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Database: PDB
Entry: 3OKS
LinkDB: 3OKS
Original site: 3OKS 
HEADER    TRANSFERASE                             25-AUG-10   3OKS              
TITLE     CRYSTAL STRUCTURE OF 4-AMINOBUTYRATE TRANSAMINASE FROM MYCOBACTERIUM  
TITLE    2 SMEGMATIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-AMINOBUTYRATE TRANSAMINASE;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.6.1.19;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;                        
SOURCE   3 ORGANISM_TAXID: 246196;                                              
SOURCE   4 STRAIN: ATCC 700084/MC(2)155;                                        
SOURCE   5 GENE: GABT, MSMEG_2959;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    SSGCID, TRANSFERASE, SEATTLE STRUCTURAL GENOMICS CENTER FOR           
KEYWDS   2 INFECTIOUS DISEASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   1   27-OCT-10 3OKS    0                                                
JRNL        AUTH   A.GARDBERG,B.SANKARAN,J.ABENDROTH,B.STAKER,SSGCID            
JRNL        TITL   CRYSTAL STRUCTURE OF 4-AMINOBUTYRATE TRANSAMINASE FROM       
JRNL        TITL 2 MYCOBACTERIUM SMEGMATIS                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 48.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 154935                         
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) : 0.128                           
REMARK   3   R VALUE            (WORKING SET) : 0.126                           
REMARK   3   FREE R VALUE                     : 0.159                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7782                            
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) : 10886                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 548                          
REMARK   3   BIN FREE R VALUE                    : 0.2290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13110                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 1541                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : 0.29000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.093         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.054         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.813         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 13694 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  9098 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 18646 ; 1.456 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22257 ; 0.957 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1867 ; 5.797 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   553 ;34.976 ;23.671       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2149 ;11.828 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   103 ;15.993 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2149 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15640 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2683 ; 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):  8959 ; 0.711 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3726 ; 0.225 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14325 ; 1.235 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4735 ; 2.226 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4277 ; 3.683 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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     0        A   445                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5830  89.9320   6.0040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0162 T22:   0.0237                                     
REMARK   3      T33:   0.0503 T12:  -0.0078                                     
REMARK   3      T13:  -0.0272 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3337 L22:   0.2229                                     
REMARK   3      L33:   0.2280 L12:  -0.0244                                     
REMARK   3      L13:   0.1162 L23:  -0.0888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0298 S12:   0.0044 S13:   0.0638                       
REMARK   3      S21:   0.0382 S22:  -0.0197 S23:  -0.0809                       
REMARK   3      S31:  -0.0338 S32:   0.0434 S33:   0.0495                       
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     0        B   445                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8530  71.2090  11.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0220 T22:   0.0310                                     
REMARK   3      T33:   0.0153 T12:  -0.0049                                     
REMARK   3      T13:  -0.0114 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3383 L22:   0.2076                                     
REMARK   3      L33:   0.1511 L12:   0.0494                                     
REMARK   3      L13:   0.1176 L23:   0.0109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0131 S12:  -0.0568 S13:  -0.0431                       
REMARK   3      S21:   0.0313 S22:  -0.0035 S23:  -0.0108                       
REMARK   3      S31:   0.0235 S32:  -0.0307 S33:  -0.0096                       
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     0        C   445                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1030  25.7380  16.9520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0187 T22:   0.0287                                     
REMARK   3      T33:   0.0300 T12:  -0.0134                                     
REMARK   3      T13:   0.0109 T23:  -0.0270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2530 L22:   0.1444                                     
REMARK   3      L33:   0.2307 L12:  -0.0322                                     
REMARK   3      L13:  -0.1015 L23:   0.0634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0236 S12:   0.0533 S13:  -0.0493                       
REMARK   3      S21:  -0.0025 S22:  -0.0199 S23:   0.0378                       
REMARK   3      S31:   0.0441 S32:  -0.0559 S33:   0.0435                       
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     0        D   445                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2530  46.0420  27.6940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0117 T22:   0.0203                                     
REMARK   3      T33:   0.0096 T12:  -0.0033                                     
REMARK   3      T13:   0.0072 T23:  -0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2165 L22:   0.1255                                     
REMARK   3      L33:   0.2297 L12:  -0.0076                                     
REMARK   3      L13:  -0.1528 L23:  -0.0151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0141 S12:  -0.0251 S13:   0.0123                       
REMARK   3      S21:   0.0047 S22:  -0.0119 S23:  -0.0052                       
REMARK   3      S31:  -0.0126 S32:   0.0373 S33:  -0.0023                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 3OKS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061240.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.90                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977400                           
REMARK 200  MONOCHROMATOR                  : SI(220) ASYMMETRIC CUT SINGLE      
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 155089                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.350                              
REMARK 200  R MERGE                    (I) : 0.10900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9100                            
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR, MR                       
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG SCREEN CONDITION A5, TRAY BARCODE   
REMARK 280  216078: 200MM MG FORMATE PH 5.9, 20% PEG 3350, MYSMA.01026.C.A1     
REMARK 280  AT 25.11 MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.04000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       78.06000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       26.02000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11480 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     VAL A     2                                                      
REMARK 465     ALA A   447                                                      
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     ALA B   447                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     ALA C   447                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     ALA D   447                                                      
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     GLU A 195    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 198    CG   CD   CE   NZ                                   
REMARK 470     GLU A 199    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 200    CG   CD1  CD2                                       
REMARK 470     ARG A 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 365    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 169    CG   SD   CE                                        
REMARK 470     GLU B 195    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 340    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 365    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 195    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 198    CG   CD   CE   NZ                                   
REMARK 470     GLU C 199    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 200    CG   CD1  CD2                                       
REMARK 470     GLU C 337    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 340    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 365    CG   CD   OE1  OE2                                  
REMARK 470     MET D 169    CG   SD   CE                                        
REMARK 470     GLU D 195    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 198    CG   CD   CE   NZ                                   
REMARK 470     GLU D 199    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 206    CG   CD1  CD2                                       
REMARK 470     ARG D 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 365    CG   CD   OE1  OE2                                  
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   OE1  GLU B   337     O    HOH B  1534              2.01            
REMARK 500   O    HOH A   939     O    HOH A  1446              2.11            
REMARK 500   OE2  GLU D   441     O    HOH D  1373              2.16            
REMARK 500   OE2  GLU A   441     O    HOH A   615              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1479     O    HOH C  1478     4565     2.02            
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 B 431   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG D 375   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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  40       35.10    -87.16                                   
REMARK 500    ILE A  66       61.93     63.52                                   
REMARK 500    HIS A  91      130.49   -173.92                                   
REMARK 500    CYS A  93      111.78     65.72                                   
REMARK 500    VAL A  96      -71.79    -97.92                                   
REMARK 500    ILE A 219      -54.23   -128.95                                   
REMARK 500    PHE A 269       62.63     61.01                                   
REMARK 500    ALA A 270      -13.83     79.63                                   
REMARK 500    ALA A 291     -139.24   -169.08                                   
REMARK 500    LLP A 292      -95.22     39.64                                   
REMARK 500    CYS A 413     -170.82   -170.01                                   
REMARK 500    PRO B  40       33.12    -82.06                                   
REMARK 500    ILE B  66       60.79     64.67                                   
REMARK 500    HIS B  91      131.07   -172.34                                   
REMARK 500    CYS B  93      108.01     68.06                                   
REMARK 500    VAL B  96      -74.37    -96.84                                   
REMARK 500    ILE B 219      -56.64   -126.06                                   
REMARK 500    PHE B 269       64.03     63.17                                   
REMARK 500    ALA B 270      -12.34     77.44                                   
REMARK 500    ALA B 291     -140.03   -168.52                                   
REMARK 500    LLP B 292      -94.33     40.36                                   
REMARK 500    ASP B 367        0.94    -69.10                                   
REMARK 500    ALA B 377       34.32    -99.61                                   
REMARK 500    PRO C  40       31.64    -87.29                                   
REMARK 500    HIS C  91      129.56   -174.12                                   
REMARK 500    CYS C  93      109.46     65.29                                   
REMARK 500    VAL C  96      -70.84    -99.77                                   
REMARK 500    ILE C 219      -56.16   -127.75                                   
REMARK 500    PHE C 269       63.61     60.04                                   
REMARK 500    ALA C 270      -10.36     77.75                                   
REMARK 500    ALA C 291     -139.74   -170.92                                   
REMARK 500    LLP C 292      -91.52     38.77                                   
REMARK 500    GLN D   7       46.92    -90.68                                   
REMARK 500    PRO D  40       39.14    -87.96                                   
REMARK 500    HIS D  91      131.28   -174.88                                   
REMARK 500    CYS D  93      113.61     60.88                                   
REMARK 500    VAL D  96      -75.29    -98.49                                   
REMARK 500    ILE D 219      -55.05   -126.04                                   
REMARK 500    ALA D 270       -5.73     80.04                                   
REMARK 500    ALA D 291     -139.35   -173.30                                   
REMARK 500    LLP D 292      -93.14     36.70                                   
REMARK 500    ALA D 377       36.74    -99.77                                   
REMARK 500    ALA D 386      108.00    -37.48                                   
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                              MG C 448  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1364   O                                                      
REMARK 620 2 HOH C 459   O   172.5                                              
REMARK 620 3 HOH C1319   O    89.9  88.8                                        
REMARK 620 4 HOH C1352   O    92.5  95.0  96.9                                  
REMARK 620 5 HOH C 564   O    85.5  87.1  89.4 173.4                            
REMARK 620 6 HOH C1442   O    95.0  85.6 172.4  88.8  85.1                      
REMARK 620 N                    1     2     3     4     5                       
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 455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 465                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 465                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 470                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 448                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 465                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 455                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 465                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 470                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MYSMA.01026.C   RELATED DB: TARGETDB                     
DBREF  3OKS A    1   447  UNP    A0QWJ0   A0QWJ0_MYCS2     1    446             
DBREF  3OKS B    1   447  UNP    A0QWJ0   A0QWJ0_MYCS2     1    446             
DBREF  3OKS C    1   447  UNP    A0QWJ0   A0QWJ0_MYCS2     1    446             
DBREF  3OKS D    1   447  UNP    A0QWJ0   A0QWJ0_MYCS2     1    446             
SEQADV 3OKS GLY A   -3  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS PRO A   -2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY A   -1  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS SER A    0  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS VAL A    2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY B   -3  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS PRO B   -2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY B   -1  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS SER B    0  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS VAL B    2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY C   -3  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS PRO C   -2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY C   -1  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS SER C    0  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS VAL C    2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY D   -3  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS PRO D   -2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS GLY D   -1  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS SER D    0  UNP  A0QWJ0              EXPRESSION TAG                 
SEQADV 3OKS VAL D    2  UNP  A0QWJ0              EXPRESSION TAG                 
SEQRES   1 A  451  GLY PRO GLY SER MET VAL SER HIS PRO GLU GLN SER ARG          
SEQRES   2 A  451  HIS LEU ALA THR ALA ILE PRO GLY PRO ARG SER GLN ALA          
SEQRES   3 A  451  LEU ILE ASP ARG LYS GLY THR ALA VAL ALA ARG GLY VAL          
SEQRES   4 A  451  GLY THR THR MET PRO VAL TYR ALA VAL ARG ALA GLY GLY          
SEQRES   5 A  451  GLY ILE VAL GLU ASP VAL ASP GLY ASN ARG LEU ILE ASP          
SEQRES   6 A  451  LEU GLY SER GLY ILE ALA VAL THR THR VAL GLY ASN SER          
SEQRES   7 A  451  ALA PRO LYS VAL VAL GLU ALA VAL ARG SER GLN VAL GLY          
SEQRES   8 A  451  ASP PHE THR HIS THR CYS PHE MET VAL THR PRO TYR GLU          
SEQRES   9 A  451  GLY TYR VAL ALA VAL CYS GLU GLN LEU ASN ARG LEU THR          
SEQRES  10 A  451  PRO VAL ARG GLY ASP LYS ARG SER ALA LEU PHE ASN SER          
SEQRES  11 A  451  GLY SER GLU ALA VAL GLU ASN ALA VAL LYS ILE ALA ARG          
SEQRES  12 A  451  SER HIS THR HIS LYS PRO ALA VAL VAL ALA PHE ASP HIS          
SEQRES  13 A  451  ALA TYR HIS GLY ARG THR ASN LEU THR MET ALA LEU THR          
SEQRES  14 A  451  ALA LYS VAL MET PRO TYR LYS ASP GLY PHE GLY PRO PHE          
SEQRES  15 A  451  ALA PRO GLU ILE TYR ARG ALA PRO LEU SER TYR PRO PHE          
SEQRES  16 A  451  ARG ASP ALA GLU PHE GLY LYS GLU LEU ALA THR ASP GLY          
SEQRES  17 A  451  GLU LEU ALA ALA LYS ARG ALA ILE THR VAL ILE ASP LYS          
SEQRES  18 A  451  GLN ILE GLY ALA ASP ASN LEU ALA ALA VAL VAL ILE GLU          
SEQRES  19 A  451  PRO ILE GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA ASP          
SEQRES  20 A  451  GLY PHE LEU PRO THR LEU LEU ASP TRP CYS ARG LYS ASN          
SEQRES  21 A  451  ASP VAL VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE          
SEQRES  22 A  451  ALA ARG THR GLY ALA MET PHE ALA CYS GLU HIS GLU GLY          
SEQRES  23 A  451  ILE ASP PRO ASP LEU ILE VAL THR ALA LLP GLY ILE ALA          
SEQRES  24 A  451  GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA GLU          
SEQRES  25 A  451  ILE MET ASP SER PRO HIS VAL SER GLY LEU GLY GLY THR          
SEQRES  26 A  451  TYR GLY GLY ASN PRO ILE ALA CYS ALA ALA ALA LEU ALA          
SEQRES  27 A  451  THR ILE GLU THR ILE GLU SER GLU GLY LEU VAL ALA ARG          
SEQRES  28 A  451  ALA GLN GLN ILE GLU LYS ILE MET LYS ASP ARG LEU GLY          
SEQRES  29 A  451  ARG LEU GLN ALA GLU ASP ASP ARG ILE GLY ASP VAL ARG          
SEQRES  30 A  451  GLY ARG GLY ALA MET ILE ALA MET GLU LEU VAL LYS ALA          
SEQRES  31 A  451  GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ALA LEU          
SEQRES  32 A  451  CYS ALA GLY ALA HIS ALA ALA GLY VAL ILE VAL LEU SER          
SEQRES  33 A  451  CYS GLY THR TYR GLY ASN VAL VAL ARG PHE LEU PRO PRO          
SEQRES  34 A  451  LEU SER ILE GLY ASP ASP LEU LEU ASN GLU GLY LEU ASP          
SEQRES  35 A  451  VAL LEU GLU GLU VAL LEU ARG GLY ALA                          
SEQRES   1 B  451  GLY PRO GLY SER MET VAL SER HIS PRO GLU GLN SER ARG          
SEQRES   2 B  451  HIS LEU ALA THR ALA ILE PRO GLY PRO ARG SER GLN ALA          
SEQRES   3 B  451  LEU ILE ASP ARG LYS GLY THR ALA VAL ALA ARG GLY VAL          
SEQRES   4 B  451  GLY THR THR MET PRO VAL TYR ALA VAL ARG ALA GLY GLY          
SEQRES   5 B  451  GLY ILE VAL GLU ASP VAL ASP GLY ASN ARG LEU ILE ASP          
SEQRES   6 B  451  LEU GLY SER GLY ILE ALA VAL THR THR VAL GLY ASN SER          
SEQRES   7 B  451  ALA PRO LYS VAL VAL GLU ALA VAL ARG SER GLN VAL GLY          
SEQRES   8 B  451  ASP PHE THR HIS THR CYS PHE MET VAL THR PRO TYR GLU          
SEQRES   9 B  451  GLY TYR VAL ALA VAL CYS GLU GLN LEU ASN ARG LEU THR          
SEQRES  10 B  451  PRO VAL ARG GLY ASP LYS ARG SER ALA LEU PHE ASN SER          
SEQRES  11 B  451  GLY SER GLU ALA VAL GLU ASN ALA VAL LYS ILE ALA ARG          
SEQRES  12 B  451  SER HIS THR HIS LYS PRO ALA VAL VAL ALA PHE ASP HIS          
SEQRES  13 B  451  ALA TYR HIS GLY ARG THR ASN LEU THR MET ALA LEU THR          
SEQRES  14 B  451  ALA LYS VAL MET PRO TYR LYS ASP GLY PHE GLY PRO PHE          
SEQRES  15 B  451  ALA PRO GLU ILE TYR ARG ALA PRO LEU SER TYR PRO PHE          
SEQRES  16 B  451  ARG ASP ALA GLU PHE GLY LYS GLU LEU ALA THR ASP GLY          
SEQRES  17 B  451  GLU LEU ALA ALA LYS ARG ALA ILE THR VAL ILE ASP LYS          
SEQRES  18 B  451  GLN ILE GLY ALA ASP ASN LEU ALA ALA VAL VAL ILE GLU          
SEQRES  19 B  451  PRO ILE GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA ASP          
SEQRES  20 B  451  GLY PHE LEU PRO THR LEU LEU ASP TRP CYS ARG LYS ASN          
SEQRES  21 B  451  ASP VAL VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE          
SEQRES  22 B  451  ALA ARG THR GLY ALA MET PHE ALA CYS GLU HIS GLU GLY          
SEQRES  23 B  451  ILE ASP PRO ASP LEU ILE VAL THR ALA LLP GLY ILE ALA          
SEQRES  24 B  451  GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA GLU          
SEQRES  25 B  451  ILE MET ASP SER PRO HIS VAL SER GLY LEU GLY GLY THR          
SEQRES  26 B  451  TYR GLY GLY ASN PRO ILE ALA CYS ALA ALA ALA LEU ALA          
SEQRES  27 B  451  THR ILE GLU THR ILE GLU SER GLU GLY LEU VAL ALA ARG          
SEQRES  28 B  451  ALA GLN GLN ILE GLU LYS ILE MET LYS ASP ARG LEU GLY          
SEQRES  29 B  451  ARG LEU GLN ALA GLU ASP ASP ARG ILE GLY ASP VAL ARG          
SEQRES  30 B  451  GLY ARG GLY ALA MET ILE ALA MET GLU LEU VAL LYS ALA          
SEQRES  31 B  451  GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ALA LEU          
SEQRES  32 B  451  CYS ALA GLY ALA HIS ALA ALA GLY VAL ILE VAL LEU SER          
SEQRES  33 B  451  CYS GLY THR TYR GLY ASN VAL VAL ARG PHE LEU PRO PRO          
SEQRES  34 B  451  LEU SER ILE GLY ASP ASP LEU LEU ASN GLU GLY LEU ASP          
SEQRES  35 B  451  VAL LEU GLU GLU VAL LEU ARG GLY ALA                          
SEQRES   1 C  451  GLY PRO GLY SER MET VAL SER HIS PRO GLU GLN SER ARG          
SEQRES   2 C  451  HIS LEU ALA THR ALA ILE PRO GLY PRO ARG SER GLN ALA          
SEQRES   3 C  451  LEU ILE ASP ARG LYS GLY THR ALA VAL ALA ARG GLY VAL          
SEQRES   4 C  451  GLY THR THR MET PRO VAL TYR ALA VAL ARG ALA GLY GLY          
SEQRES   5 C  451  GLY ILE VAL GLU ASP VAL ASP GLY ASN ARG LEU ILE ASP          
SEQRES   6 C  451  LEU GLY SER GLY ILE ALA VAL THR THR VAL GLY ASN SER          
SEQRES   7 C  451  ALA PRO LYS VAL VAL GLU ALA VAL ARG SER GLN VAL GLY          
SEQRES   8 C  451  ASP PHE THR HIS THR CYS PHE MET VAL THR PRO TYR GLU          
SEQRES   9 C  451  GLY TYR VAL ALA VAL CYS GLU GLN LEU ASN ARG LEU THR          
SEQRES  10 C  451  PRO VAL ARG GLY ASP LYS ARG SER ALA LEU PHE ASN SER          
SEQRES  11 C  451  GLY SER GLU ALA VAL GLU ASN ALA VAL LYS ILE ALA ARG          
SEQRES  12 C  451  SER HIS THR HIS LYS PRO ALA VAL VAL ALA PHE ASP HIS          
SEQRES  13 C  451  ALA TYR HIS GLY ARG THR ASN LEU THR MET ALA LEU THR          
SEQRES  14 C  451  ALA LYS VAL MET PRO TYR LYS ASP GLY PHE GLY PRO PHE          
SEQRES  15 C  451  ALA PRO GLU ILE TYR ARG ALA PRO LEU SER TYR PRO PHE          
SEQRES  16 C  451  ARG ASP ALA GLU PHE GLY LYS GLU LEU ALA THR ASP GLY          
SEQRES  17 C  451  GLU LEU ALA ALA LYS ARG ALA ILE THR VAL ILE ASP LYS          
SEQRES  18 C  451  GLN ILE GLY ALA ASP ASN LEU ALA ALA VAL VAL ILE GLU          
SEQRES  19 C  451  PRO ILE GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA ASP          
SEQRES  20 C  451  GLY PHE LEU PRO THR LEU LEU ASP TRP CYS ARG LYS ASN          
SEQRES  21 C  451  ASP VAL VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE          
SEQRES  22 C  451  ALA ARG THR GLY ALA MET PHE ALA CYS GLU HIS GLU GLY          
SEQRES  23 C  451  ILE ASP PRO ASP LEU ILE VAL THR ALA LLP GLY ILE ALA          
SEQRES  24 C  451  GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA GLU          
SEQRES  25 C  451  ILE MET ASP SER PRO HIS VAL SER GLY LEU GLY GLY THR          
SEQRES  26 C  451  TYR GLY GLY ASN PRO ILE ALA CYS ALA ALA ALA LEU ALA          
SEQRES  27 C  451  THR ILE GLU THR ILE GLU SER GLU GLY LEU VAL ALA ARG          
SEQRES  28 C  451  ALA GLN GLN ILE GLU LYS ILE MET LYS ASP ARG LEU GLY          
SEQRES  29 C  451  ARG LEU GLN ALA GLU ASP ASP ARG ILE GLY ASP VAL ARG          
SEQRES  30 C  451  GLY ARG GLY ALA MET ILE ALA MET GLU LEU VAL LYS ALA          
SEQRES  31 C  451  GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ALA LEU          
SEQRES  32 C  451  CYS ALA GLY ALA HIS ALA ALA GLY VAL ILE VAL LEU SER          
SEQRES  33 C  451  CYS GLY THR TYR GLY ASN VAL VAL ARG PHE LEU PRO PRO          
SEQRES  34 C  451  LEU SER ILE GLY ASP ASP LEU LEU ASN GLU GLY LEU ASP          
SEQRES  35 C  451  VAL LEU GLU GLU VAL LEU ARG GLY ALA                          
SEQRES   1 D  451  GLY PRO GLY SER MET VAL SER HIS PRO GLU GLN SER ARG          
SEQRES   2 D  451  HIS LEU ALA THR ALA ILE PRO GLY PRO ARG SER GLN ALA          
SEQRES   3 D  451  LEU ILE ASP ARG LYS GLY THR ALA VAL ALA ARG GLY VAL          
SEQRES   4 D  451  GLY THR THR MET PRO VAL TYR ALA VAL ARG ALA GLY GLY          
SEQRES   5 D  451  GLY ILE VAL GLU ASP VAL ASP GLY ASN ARG LEU ILE ASP          
SEQRES   6 D  451  LEU GLY SER GLY ILE ALA VAL THR THR VAL GLY ASN SER          
SEQRES   7 D  451  ALA PRO LYS VAL VAL GLU ALA VAL ARG SER GLN VAL GLY          
SEQRES   8 D  451  ASP PHE THR HIS THR CYS PHE MET VAL THR PRO TYR GLU          
SEQRES   9 D  451  GLY TYR VAL ALA VAL CYS GLU GLN LEU ASN ARG LEU THR          
SEQRES  10 D  451  PRO VAL ARG GLY ASP LYS ARG SER ALA LEU PHE ASN SER          
SEQRES  11 D  451  GLY SER GLU ALA VAL GLU ASN ALA VAL LYS ILE ALA ARG          
SEQRES  12 D  451  SER HIS THR HIS LYS PRO ALA VAL VAL ALA PHE ASP HIS          
SEQRES  13 D  451  ALA TYR HIS GLY ARG THR ASN LEU THR MET ALA LEU THR          
SEQRES  14 D  451  ALA LYS VAL MET PRO TYR LYS ASP GLY PHE GLY PRO PHE          
SEQRES  15 D  451  ALA PRO GLU ILE TYR ARG ALA PRO LEU SER TYR PRO PHE          
SEQRES  16 D  451  ARG ASP ALA GLU PHE GLY LYS GLU LEU ALA THR ASP GLY          
SEQRES  17 D  451  GLU LEU ALA ALA LYS ARG ALA ILE THR VAL ILE ASP LYS          
SEQRES  18 D  451  GLN ILE GLY ALA ASP ASN LEU ALA ALA VAL VAL ILE GLU          
SEQRES  19 D  451  PRO ILE GLN GLY GLU GLY GLY PHE ILE VAL PRO ALA ASP          
SEQRES  20 D  451  GLY PHE LEU PRO THR LEU LEU ASP TRP CYS ARG LYS ASN          
SEQRES  21 D  451  ASP VAL VAL PHE ILE ALA ASP GLU VAL GLN THR GLY PHE          
SEQRES  22 D  451  ALA ARG THR GLY ALA MET PHE ALA CYS GLU HIS GLU GLY          
SEQRES  23 D  451  ILE ASP PRO ASP LEU ILE VAL THR ALA LLP GLY ILE ALA          
SEQRES  24 D  451  GLY GLY LEU PRO LEU SER ALA VAL THR GLY ARG ALA GLU          
SEQRES  25 D  451  ILE MET ASP SER PRO HIS VAL SER GLY LEU GLY GLY THR          
SEQRES  26 D  451  TYR GLY GLY ASN PRO ILE ALA CYS ALA ALA ALA LEU ALA          
SEQRES  27 D  451  THR ILE GLU THR ILE GLU SER GLU GLY LEU VAL ALA ARG          
SEQRES  28 D  451  ALA GLN GLN ILE GLU LYS ILE MET LYS ASP ARG LEU GLY          
SEQRES  29 D  451  ARG LEU GLN ALA GLU ASP ASP ARG ILE GLY ASP VAL ARG          
SEQRES  30 D  451  GLY ARG GLY ALA MET ILE ALA MET GLU LEU VAL LYS ALA          
SEQRES  31 D  451  GLY THR THR GLU PRO ASP ALA ASP LEU THR LYS ALA LEU          
SEQRES  32 D  451  CYS ALA GLY ALA HIS ALA ALA GLY VAL ILE VAL LEU SER          
SEQRES  33 D  451  CYS GLY THR TYR GLY ASN VAL VAL ARG PHE LEU PRO PRO          
SEQRES  34 D  451  LEU SER ILE GLY ASP ASP LEU LEU ASN GLU GLY LEU ASP          
SEQRES  35 D  451  VAL LEU GLU GLU VAL LEU ARG GLY ALA                          
MODRES 3OKS LLP A  292  LYS                                                     
MODRES 3OKS LLP B  292  LYS                                                     
MODRES 3OKS LLP C  292  LYS                                                     
MODRES 3OKS LLP D  292  LYS                                                     
HET    LLP  A 292      30                                                       
HET    LLP  B 292      30                                                       
HET    LLP  C 292      30                                                       
HET    LLP  D 292      30                                                       
HET    EDO  A 455       4                                                       
HET    EDO  A 480       4                                                       
HET    FMT  A 460       3                                                       
HET    FMT  A 465       3                                                       
HET    FMT  A 470       3                                                       
HET    EDO  B 455       4                                                       
HET    EDO  B 480       4                                                       
HET    FMT  B 460       3                                                       
HET    FMT  B 465       3                                                       
HET    FMT  B 470       3                                                       
HET    FMT  B 475       3                                                       
HET     MG  C 448       1                                                       
HET    EDO  C 455       4                                                       
HET    EDO  C 480       4                                                       
HET    FMT  C 460       3                                                       
HET    FMT  C 465       3                                                       
HET    EDO  D 455       4                                                       
HET    EDO  D 480       4                                                       
HET    EDO  D 485       4                                                       
HET    FMT  D 460       3                                                       
HET    FMT  D 465       3                                                       
HET    FMT  D 470       3                                                       
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-                
HETNAM   2 LLP  PYRIDIN-4-YLMETHANE)                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     FMT FORMIC ACID                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  LLP    4(C14 H24 N3 O7 P)                                           
FORMUL   5  EDO    9(C2 H6 O2)                                                  
FORMUL   7  FMT    12(C H2 O2)                                                  
FORMUL  16   MG    MG 2+                                                        
FORMUL  27  HOH   *1541(H2 O)                                                   
HELIX    1   1 GLY A   17  VAL A   31  1                                  15    
HELIX    2   2 GLY A   63  VAL A   68  1                                   6    
HELIX    3   3 ALA A   75  GLY A   87  1                                  13    
HELIX    4   4 TYR A   99  THR A  113  1                                  15    
HELIX    5   5 SER A  126  HIS A  143  1                                  18    
HELIX    6   6 THR A  158  THR A  165  1                                   8    
HELIX    7   7 TYR A  189  ALA A  194  1                                   6    
HELIX    8   8 GLU A  195  GLY A  197  5                                   3    
HELIX    9   9 ASP A  203  ILE A  219  1                                  17    
HELIX   10  10 GLY A  220  ASP A  222  5                                   3    
HELIX   11  11 GLY A  244  ASN A  256  1                                  13    
HELIX   12  12 PHE A  276  GLY A  282  5                                   7    
HELIX   13  13 ALA A  291  GLY A  296  5                                   6    
HELIX   14  14 ALA A  307  ASP A  311  1                                   5    
HELIX   15  15 ASN A  325  GLU A  342  1                                  18    
HELIX   16  16 GLY A  343  ASP A  366  1                                  24    
HELIX   17  17 ASP A  392  ALA A  406  1                                  15    
HELIX   18  18 GLY A  429  GLY A  446  1                                  18    
HELIX   19  19 GLY B   17  VAL B   31  1                                  15    
HELIX   20  20 GLY B   63  VAL B   68  1                                   6    
HELIX   21  21 ALA B   75  GLY B   87  1                                  13    
HELIX   22  22 TYR B   99  THR B  113  1                                  15    
HELIX   23  23 SER B  126  HIS B  143  1                                  18    
HELIX   24  24 THR B  158  THR B  165  1                                   8    
HELIX   25  25 TYR B  189  ALA B  194  1                                   6    
HELIX   26  26 GLY B  197  THR B  202  1                                   6    
HELIX   27  27 ASP B  203  ILE B  219  1                                  17    
HELIX   28  28 GLY B  220  ASP B  222  5                                   3    
HELIX   29  29 GLY B  244  ASN B  256  1                                  13    
HELIX   30  30 PHE B  276  HIS B  280  5                                   5    
HELIX   31  31 ALA B  291  GLY B  296  5                                   6    
HELIX   32  32 ALA B  307  ASP B  311  1                                   5    
HELIX   33  33 ASN B  325  GLU B  342  1                                  18    
HELIX   34  34 GLY B  343  ASP B  366  1                                  24    
HELIX   35  35 ASP B  392  ALA B  406  1                                  15    
HELIX   36  36 GLY B  429  GLY B  446  1                                  18    
HELIX   37  37 GLY C   17  VAL C   31  1                                  15    
HELIX   38  38 GLY C   63  VAL C   68  1                                   6    
HELIX   39  39 ALA C   75  GLY C   87  1                                  13    
HELIX   40  40 TYR C   99  THR C  113  1                                  15    
HELIX   41  41 SER C  126  HIS C  143  1                                  18    
HELIX   42  42 THR C  158  THR C  165  1                                   8    
HELIX   43  43 TYR C  189  ALA C  194  1                                   6    
HELIX   44  44 GLY C  197  ASP C  203  1                                   7    
HELIX   45  45 ASP C  203  ILE C  219  1                                  17    
HELIX   46  46 GLY C  220  ASP C  222  5                                   3    
HELIX   47  47 GLY C  244  ASN C  256  1                                  13    
HELIX   48  48 PHE C  276  GLY C  282  5                                   7    
HELIX   49  49 ALA C  291  GLY C  296  5                                   6    
HELIX   50  50 ALA C  307  ASP C  311  1                                   5    
HELIX   51  51 ASN C  325  GLU C  342  1                                  18    
HELIX   52  52 GLY C  343  ASP C  366  1                                  24    
HELIX   53  53 ASP C  392  ALA C  406  1                                  15    
HELIX   54  54 GLY C  429  GLY C  446  1                                  18    
HELIX   55  55 GLY D   17  VAL D   31  1                                  15    
HELIX   56  56 GLY D   63  VAL D   68  1                                   6    
HELIX   57  57 ALA D   75  GLY D   87  1                                  13    
HELIX   58  58 TYR D   99  THR D  113  1                                  15    
HELIX   59  59 SER D  126  HIS D  143  1                                  18    
HELIX   60  60 THR D  158  THR D  165  1                                   8    
HELIX   61  61 TYR D  189  ALA D  194  1                                   6    
HELIX   62  62 GLY D  197  ASP D  203  1                                   7    
HELIX   63  63 ASP D  203  ILE D  219  1                                  17    
HELIX   64  64 GLY D  220  ASP D  222  5                                   3    
HELIX   65  65 GLY D  244  ASP D  257  1                                  14    
HELIX   66  66 PHE D  276  GLY D  282  5                                   7    
HELIX   67  67 ALA D  291  GLY D  296  5                                   6    
HELIX   68  68 ALA D  307  ASP D  311  1                                   5    
HELIX   69  69 ASN D  325  GLY D  343  1                                  19    
HELIX   70  70 GLY D  343  GLU D  365  1                                  23    
HELIX   71  71 ASP D  392  ALA D  406  1                                  15    
HELIX   72  72 GLY D  429  GLY D  446  1                                  18    
SHEET    1   A 4 ALA A  43  GLY A  47  0                                        
SHEET    2   A 4 ILE A  50  ASP A  53 -1  O  GLU A  52   N  ARG A  45           
SHEET    3   A 4 ARG A  58  ASP A  61 -1  O  LEU A  59   N  VAL A  51           
SHEET    4   A 4 VAL A 408  ILE A 409  1  O  ILE A 409   N  ILE A  60           
SHEET    1   B 7 LYS A 119  PHE A 124  0                                        
SHEET    2   B 7 SER A 301  ARG A 306 -1  O  SER A 301   N  PHE A 124           
SHEET    3   B 7 LEU A 287  THR A 290 -1  N  ILE A 288   O  THR A 304           
SHEET    4   B 7 VAL A 259  ASP A 263  1  N  ALA A 262   O  VAL A 289           
SHEET    5   B 7 LEU A 224  ILE A 229  1  N  VAL A 227   O  ILE A 261           
SHEET    6   B 7 ALA A 146  PHE A 150  1  N  ALA A 146   O  ALA A 225           
SHEET    7   B 7 ILE A 182  ALA A 185  1  O  TYR A 183   N  ALA A 149           
SHEET    1   C 4 ILE A 369  ARG A 375  0                                        
SHEET    2   C 4 MET A 378  LEU A 383 -1  O  ALA A 380   N  ARG A 373           
SHEET    3   C 4 VAL A 419  PHE A 422 -1  O  PHE A 422   N  ILE A 379           
SHEET    4   C 4 LEU A 411  CYS A 413 -1  N  LEU A 411   O  ARG A 421           
SHEET    1   D 4 ALA B  43  GLY B  47  0                                        
SHEET    2   D 4 ILE B  50  ASP B  53 -1  O  GLU B  52   N  ARG B  45           
SHEET    3   D 4 ARG B  58  ASP B  61 -1  O  LEU B  59   N  VAL B  51           
SHEET    4   D 4 VAL B 408  ILE B 409  1  O  ILE B 409   N  ILE B  60           
SHEET    1   E 7 LYS B 119  PHE B 124  0                                        
SHEET    2   E 7 SER B 301  ARG B 306 -1  O  SER B 301   N  PHE B 124           
SHEET    3   E 7 LEU B 287  THR B 290 -1  N  ILE B 288   O  THR B 304           
SHEET    4   E 7 VAL B 259  ASP B 263  1  N  ALA B 262   O  LEU B 287           
SHEET    5   E 7 LEU B 224  ILE B 229  1  N  VAL B 227   O  ILE B 261           
SHEET    6   E 7 ALA B 146  PHE B 150  1  N  ALA B 146   O  ALA B 225           
SHEET    7   E 7 ILE B 182  ALA B 185  1  O  TYR B 183   N  ALA B 149           
SHEET    1   F 4 ILE B 369  ARG B 375  0                                        
SHEET    2   F 4 MET B 378  LEU B 383 -1  O  GLU B 382   N  GLY B 370           
SHEET    3   F 4 VAL B 419  PHE B 422 -1  O  PHE B 422   N  ILE B 379           
SHEET    4   F 4 LEU B 411  CYS B 413 -1  N  LEU B 411   O  ARG B 421           
SHEET    1   G 4 ALA C  43  GLY C  47  0                                        
SHEET    2   G 4 ILE C  50  ASP C  53 -1  O  GLU C  52   N  ARG C  45           
SHEET    3   G 4 ARG C  58  ASP C  61 -1  O  LEU C  59   N  VAL C  51           
SHEET    4   G 4 VAL C 408  ILE C 409  1  O  ILE C 409   N  ILE C  60           
SHEET    1   H 7 LYS C 119  PHE C 124  0                                        
SHEET    2   H 7 SER C 301  ARG C 306 -1  O  SER C 301   N  PHE C 124           
SHEET    3   H 7 LEU C 287  THR C 290 -1  N  ILE C 288   O  THR C 304           
SHEET    4   H 7 VAL C 259  ASP C 263  1  N  ALA C 262   O  VAL C 289           
SHEET    5   H 7 LEU C 224  ILE C 229  1  N  VAL C 227   O  ILE C 261           
SHEET    6   H 7 ALA C 146  PHE C 150  1  N  VAL C 148   O  VAL C 228           
SHEET    7   H 7 ILE C 182  ALA C 185  1  O  TYR C 183   N  ALA C 149           
SHEET    1   I 4 ILE C 369  ARG C 375  0                                        
SHEET    2   I 4 MET C 378  LEU C 383 -1  O  GLU C 382   N  GLY C 370           
SHEET    3   I 4 VAL C 419  PHE C 422 -1  O  PHE C 422   N  ILE C 379           
SHEET    4   I 4 LEU C 411  CYS C 413 -1  N  LEU C 411   O  ARG C 421           
SHEET    1   J 4 ALA D  43  GLY D  47  0                                        
SHEET    2   J 4 ILE D  50  ASP D  53 -1  O  GLU D  52   N  VAL D  44           
SHEET    3   J 4 ARG D  58  ASP D  61 -1  O  LEU D  59   N  VAL D  51           
SHEET    4   J 4 VAL D 408  ILE D 409  1  O  ILE D 409   N  ILE D  60           
SHEET    1   K 7 LYS D 119  PHE D 124  0                                        
SHEET    2   K 7 SER D 301  ARG D 306 -1  O  SER D 301   N  PHE D 124           
SHEET    3   K 7 LEU D 287  THR D 290 -1  N  ILE D 288   O  THR D 304           
SHEET    4   K 7 VAL D 259  ASP D 263  1  N  ALA D 262   O  VAL D 289           
SHEET    5   K 7 LEU D 224  ILE D 229  1  N  VAL D 227   O  ILE D 261           
SHEET    6   K 7 ALA D 146  PHE D 150  1  N  VAL D 148   O  VAL D 228           
SHEET    7   K 7 ILE D 182  ALA D 185  1  O  TYR D 183   N  ALA D 149           
SHEET    1   L 4 ILE D 369  ARG D 375  0                                        
SHEET    2   L 4 MET D 378  LEU D 383 -1  O  ALA D 380   N  ARG D 373           
SHEET    3   L 4 VAL D 419  PHE D 422 -1  O  PHE D 422   N  ILE D 379           
SHEET    4   L 4 LEU D 411  CYS D 413 -1  N  LEU D 411   O  ARG D 421           
LINK         C   LLP A 292                 N   GLY A 293     1555   1555  1.34  
LINK         C   LLP B 292                 N   GLY B 293     1555   1555  1.33  
LINK         C   LLP C 292                 N   GLY C 293     1555   1555  1.32  
LINK         C   LLP D 292                 N   GLY D 293     1555   1555  1.32  
LINK        MG    MG C 448                 O   HOH C1364     1555   1555  2.03  
LINK        MG    MG C 448                 O   HOH C 459     1555   1555  2.04  
LINK        MG    MG C 448                 O   HOH C1319     1555   1555  2.04  
LINK        MG    MG C 448                 O   HOH C1352     1555   1555  2.14  
LINK        MG    MG C 448                 O   HOH C 564     1555   1555  2.16  
LINK        MG    MG C 448                 O   HOH C1442     1555   1555  2.17  
CISPEP   1 ILE A   15    PRO A   16          0        -1.61                     
CISPEP   2 MET A  169    PRO A  170          0         3.91                     
CISPEP   3 GLY A  176    PRO A  177          0         4.79                     
CISPEP   4 ILE B   15    PRO B   16          0         0.96                     
CISPEP   5 MET B  169    PRO B  170          0         2.88                     
CISPEP   6 GLY B  176    PRO B  177          0         7.90                     
CISPEP   7 ILE C   15    PRO C   16          0         0.89                     
CISPEP   8 MET C  169    PRO C  170          0         4.17                     
CISPEP   9 GLY C  176    PRO C  177          0         5.76                     
CISPEP  10 ILE D   15    PRO D   16          0         1.82                     
CISPEP  11 MET D  169    PRO D  170          0         6.14                     
CISPEP  12 GLY D  176    PRO D  177          0         4.47                     
SITE     1 AC1  8 ALA A 163  LYS A 172  ILE A 182  ARG A 184                    
SITE     2 AC1  8 HOH A 587  HOH A 588  TYR C 183  HOH C 486                    
SITE     1 AC2  5 ASP A 151  HIS A 152  FMT A 470  HOH A 816                    
SITE     2 AC2  5 GLN C 218                                                     
SITE     1 AC3  6 TYR A 154  ARG A 157  HOH A 492  HOH A1264                    
SITE     2 AC3  6 MET B  95  GLY B 320                                          
SITE     1 AC4  5 ASP A 257  ARG A 306  ILE A 309  HOH A 659                    
SITE     2 AC4  5 HOH A 988                                                     
SITE     1 AC5  5 ASP A 151  HIS A 152  TYR A 416  EDO A 480                    
SITE     2 AC5  5 HOH A1503                                                     
SITE     1 AC6  8 ALA B 163  LYS B 172  ILE B 182  ARG B 184                    
SITE     2 AC6  8 HOH B 494  HOH B 496  HOH B 505  TYR D 183                    
SITE     1 AC7  6 ASP B 151  HIS B 152  TYR B 416  FMT B 470                    
SITE     2 AC7  6 HOH B1590  GLN D 218                                          
SITE     1 AC8  6 MET A  95  GLY A 320  TYR B 154  ARG B 157                    
SITE     2 AC8  6 HOH B 530  HOH B1316                                          
SITE     1 AC9  3 HIS B 141  ASP B 257  HOH B 700                               
SITE     1 BC1  4 HIS B 152  TYR B 416  EDO B 480  HOH B1335                    
SITE     1 BC2  7 GLU A 100  HOH A 478  ARG B  19  VAL B  54                    
SITE     2 BC2  7 HOH B 554  HOH B1573  HIS C  10                               
SITE     1 BC3  6 HOH C 459  HOH C 564  HOH C1319  HOH C1352                    
SITE     2 BC3  6 HOH C1364  HOH C1442                                          
SITE     1 BC4  8 TYR A 183  ALA C 163  LYS C 172  ILE C 182                    
SITE     2 BC4  8 ARG C 184  HOH C 487  HOH C 638  HOH C1453                    
SITE     1 BC5  4 GLN A 218  ASP C 151  HIS C 152  HOH C 481                    
SITE     1 BC6  6 TYR C 154  ARG C 157  HOH C 523  HOH C1275                    
SITE     2 BC6  6 MET D  95  GLY D 320                                          
SITE     1 BC7  5 HIS C 141  ASP C 257  ARG C 306  HOH C 586                    
SITE     2 BC7  5 HOH C 737                                                     
SITE     1 BC8  8 TYR B 183  ALA D 163  LYS D 172  ILE D 182                    
SITE     2 BC8  8 ARG D 184  HOH D 484  HOH D 493  HOH D 682                    
SITE     1 BC9  5 GLN B 218  ASP D 151  HIS D 152  TYR D 416                    
SITE     2 BC9  5 FMT D 470                                                     
SITE     1 CC1  7 THR D  38  CYS D 400  HIS D 404  VAL D 410                    
SITE     2 CC1  7 LEU D 411  SER D 412  HOH D 451                               
SITE     1 CC2  6 MET C  95  GLY C 320  TYR D 154  ARG D 157                    
SITE     2 CC2  6 HOH D 944  HOH D1269                                          
SITE     1 CC3  4 HIS D 141  ASP D 257  ARG D 306  HOH D 605                    
SITE     1 CC4  4 ASP D 151  HIS D 152  TYR D 416  EDO D 480                    
CRYST1  128.010  128.010  104.080  90.00  90.00  90.00 P 43         16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007812  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007812  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009608        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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