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LongText Report for: 3O4G-pdb

Name Class
3O4G-pdb
HEADER    HYDROLASE                               27-JUL-10   3O4G              
TITLE     STRUCTURE AND CATALYSIS OF ACYLAMINOACYL PEPTIDASE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-PEPTIDASE; 
COMPND   5 EC: 3.4.19.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;                               
SOURCE   3 ORGANISM_TAXID: 56636;                                               
SOURCE   4 GENE: APE_1547.1;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    ALPHA/BETA HYDROLASE FOLD, BETA PROPELLER, HYDROLASE, OLIGOPEPTIDASE, 
KEYWDS   2 SIZE SELECTIVITY                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.HARMAT,K.DOMOKOS,D.K.MENYHARD,A.PALLO,Z.SZELTNER,I.SZAMOSI,T.BEKE-  
AUTHOR   2 SOMFAI,G.NARAY-SZABO,L.POLGAR                                        
REVDAT   1   17-NOV-10 3O4G    0                                                
JRNL        AUTH   V.HARMAT,K.DOMOKOS,D.K.MENYHARD,A.PALLO,Z.SZELTNER,          
JRNL        AUTH 2 I.SZAMOSI,T.BEKE-SOMFAI,G.NARAY-SZABO,L.POLGAR               
JRNL        TITL   STRUCTURE AND CATALYSIS OF ACYLAMINOACYL PEPTIDASE: CLOSED   
JRNL        TITL 2 AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 84232                          
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) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4439                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6206                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 321                          
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17159                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 340                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : -0.02000                                             
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): 0.309         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.268         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.672        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17544 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 11949 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23818 ; 1.218 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 28983 ; 0.861 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2298 ; 6.157 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   689 ;33.298 ;22.642       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2735 ;15.958 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   147 ;18.081 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2681 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19864 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3658 ; 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): 11374 ; 0.316 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4744 ; 0.138 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18157 ; 0.538 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6170 ; 0.947 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5661 ; 1.472 ; 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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      6       A      21      3                      
REMARK   3           1     C      6       C      21      3                      
REMARK   3           2     A    322       A     510      3                      
REMARK   3           2     C    322       C     510      3                      
REMARK   3           3     A    512       A     580      3                      
REMARK   3           3     C    512       C     580      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1602 ; 0.030 ; 0.050           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1912 ; 0.030 ; 5.000           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1602 ; 0.070 ; 0.500           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1912 ; 0.070 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      8       B      21      3                      
REMARK   3           1     D      8       D      21      3                      
REMARK   3           2     B    322       B     580      3                      
REMARK   3           2     D    322       D     580      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1592 ; 0.030 ; 0.050           
REMARK   3   LOOSE POSITIONAL   2    B    (A):   1770 ; 0.040 ; 5.000           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1592 ; 0.060 ; 0.500           
REMARK   3   LOOSE THERMAL      2    B (A**2):   1770 ; 0.060 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     25       A     317      3                      
REMARK   3           1     C     25       C     317      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):   1704 ; 0.020 ; 0.050           
REMARK   3   LOOSE POSITIONAL   3    A    (A):   1932 ; 0.060 ; 5.000           
REMARK   3   TIGHT THERMAL      3    A (A**2):   1704 ; 0.060 ; 0.500           
REMARK   3   LOOSE THERMAL      3    A (A**2):   1932 ; 0.060 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     25       B      95      3                      
REMARK   3           1     D     25       D      95      3                      
REMARK   3           2     B     97       B     317      4                      
REMARK   3           2     D     97       D     317      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    B    (A):    415 ; 0.080 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  4    B    (A):   2715 ; 0.120 ; 0.500           
REMARK   3   LOOSE POSITIONAL   4    B    (A):    426 ; 0.140 ; 5.000           
REMARK   3   TIGHT THERMAL      4    B (A**2):    415 ; 0.260 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    B (A**2):   2715 ; 0.350 ; 2.000           
REMARK   3   LOOSE THERMAL      4    B (A**2):    426 ; 0.380 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A    23                          
REMARK   3    RESIDUE RANGE :   A   319        A   581                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0746   5.9527  -2.4570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0793 T22:   0.0935                                     
REMARK   3      T33:   0.0788 T12:   0.1027                                     
REMARK   3      T13:   0.0394 T23:   0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5042 L22:   1.3738                                     
REMARK   3      L33:   2.0104 L12:   0.4890                                     
REMARK   3      L13:  -0.2716 L23:  -0.0297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1755 S12:  -0.1030 S13:  -0.1303                       
REMARK   3      S21:   0.0517 S22:  -0.0493 S23:  -0.0429                       
REMARK   3      S31:   0.2831 S32:   0.3908 S33:   0.2249                       
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     7        B    23                          
REMARK   3    RESIDUE RANGE :   B   319        B   581                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4219  -6.0817  -0.0964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0827 T22:   0.1831                                     
REMARK   3      T33:   0.2083 T12:   0.0846                                     
REMARK   3      T13:   0.0601 T23:   0.0756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9603 L22:   2.0656                                     
REMARK   3      L33:   3.6305 L12:   1.1558                                     
REMARK   3      L13:  -0.4675 L23:  -1.9132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0769 S12:   0.4474 S13:   0.1266                       
REMARK   3      S21:  -0.0794 S22:   0.4564 S23:   0.2186                       
REMARK   3      S31:  -0.0065 S32:  -0.4025 S33:  -0.3795                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C    23                          
REMARK   3    RESIDUE RANGE :   C   319        C   581                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.0607  -0.4296  59.8544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0921 T22:   0.0091                                     
REMARK   3      T33:   0.0360 T12:  -0.0142                                     
REMARK   3      T13:  -0.0408 T23:  -0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1219 L22:   2.0848                                     
REMARK   3      L33:   1.7826 L12:   0.0661                                     
REMARK   3      L13:  -0.2498 L23:  -0.3812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0522 S12:  -0.0342 S13:   0.0652                       
REMARK   3      S21:   0.1236 S22:  -0.0406 S23:  -0.1396                       
REMARK   3      S31:   0.0920 S32:  -0.0164 S33:  -0.0116                       
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     6        D    23                          
REMARK   3    RESIDUE RANGE :   D   319        D   581                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.9060  27.2165  39.1140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0422 T22:   0.0263                                     
REMARK   3      T33:   0.0944 T12:   0.0135                                     
REMARK   3      T13:  -0.0502 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8535 L22:   2.1908                                     
REMARK   3      L33:   1.5103 L12:   0.4334                                     
REMARK   3      L13:  -0.6104 L23:  -1.0400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0706 S12:  -0.2313 S13:   0.0000                       
REMARK   3      S21:   0.1252 S22:   0.0621 S23:   0.0918                       
REMARK   3      S31:  -0.0692 S32:  -0.0727 S33:  -0.1326                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    24        A   318                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1310  33.7540  -4.1532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1621 T22:   0.0477                                     
REMARK   3      T33:   0.0605 T12:  -0.0190                                     
REMARK   3      T13:  -0.0305 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3690 L22:   1.2308                                     
REMARK   3      L33:   1.6387 L12:   0.6178                                     
REMARK   3      L13:   0.1708 L23:   0.1483                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0159 S12:   0.1277 S13:   0.2136                       
REMARK   3      S21:  -0.1683 S22:   0.0523 S23:   0.1500                       
REMARK   3      S31:  -0.3913 S32:   0.2003 S33:  -0.0363                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    24        B   318                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.9137 -32.8839  19.7980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1207 T22:   0.0344                                     
REMARK   3      T33:   0.0857 T12:   0.0047                                     
REMARK   3      T13:  -0.0333 T23:   0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7403 L22:   2.0904                                     
REMARK   3      L33:   1.1146 L12:  -0.0448                                     
REMARK   3      L13:  -0.5011 L23:   0.5609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0760 S12:   0.2015 S13:   0.0238                       
REMARK   3      S21:   0.1029 S22:  -0.0661 S23:  -0.2859                       
REMARK   3      S31:   0.2237 S32:  -0.0985 S33:  -0.0099                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    24        C   318                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.5318 -15.5807  46.8990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0810 T22:   0.2245                                     
REMARK   3      T33:   0.0886 T12:  -0.0978                                     
REMARK   3      T13:   0.0029 T23:  -0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9937 L22:   2.1193                                     
REMARK   3      L33:   1.3283 L12:  -0.1764                                     
REMARK   3      L13:  -0.1650 L23:  -0.2022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0433 S12:   0.1544 S13:   0.1645                       
REMARK   3      S21:   0.0456 S22:  -0.0672 S23:   0.1734                       
REMARK   3      S31:   0.2882 S32:  -0.5008 S33:   0.0240                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    24        D   318                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0290  35.5933  41.2192              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0983 T22:   0.2312                                     
REMARK   3      T33:   0.1576 T12:  -0.0789                                     
REMARK   3      T13:  -0.0594 T23:   0.0778                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4238 L22:   2.5245                                     
REMARK   3      L33:   2.0449 L12:   0.8932                                     
REMARK   3      L13:  -0.1235 L23:   0.1554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1179 S12:  -0.4881 S13:  -0.3405                       
REMARK   3      S21:   0.3064 S22:  -0.2310 S23:  -0.3112                       
REMARK   3      S31:  -0.2351 S32:   0.3831 S33:   0.1131                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3O4G COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB060652.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X12                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111),            
REMARK 200                                   HORIZONTALLY FOCUSSING             
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88675                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 1.990                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.5500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.99                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.010                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: HYDROLASE AND PROPELLER DOMAINS OF PDB ENTRY 2HU5.   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 78MM SODIUM ACETATE, 0.44MM EDTA,        
REMARK 280  6.7MM DITHIOTHREITOL, 2.4% PEG 4000 , PH 5.5, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
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, 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS HOMODIMER. ONE DIMER CONSISTS OF  
REMARK 300 CHAINS A AND B, AND THE OTHER DIMER CONSISTS OF CHAINS C AND D.      
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: 3290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     ARG A   582                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     PRO B     6                                                      
REMARK 465     GLY B   555                                                      
REMARK 465     ARG B   582                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     ILE C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     MET C     5                                                      
REMARK 465     ARG C   582                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     MET D     5                                                      
REMARK 465     ARG D   582                                                      
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     MET A   5    CG   SD   CE                                        
REMARK 470     VAL A   7    CG1  CG2                                            
REMARK 470     GLU A   8    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  11    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP A  34    CG   OD1  OD2                                       
REMARK 470     ARG A  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  69    CG   OD1  OD2                                       
REMARK 470     LYS A 110    NZ                                                  
REMARK 470     ARG A 149    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 188    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 216    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 217    CD   OE1  OE2                                       
REMARK 470     GLU A 324    CD   OE1  OE2                                       
REMARK 470     ARG A 327    CZ   NH1  NH2                                       
REMARK 470     ARG A 428    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 431    NH1  NH2                                            
REMARK 470     VAL B   7    CG1  CG2                                            
REMARK 470     GLU B   8    OE1  OE2                                            
REMARK 470     ARG B  11    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  17    OE2                                                 
REMARK 470     GLU B  23    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  41    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU B  55    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  85    CG   CD   CE   NZ                                   
REMARK 470     GLN B  89    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 131    CD   OE1  OE2                                       
REMARK 470     ARG B 149    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 174    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 194    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 216    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 217    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 234    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 324    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 327    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 328    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 346    CG1  CG2                                            
REMARK 470     GLU B 406    OE1  OE2                                            
REMARK 470     ARG B 428    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B 479    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 482    CG   OD1  OD2                                       
REMARK 470     ARG B 486    CZ   NH1  NH2                                       
REMARK 470     ASN B 487    CG   OD1  ND2                                       
REMARK 470     PHE B 488    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 491    CD   OE1  NE2                                       
REMARK 470     LEU B 492    CD1  CD2                                            
REMARK 470     ARG B 497    CZ   NH1  NH2                                       
REMARK 470     GLU B 498    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 513    CE   NZ                                             
REMARK 470     ARG B 526    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 553    CG   OD1  OD2                                       
REMARK 470     HIS B 556    ND1  CD2  CE1  NE2                                  
REMARK 470     MET B 561    CE                                                  
REMARK 470     LYS B 566    CE   NZ                                             
REMARK 470     VAL C   7    CG1  CG2                                            
REMARK 470     ARG C  11    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  61    CZ   NH1  NH2                                       
REMARK 470     ARG C  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 110    CD   CE   NZ                                        
REMARK 470     GLU C 122    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 149    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 194    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 216    CZ   NH1  NH2                                       
REMARK 470     GLU C 324    CD   OE1  OE2                                       
REMARK 470     ARG C 327    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C 431    CZ   NH1  NH2                                       
REMARK 470     GLU C 498    CD   OE1  OE2                                       
REMARK 470     ARG C 501    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP C 510    CG   OD1  OD2                                       
REMARK 470     VAL D   7    CG1  CG2                                            
REMARK 470     PHE D   9    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG D  11    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D  24    CE   NZ                                             
REMARK 470     GLU D  55    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  85    CG   CD   CE   NZ                                   
REMARK 470     GLN D  89    CD   OE1  NE2                                       
REMARK 470     LYS D  94    CG   CD   CE   NZ                                   
REMARK 470     ARG D  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 103    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 122    CD   OE1  OE2                                       
REMARK 470     GLU D 131    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 139    CG   CD1  CD2                                       
REMARK 470     ARG D 149    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG D 174    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 194    CD   OE1  OE2                                       
REMARK 470     ARG D 216    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU D 217    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 244    CZ   NH1  NH2                                       
REMARK 470     LYS D 294    NZ                                                  
REMARK 470     GLU D 324    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 328    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP D 342    CG   OD1  OD2                                       
REMARK 470     ARG D 486    CZ   NH1  NH2                                       
REMARK 470     GLU D 490    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 498    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 501    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 526    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 553    CG   OD1  OD2                                       
REMARK 470     HIS D 556    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE D 558    CD1                                                 
REMARK 470     GLU D 562    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 566    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  43       39.36     39.19                                   
REMARK 500    ARG A  61      -78.83   -102.26                                   
REMARK 500    SER A  66     -163.00   -170.64                                   
REMARK 500    ALA A 148      143.17   -170.47                                   
REMARK 500    PHE A 153      128.10    -39.94                                   
REMARK 500    ARG A 216       20.04   -141.21                                   
REMARK 500    SER A 445     -127.09     60.25                                   
REMARK 500    ARG B  61      -79.19    -93.02                                   
REMARK 500    SER B  84       25.88   -148.10                                   
REMARK 500    ARG B 216     -114.67   -131.54                                   
REMARK 500    ASP B 227        1.78   -152.22                                   
REMARK 500    PRO B 306      125.97    -39.82                                   
REMARK 500    ILE B 330       67.88   -105.07                                   
REMARK 500    ASP B 414       60.49   -156.34                                   
REMARK 500    SER B 445     -116.14     57.46                                   
REMARK 500    HIS B 508       25.57   -143.14                                   
REMARK 500    ASN B 523       49.37   -146.92                                   
REMARK 500    GLU B 580       48.49    -97.14                                   
REMARK 500    ARG C  61      -80.49   -104.64                                   
REMARK 500    SER C  66     -162.29   -172.08                                   
REMARK 500    ALA C 148      143.04   -171.40                                   
REMARK 500    PHE C 153      131.39    -39.67                                   
REMARK 500    ARG C 216       19.00   -141.31                                   
REMARK 500    ASP C 414       44.46   -141.13                                   
REMARK 500    SER C 445     -127.47     60.16                                   
REMARK 500    ARG D  61      -86.51    -82.68                                   
REMARK 500    TYR D  72      124.62    -39.21                                   
REMARK 500    SER D  84       22.50   -148.59                                   
REMARK 500    ALA D 148      143.85   -176.93                                   
REMARK 500    ARG D 216     -109.14   -127.30                                   
REMARK 500    TRP D 250      146.98   -171.70                                   
REMARK 500    PRO D 306      132.10    -39.89                                   
REMARK 500    ILE D 330       66.06   -102.95                                   
REMARK 500    TYR D 403       33.30   -140.21                                   
REMARK 500    ASP D 414       58.19   -157.04                                   
REMARK 500    SER D 445     -117.59     59.33                                   
REMARK 500    HIS D 508       26.96   -142.29                                   
REMARK 500    ASN D 523       51.34   -146.23                                   
REMARK 500    THR D 527       68.02   -150.15                                   
REMARK 500    ALA D 554       31.27    -95.23                                   
REMARK 500    GLU D 580       51.74    -96.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 612        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH D 613        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 617        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH D 624        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B 627        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 630        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH C 630        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH B 636        DISTANCE =  7.90 ANGSTROMS                       
REMARK 525    HOH C 638        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH C 640        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH C 642        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH A 646        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH C 645        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH A 649        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH B 651        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH B 673        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH D 655        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH C 659        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A 663        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH A 677        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH A 687        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A 691        DISTANCE =  7.42 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 583                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 584                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 583                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 583                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3O4H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O4I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3O4J   RELATED DB: PDB                                   
DBREF  3O4G A    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
DBREF  3O4G B    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
DBREF  3O4G C    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
DBREF  3O4G D    1   582  UNP    Q9YBQ2   APEH_AERPE       1    582             
SEQRES   1 A  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 A  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 A  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 A  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 A  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 A  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 A  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 A  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 A  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 A  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 A  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 A  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 A  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 A  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 A  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 A  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 A  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 A  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 A  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 A  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 A  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 A  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 A  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 A  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 A  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 A  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 A  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 A  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 A  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 A  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 A  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 A  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 A  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 A  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 A  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 A  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 A  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 A  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 A  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 A  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 A  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 A  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 A  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 A  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 A  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
SEQRES   1 B  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 B  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 B  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 B  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 B  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 B  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 B  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 B  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 B  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 B  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 B  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 B  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 B  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 B  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 B  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 B  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 B  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 B  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 B  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 B  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 B  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 B  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 B  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 B  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 B  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 B  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 B  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 B  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 B  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 B  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 B  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 B  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 B  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 B  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 B  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 B  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 B  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 B  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 B  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 B  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 B  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 B  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 B  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 B  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 B  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
SEQRES   1 C  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 C  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 C  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 C  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 C  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 C  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 C  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 C  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 C  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 C  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 C  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 C  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 C  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 C  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 C  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 C  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 C  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 C  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 C  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 C  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 C  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 C  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 C  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 C  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 C  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 C  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 C  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 C  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 C  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 C  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 C  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 C  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 C  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 C  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 C  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 C  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 C  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 C  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 C  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 C  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 C  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 C  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 C  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 C  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 C  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
SEQRES   1 D  582  MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL          
SEQRES   2 D  582  ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER          
SEQRES   3 D  582  LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL          
SEQRES   4 D  582  GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP          
SEQRES   5 D  582  GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN          
SEQRES   6 D  582  SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE          
SEQRES   7 D  582  LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA          
SEQRES   8 D  582  LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN          
SEQRES   9 D  582  ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY          
SEQRES  10 D  582  VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR          
SEQRES  11 D  582  GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY          
SEQRES  12 D  582  LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL          
SEQRES  13 D  582  SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE          
SEQRES  14 D  582  PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU          
SEQRES  15 D  582  SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY          
SEQRES  16 D  582  SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL          
SEQRES  17 D  582  THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL          
SEQRES  18 D  582  THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU          
SEQRES  19 D  582  LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA          
SEQRES  20 D  582  ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA          
SEQRES  21 D  582  VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE          
SEQRES  22 D  582  ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY          
SEQRES  23 D  582  ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS          
SEQRES  24 D  582  THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO          
SEQRES  25 D  582  SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP          
SEQRES  26 D  582  LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL          
SEQRES  27 D  582  GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU          
SEQRES  28 D  582  GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL          
SEQRES  29 D  582  LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER          
SEQRES  30 D  582  TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE          
SEQRES  31 D  582  HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR          
SEQRES  32 D  582  GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS          
SEQRES  33 D  582  GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP          
SEQRES  34 D  582  ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET          
SEQRES  35 D  582  GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU          
SEQRES  36 D  582  THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY          
SEQRES  37 D  582  ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER          
SEQRES  38 D  582  ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY          
SEQRES  39 D  582  GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN          
SEQRES  40 D  582  HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS          
SEQRES  41 D  582  PRO GLN ASN ASP SER ARG THR PRO LEU LYS PRO LEU LEU          
SEQRES  42 D  582  ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE          
SEQRES  43 D  582  GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN          
SEQRES  44 D  582  THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL          
SEQRES  45 D  582  PHE PHE LEU ALA THR GLN ARG GLU ARG ARG                      
HET    GOL  A 583       6                                                       
HET    GOL  A 584       6                                                       
HET    GOL  B 583       6                                                       
HET    GOL  C 583       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    4(C3 H8 O3)                                                  
FORMUL   9  HOH   *340(H2 O)                                                    
HELIX    1   1 GLU A    8  VAL A   22  1                                  15    
HELIX    2   2 LYS A  238  ARG A  244  1                                   7    
HELIX    3   3 PRO A  323  ARG A  328  1                                   6    
HELIX    4   4 ASP A  379  GLY A  389  1                                  11    
HELIX    5   5 GLY A  404  LYS A  410  1                                   7    
HELIX    6   6 GLY A  417  SER A  433  1                                  17    
HELIX    7   7 SER A  445  LYS A  458  1                                  14    
HELIX    8   8 ASP A  473  LEU A  480  1                                   8    
HELIX    9   9 ASP A  482  GLY A  494  1                                  13    
HELIX   10  10 SER A  496  ARG A  503  1                                   8    
HELIX   11  11 SER A  504  ILE A  512  5                                   9    
HELIX   12  12 LEU A  529  ARG A  542  1                                  14    
HELIX   13  13 THR A  560  ARG A  581  1                                  22    
HELIX   14  14 GLU B    8  VAL B   22  1                                  15    
HELIX   15  15 LYS B  238  ARG B  244  1                                   7    
HELIX   16  16 PRO B  323  ILE B  330  1                                   8    
HELIX   17  17 ASP B  379  ALA B  388  1                                  10    
HELIX   18  18 GLY B  404  LYS B  410  1                                   7    
HELIX   19  19 GLY B  417  SER B  433  1                                  17    
HELIX   20  20 SER B  445  LYS B  458  1                                  14    
HELIX   21  21 ASP B  473  LEU B  480  1                                   8    
HELIX   22  22 ASP B  482  THR B  493  1                                  12    
HELIX   23  23 SER B  496  ARG B  503  1                                   8    
HELIX   24  24 SER B  504  ILE B  512  5                                   9    
HELIX   25  25 LEU B  529  ARG B  542  1                                  14    
HELIX   26  26 THR B  560  LEU B  568  1                                   9    
HELIX   27  27 LEU B  568  ARG B  579  1                                  12    
HELIX   28  28 GLU C    8  VAL C   22  1                                  15    
HELIX   29  29 LYS C  238  ARG C  244  1                                   7    
HELIX   30  30 PRO C  323  ARG C  328  1                                   6    
HELIX   31  31 ASP C  379  GLY C  389  1                                  11    
HELIX   32  32 GLY C  404  LYS C  410  1                                   7    
HELIX   33  33 GLY C  417  SER C  433  1                                  17    
HELIX   34  34 SER C  445  LYS C  458  1                                  14    
HELIX   35  35 ASP C  473  LEU C  480  1                                   8    
HELIX   36  36 ASP C  482  GLY C  494  1                                  13    
HELIX   37  37 SER C  496  ARG C  503  1                                   8    
HELIX   38  38 SER C  504  ILE C  512  5                                   9    
HELIX   39  39 PRO C  528  ARG C  542  1                                  15    
HELIX   40  40 THR C  560  ARG C  581  1                                  22    
HELIX   41  41 GLU D    8  VAL D   22  1                                  15    
HELIX   42  42 LYS D  238  ARG D  244  1                                   7    
HELIX   43  43 PRO D  323  SER D  329  1                                   7    
HELIX   44  44 ASP D  379  ALA D  388  1                                  10    
HELIX   45  45 GLY D  404  LYS D  410  1                                   7    
HELIX   46  46 GLY D  417  SER D  433  1                                  17    
HELIX   47  47 SER D  445  LYS D  458  1                                  14    
HELIX   48  48 ASP D  473  LEU D  480  1                                   8    
HELIX   49  49 ASP D  482  THR D  493  1                                  12    
HELIX   50  50 SER D  496  ARG D  503  1                                   8    
HELIX   51  51 SER D  504  ILE D  512  5                                   9    
HELIX   52  52 LEU D  529  ARG D  542  1                                  14    
HELIX   53  53 THR D  560  LEU D  568  1                                   9    
HELIX   54  54 LEU D  568  ARG D  579  1                                  12    
SHEET    1   A 4 LYS A  24  VAL A  31  0                                        
SHEET    2   A 4 LYS A  35  SER A  42 -1  O  PHE A  41   N  LYS A  24           
SHEET    3   A 4 SER A  45  ASP A  52 -1  O  TYR A  49   N  VAL A  38           
SHEET    4   A 4 GLU A  55  LYS A  58 -1  O  VAL A  57   N  LEU A  50           
SHEET    1   B 4 SER A  66  VAL A  67  0                                        
SHEET    2   B 4 ARG A  76  ASP A  82 -1  O  VAL A  80   N  SER A  66           
SHEET    3   B 4 HIS A  90  ASN A  96 -1  O  PHE A  93   N  LEU A  79           
SHEET    4   B 4 GLU A 103  ARG A 105 -1  O  GLN A 104   N  LYS A  94           
SHEET    1   C 5 ASP A  69  PRO A  70  0                                        
SHEET    2   C 5 ARG A 113  ASP A 119  1  O  GLY A 117   N  ASP A  69           
SHEET    3   C 5 VAL A 124  ALA A 129 -1  O  VAL A 125   N  VAL A 118           
SHEET    4   C 5 VAL A 134  ASP A 140 -1  O  TYR A 137   N  PHE A 126           
SHEET    5   C 5 GLY A 143  LEU A 150 -1  O  ALA A 148   N  LEU A 136           
SHEET    1   D 4 GLY A 154  ARG A 160  0                                        
SHEET    2   D 4 LEU A 163  GLY A 171 -1  O  LEU A 167   N  PHE A 155           
SHEET    3   D 4 ARG A 174  ASN A 181 -1  O  SER A 176   N  GLY A 168           
SHEET    4   D 4 GLY A 185  PHE A 190 -1  O  PHE A 190   N  LEU A 177           
SHEET    1   E 4 SER A 196  ILE A 202  0                                        
SHEET    2   E 4 VAL A 208  GLU A 213 -1  O  THR A 209   N  SER A 201           
SHEET    3   E 4 ALA A 218  VAL A 223 -1  O  VAL A 223   N  VAL A 208           
SHEET    4   E 4 VAL A 230  ASP A 232 -1  O  GLU A 231   N  THR A 222           
SHEET    1   F 4 ALA A 247  TYR A 253  0                                        
SHEET    2   F 4 LEU A 259  ARG A 265 -1  O  VAL A 262   N  TRP A 250           
SHEET    3   F 4 ARG A 268  ILE A 273 -1  O  PHE A 272   N  VAL A 261           
SHEET    4   F 4 GLU A 276  VAL A 278 -1  O  VAL A 278   N  VAL A 271           
SHEET    1   G 4 ASN A 284  TRP A 291  0                                        
SHEET    2   G 4 LYS A 294  THR A 300 -1  O  VAL A 296   N  VAL A 289           
SHEET    3   G 4 ARG A 307  LEU A 311 -1  O  VAL A 309   N  THR A 297           
SHEET    4   G 4 PRO A 316  LEU A 318 -1  O  LEU A 317   N  ILE A 308           
SHEET    1   H16 ILE A 330  GLU A 339  0                                        
SHEET    2   H16 ARG A 345  SER A 353 -1  O  THR A 348   N  VAL A 336           
SHEET    3   H16 HIS A 391  PRO A 395 -1  O  MET A 394   N  TYR A 349           
SHEET    4   H16 GLY A 360  VAL A 366  1  N  VAL A 363   O  HIS A 391           
SHEET    5   H16 ALA A 436  TYR A 444  1  O  TYR A 440   N  VAL A 364           
SHEET    6   H16 GLY A 465  GLY A 468  1  O  VAL A 466   N  ILE A 441           
SHEET    7   H16 LEU A 516  PRO A 521  1  O  ALA A 517   N  GLY A 465           
SHEET    8   H16 PHE A 546  ILE A 551  1  O  HIS A 549   N  HIS A 520           
SHEET    9   H16 PHE B 546  ILE B 551 -1  O  ALA B 548   N  ILE A 550           
SHEET   10   H16 LEU B 516  PRO B 521  1  N  LEU B 518   O  GLU B 547           
SHEET   11   H16 ALA B 464  GLY B 468  1  N  GLY B 465   O  ALA B 517           
SHEET   12   H16 ALA B 436  TYR B 444  1  N  GLY B 443   O  GLY B 468           
SHEET   13   H16 GLY B 360  VAL B 366  1  N  VAL B 364   O  TYR B 440           
SHEET   14   H16 HIS B 391  PRO B 395  1  O  HIS B 391   N  VAL B 363           
SHEET   15   H16 ARG B 345  LEU B 351 -1  N  TYR B 349   O  MET B 394           
SHEET   16   H16 SER B 333  GLU B 339 -1  N  VAL B 338   O  VAL B 346           
SHEET    1   I 4 LYS B  24  VAL B  31  0                                        
SHEET    2   I 4 LYS B  35  SER B  42 -1  O  LEU B  37   N  GLY B  29           
SHEET    3   I 4 SER B  45  ASP B  52 -1  O  ASN B  47   N  GLY B  40           
SHEET    4   I 4 GLU B  55  LYS B  58 -1  O  VAL B  57   N  LEU B  50           
SHEET    1   J 4 SER B  66  VAL B  67  0                                        
SHEET    2   J 4 ARG B  76  ASP B  82 -1  O  VAL B  80   N  SER B  66           
SHEET    3   J 4 HIS B  90  ASN B  96 -1  O  PHE B  93   N  LEU B  79           
SHEET    4   J 4 GLN B 104  ARG B 105 -1  O  GLN B 104   N  LYS B  94           
SHEET    1   K 5 ASP B  69  PRO B  70  0                                        
SHEET    2   K 5 ARG B 113  ASP B 119  1  O  ASP B 119   N  ASP B  69           
SHEET    3   K 5 VAL B 124  THR B 130 -1  O  VAL B 125   N  VAL B 118           
SHEET    4   K 5 ARG B 133  ASP B 140 -1  O  TYR B 137   N  PHE B 126           
SHEET    5   K 5 GLY B 143  LEU B 150 -1  O  ALA B 148   N  LEU B 136           
SHEET    1   L 4 GLY B 154  ARG B 160  0                                        
SHEET    2   L 4 LEU B 163  GLY B 168 -1  O  ALA B 165   N  ASP B 158           
SHEET    3   L 4 SER B 176  ASN B 181 -1  O  PHE B 178   N  GLY B 166           
SHEET    4   L 4 ARG B 188  PHE B 190 -1  O  PHE B 190   N  LEU B 177           
SHEET    1   M 4 SER B 196  ILE B 202  0                                        
SHEET    2   M 4 VAL B 208  GLU B 213 -1  O  THR B 209   N  SER B 201           
SHEET    3   M 4 ARG B 219  VAL B 223 -1  O  VAL B 223   N  VAL B 208           
SHEET    4   M 4 VAL B 230  ASP B 232 -1  O  GLU B 231   N  THR B 222           
SHEET    1   N 4 ALA B 247  TYR B 253  0                                        
SHEET    2   N 4 LEU B 259  ARG B 265 -1  O  ARG B 264   N  ALA B 247           
SHEET    3   N 4 ARG B 268  ILE B 273 -1  O  PHE B 272   N  VAL B 261           
SHEET    4   N 4 GLU B 276  VAL B 278 -1  O  VAL B 278   N  VAL B 271           
SHEET    1   O 4 ASN B 284  TRP B 291  0                                        
SHEET    2   O 4 LYS B 294  SER B 301 -1  O  LYS B 294   N  TRP B 291           
SHEET    3   O 4 THR B 304  LEU B 311 -1  O  VAL B 309   N  THR B 297           
SHEET    4   O 4 PRO B 316  LEU B 318 -1  O  LEU B 317   N  ILE B 308           
SHEET    1   P 4 LYS C  24  VAL C  31  0                                        
SHEET    2   P 4 LYS C  35  SER C  42 -1  O  VAL C  39   N  SER C  26           
SHEET    3   P 4 SER C  45  ASP C  52 -1  O  TYR C  49   N  VAL C  38           
SHEET    4   P 4 GLU C  55  LYS C  58 -1  O  VAL C  57   N  LEU C  50           
SHEET    1   Q 4 SER C  66  VAL C  67  0                                        
SHEET    2   Q 4 ARG C  76  ASP C  82 -1  O  VAL C  80   N  SER C  66           
SHEET    3   Q 4 HIS C  90  ASN C  96 -1  O  PHE C  93   N  LEU C  79           
SHEET    4   Q 4 GLU C 103  ARG C 105 -1  O  GLN C 104   N  LYS C  94           
SHEET    1   R 5 ASP C  69  PRO C  70  0                                        
SHEET    2   R 5 ARG C 113  ASP C 119  1  O  ASP C 119   N  ASP C  69           
SHEET    3   R 5 VAL C 124  ALA C 129 -1  O  THR C 127   N  LEU C 115           
SHEET    4   R 5 VAL C 134  ASP C 140 -1  O  TYR C 137   N  PHE C 126           
SHEET    5   R 5 GLY C 143  LEU C 150 -1  O  ALA C 148   N  LEU C 136           
SHEET    1   S 4 GLY C 154  ARG C 160  0                                        
SHEET    2   S 4 LEU C 163  GLY C 171 -1  O  LEU C 167   N  PHE C 155           
SHEET    3   S 4 ARG C 174  ASN C 181 -1  O  SER C 176   N  GLY C 168           
SHEET    4   S 4 GLY C 185  PHE C 190 -1  O  PHE C 190   N  LEU C 177           
SHEET    1   T 4 GLY C 195  ILE C 202  0                                        
SHEET    2   T 4 VAL C 208  THR C 214 -1  O  GLU C 213   N  SER C 196           
SHEET    3   T 4 ALA C 218  VAL C 223 -1  O  VAL C 223   N  VAL C 208           
SHEET    4   T 4 VAL C 230  ASP C 232 -1  O  GLU C 231   N  THR C 222           
SHEET    1   U 4 ALA C 247  TYR C 253  0                                        
SHEET    2   U 4 LEU C 259  ARG C 265 -1  O  VAL C 262   N  TRP C 250           
SHEET    3   U 4 ARG C 268  ILE C 273 -1  O  PHE C 272   N  VAL C 261           
SHEET    4   U 4 GLU C 276  VAL C 278 -1  O  VAL C 278   N  VAL C 271           
SHEET    1   V 4 ASN C 284  TRP C 291  0                                        
SHEET    2   V 4 LYS C 294  THR C 300 -1  O  LYS C 294   N  TRP C 291           
SHEET    3   V 4 ARG C 307  LEU C 311 -1  O  VAL C 309   N  THR C 297           
SHEET    4   V 4 PRO C 316  LEU C 318 -1  O  LEU C 317   N  ILE C 308           
SHEET    1   W16 ILE C 330  GLU C 339  0                                        
SHEET    2   W16 ARG C 345  SER C 353 -1  O  THR C 348   N  VAL C 336           
SHEET    3   W16 HIS C 391  PRO C 395 -1  O  MET C 394   N  TYR C 349           
SHEET    4   W16 GLY C 360  VAL C 366  1  N  VAL C 363   O  HIS C 391           
SHEET    5   W16 ALA C 436  TYR C 444  1  O  TYR C 440   N  VAL C 364           
SHEET    6   W16 ALA C 464  GLY C 468  1  O  GLY C 468   N  GLY C 443           
SHEET    7   W16 LEU C 516  PRO C 521  1  O  ALA C 517   N  GLY C 465           
SHEET    8   W16 PHE C 546  ILE C 551  1  O  GLU C 547   N  LEU C 518           
SHEET    9   W16 PHE D 546  ILE D 551 -1  O  ALA D 548   N  ILE C 550           
SHEET   10   W16 LEU D 516  PRO D 521  1  N  LEU D 516   O  GLU D 547           
SHEET   11   W16 ALA D 464  GLY D 468  1  N  GLY D 465   O  ALA D 517           
SHEET   12   W16 ALA D 436  TYR D 444  1  N  GLY D 443   O  GLY D 468           
SHEET   13   W16 GLY D 360  VAL D 366  1  N  VAL D 366   O  MET D 442           
SHEET   14   W16 HIS D 391  PRO D 395  1  O  HIS D 391   N  VAL D 363           
SHEET   15   W16 ARG D 345  SER D 353 -1  N  TYR D 349   O  MET D 394           
SHEET   16   W16 ILE D 330  GLU D 339 -1  N  VAL D 338   O  VAL D 346           
SHEET    1   X 4 LYS D  24  VAL D  31  0                                        
SHEET    2   X 4 LYS D  35  SER D  42 -1  O  PHE D  41   N  LYS D  24           
SHEET    3   X 4 SER D  45  ASP D  52 -1  O  ASN D  47   N  GLY D  40           
SHEET    4   X 4 GLU D  55  LYS D  58 -1  O  VAL D  57   N  LEU D  50           
SHEET    1   Y 4 SER D  66  VAL D  67  0                                        
SHEET    2   Y 4 ARG D  76  ASP D  82 -1  O  VAL D  80   N  SER D  66           
SHEET    3   Y 4 HIS D  90  ASN D  96 -1  O  PHE D  93   N  LEU D  79           
SHEET    4   Y 4 GLN D 104  ARG D 105 -1  O  GLN D 104   N  LYS D  94           
SHEET    1   Z 5 ASP D  69  PRO D  70  0                                        
SHEET    2   Z 5 ARG D 113  ASP D 119  1  O  ASP D 119   N  ASP D  69           
SHEET    3   Z 5 VAL D 124  THR D 130 -1  O  VAL D 125   N  VAL D 118           
SHEET    4   Z 5 ARG D 133  ASP D 140 -1  O  TYR D 137   N  PHE D 126           
SHEET    5   Z 5 GLY D 143  LEU D 150 -1  O  ALA D 148   N  LEU D 136           
SHEET    1  AA 4 GLY D 154  ARG D 160  0                                        
SHEET    2  AA 4 LEU D 163  GLY D 168 -1  O  LEU D 167   N  PHE D 155           
SHEET    3  AA 4 SER D 176  ASN D 181 -1  O  SER D 180   N  ILE D 164           
SHEET    4  AA 4 ARG D 188  PHE D 190 -1  O  PHE D 190   N  LEU D 177           
SHEET    1  AB 4 GLY D 195  ILE D 202  0                                        
SHEET    2  AB 4 VAL D 208  THR D 214 -1  O  THR D 209   N  SER D 201           
SHEET    3  AB 4 ARG D 219  VAL D 223 -1  O  ARG D 219   N  LEU D 212           
SHEET    4  AB 4 VAL D 230  ASP D 232 -1  O  GLU D 231   N  THR D 222           
SHEET    1  AC 4 ALA D 247  TYR D 253  0                                        
SHEET    2  AC 4 LEU D 259  ARG D 265 -1  O  VAL D 262   N  TRP D 250           
SHEET    3  AC 4 ARG D 268  ILE D 273 -1  O  PHE D 272   N  VAL D 261           
SHEET    4  AC 4 GLU D 276  VAL D 278 -1  O  VAL D 278   N  VAL D 271           
SHEET    1  AD 4 ASN D 284  TRP D 291  0                                        
SHEET    2  AD 4 LYS D 294  SER D 301 -1  O  LYS D 294   N  TRP D 291           
SHEET    3  AD 4 THR D 304  LEU D 311 -1  O  ARG D 307   N  HIS D 299           
SHEET    4  AD 4 PRO D 316  LEU D 318 -1  O  LEU D 317   N  ILE D 308           
CISPEP   1 LEU A  311    PRO A  312          0         5.57                     
CISPEP   2 THR A  358    PRO A  359          0         3.26                     
CISPEP   3 GLY A  369    PRO A  370          0         4.85                     
CISPEP   4 LEU B  311    PRO B  312          0         0.66                     
CISPEP   5 THR B  358    PRO B  359          0        -2.32                     
CISPEP   6 GLY B  369    PRO B  370          0         6.87                     
CISPEP   7 LEU C  311    PRO C  312          0         7.14                     
CISPEP   8 THR C  358    PRO C  359          0        -0.03                     
CISPEP   9 GLY C  369    PRO C  370          0         8.92                     
CISPEP  10 LEU D  311    PRO D  312          0         4.81                     
CISPEP  11 THR D  358    PRO D  359          0        -3.60                     
CISPEP  12 GLY D  369    PRO D  370          0         8.60                     
SITE     1 AC1  2 SER A  66  ILE A 114                                          
SITE     1 AC2  6 ASP A 473  GLU A 475  GLU A 476  GLU A 479                    
SITE     2 AC2  6 GLU C 421  LYS C 458                                          
SITE     1 AC3  2 HIS B 285  SER B 298                                          
SITE     1 AC4  4 THR C 249  ARG C 264  ASN C 284  THR C 401                    
CRYST1   71.212   97.016  109.494  89.01 109.20 100.21 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      0.014043  0.002528  0.005008        0.00000                         
SCALE2      0.000000  0.010473  0.000463        0.00000                         
SCALE3      0.000000  0.000000  0.009681        0.00000                         
TER    4339      ARG A 581                                                      
TER    8583      ARG B 581                                                      
TER   12908      ARG C 581                                                      
TER   17163      ARG D 581                                                      
MASTER      698    0    4   54  148    0    5    617523    4   24  180          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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