS THR ARG GLY THR PRO LEU ASP THR          
SEQRES  29 A  718  GLU VAL PRO MET GLU ARG VAL PHE ASP TYR SER GLU TYR          
SEQRES  30 A  718  TRP GLU GLY ALA ARG GLY LEU TYR ALA ALA PHE ASP CYS          
SEQRES  31 A  718  THR ALA THR MET LYS SER GLY ASN SER ASP VAL TYR GLU          
SEQRES  32 A  718  ASN GLU ILE PRO GLY GLY GLN TYR THR ASN LEU HIS PHE          
SEQRES  33 A  718  GLN ALA HIS SER MET GLY LEU GLY SER LYS PHE LYS GLU          
SEQRES  34 A  718  VAL LYS LYS ALA TYR VAL GLU ALA ASN GLN MET LEU GLY          
SEQRES  35 A  718  ASP LEU ILE LYS VAL THR PRO SER SER LYS ILE VAL GLY          
SEQRES  36 A  718  ASP LEU ALA GLN PHE MET VAL GLN ASN GLY LEU SER ARG          
SEQRES  37 A  718  ALA GLU ALA GLU ALA GLN ALA GLU GLU LEU SER PHE PRO          
SEQRES  38 A  718  ARG SER VAL VAL GLU PHE LEU GLN GLY TYR ILE GLY VAL          
SEQRES  39 A  718  PRO HIS GLY GLY PHE PRO GLU PRO PHE ARG SER LYS VAL          
SEQRES  40 A  718  LEU LYS ASP LEU PRO ARG VAL GLU GLY ARG PRO GLY ALA          
SEQRES  41 A  718  SER LEU PRO PRO LEU ASP LEU GLN ALA LEU GLU LYS GLU          
SEQRES  42 A  718  LEU VAL ASP ARG HIS GLY GLU GLU VAL THR PRO GLU ASP          
SEQRES  43 A  718  VAL LEU SER ALA ALA MET TYR PRO ASP VAL PHE ALA HIS          
SEQRES  44 A  718  PHE LYS ASP PHE THR ALA THR PHE GLY PRO LEU ASP SER          
SEQRES  45 A  718  LEU ASN THR ARG LEU PHE LEU GLN GLY PRO LYS ILE ALA          
SEQRES  46 A  718  GLU GLU PHE GLU VAL GLU LEU GLU ARG GLY LYS THR LEU          
SEQRES  47 A  718  HIS ILE LYS ALA LEU ALA VAL SER ASP LEU ASN ARG ALA          
SEQRES  48 A  718  GLY GLN ARG GLN VAL PHE PHE GLU LEU ASN GLY GLN LEU          
SEQRES  49 A  718  ARG SER ILE LEU VAL LYS ASP THR GLN ALA MET LYS GLU          
SEQRES  50 A  718  MET HIS PHE HIS PRO LYS ALA LEU LYS ASP VAL LYS GLY          
SEQRES  51 A  718  GLN ILE GLY ALA PRO MET PRO GLY LYS VAL ILE ASP ILE          
SEQRES  52 A  718  LYS VAL VAL ALA GLY ALA LYS VAL ALA LYS GLY GLN PRO          
SEQRES  53 A  718  LEU CYS VAL LEU SER ALA MET LYS MET GLU THR VAL VAL          
SEQRES  54 A  718  THR SER PRO MET GLU GLY THR VAL ARG LYS VAL HIS VAL          
SEQRES  55 A  718  THR LYS ASP MET THR LEU GLU GLY ASP ASP LEU ILE LEU          
SEQRES  56 A  718  GLU ILE GLU                                                  
SEQRES   1 B  718  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  718  LEU VAL PRO ARG GLY SER HIS MET ASP GLU ASN PRO GLU          
SEQRES   3 B  718  LEU PHE GLN LEU ARG PRO ALA GLN ASN ARG ALA GLN LYS          
SEQRES   4 B  718  LEU LEU HIS TYR LEU GLY HIS VAL MET VAL ASN GLY PRO          
SEQRES   5 B  718  THR THR PRO ILE PRO VAL LYS ALA SER PRO SER PRO THR          
SEQRES   6 B  718  ASP PRO VAL VAL PRO ALA VAL PRO ILE GLY PRO PRO PRO          
SEQRES   7 B  718  ALA GLY PHE ARG ASP ILE LEU LEU ARG GLU GLY PRO GLU          
SEQRES   8 B  718  GLY PHE ALA ARG ALA VAL ARG ASN HIS PRO GLY LEU LEU          
SEQRES   9 B  718  LEU MET ASP THR THR PHE ARG ASP ALA HIS GLN SER LEU          
SEQRES  10 B  718  LEU ALA THR ARG VAL ARG THR HIS ASP LEU LYS LYS ILE          
SEQRES  11 B  718  ALA PRO TYR VAL ALA HIS ASN PHE SER LYS LEU PHE SER          
SEQRES  12 B  718  MET GLU ASN TRP GLY GLY ALA THR PHE ASP VAL ALA MET          
SEQRES  13 B  718  ARG PHE LEU TYR GLU CYS PRO TRP ARG ARG LEU GLN GLU          
SEQRES  14 B  718  LEU ARG GLU LEU ILE PRO ASN ILE PRO PHE GLN MET LEU          
SEQRES  15 B  718  LEU ARG GLY ALA ASN ALA VAL GLY TYR THR ASN TYR PRO          
SEQRES  16 B  718  ASP ASN VAL VAL PHE LYS PHE CYS GLU VAL ALA LYS GLU          
SEQRES  17 B  718  ASN GLY MET ASP VAL PHE ARG VAL PHE ASP SER LEU ASN          
SEQRES  18 B  718  TYR LEU PRO ASN MET LEU LEU GLY MET GLU ALA ALA GLY          
SEQRES  19 B  718  SER ALA GLY GLY VAL VAL GLU ALA ALA ILE SER TYR THR          
SEQRES  20 B  718  GLY ASP VAL ALA ASP PRO SER ARG THR LYS TYR SER LEU          
SEQRES  21 B  718  GLN TYR TYR MET GLY LEU ALA GLU GLU LEU VAL ARG ALA          
SEQRES  22 B  718  GLY THR HIS ILE LEU CYS ILE KCX ASP MET ALA GLY LEU          
SEQRES  23 B  718  LEU LYS PRO THR ALA CYS THR MET LEU VAL SER SER LEU          
SEQRES  24 B  718  ARG ASP ARG PHE PRO ASP LEU PRO LEU HIS ILE HIS THR          
SEQRES  25 B  718  HIS ASP THR SER GLY ALA GLY VAL ALA ALA MET LEU ALA          
SEQRES  26 B  718  CYS ALA GLN ALA GLY ALA ASP VAL VAL ASP VAL ALA ALA          
SEQRES  27 B  718  ASP SER MET SER GLY MET THR SER GLN PRO SER MET GLY          
SEQRES  28 B  718  ALA LEU VAL ALA CYS THR ARG GLY THR PRO LEU ASP THR          
SEQRES  29 B  718  GLU VAL PRO MET GLU ARG VAL PHE ASP TYR SER GLU TYR          
SEQRES  30 B  718  TRP GLU GLY ALA ARG GLY LEU TYR ALA ALA PHE ASP CYS          
SEQRES  31 B  718  THR ALA THR MET LYS SER GLY ASN SER ASP VAL TYR GLU          
SEQRES  32 B  718  ASN GLU ILE PRO GLY GLY GLN TYR THR ASN LEU HIS PHE          
SEQRES  33 B  718  GLN ALA HIS SER MET GLY LEU GLY SER LYS PHE LYS GLU          
SEQRES  34 B  718  VAL LYS LYS ALA TYR VAL GLU ALA ASN GLN MET LEU GLY          
SEQRES  35 B  718  ASP LEU ILE LYS VAL THR PRO SER SER LYS ILE VAL GLY          
SEQRES  36 B  718  ASP LEU ALA GLN PHE MET VAL GLN ASN GLY LEU SER ARG          
SEQRES  37 B  718  ALA GLU ALA GLU ALA GLN ALA GLU GLU LEU SER PHE PRO          
SEQRES  38 B  718  ARG SER VAL VAL GLU PHE LEU GLN GLY TYR ILE GLY VAL          
SEQRES  39 B  718  PRO HIS GLY GLY PHE PRO GLU PRO PHE ARG SER LYS VAL          
SEQRES  40 B  718  LEU LYS ASP LEU PRO ARG VAL GLU GLY ARG PRO GLY ALA          
SEQRES  41 B  718  SER LEU PRO PRO LEU ASP LEU GLN ALA LEU GLU LYS GLU          
SEQRES  42 B  718  LEU VAL ASP ARG HIS GLY GLU GLU VAL THR PRO GLU ASP          
SEQRES  43 B  718  VAL LEU SER ALA ALA MET TYR PRO ASP VAL PHE ALA HIS          
SEQRES  44 B  718  PHE LYS ASP PHE THR ALA THR PHE GLY PRO LEU ASP SER          
SEQRES  45 B  718  LEU ASN THR ARG LEU PHE LEU GLN GLY PRO LYS ILE ALA          
SEQRES  46 B  718  GLU GLU PHE GLU VAL GLU LEU GLU ARG GLY LYS THR LEU          
SEQRES  47 B  718  HIS ILE LYS ALA LEU ALA VAL SER ASP LEU ASN ARG ALA          
SEQRES  48 B  718  GLY GLN ARG GLN VAL PHE PHE GLU LEU ASN GLY GLN LEU          
SEQRES  49 B  718  ARG SER ILE LEU VAL LYS ASP THR GLN ALA MET LYS GLU          
SEQRES  50 B  718  MET HIS PHE HIS PRO LYS ALA LEU LYS ASP VAL LYS GLY          
SEQRES  51 B  718  GLN ILE GLY ALA PRO MET PRO GLY LYS VAL ILE ASP ILE          
SEQRES  52 B  718  LYS VAL VAL ALA GLY ALA LYS VAL ALA LYS GLY GLN PRO          
SEQRES  53 B  718  LEU CYS VAL LEU SER ALA MET LYS MET GLU THR VAL VAL          
SEQRES  54 B  718  THR SER PRO MET GLU GLY THR VAL ARG LYS VAL HIS VAL          
SEQRES  55 B  718  THR LYS ASP MET THR LEU GLU GLY ASP ASP LEU ILE LEU          
SEQRES  56 B  718  GLU ILE GLU                                                  
SEQRES   1 C  718  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  718  LEU VAL PRO ARG GLY SER HIS MET ASP GLU ASN PRO GLU          
SEQRES   3 C  718  LEU PHE GLN LEU ARG PRO ALA GLN ASN ARG ALA GLN LYS          
SEQRES   4 C  718  LEU LEU HIS TYR LEU GLY HIS VAL MET VAL ASN GLY PRO          
SEQRES   5 C  718  THR THR PRO ILE PRO VAL LYS ALA SER PRO SER PRO THR          
SEQRES   6 C  718  ASP PRO VAL VAL PRO ALA VAL PRO ILE GLY PRO PRO PRO          
SEQRES   7 C  718  ALA GLY PHE ARG ASP ILE LEU LEU ARG GLU GLY PRO GLU          
SEQRES   8 C  718  GLY PHE ALA ARG ALA VAL ARG ASN HIS PRO GLY LEU LEU          
SEQRES   9 C  718  LEU MET ASP THR THR PHE ARG ASP ALA HIS GLN SER LEU          
SEQRES  10 C  718  LEU ALA THR ARG VAL ARG THR HIS ASP LEU LYS LYS ILE          
SEQRES  11 C  718  ALA PRO TYR VAL ALA HIS ASN PHE SER LYS LEU PHE SER          
SEQRES  12 C  718  MET GLU ASN TRP GLY GLY ALA THR PHE ASP VAL ALA MET          
SEQRES  13 C  718  ARG PHE LEU TYR GLU CYS PRO TRP ARG ARG LEU GLN GLU          
SEQRES  14 C  718  LEU ARG GLU LEU ILE PRO ASN ILE PRO PHE GLN MET LEU          
SEQRES  15 C  718  LEU ARG GLY ALA ASN ALA VAL GLY TYR THR ASN TYR PRO          
SEQRES  16 C  718  ASP ASN VAL VAL PHE LYS PHE CYS GLU VAL ALA LYS GLU          
SEQRES  17 C  718  ASN GLY MET ASP VAL PHE ARG VAL PHE ASP SER LEU ASN          
SEQRES  18 C  718  TYR LEU PRO ASN MET LEU LEU GLY MET GLU ALA ALA GLY          
SEQRES  19 C  718  SER ALA GLY GLY VAL VAL GLU ALA ALA ILE SER TYR THR          
SEQRES  20 C  718  GLY ASP VAL ALA ASP PRO SER ARG THR LYS TYR SER LEU          
SEQRES  21 C  718  GLN TYR TYR MET GLY LEU ALA GLU GLU LEU VAL ARG ALA          
SEQRES  22 C  718  GLY THR HIS ILE LEU CYS ILE KCX ASP MET ALA GLY LEU          
SEQRES  23 C  718  LEU LYS PRO THR ALA CYS THR MET LEU VAL SER SER LEU          
SEQRES  24 C  718  ARG ASP ARG PHE PRO ASP LEU PRO LEU HIS ILE HIS THR          
SEQRES  25 C  718  HIS ASP THR SER GLY ALA GLY VAL ALA ALA MET LEU ALA          
SEQRES  26 C  718  CYS ALA GLN ALA GLY ALA ASP VAL VAL ASP VAL ALA ALA          
SEQRES  27 C  718  ASP SER MET SER GLY MET THR SER GLN PRO SER MET GLY          
SEQRES  28 C  718  ALA LEU VAL ALA CYS THR ARG GLY THR PRO LEU ASP THR          
SEQRES  29 C  718  GLU VAL PRO MET GLU ARG VAL PHE ASP TYR SER GLU TYR          
SEQRES  30 C  718  TRP GLU GLY ALA ARG GLY LEU TYR ALA ALA PHE ASP CYS          
SEQRES  31 C  718  THR ALA THR MET LYS SER GLY ASN SER ASP VAL TYR GLU          
SEQRES  32 C  718  ASN GLU ILE PRO GLY GLY GLN TYR THR ASN LEU HIS PHE          
SEQRES  33 C  718  GLN ALA HIS SER MET GLY LEU GLY SER LYS PHE LYS GLU          
SEQRES  34 C  718  VAL LYS LYS ALA TYR VAL GLU ALA ASN GLN MET LEU GLY          
SEQRES  35 C  718  ASP LEU ILE LYS VAL THR PRO SER SER LYS ILE VAL GLY          
SEQRES  36 C  718  ASP LEU ALA GLN PHE MET VAL GLN ASN GLY LEU SER ARG          
SEQRES  37 C  718  ALA GLU ALA GLU ALA GLN ALA GLU GLU LEU SER PHE PRO          
SEQRES  38 C  718  ARG SER VAL VAL GLU PHE LEU GLN GLY TYR ILE GLY VAL          
SEQRES  39 C  718  PRO HIS GLY GLY PHE PRO GLU PRO PHE ARG SER LYS VAL          
SEQRES  40 C  718  LEU LYS ASP LEU PRO ARG VAL GLU GLY ARG PRO GLY ALA          
SEQRES  41 C  718  SER LEU PRO PRO LEU ASP LEU GLN ALA LEU GLU LYS GLU          
SEQRES  42 C  718  LEU VAL ASP ARG HIS GLY GLU GLU VAL THR PRO GLU ASP          
SEQRES  43 C  718  VAL LEU SER ALA ALA MET TYR PRO ASP VAL PHE ALA HIS          
SEQRES  44 C  718  PHE LYS ASP PHE THR ALA THR PHE GLY PRO LEU ASP SER          
SEQRES  45 C  718  LEU ASN THR ARG LEU PHE LEU GLN GLY PRO LYS ILE ALA          
SEQRES  46 C  718  GLU GLU PHE GLU VAL GLU LEU GLU ARG GLY LYS THR LEU          
SEQRES  47 C  718  HIS ILE LYS ALA LEU ALA VAL SER ASP LEU ASN ARG ALA          
SEQRES  48 C  718  GLY GLN ARG GLN VAL PHE PHE GLU LEU ASN GLY GLN LEU          
SEQRES  49 C  718  ARG SER ILE LEU VAL LYS ASP THR GLN ALA MET LYS GLU          
SEQRES  50 C  718  MET HIS PHE HIS PRO LYS ALA LEU LYS ASP VAL LYS GLY          
SEQRES  51 C  718  GLN ILE GLY ALA PRO MET PRO GLY LYS VAL ILE ASP ILE          
SEQRES  52 C  718  LYS VAL VAL ALA GLY ALA LYS VAL ALA LYS GLY GLN PRO          
SEQRES  53 C  718  LEU CYS VAL LEU SER ALA MET LYS MET GLU THR VAL VAL          
SEQRES  54 C  718  THR SER PRO MET GLU GLY THR VAL ARG LYS VAL HIS VAL          
SEQRES  55 C  718  THR LYS ASP MET THR LEU GLU GLY ASP ASP LEU ILE LEU          
SEQRES  56 C  718  GLU ILE GLU                                                  
SEQRES   1 D  718  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  718  LEU VAL PRO ARG GLY SER HIS MET ASP GLU ASN PRO GLU          
SEQRES   3 D  718  LEU PHE GLN LEU ARG PRO ALA GLN ASN ARG ALA GLN LYS          
SEQRES   4 D  718  LEU LEU HIS TYR LEU GLY HIS VAL MET VAL ASN GLY PRO          
SEQRES   5 D  718  THR THR PRO ILE PRO VAL LYS ALA SER PRO SER PRO THR          
SEQRES   6 D  718  ASP PRO VAL VAL PRO ALA VAL PRO ILE GLY PRO PRO PRO          
SEQRES   7 D  718  ALA GLY PHE ARG ASP ILE LEU LEU ARG GLU GLY PRO GLU          
SEQRES   8 D  718  GLY PHE ALA ARG ALA VAL ARG ASN HIS PRO GLY LEU LEU          
SEQRES   9 D  718  LEU MET ASP THR THR PHE ARG ASP ALA HIS GLN SER LEU          
SEQRES  10 D  718  LEU ALA THR ARG VAL ARG THR HIS ASP LEU LYS LYS ILE          
SEQRES  11 D  718  ALA PRO TYR VAL ALA HIS ASN PHE SER LYS LEU PHE SER          
SEQRES  12 D  718  MET GLU ASN TRP GLY GLY ALA THR PHE ASP VAL ALA MET          
SEQRES  13 D  718  ARG PHE LEU TYR GLU CYS PRO TRP ARG ARG LEU GLN GLU          
SEQRES  14 D  718  LEU ARG GLU LEU ILE PRO ASN ILE PRO PHE GLN MET LEU          
SEQRES  15 D  718  LEU ARG GLY ALA ASN ALA VAL GLY TYR THR ASN TYR PRO          
SEQRES  16 D  718  ASP ASN VAL VAL PHE LYS PHE CYS GLU VAL ALA LYS GLU          
SEQRES  17 D  718  ASN GLY MET ASP VAL PHE ARG VAL PHE ASP SER LEU ASN          
SEQRES  18 D  718  TYR LEU PRO ASN MET LEU LEU GLY MET GLU ALA ALA GLY          
SEQRES  19 D  718  SER ALA GLY GLY VAL VAL GLU ALA ALA ILE SER TYR THR          
SEQRES  20 D  718  GLY ASP VAL ALA ASP PRO SER ARG THR LYS TYR SER LEU          
SEQRES  21 D  718  GLN TYR TYR MET GLY LEU ALA GLU GLU LEU VAL ARG ALA          
SEQRES  22 D  718  GLY THR HIS ILE LEU CYS ILE KCX ASP MET ALA GLY LEU          
SEQRES  23 D  718  LEU LYS PRO THR ALA CYS THR MET LEU VAL SER SER LEU          
SEQRES  24 D  718  ARG ASP ARG PHE PRO ASP LEU PRO LEU HIS ILE HIS THR          
SEQRES  25 D  718  HIS ASP THR SER GLY ALA GLY VAL ALA ALA MET LEU ALA          
SEQRES  26 D  718  CYS ALA GLN ALA GLY ALA ASP VAL VAL ASP VAL ALA ALA          
SEQRES  27 D  718  ASP SER MET SER GLY MET THR SER GLN PRO SER MET GLY          
SEQRES  28 D  718  ALA LEU VAL ALA CYS THR ARG GLY THR PRO LEU ASP THR          
SEQRES  29 D  718  GLU VAL PRO MET GLU ARG VAL PHE ASP TYR SER GLU TYR          
SEQRES  30 D  718  TRP GLU GLY ALA ARG GLY LEU TYR ALA ALA PHE ASP CYS          
SEQRES  31 D  718  THR ALA THR MET LYS SER GLY ASN SER ASP VAL TYR GLU          
SEQRES  32 D  718  ASN GLU ILE PRO GLY GLY GLN TYR THR ASN LEU HIS PHE          
SEQRES  33 D  718  GLN ALA HIS SER MET GLY LEU GLY SER LYS PHE LYS GLU          
SEQRES  34 D  718  VAL LYS LYS ALA TYR VAL GLU ALA ASN GLN MET LEU GLY          
SEQRES  35 D  718  ASP LEU ILE LYS VAL THR PRO SER SER LYS ILE VAL GLY          
SEQRES  36 D  718  ASP LEU ALA GLN PHE MET VAL GLN ASN GLY LEU SER ARG          
SEQRES  37 D  718  ALA GLU ALA GLU ALA GLN ALA GLU GLU LEU SER PHE PRO          
SEQRES  38 D  718  ARG SER VAL VAL GLU PHE LEU GLN GLY TYR ILE GLY VAL          
SEQRES  39 D  718  PRO HIS GLY GLY PHE PRO GLU PRO PHE ARG SER LYS VAL          
SEQRES  40 D  718  LEU LYS ASP LEU PRO ARG VAL GLU GLY ARG PRO GLY ALA          
SEQRES  41 D  718  SER LEU PRO PRO LEU ASP LEU GLN ALA LEU GLU LYS GLU          
SEQRES  42 D  718  LEU VAL ASP ARG HIS GLY GLU GLU VAL THR PRO GLU ASP          
SEQRES  43 D  718  VAL LEU SER ALA ALA MET TYR PRO ASP VAL PHE ALA HIS          
SEQRES  44 D  718  PHE LYS ASP PHE THR ALA THR PHE GLY PRO LEU ASP SER          
SEQRES  45 D  718  LEU ASN THR ARG LEU PHE LEU GLN GLY PRO LYS ILE ALA          
SEQRES  46 D  718  GLU GLU PHE GLU VAL GLU LEU GLU ARG GLY LYS THR LEU          
SEQRES  47 D  718  HIS ILE LYS ALA LEU ALA VAL SER ASP LEU ASN ARG ALA          
SEQRES  48 D  718  GLY GLN ARG GLN VAL PHE PHE GLU LEU ASN GLY GLN LEU          
SEQRES  49 D  718  ARG SER ILE LEU VAL LYS ASP THR GLN ALA MET LYS GLU          
SEQRES  50 D  718  MET HIS PHE HIS PRO LYS ALA LEU LYS ASP VAL LYS GLY          
SEQRES  51 D  718  GLN ILE GLY ALA PRO MET PRO GLY LYS VAL ILE ASP ILE          
SEQRES  52 D  718  LYS VAL VAL ALA GLY ALA LYS VAL ALA LYS GLY GLN PRO          
SEQRES  53 D  718  LEU CYS VAL LEU SER ALA MET LYS MET GLU THR VAL VAL          
SEQRES  54 D  718  THR SER PRO MET GLU GLY THR VAL ARG LYS VAL HIS VAL          
SEQRES  55 D  718  THR LYS ASP MET THR LEU GLU GLY ASP ASP LEU ILE LEU          
SEQRES  56 D  718  GLU ILE GLU                                                  
MODRES 3BG3 KCX A  741  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3BG3 KCX B  741  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3BG3 KCX C  741  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3BG3 KCX D  741  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    KCX  A 741      12                                                       
HET    KCX  B 741      12                                                       
HET    KCX  C 741      12                                                       
HET    KCX  D 741      12                                                       
HET     MN  A2001       1                                                       
HET    PYR  A2000       6                                                       
HET    BTI  A2100      15                                                       
HET     MN  B2001       1                                                       
HET    PYR  B2000       6                                                       
HET     MN  C2001       1                                                       
HET    PYR  C2000       6                                                       
HET     MN  D2001       1                                                       
HET    PYR  D2000       6                                                       
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PYR PYRUVIC ACID                                                     
HETNAM     BTI 5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)                
HETNAM   2 BTI  PENTANAL                                                        
FORMUL   1  KCX    4(C7 H14 N2 O4)                                              
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   6  PYR    4(C3 H4 O3)                                                  
FORMUL   7  BTI    C10 H16 N2 O2 S                                              
HELIX    1   1 GLN A  494  GLY A  511  1                                  18    
HELIX    2   2 GLY A  540  HIS A  560  1                                  21    
HELIX    3   3 ARG A  571  LEU A  578  1                                   8    
HELIX    4   4 ARG A  583  PHE A  598  1                                  16    
HELIX    5   5 ALA A  610  PHE A  618  1                                   9    
HELIX    6   6 CYS A  622  ILE A  634  1                                  13    
HELIX    7   7 ARG A  644  ALA A  648  5                                   5    
HELIX    8   8 PRO A  655  GLY A  670  1                                  16    
HELIX    9   9 TYR A  682  SER A  695  1                                  14    
HELIX   10  10 SER A  719  GLY A  734  1                                  16    
HELIX   11  11 LYS A  748  PHE A  763  1                                  16    
HELIX   12  12 ALA A  778  ALA A  789  1                                  12    
HELIX   13  13 ALA A  798  SER A  802  5                                   5    
HELIX   14  14 SER A  809  ARG A  818  1                                  10    
HELIX   15  15 PRO A  827  TYR A  845  1                                  19    
HELIX   16  16 ALA A  846  THR A  853  5                                   8    
HELIX   17  17 ASP A  860  GLU A  865  1                                   6    
HELIX   18  18 PRO A  867  PHE A  876  1                                  10    
HELIX   19  19 GLN A  877  HIS A  879  5                                   3    
HELIX   20  20 SER A  885  LEU A  901  1                                  17    
HELIX   21  21 PRO A  909  ASN A  924  1                                  16    
HELIX   22  22 SER A  927  ALA A  935  1                                   9    
HELIX   23  23 PRO A  941  LEU A  948  1                                   8    
HELIX   24  24 PRO A  960  LYS A  969  1                                  10    
HELIX   25  25 ARG A  977  LEU A  982  1                                   6    
HELIX   26  26 GLN A  988  HIS A  998  1                                  11    
HELIX   27  27 THR A 1003  TYR A 1013  1                                  11    
HELIX   28  28 TYR A 1013  PHE A 1027  1                                  15    
HELIX   29  29 ASN A 1034  GLY A 1041  1                                   8    
HELIX   30  30 THR A 1092  MET A 1095  5                                   4    
HELIX   31  31 ALA B  497  GLY B  511  1                                  15    
HELIX   32  32 GLY B  540  HIS B  560  1                                  21    
HELIX   33  33 ARG B  571  LEU B  578  1                                   8    
HELIX   34  34 ARG B  583  ILE B  590  1                                   8    
HELIX   35  35 ILE B  590  PHE B  598  1                                   9    
HELIX   36  36 ALA B  610  PHE B  618  1                                   9    
HELIX   37  37 CYS B  622  ILE B  634  1                                  13    
HELIX   38  38 ARG B  644  ALA B  648  5                                   5    
HELIX   39  39 PRO B  655  GLU B  668  1                                  14    
HELIX   40  40 TYR B  682  GLY B  697  1                                  16    
HELIX   41  41 SER B  719  GLY B  734  1                                  16    
HELIX   42  42 LYS B  748  ASP B  761  1                                  14    
HELIX   43  43 ALA B  778  ALA B  789  1                                  12    
HELIX   44  44 ALA B  798  SER B  802  5                                   5    
HELIX   45  45 SER B  809  CYS B  816  1                                   8    
HELIX   46  46 PRO B  827  LEU B  844  1                                  18    
HELIX   47  47 TYR B  845  THR B  853  5                                   9    
HELIX   48  48 ASP B  860  GLU B  865  1                                   6    
HELIX   49  49 PRO B  867  ASN B  873  1                                   7    
HELIX   50  50 LYS B  886  LEU B  901  1                                  16    
HELIX   51  51 PRO B  909  ASN B  924  1                                  16    
HELIX   52  52 ARG B  928  ALA B  933  1                                   6    
HELIX   53  53 PRO B  941  GLN B  949  1                                   9    
HELIX   54  54 PRO B  960  LYS B  969  1                                  10    
HELIX   55  55 ARG B  977  LEU B  982  1                                   6    
HELIX   56  56 ASP B  986  HIS B  998  1                                  13    
HELIX   57  57 THR B 1003  TYR B 1013  1                                  11    
HELIX   58  58 TYR B 1013  GLY B 1028  1                                  16    
HELIX   59  59 ASN B 1034  GLY B 1041  1                                   8    
HELIX   60  60 ARG C  496  GLY C  511  1                                  16    
HELIX   61  61 PHE C  541  GLY C  549  1                                   9    
HELIX   62  62 GLY C  549  HIS C  560  1                                  12    
HELIX   63  63 ARG C  571  LEU C  578  1                                   8    
HELIX   64  64 ARG C  583  PHE C  598  1                                  16    
HELIX   65  65 ALA C  610  PHE C  618  1                                   9    
HELIX   66  66 CYS C  622  ILE C  634  1                                  13    
HELIX   67  67 ARG C  644  ALA C  648  5                                   5    
HELIX   68  68 PRO C  655  ASN C  669  1                                  15    
HELIX   69  69 TYR C  682  SER C  695  1                                  14    
HELIX   70  70 SER C  719  GLY C  734  1                                  16    
HELIX   71  71 LYS C  748  PHE C  763  1                                  16    
HELIX   72  72 ALA C  778  ALA C  789  1                                  12    
HELIX   73  73 ALA C  798  SER C  802  5                                   5    
HELIX   74  74 SER C  809  CYS C  816  1                                   8    
HELIX   75  75 PRO C  827  LEU C  844  1                                  18    
HELIX   76  76 TYR C  845  THR C  853  5                                   9    
HELIX   77  77 ASP C  860  GLU C  865  1                                   6    
HELIX   78  78 PRO C  867  MET C  881  1                                  15    
HELIX   79  79 SER C  885  LEU C  901  1                                  17    
HELIX   80  80 PRO C  909  VAL C  922  1                                  14    
HELIX   81  81 SER C  927  GLN C  934  1                                   8    
HELIX   82  82 PRO C  941  LEU C  948  1                                   8    
HELIX   83  83 PRO C  960  LYS C  969  1                                  10    
HELIX   84  84 ASP C  986  GLY C  999  1                                  14    
HELIX   85  85 THR C 1003  TYR C 1013  1                                  11    
HELIX   86  86 TYR C 1013  GLY C 1028  1                                  16    
HELIX   87  87 ASN C 1034  GLY C 1041  1                                   8    
HELIX   88  88 GLN D  494  GLY D  511  1                                  18    
HELIX   89  89 GLY D  540  GLY D  549  1                                  10    
HELIX   90  90 GLY D  549  HIS D  560  1                                  12    
HELIX   91  91 ARG D  571  LEU D  578  1                                   8    
HELIX   92  92 ARG D  583  PHE D  598  1                                  16    
HELIX   93  93 ALA D  610  PHE D  618  1                                   9    
HELIX   94  94 CYS D  622  ILE D  634  1                                  13    
HELIX   95  95 PRO D  655  GLY D  670  1                                  16    
HELIX   96  96 TYR D  682  GLY D  694  1                                  13    
HELIX   97  97 SER D  719  ALA D  733  1                                  15    
HELIX   98  98 LYS D  748  PHE D  763  1                                  16    
HELIX   99  99 ALA D  778  ALA D  789  1                                  12    
HELIX  100 100 ALA D  798  SER D  802  5                                   5    
HELIX  101 101 SER D  809  ARG D  818  1                                  10    
HELIX  102 102 PRO D  827  GLY D  843  1                                  17    
HELIX  103 103 LEU D  844  THR D  853  5                                  10    
HELIX  104 104 ASP D  860  GLU D  865  1                                   6    
HELIX  105 105 PRO D  867  MET D  881  1                                  15    
HELIX  106 106 SER D  885  LEU D  901  1                                  17    
HELIX  107 107 PRO D  909  GLY D  925  1                                  17    
HELIX  108 108 SER D  927  GLN D  934  1                                   8    
HELIX  109 109 PRO D  941  GLN D  949  1                                   9    
HELIX  110 110 PRO D  960  LYS D  969  1                                  10    
HELIX  111 111 ARG D  977  LEU D  982  1                                   6    
HELIX  112 112 ASP D  986  HIS D  998  1                                  13    
HELIX  113 113 THR D 1003  TYR D 1013  1                                  11    
HELIX  114 114 TYR D 1013  GLY D 1028  1                                  16    
HELIX  115 115 PRO D 1029  LEU D 1033  5                                   5    
HELIX  116 116 ASN D 1034  GLY D 1041  1                                   8    
SHEET    1   A 9 LEU A 564  ASP A 567  0                                        
SHEET    2   A 9 SER A 603  GLY A 608  1  O  GLU A 605   N  ASP A 567           
SHEET    3   A 9 PHE A 639  LEU A 643  1  O  GLN A 640   N  ASN A 606           
SHEET    4   A 9 VAL A 673  PHE A 677  1  O  ARG A 675   N  LEU A 643           
SHEET    5   A 9 VAL A 699  SER A 705  1  O  ALA A 703   N  VAL A 676           
SHEET    6   A 9 ILE A 737  KCX A 741  1  O  KCX A 741   N  ILE A 704           
SHEET    7   A 9 LEU A 768  HIS A 771  1  O  HIS A 769   N  LEU A 738           
SHEET    8   A 9 VAL A 793  VAL A 796  1  O  VAL A 793   N  ILE A 770           
SHEET    9   A 9 LEU A 564  ASP A 567  1  N  MET A 566   O  VAL A 794           
SHEET    1   B 4 GLU A1047  GLU A1051  0                                        
SHEET    2   B 4 THR A1057  LEU A1068 -1  O  ILE A1060   N  PHE A1048           
SHEET    3   B 4 GLN A1073  GLU A1079 -1  O  PHE A1077   N  LEU A1063           
SHEET    4   B 4 LEU A1084  LYS A1090 -1  O  ARG A1085   N  PHE A1078           
SHEET    1   C 2 ILE A1112  GLY A1113  0                                        
SHEET    2   C 2 LEU A1173  LEU A1175 -1  O  LEU A1175   N  ILE A1112           
SHEET    1   D 4 GLU A1146  VAL A1149  0                                        
SHEET    2   D 4 CYS A1138  SER A1141 -1  N  CYS A1138   O  VAL A1149           
SHEET    3   D 4 GLY A1118  ILE A1123 -1  N  ILE A1121   O  VAL A1139           
SHEET    4   D 4 ASP A1165  LEU A1168 -1  O  ASP A1165   N  VAL A1120           
SHEET    1   E 9 LEU B 564  ASP B 567  0                                        
SHEET    2   E 9 SER B 603  GLY B 608  1  O  GLU B 605   N  ASP B 567           
SHEET    3   E 9 PHE B 639  LEU B 643  1  O  GLN B 640   N  MET B 604           
SHEET    4   E 9 VAL B 673  VAL B 676  1  O  VAL B 673   N  MET B 641           
SHEET    5   E 9 VAL B 699  SER B 705  1  O  GLU B 701   N  VAL B 676           
SHEET    6   E 9 ILE B 737  ASP B 742  1  O  CYS B 739   N  ALA B 702           
SHEET    7   E 9 LEU B 768  THR B 772  1  O  HIS B 769   N  LEU B 738           
SHEET    8   E 9 VAL B 793  VAL B 796  1  O  VAL B 793   N  ILE B 770           
SHEET    9   E 9 LEU B 564  ASP B 567  1  N  MET B 566   O  VAL B 796           
SHEET    1   F 4 PHE B1048  VAL B1050  0                                        
SHEET    2   F 4 LEU B1058  VAL B1065 -1  O  ILE B1060   N  PHE B1048           
SHEET    3   F 4 GLN B1073  LEU B1080 -1  O  PHE B1077   N  LEU B1063           
SHEET    4   F 4 GLN B1083  LYS B1090 -1  O  ARG B1085   N  PHE B1078           
SHEET    1   G 9 LEU C 564  ASP C 567  0                                        
SHEET    2   G 9 SER C 603  GLY C 608  1  O  GLU C 605   N  ASP C 567           
SHEET    3   G 9 PHE C 639  LEU C 643  1  O  GLN C 640   N  MET C 604           
SHEET    4   G 9 VAL C 673  PHE C 677  1  O  ARG C 675   N  LEU C 643           
SHEET    5   G 9 VAL C 699  SER C 705  1  O  ALA C 703   N  VAL C 676           
SHEET    6   G 9 ILE C 737  KCX C 741  1  O  KCX C 741   N  ILE C 704           
SHEET    7   G 9 LEU C 768  HIS C 771  1  O  HIS C 769   N  LEU C 738           
SHEET    8   G 9 VAL C 793  VAL C 796  1  O  VAL C 793   N  LEU C 768           
SHEET    9   G 9 LEU C 564  ASP C 567  1  N  MET C 566   O  VAL C 796           
SHEET    1   H 4 GLU C1047  VAL C1050  0                                        
SHEET    2   H 4 LEU C1058  VAL C1065 -1  O  ILE C1060   N  PHE C1048           
SHEET    3   H 4 GLN C1073  LEU C1080 -1  O  PHE C1077   N  LEU C1063           
SHEET    4   H 4 GLN C1083  LYS C1090 -1  O  ARG C1085   N  PHE C1078           
SHEET    1   I 9 LEU D 564  ASP D 567  0                                        
SHEET    2   I 9 SER D 603  GLY D 608  1  O  GLU D 605   N  ASP D 567           
SHEET    3   I 9 PHE D 639  LEU D 643  1  O  GLN D 640   N  MET D 604           
SHEET    4   I 9 VAL D 673  PHE D 677  1  O  ARG D 675   N  MET D 641           
SHEET    5   I 9 VAL D 699  SER D 705  1  O  ALA D 703   N  VAL D 676           
SHEET    6   I 9 ILE D 737  ASP D 742  1  O  KCX D 741   N  ILE D 704           
SHEET    7   I 9 LEU D 768  THR D 772  1  O  HIS D 769   N  LEU D 738           
SHEET    8   I 9 VAL D 793  VAL D 796  1  O  VAL D 793   N  ILE D 770           
SHEET    9   I 9 LEU D 564  ASP D 567  1  N  MET D 566   O  VAL D 796           
SHEET    1   J 4 GLU D1047  GLU D1051  0                                        
SHEET    2   J 4 THR D1057  VAL D1065 -1  O  ILE D1060   N  PHE D1048           
SHEET    3   J 4 VAL D1076  LEU D1080 -1  O  PHE D1077   N  ALA D1064           
SHEET    4   J 4 GLN D1083  ILE D1087 -1  O  ARG D1085   N  PHE D1078           
SHEET    1   K 2 GLN D1111  ILE D1112  0                                        
SHEET    2   K 2 LEU D1175  GLU D1176 -1  N  LEU D1175   O  ILE D1112           
SHEET    1   L 3 LYS D1119  VAL D1120  0                                        
SHEET    2   L 3 VAL D1139  SER D1141 -1  O  SER D1141   N  LYS D1119           
SHEET    3   L 3 THR D1147  VAL D1148 -1  O  THR D1147   N  LEU D1140           
SHEET    1   M 2 LYS D1130  VAL D1131  0                                        
SHEET    2   M 2 GLY D1155  THR D1156 -1  O  GLY D1155   N  VAL D1131           
LINK         OD1 ASP A 572                MN    MN A2001     1555   1555  2.10  
LINK         OQ1 KCX A 741                MN    MN A2001     1555   1555  1.96  
LINK         OQ2 KCX A 741                MN    MN A2001     1555   1555  2.44  
LINK         OD1 ASP B 572                MN    MN B2001     1555   1555  2.29  
LINK         OQ1 KCX B 741                MN    MN B2001     1555   1555  2.30  
LINK         OQ2 KCX B 741                MN    MN B2001     1555   1555  2.31  
LINK         OD1 ASP C 572                MN    MN C2001     1555   1555  2.11  
LINK         OQ1 KCX C 741                MN    MN C2001     1555   1555  2.76  
LINK         OQ2 KCX C 741                MN    MN C2001     1555   1555  2.10  
LINK         OD1 ASP D 572                MN    MN D2001     1555   1555  2.04  
LINK         OQ1 KCX D 741                MN    MN D2001     1555   1555  2.60  
LINK         OQ2 KCX D 741                MN    MN D2001     1555   1555  2.13  
LINK         NZ  LYS A1144                 C11 BTI A2100     1555   1555  1.33  
CISPEP   1 THR A  908    PRO A  909          0       -14.79                     
CISPEP   2 THR B  908    PRO B  909          0        -8.52                     
CISPEP   3 THR C  908    PRO C  909          0       -19.44                     
CISPEP   4 THR D  908    PRO D  909          0        -8.15                     
SITE     1 AC1  3 ASP A 572  HIS A 771  HIS A 773                               
SITE     1 AC2  3 ASP B 572  HIS B 771  HIS B 773                               
SITE     1 AC3  3 ASP C 572  HIS C 771  HIS C 773                               
SITE     1 AC4  3 ASP D 572  HIS D 771  HIS D 773                               
SITE     1 AC5  6 ARG A 571  GLN A 575  GLY A 609  LEU A 642                    
SITE     2 AC5  6 ARG A 644  THR A 908                                          
SITE     1 AC6  9 LYS A1144  GLN B 575  PHE B 618  ARG B 644                    
SITE     2 AC6  9 TYR B 651  GLN B 870  THR B 908  SER B 911                    
SITE     3 AC6  9 LYS B 912                                                     
SITE     1 AC7  7 ARG B 571  ASP B 572  GLN B 575  GLY B 609                    
SITE     2 AC7  7 LEU B 642  ARG B 644  THR B 908                               
SITE     1 AC8  5 ARG C 571  GLN C 575  LEU C 642  ARG C 644                    
SITE     2 AC8  5 THR C 908                                                     
SITE     1 AC9  6 ARG D 571  GLN D 575  GLY D 609  LEU D 642                    
SITE     2 AC9  6 ARG D 644  THR D 908                                          
CRYST1   81.274  173.321  118.194  90.00  95.87  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012304  0.000000  0.001265        0.00000                         
SCALE2      0.000000  0.005770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008505        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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