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Database: PDB
Entry: 4FFC
LinkDB: 4FFC
Original site: 4FFC 
HEADER    TRANSFERASE                             31-MAY-12   4FFC              
TITLE     CRYSTAL STRUCTURE OF A 4-AMINOBUTYRATE AMINOTRANSFERASE (GABT) FROM   
TITLE    2 MYCOBACTERIUM ABSCESSUS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-AMINOBUTYRATE AMINOTRANSFERASE (GABT);                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM ABSCESSUS;                        
SOURCE   3 ORGANISM_TAXID: 561007;                                              
SOURCE   4 STRAIN: ATCC 19977 / DSM 44196;                                      
SOURCE   5 GENE: MAB_4207;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAVA0421                                  
KEYWDS    STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND         
KEYWDS   2 INFECTIOUS DISEASES, SEATTLE STRUCTURAL GENOMICS CENTER FOR          
KEYWDS   3 INFECTIOUS DISEASE, SSGCID, MYCOBACTERIUM, GABT, PYRIDOXAL PHOSPHATE 
KEYWDS   4 BINDING, AMINOTRANSFERASE, TRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   13-JUN-12 4FFC    0                                                
JRNL        AUTH   T.E.EDWARDS,D.FOX III,J.ABENDROTH,                           
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 3 (SSGCID)                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A 4-AMINOBUTYRATE AMINOTRANSFERASE      
JRNL        TITL 2 (GABT) FROM MYCOBACTERIUM ABSCESSUS                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 145353                         
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) : 0.140                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.167                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7697                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9563                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 502                          
REMARK   3   BIN FREE R VALUE                    : 0.2110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12901                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 1912                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.44000                                              
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : -0.26000                                             
REMARK   3    B12 (A**2) : -0.39000                                             
REMARK   3    B13 (A**2) : 0.20000                                              
REMARK   3    B23 (A**2) : -0.09000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.108         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.447         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13385 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8820 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18299 ; 1.392 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 21545 ; 0.931 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1834 ; 5.715 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   507 ;35.145 ;23.097       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1989 ;11.066 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   113 ;15.096 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2161 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15319 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2678 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   446                          
REMARK   3    RESIDUE RANGE :   A   501        A   502                          
REMARK   3    RESIDUE RANGE :   A   601        A  1088                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.6993 -13.7358  12.3364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0111 T22:   0.0283                                     
REMARK   3      T33:   0.0305 T12:   0.0027                                     
REMARK   3      T13:   0.0000 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1102 L22:   0.0589                                     
REMARK   3      L33:   0.1505 L12:   0.0094                                     
REMARK   3      L13:  -0.0233 L23:  -0.0257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0033 S12:   0.0304 S13:  -0.0293                       
REMARK   3      S21:   0.0141 S22:   0.0027 S23:  -0.0116                       
REMARK   3      S31:   0.0247 S32:   0.0065 S33:   0.0006                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B   446                          
REMARK   3    RESIDUE RANGE :   B   501        B   997                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5469  11.2156  12.3815              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0085 T22:   0.0330                                     
REMARK   3      T33:   0.0201 T12:   0.0038                                     
REMARK   3      T13:  -0.0010 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1149 L22:   0.0583                                     
REMARK   3      L33:   0.1520 L12:  -0.0005                                     
REMARK   3      L13:   0.0590 L23:   0.0359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0122 S12:   0.0157 S13:   0.0154                       
REMARK   3      S21:   0.0059 S22:   0.0016 S23:   0.0005                       
REMARK   3      S31:  -0.0281 S32:  -0.0157 S33:   0.0106                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   447                          
REMARK   3    RESIDUE RANGE :   C   501        C   502                          
REMARK   3    RESIDUE RANGE :   C   601        C  1041                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.2202 -13.4924  59.3873              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0589 T22:   0.0076                                     
REMARK   3      T33:   0.0162 T12:   0.0030                                     
REMARK   3      T13:  -0.0182 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0247 L22:   0.1507                                     
REMARK   3      L33:   0.1495 L12:   0.0122                                     
REMARK   3      L13:  -0.0242 L23:  -0.0118                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0134 S12:   0.0102 S13:   0.0021                       
REMARK   3      S21:   0.0571 S22:  -0.0075 S23:  -0.0469                       
REMARK   3      S31:   0.0472 S32:   0.0003 S33:  -0.0058                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     4        D   446                          
REMARK   3    RESIDUE RANGE :   D   501        D   986                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1831  10.8621  59.4353              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0231 T22:   0.0293                                     
REMARK   3      T33:   0.0115 T12:  -0.0084                                     
REMARK   3      T13:   0.0107 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0343 L22:   0.1465                                     
REMARK   3      L33:   0.2158 L12:  -0.0162                                     
REMARK   3      L13:   0.0505 L23:   0.0827                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:   0.0035 S13:   0.0113                       
REMARK   3      S21:   0.0325 S22:  -0.0309 S23:   0.0103                       
REMARK   3      S31:   0.0065 S32:  -0.0453 S33:   0.0309                       
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: U VALUES      : WITH TLS ADDED            
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   4                                                                      
REMARK   4 4FFC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072830.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 152966                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.1400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.12300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.030                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3OKS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MYABA.01026.B.A1 PS00899 AT 20 MG/ML     
REMARK 280  AGAINST PACT F6 0.2 M SODIUM FORMATE, 0.1 M BIS TRIS PROPANE PH     
REMARK 280  6.5, 20% PEG 3350, CRYSTAL TRACKING ID 233334F6, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 22740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 48980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL                        
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 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     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     SER A   447                                                      
REMARK 465     HIS A   448                                                      
REMARK 465     GLN A   449                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     SER B   447                                                      
REMARK 465     HIS B   448                                                      
REMARK 465     GLN B   449                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     HIS C   448                                                      
REMARK 465     GLN C   449                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     SER D   447                                                      
REMARK 465     HIS D   448                                                      
REMARK 465     GLN D   449                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A   3    CG   OD1  OD2                                       
REMARK 470     LYS A  11    CG   CD   CE   NZ                                   
REMARK 470     LYS A 395    CG   CD   CE   NZ                                   
REMARK 470     GLU A 400    CG   CD   OE1  OE2                                  
REMARK 470     ILE B   4    CG1  CG2  CD1                                       
REMARK 470     LYS B  11    CG   CD   CE   NZ                                   
REMARK 470     LYS B 395    CG   CD   CE   NZ                                   
REMARK 470     GLU B 400    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  11    CG   CD   CE   NZ                                   
REMARK 470     LYS C 395    CG   CD   CE   NZ                                   
REMARK 470     GLU C 400    CG   CD   OE1  OE2                                  
REMARK 470     ILE D   4    CG1  CG2  CD1                                       
REMARK 470     LYS D 395    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    GLY D    39     O    HOH D   955              2.16            
REMARK 500   O    HOH A   699     O    HOH A   996              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    HIS A 278   CG    HIS A 278   CD2     0.055                       
REMARK 500    HIS B 278   CG    HIS B 278   CD2     0.058                       
REMARK 500    HIS D 278   CG    HIS D 278   CD2     0.067                       
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    MET A 172   CG  -  SD  -  CE  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  38      -70.26    -74.34                                   
REMARK 500    ILE A  69       60.85     64.16                                   
REMARK 500    SER A  77       44.99   -150.25                                   
REMARK 500    PHE A  92      140.44   -170.37                                   
REMARK 500    HIS A  94      134.44   -175.45                                   
REMARK 500    CYS A  96      106.07     66.79                                   
REMARK 500    VAL A  99      -69.44   -100.03                                   
REMARK 500    PHE A 127     -159.45   -135.67                                   
REMARK 500    ALA A 190     -134.98   -109.90                                   
REMARK 500    ILE A 217      -53.36   -124.69                                   
REMARK 500    PHE A 267       71.97     72.59                                   
REMARK 500    ALA A 268      -27.71     79.58                                   
REMARK 500    ALA A 289     -130.06   -162.52                                   
REMARK 500    LLP A 290      -99.84     37.05                                   
REMARK 500    ASP A 341       63.38     38.35                                   
REMARK 500    ILE B  69       61.36     67.29                                   
REMARK 500    SER B  77       46.90   -151.70                                   
REMARK 500    PHE B  92      136.84   -171.06                                   
REMARK 500    HIS B  94      134.79   -174.46                                   
REMARK 500    CYS B  96      105.70     70.22                                   
REMARK 500    VAL B  99      -68.72   -100.05                                   
REMARK 500    PHE B 127     -159.74   -134.70                                   
REMARK 500    ALA B 190     -135.53   -110.51                                   
REMARK 500    ILE B 217      -52.94   -124.10                                   
REMARK 500    PHE B 267       70.94     75.21                                   
REMARK 500    ALA B 268      -25.20     79.57                                   
REMARK 500    ALA B 289     -130.17   -164.19                                   
REMARK 500    LLP B 290      -95.49     35.27                                   
REMARK 500    CYS B 411     -169.24   -166.81                                   
REMARK 500    THR C  72       53.32    -91.69                                   
REMARK 500    SER C  77       46.86   -150.24                                   
REMARK 500    HIS C  94      135.50   -175.70                                   
REMARK 500    CYS C  96      106.10     69.74                                   
REMARK 500    VAL C  99      -68.77   -100.66                                   
REMARK 500    PHE C 127     -159.68   -134.78                                   
REMARK 500    ALA C 190     -136.90   -107.36                                   
REMARK 500    ILE C 217      -54.00   -121.24                                   
REMARK 500    PHE C 267       73.78     73.35                                   
REMARK 500    ALA C 268      -24.79     77.70                                   
REMARK 500    ALA C 289     -129.46   -161.45                                   
REMARK 500    LLP C 290      -94.44     35.62                                   
REMARK 500    CYS C 411     -168.41   -167.44                                   
REMARK 500    ILE D  69       61.35     68.43                                   
REMARK 500    SER D  77       48.51   -152.14                                   
REMARK 500    HIS D  94      134.56   -175.04                                   
REMARK 500    CYS D  96      107.41     67.41                                   
REMARK 500    VAL D  99      -68.48   -101.37                                   
REMARK 500    PHE D 127     -158.42   -132.15                                   
REMARK 500    ALA D 190     -135.74   -111.45                                   
REMARK 500    ILE D 217      -53.18   -124.19                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MYABA.01026.B   RELATED DB: TARGETTRACK                  
DBREF  4FFC A    1   449  UNP    B1MIQ9   B1MIQ9_MYCA9     1    449             
DBREF  4FFC B    1   449  UNP    B1MIQ9   B1MIQ9_MYCA9     1    449             
DBREF  4FFC C    1   449  UNP    B1MIQ9   B1MIQ9_MYCA9     1    449             
DBREF  4FFC D    1   449  UNP    B1MIQ9   B1MIQ9_MYCA9     1    449             
SEQADV 4FFC GLY A   -3  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC PRO A   -2  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLY A   -1  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC SER A    0  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLN A  104  UNP  B1MIQ9    GLY   104 CONFLICT                       
SEQADV 4FFC GLY B   -3  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC PRO B   -2  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLY B   -1  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC SER B    0  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLN B  104  UNP  B1MIQ9    GLY   104 CONFLICT                       
SEQADV 4FFC GLY C   -3  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC PRO C   -2  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLY C   -1  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC SER C    0  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLN C  104  UNP  B1MIQ9    GLY   104 CONFLICT                       
SEQADV 4FFC GLY D   -3  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC PRO D   -2  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLY D   -1  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC SER D    0  UNP  B1MIQ9              EXPRESSION TAG                 
SEQADV 4FFC GLN D  104  UNP  B1MIQ9    GLY   104 CONFLICT                       
SEQRES   1 A  453  GLY PRO GLY SER MET THR ASP ILE THR TYR ARG LEU ALA          
SEQRES   2 A  453  GLN LYS ARG THR ILE VAL THR PRO LEU PRO GLY PRO ARG          
SEQRES   3 A  453  SER GLY ALA LEU ALA GLU ARG ARG ARG ALA ALA VAL SER          
SEQRES   4 A  453  ALA GLY VAL GLY SER THR ALA PRO VAL TYR ALA VAL ASP          
SEQRES   5 A  453  ALA ASP GLY GLY VAL ILE VAL ASP ALA ASP GLY ASN SER          
SEQRES   6 A  453  PHE ILE ASP LEU GLY ALA GLY ILE ALA VAL THR THR VAL          
SEQRES   7 A  453  GLY ALA SER HIS PRO ALA VAL ALA ALA ALA ILE ALA ASP          
SEQRES   8 A  453  GLN ALA THR HIS PHE THR HIS THR CYS PHE MET VAL THR          
SEQRES   9 A  453  PRO TYR GLU GLN TYR VAL GLN VAL ALA GLU LEU LEU ASN          
SEQRES  10 A  453  ALA LEU THR PRO GLY ASP HIS ASP LYS ARG THR ALA LEU          
SEQRES  11 A  453  PHE ASN SER GLY ALA GLU ALA VAL GLU ASN ALA ILE LYS          
SEQRES  12 A  453  VAL ALA ARG LEU ALA THR GLY ARG PRO ALA VAL VAL ALA          
SEQRES  13 A  453  PHE ASP ASN ALA TYR HIS GLY ARG THR ASN LEU THR MET          
SEQRES  14 A  453  ALA LEU THR ALA LYS SER MET PRO TYR LYS SER GLN PHE          
SEQRES  15 A  453  GLY PRO PHE ALA PRO GLU VAL TYR ARG MET PRO ALA SER          
SEQRES  16 A  453  TYR PRO LEU ARG ASP GLU PRO GLY LEU THR GLY GLU GLU          
SEQRES  17 A  453  ALA ALA ARG ARG ALA ILE SER ARG ILE GLU THR GLN ILE          
SEQRES  18 A  453  GLY ALA GLN SER LEU ALA ALA ILE ILE ILE GLU PRO ILE          
SEQRES  19 A  453  GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA PRO GLY PHE          
SEQRES  20 A  453  LEU ALA THR LEU THR ALA TRP ALA SER GLU ASN GLY VAL          
SEQRES  21 A  453  VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE ALA ARG          
SEQRES  22 A  453  THR GLY ALA TRP PHE ALA SER GLU HIS GLU GLY ILE VAL          
SEQRES  23 A  453  PRO ASP ILE VAL THR MET ALA LLP GLY ILE ALA GLY GLY          
SEQRES  24 A  453  MET PRO LEU SER ALA VAL THR GLY ARG ALA GLU LEU MET          
SEQRES  25 A  453  ASP ALA VAL TYR ALA GLY GLY LEU GLY GLY THR TYR GLY          
SEQRES  26 A  453  GLY ASN PRO VAL THR CYS ALA ALA ALA VAL ALA ALA LEU          
SEQRES  27 A  453  GLY VAL MET ARG GLU LEU ASP LEU PRO ALA ARG ALA ARG          
SEQRES  28 A  453  ALA ILE GLU ALA SER VAL THR SER ARG LEU SER ALA LEU          
SEQRES  29 A  453  ALA GLU GLU VAL ASP ILE ILE GLY GLU VAL ARG GLY ARG          
SEQRES  30 A  453  GLY ALA MET LEU ALA ILE GLU ILE VAL LYS PRO GLY THR          
SEQRES  31 A  453  LEU GLU PRO ASP ALA ALA LEU THR LYS SER ILE ALA ALA          
SEQRES  32 A  453  GLU ALA LEU SER GLN GLY VAL LEU ILE LEU THR CYS GLY          
SEQRES  33 A  453  THR PHE GLY ASN VAL ILE ARG LEU LEU PRO PRO LEU VAL          
SEQRES  34 A  453  ILE GLY ASP ASP LEU LEU ASP GLU GLY ILE THR ALA LEU          
SEQRES  35 A  453  SER ASP ILE ILE ARG ALA LYS ALA SER HIS GLN                  
SEQRES   1 B  453  GLY PRO GLY SER MET THR ASP ILE THR TYR ARG LEU ALA          
SEQRES   2 B  453  GLN LYS ARG THR ILE VAL THR PRO LEU PRO GLY PRO ARG          
SEQRES   3 B  453  SER GLY ALA LEU ALA GLU ARG ARG ARG ALA ALA VAL SER          
SEQRES   4 B  453  ALA GLY VAL GLY SER THR ALA PRO VAL TYR ALA VAL ASP          
SEQRES   5 B  453  ALA ASP GLY GLY VAL ILE VAL ASP ALA ASP GLY ASN SER          
SEQRES   6 B  453  PHE ILE ASP LEU GLY ALA GLY ILE ALA VAL THR THR VAL          
SEQRES   7 B  453  GLY ALA SER HIS PRO ALA VAL ALA ALA ALA ILE ALA ASP          
SEQRES   8 B  453  GLN ALA THR HIS PHE THR HIS THR CYS PHE MET VAL THR          
SEQRES   9 B  453  PRO TYR GLU GLN TYR VAL GLN VAL ALA GLU LEU LEU ASN          
SEQRES  10 B  453  ALA LEU THR PRO GLY ASP HIS ASP LYS ARG THR ALA LEU          
SEQRES  11 B  453  PHE ASN SER GLY ALA GLU ALA VAL GLU ASN ALA ILE LYS          
SEQRES  12 B  453  VAL ALA ARG LEU ALA THR GLY ARG PRO ALA VAL VAL ALA          
SEQRES  13 B  453  PHE ASP ASN ALA TYR HIS GLY ARG THR ASN LEU THR MET          
SEQRES  14 B  453  ALA LEU THR ALA LYS SER MET PRO TYR LYS SER GLN PHE          
SEQRES  15 B  453  GLY PRO PHE ALA PRO GLU VAL TYR ARG MET PRO ALA SER          
SEQRES  16 B  453  TYR PRO LEU ARG ASP GLU PRO GLY LEU THR GLY GLU GLU          
SEQRES  17 B  453  ALA ALA ARG ARG ALA ILE SER ARG ILE GLU THR GLN ILE          
SEQRES  18 B  453  GLY ALA GLN SER LEU ALA ALA ILE ILE ILE GLU PRO ILE          
SEQRES  19 B  453  GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA PRO GLY PHE          
SEQRES  20 B  453  LEU ALA THR LEU THR ALA TRP ALA SER GLU ASN GLY VAL          
SEQRES  21 B  453  VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE ALA ARG          
SEQRES  22 B  453  THR GLY ALA TRP PHE ALA SER GLU HIS GLU GLY ILE VAL          
SEQRES  23 B  453  PRO ASP ILE VAL THR MET ALA LLP GLY ILE ALA GLY GLY          
SEQRES  24 B  453  MET PRO LEU SER ALA VAL THR GLY ARG ALA GLU LEU MET          
SEQRES  25 B  453  ASP ALA VAL TYR ALA GLY GLY LEU GLY GLY THR TYR GLY          
SEQRES  26 B  453  GLY ASN PRO VAL THR CYS ALA ALA ALA VAL ALA ALA LEU          
SEQRES  27 B  453  GLY VAL MET ARG GLU LEU ASP LEU PRO ALA ARG ALA ARG          
SEQRES  28 B  453  ALA ILE GLU ALA SER VAL THR SER ARG LEU SER ALA LEU          
SEQRES  29 B  453  ALA GLU GLU VAL ASP ILE ILE GLY GLU VAL ARG GLY ARG          
SEQRES  30 B  453  GLY ALA MET LEU ALA ILE GLU ILE VAL LYS PRO GLY THR          
SEQRES  31 B  453  LEU GLU PRO ASP ALA ALA LEU THR LYS SER ILE ALA ALA          
SEQRES  32 B  453  GLU ALA LEU SER GLN GLY VAL LEU ILE LEU THR CYS GLY          
SEQRES  33 B  453  THR PHE GLY ASN VAL ILE ARG LEU LEU PRO PRO LEU VAL          
SEQRES  34 B  453  ILE GLY ASP ASP LEU LEU ASP GLU GLY ILE THR ALA LEU          
SEQRES  35 B  453  SER ASP ILE ILE ARG ALA LYS ALA SER HIS GLN                  
SEQRES   1 C  453  GLY PRO GLY SER MET THR ASP ILE THR TYR ARG LEU ALA          
SEQRES   2 C  453  GLN LYS ARG THR ILE VAL THR PRO LEU PRO GLY PRO ARG          
SEQRES   3 C  453  SER GLY ALA LEU ALA GLU ARG ARG ARG ALA ALA VAL SER          
SEQRES   4 C  453  ALA GLY VAL GLY SER THR ALA PRO VAL TYR ALA VAL ASP          
SEQRES   5 C  453  ALA ASP GLY GLY VAL ILE VAL ASP ALA ASP GLY ASN SER          
SEQRES   6 C  453  PHE ILE ASP LEU GLY ALA GLY ILE ALA VAL THR THR VAL          
SEQRES   7 C  453  GLY ALA SER HIS PRO ALA VAL ALA ALA ALA ILE ALA ASP          
SEQRES   8 C  453  GLN ALA THR HIS PHE THR HIS THR CYS PHE MET VAL THR          
SEQRES   9 C  453  PRO TYR GLU GLN TYR VAL GLN VAL ALA GLU LEU LEU ASN          
SEQRES  10 C  453  ALA LEU THR PRO GLY ASP HIS ASP LYS ARG THR ALA LEU          
SEQRES  11 C  453  PHE ASN SER GLY ALA GLU ALA VAL GLU ASN ALA ILE LYS          
SEQRES  12 C  453  VAL ALA ARG LEU ALA THR GLY ARG PRO ALA VAL VAL ALA          
SEQRES  13 C  453  PHE ASP ASN ALA TYR HIS GLY ARG THR ASN LEU THR MET          
SEQRES  14 C  453  ALA LEU THR ALA LYS SER MET PRO TYR LYS SER GLN PHE          
SEQRES  15 C  453  GLY PRO PHE ALA PRO GLU VAL TYR ARG MET PRO ALA SER          
SEQRES  16 C  453  TYR PRO LEU ARG ASP GLU PRO GLY LEU THR GLY GLU GLU          
SEQRES  17 C  453  ALA ALA ARG ARG ALA ILE SER ARG ILE GLU THR GLN ILE          
SEQRES  18 C  453  GLY ALA GLN SER LEU ALA ALA ILE ILE ILE GLU PRO ILE          
SEQRES  19 C  453  GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA PRO GLY PHE          
SEQRES  20 C  453  LEU ALA THR LEU THR ALA TRP ALA SER GLU ASN GLY VAL          
SEQRES  21 C  453  VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE ALA ARG          
SEQRES  22 C  453  THR GLY ALA TRP PHE ALA SER GLU HIS GLU GLY ILE VAL          
SEQRES  23 C  453  PRO ASP ILE VAL THR MET ALA LLP GLY ILE ALA GLY GLY          
SEQRES  24 C  453  MET PRO LEU SER ALA VAL THR GLY ARG ALA GLU LEU MET          
SEQRES  25 C  453  ASP ALA VAL TYR ALA GLY GLY LEU GLY GLY THR TYR GLY          
SEQRES  26 C  453  GLY ASN PRO VAL THR CYS ALA ALA ALA VAL ALA ALA LEU          
SEQRES  27 C  453  GLY VAL MET ARG GLU LEU ASP LEU PRO ALA ARG ALA ARG          
SEQRES  28 C  453  ALA ILE GLU ALA SER VAL THR SER ARG LEU SER ALA LEU          
SEQRES  29 C  453  ALA GLU GLU VAL ASP ILE ILE GLY GLU VAL ARG GLY ARG          
SEQRES  30 C  453  GLY ALA MET LEU ALA ILE GLU ILE VAL LYS PRO GLY THR          
SEQRES  31 C  453  LEU GLU PRO ASP ALA ALA LEU THR LYS SER ILE ALA ALA          
SEQRES  32 C  453  GLU ALA LEU SER GLN GLY VAL LEU ILE LEU THR CYS GLY          
SEQRES  33 C  453  THR PHE GLY ASN VAL ILE ARG LEU LEU PRO PRO LEU VAL          
SEQRES  34 C  453  ILE GLY ASP ASP LEU LEU ASP GLU GLY ILE THR ALA LEU          
SEQRES  35 C  453  SER ASP ILE ILE ARG ALA LYS ALA SER HIS GLN                  
SEQRES   1 D  453  GLY PRO GLY SER MET THR ASP ILE THR TYR ARG LEU ALA          
SEQRES   2 D  453  GLN LYS ARG THR ILE VAL THR PRO LEU PRO GLY PRO ARG          
SEQRES   3 D  453  SER GLY ALA LEU ALA GLU ARG ARG ARG ALA ALA VAL SER          
SEQRES   4 D  453  ALA GLY VAL GLY SER THR ALA PRO VAL TYR ALA VAL ASP          
SEQRES   5 D  453  ALA ASP GLY GLY VAL ILE VAL ASP ALA ASP GLY ASN SER          
SEQRES   6 D  453  PHE ILE ASP LEU GLY ALA GLY ILE ALA VAL THR THR VAL          
SEQRES   7 D  453  GLY ALA SER HIS PRO ALA VAL ALA ALA ALA ILE ALA ASP          
SEQRES   8 D  453  GLN ALA THR HIS PHE THR HIS THR CYS PHE MET VAL THR          
SEQRES   9 D  453  PRO TYR GLU GLN TYR VAL GLN VAL ALA GLU LEU LEU ASN          
SEQRES  10 D  453  ALA LEU THR PRO GLY ASP HIS ASP LYS ARG THR ALA LEU          
SEQRES  11 D  453  PHE ASN SER GLY ALA GLU ALA VAL GLU ASN ALA ILE LYS          
SEQRES  12 D  453  VAL ALA ARG LEU ALA THR GLY ARG PRO ALA VAL VAL ALA          
SEQRES  13 D  453  PHE ASP ASN ALA TYR HIS GLY ARG THR ASN LEU THR MET          
SEQRES  14 D  453  ALA LEU THR ALA LYS SER MET PRO TYR LYS SER GLN PHE          
SEQRES  15 D  453  GLY PRO PHE ALA PRO GLU VAL TYR ARG MET PRO ALA SER          
SEQRES  16 D  453  TYR PRO LEU ARG ASP GLU PRO GLY LEU THR GLY GLU GLU          
SEQRES  17 D  453  ALA ALA ARG ARG ALA ILE SER ARG ILE GLU THR GLN ILE          
SEQRES  18 D  453  GLY ALA GLN SER LEU ALA ALA ILE ILE ILE GLU PRO ILE          
SEQRES  19 D  453  GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA PRO GLY PHE          
SEQRES  20 D  453  LEU ALA THR LEU THR ALA TRP ALA SER GLU ASN GLY VAL          
SEQRES  21 D  453  VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE ALA ARG          
SEQRES  22 D  453  THR GLY ALA TRP PHE ALA SER GLU HIS GLU GLY ILE VAL          
SEQRES  23 D  453  PRO ASP ILE VAL THR MET ALA LLP GLY ILE ALA GLY GLY          
SEQRES  24 D  453  MET PRO LEU SER ALA VAL THR GLY ARG ALA GLU LEU MET          
SEQRES  25 D  453  ASP ALA VAL TYR ALA GLY GLY LEU GLY GLY THR TYR GLY          
SEQRES  26 D  453  GLY ASN PRO VAL THR CYS ALA ALA ALA VAL ALA ALA LEU          
SEQRES  27 D  453  GLY VAL MET ARG GLU LEU ASP LEU PRO ALA ARG ALA ARG          
SEQRES  28 D  453  ALA ILE GLU ALA SER VAL THR SER ARG LEU SER ALA LEU          
SEQRES  29 D  453  ALA GLU GLU VAL ASP ILE ILE GLY GLU VAL ARG GLY ARG          
SEQRES  30 D  453  GLY ALA MET LEU ALA ILE GLU ILE VAL LYS PRO GLY THR          
SEQRES  31 D  453  LEU GLU PRO ASP ALA ALA LEU THR LYS SER ILE ALA ALA          
SEQRES  32 D  453  GLU ALA LEU SER GLN GLY VAL LEU ILE LEU THR CYS GLY          
SEQRES  33 D  453  THR PHE GLY ASN VAL ILE ARG LEU LEU PRO PRO LEU VAL          
SEQRES  34 D  453  ILE GLY ASP ASP LEU LEU ASP GLU GLY ILE THR ALA LEU          
SEQRES  35 D  453  SER ASP ILE ILE ARG ALA LYS ALA SER HIS GLN                  
MODRES 4FFC LLP A  290  LYS                                                     
MODRES 4FFC LLP B  290  LYS                                                     
MODRES 4FFC LLP C  290  LYS                                                     
MODRES 4FFC LLP D  290  LYS                                                     
HET    LLP  A 290      30                                                       
HET    LLP  B 290      30                                                       
HET    LLP  C 290      30                                                       
HET    LLP  D 290      30                                                       
HET    EDO  A 501       4                                                       
HET    EDO  A 502       4                                                       
HET    EDO  C 501       4                                                       
HET    EDO  C 502       4                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  LLP    4(C14 H24 N3 O7 P)                                           
FORMUL   5  EDO    4(C2 H6 O2)                                                  
FORMUL   9  HOH   *1912(H2 O)                                                   
HELIX    1   1 GLY A   20  VAL A   34  1                                  15    
HELIX    2   2 GLY A   66  VAL A   71  1                                   6    
HELIX    3   3 HIS A   78  PHE A   92  1                                  15    
HELIX    4   4 TYR A  102  THR A  116  1                                  15    
HELIX    5   5 SER A  129  GLY A  146  1                                  18    
HELIX    6   6 THR A  161  THR A  168  1                                   8    
HELIX    7   7 THR A  201  ILE A  217  1                                  17    
HELIX    8   8 GLY A  218  GLN A  220  5                                   3    
HELIX    9   9 GLY A  242  ASN A  254  1                                  13    
HELIX   10  10 PHE A  274  GLY A  280  5                                   7    
HELIX   11  11 ALA A  289  GLY A  294  5                                   6    
HELIX   12  12 ALA A  305  ASP A  309  1                                   5    
HELIX   13  13 ASN A  323  LEU A  340  1                                  18    
HELIX   14  14 ASP A  341  VAL A  364  1                                  24    
HELIX   15  15 ASP A  390  GLN A  404  1                                  15    
HELIX   16  16 GLY A  427  ALA A  446  1                                  20    
HELIX   17  17 GLY B   20  VAL B   34  1                                  15    
HELIX   18  18 GLY B   66  VAL B   71  1                                   6    
HELIX   19  19 HIS B   78  PHE B   92  1                                  15    
HELIX   20  20 TYR B  102  THR B  116  1                                  15    
HELIX   21  21 SER B  129  GLY B  146  1                                  18    
HELIX   22  22 THR B  161  THR B  168  1                                   8    
HELIX   23  23 THR B  201  ILE B  217  1                                  17    
HELIX   24  24 GLY B  218  GLN B  220  5                                   3    
HELIX   25  25 GLY B  242  GLY B  255  1                                  14    
HELIX   26  26 PHE B  274  GLY B  280  5                                   7    
HELIX   27  27 ALA B  289  GLY B  294  5                                   6    
HELIX   28  28 ALA B  305  ASP B  309  1                                   5    
HELIX   29  29 ASN B  323  LEU B  340  1                                  18    
HELIX   30  30 ASP B  341  VAL B  364  1                                  24    
HELIX   31  31 ASP B  390  GLN B  404  1                                  15    
HELIX   32  32 GLY B  427  ALA B  446  1                                  20    
HELIX   33  33 GLY C   20  VAL C   34  1                                  15    
HELIX   34  34 GLY C   66  VAL C   71  1                                   6    
HELIX   35  35 HIS C   78  PHE C   92  1                                  15    
HELIX   36  36 TYR C  102  THR C  116  1                                  15    
HELIX   37  37 SER C  129  GLY C  146  1                                  18    
HELIX   38  38 THR C  161  THR C  168  1                                   8    
HELIX   39  39 THR C  201  ILE C  217  1                                  17    
HELIX   40  40 GLY C  218  GLN C  220  5                                   3    
HELIX   41  41 GLY C  242  ASN C  254  1                                  13    
HELIX   42  42 PHE C  274  GLY C  280  5                                   7    
HELIX   43  43 ALA C  289  GLY C  294  5                                   6    
HELIX   44  44 ALA C  305  ASP C  309  1                                   5    
HELIX   45  45 ASN C  323  LEU C  340  1                                  18    
HELIX   46  46 ASP C  341  VAL C  364  1                                  24    
HELIX   47  47 ASP C  390  GLN C  404  1                                  15    
HELIX   48  48 GLY C  427  SER C  447  1                                  21    
HELIX   49  49 GLY D   20  VAL D   34  1                                  15    
HELIX   50  50 GLY D   66  VAL D   71  1                                   6    
HELIX   51  51 HIS D   78  PHE D   92  1                                  15    
HELIX   52  52 TYR D  102  THR D  116  1                                  15    
HELIX   53  53 SER D  129  GLY D  146  1                                  18    
HELIX   54  54 THR D  161  THR D  168  1                                   8    
HELIX   55  55 THR D  201  ILE D  217  1                                  17    
HELIX   56  56 GLY D  218  GLN D  220  5                                   3    
HELIX   57  57 GLY D  242  ASN D  254  1                                  13    
HELIX   58  58 PHE D  274  GLY D  280  5                                   7    
HELIX   59  59 ALA D  289  GLY D  294  5                                   6    
HELIX   60  60 ALA D  305  ASP D  309  1                                   5    
HELIX   61  61 ASN D  323  LEU D  340  1                                  18    
HELIX   62  62 ASP D  341  VAL D  364  1                                  24    
HELIX   63  63 ASP D  390  GLN D  404  1                                  15    
HELIX   64  64 GLY D  427  ALA D  446  1                                  20    
SHEET    1   A 4 ALA A  46  ASP A  50  0                                        
SHEET    2   A 4 VAL A  53  ASP A  56 -1  O  VAL A  55   N  ASP A  48           
SHEET    3   A 4 SER A  61  ASP A  64 -1  O  PHE A  62   N  ILE A  54           
SHEET    4   A 4 VAL A 406  LEU A 407  1  O  LEU A 407   N  ILE A  63           
SHEET    1   B 7 LYS A 122  PHE A 127  0                                        
SHEET    2   B 7 SER A 299  ARG A 304 -1  O  VAL A 301   N  ALA A 125           
SHEET    3   B 7 ILE A 285  MET A 288 -1  N  VAL A 286   O  THR A 302           
SHEET    4   B 7 VAL A 257  ASP A 261  1  N  ALA A 260   O  ILE A 285           
SHEET    5   B 7 LEU A 222  ILE A 227  1  N  ILE A 225   O  ILE A 259           
SHEET    6   B 7 ALA A 149  PHE A 153  1  N  VAL A 151   O  ALA A 224           
SHEET    7   B 7 VAL A 185  MET A 188  1  O  TYR A 186   N  VAL A 150           
SHEET    1   C 4 ILE A 367  ARG A 373  0                                        
SHEET    2   C 4 MET A 376  ILE A 381 -1  O  GLU A 380   N  GLY A 368           
SHEET    3   C 4 VAL A 417  LEU A 420 -1  O  LEU A 420   N  LEU A 377           
SHEET    4   C 4 THR A 410  CYS A 411 -1  N  CYS A 411   O  VAL A 417           
SHEET    1   D 4 ALA B  46  ASP B  50  0                                        
SHEET    2   D 4 VAL B  53  ASP B  56 -1  O  VAL B  55   N  ASP B  48           
SHEET    3   D 4 SER B  61  ASP B  64 -1  O  PHE B  62   N  ILE B  54           
SHEET    4   D 4 VAL B 406  LEU B 407  1  O  LEU B 407   N  ILE B  63           
SHEET    1   E 7 LYS B 122  PHE B 127  0                                        
SHEET    2   E 7 SER B 299  ARG B 304 -1  O  VAL B 301   N  ALA B 125           
SHEET    3   E 7 ILE B 285  MET B 288 -1  N  VAL B 286   O  THR B 302           
SHEET    4   E 7 VAL B 257  ASP B 261  1  N  ALA B 260   O  ILE B 285           
SHEET    5   E 7 LEU B 222  ILE B 227  1  N  ILE B 225   O  ILE B 259           
SHEET    6   E 7 ALA B 149  PHE B 153  1  N  VAL B 151   O  ILE B 226           
SHEET    7   E 7 VAL B 185  MET B 188  1  O  TYR B 186   N  VAL B 150           
SHEET    1   F 4 ILE B 367  ARG B 373  0                                        
SHEET    2   F 4 MET B 376  ILE B 381 -1  O  GLU B 380   N  GLY B 368           
SHEET    3   F 4 VAL B 417  LEU B 420 -1  O  LEU B 420   N  LEU B 377           
SHEET    4   F 4 THR B 410  CYS B 411 -1  N  CYS B 411   O  VAL B 417           
SHEET    1   G 4 ALA C  46  ASP C  50  0                                        
SHEET    2   G 4 VAL C  53  ASP C  56 -1  O  VAL C  55   N  ASP C  48           
SHEET    3   G 4 SER C  61  ASP C  64 -1  O  PHE C  62   N  ILE C  54           
SHEET    4   G 4 VAL C 406  LEU C 407  1  O  LEU C 407   N  ILE C  63           
SHEET    1   H 7 LYS C 122  PHE C 127  0                                        
SHEET    2   H 7 SER C 299  ARG C 304 -1  O  VAL C 301   N  ALA C 125           
SHEET    3   H 7 ILE C 285  MET C 288 -1  N  VAL C 286   O  THR C 302           
SHEET    4   H 7 VAL C 257  ASP C 261  1  N  ALA C 260   O  ILE C 285           
SHEET    5   H 7 LEU C 222  ILE C 227  1  N  ILE C 225   O  ILE C 259           
SHEET    6   H 7 ALA C 149  PHE C 153  1  N  VAL C 151   O  ILE C 226           
SHEET    7   H 7 VAL C 185  MET C 188  1  O  TYR C 186   N  VAL C 150           
SHEET    1   I 4 ILE C 367  ARG C 373  0                                        
SHEET    2   I 4 MET C 376  ILE C 381 -1  O  GLU C 380   N  GLY C 368           
SHEET    3   I 4 VAL C 417  LEU C 420 -1  O  LEU C 420   N  LEU C 377           
SHEET    4   I 4 LEU C 409  CYS C 411 -1  N  LEU C 409   O  ARG C 419           
SHEET    1   J 4 ALA D  46  ASP D  50  0                                        
SHEET    2   J 4 VAL D  53  ASP D  56 -1  O  VAL D  55   N  ASP D  48           
SHEET    3   J 4 SER D  61  ASP D  64 -1  O  PHE D  62   N  ILE D  54           
SHEET    4   J 4 VAL D 406  LEU D 407  1  O  LEU D 407   N  ILE D  63           
SHEET    1   K 7 LYS D 122  PHE D 127  0                                        
SHEET    2   K 7 SER D 299  ARG D 304 -1  O  VAL D 301   N  ALA D 125           
SHEET    3   K 7 ILE D 285  MET D 288 -1  N  VAL D 286   O  THR D 302           
SHEET    4   K 7 VAL D 257  ASP D 261  1  N  ALA D 260   O  ILE D 285           
SHEET    5   K 7 LEU D 222  ILE D 227  1  N  ILE D 225   O  ILE D 259           
SHEET    6   K 7 ALA D 149  PHE D 153  1  N  VAL D 151   O  ILE D 226           
SHEET    7   K 7 VAL D 185  MET D 188  1  O  TYR D 186   N  VAL D 150           
SHEET    1   L 4 ILE D 367  ARG D 373  0                                        
SHEET    2   L 4 MET D 376  ILE D 381 -1  O  GLU D 380   N  GLY D 368           
SHEET    3   L 4 VAL D 417  LEU D 420 -1  O  LEU D 420   N  LEU D 377           
SHEET    4   L 4 THR D 410  CYS D 411 -1  N  CYS D 411   O  VAL D 417           
LINK         C   ALA A 289                 N   LLP A 290     1555   1555  1.34  
LINK         C   LLP A 290                 N   GLY A 291     1555   1555  1.33  
LINK         C   ALA B 289                 N   LLP B 290     1555   1555  1.34  
LINK         C   LLP B 290                 N   GLY B 291     1555   1555  1.34  
LINK         C   ALA C 289                 N   LLP C 290     1555   1555  1.33  
LINK         C   LLP C 290                 N   GLY C 291     1555   1555  1.34  
LINK         C   ALA D 289                 N   LLP D 290     1555   1555  1.34  
LINK         C   LLP D 290                 N   GLY D 291     1555   1555  1.34  
CISPEP   1 LEU A   18    PRO A   19          0        -3.42                     
CISPEP   2 MET A  172    PRO A  173          0         3.26                     
CISPEP   3 GLY A  179    PRO A  180          0         5.38                     
CISPEP   4 LEU B   18    PRO B   19          0        -4.74                     
CISPEP   5 MET B  172    PRO B  173          0         2.95                     
CISPEP   6 GLY B  179    PRO B  180          0         4.53                     
CISPEP   7 LEU C   18    PRO C   19          0        -6.16                     
CISPEP   8 MET C  172    PRO C  173          0         4.20                     
CISPEP   9 GLY C  179    PRO C  180          0         5.19                     
CISPEP  10 LEU D   18    PRO D   19          0        -4.14                     
CISPEP  11 MET D  172    PRO D  173          0         1.57                     
CISPEP  12 GLY D  179    PRO D  180          0         3.12                     
SITE     1 AC1  7 ILE A   4  THR A   5  TYR A   6  ARG A   7                    
SITE     2 AC1  7 ASP A  50  GLY A  51  HOH A 603                               
SITE     1 AC2  7 LYS A 170  TYR A 174  GLU A 233  GLY A 234                    
SITE     2 AC2  7 GLY A 412  HOH A 664  HOH A 733                               
SITE     1 AC3  6 GLY C 255  VAL C 256  HOH C 680  HOH C 827                    
SITE     2 AC3  6 HOH C 885  HOH C1015                                          
SITE     1 AC4  7 ILE C   4  THR C   5  TYR C   6  ARG C   7                    
SITE     2 AC4  7 ASP C  50  GLY C  51  HOH C 622                               
CRYST1   67.400   67.530  102.460  78.06  81.26  77.44 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014837 -0.003307 -0.001713        0.00000                         
SCALE2      0.000000  0.015172 -0.002779        0.00000                         
SCALE3      0.000000  0.000000  0.010039        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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