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Entry: 4AOY
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HEADER    OXIDOREDUCTASE                          30-MAR-12   4AOY              
TITLE     OPEN CTIDH. THE COMPLEX STRUCTURES OF ISOCITRATE DEHYDROGENASE FROM   
TITLE    2 CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA PSYCHROPHILA, SUPPORT A    
TITLE    3 NEW ACTIVE SITE LOCKING MECHANISM                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP];                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.1.1.42                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;                       
SOURCE   3 ORGANISM_TAXID: 1515                                                 
KEYWDS    OXIDOREDUCTASE, TEMPERATURE ADAPTATION, THERMOPHILIC, PSYCHROPHILIC,  
KEYWDS   2 NADP+ SELECTIVITY, DOMAIN MOVEMENTS                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-K.S.LEIROS,A.-E.FEDOY,I.LEIROS,I.H.STEEN                           
REVDAT   3   22-MAY-13 4AOY    1       JRNL                                     
REVDAT   2   20-MAR-13 4AOY    1       JRNL                                     
REVDAT   1   25-APR-12 4AOY    0                                                
JRNL        AUTH   H.-K.S.LEIROS,A.-E.FEDOY,I.LEIROS,I.H.STEEN                  
JRNL        TITL   THE COMPLEX STRUCTURES OF ISOCITRATE DEHYDROGENASE FROM      
JRNL        TITL 2 CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA PSYCHROPHILA       
JRNL        TITL 3 SUGGEST A NEW ACTIVE SITE LOCKING MECHANISM                  
JRNL        REF    FEBS OPEN BIO.                V.   2   159 2012              
JRNL        REFN                   ISSN 2211-5463                               
JRNL        PMID   23650595                                                     
JRNL        DOI    10.1016/J.FOB.2012.06.003                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 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) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.74                          
REMARK   3   NUMBER OF REFLECTIONS             : 73524                          
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) : 0.21093                         
REMARK   3   R VALUE            (WORKING SET) : 0.20962                         
REMARK   3   FREE R VALUE                     : 0.25844                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.7                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2010                            
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) : 2.350                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.410                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5309                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.20                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.292                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 147                          
REMARK   3   BIN FREE R VALUE                    : 0.380                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11590                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.016                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31                                                 
REMARK   3    B22 (A**2) : 0.25                                                 
REMARK   3    B33 (A**2) : -0.57                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.06                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.328         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11806 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15942 ; 1.670 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1478 ; 6.795 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   523 ;36.625 ;24.608       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2046 ;19.999 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;21.393 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1771 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8843 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  7383 ; 0.746 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11861 ; 1.393 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4423 ; 2.272 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4081 ; 3.720 ; 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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     401      4                      
REMARK   3           1     B      2       B     401      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2816 ;  0.31 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2816 ;  0.31 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2816 ;  0.81 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2816 ;  0.81 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      2       C     401      4                      
REMARK   3           1     D      2       D     401      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   2851 ;  0.35 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  2    D    (A):   2851 ;  0.35 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   2851 ;  0.93 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    D (A**2):   2851 ;  0.93 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.4510  -8.3550  41.9410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2158 T22:   0.1370                                     
REMARK   3      T33:   0.1340 T12:   0.0150                                     
REMARK   3      T13:   0.0128 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7151 L22:   2.7987                                     
REMARK   3      L33:   1.4764 L12:  -0.7060                                     
REMARK   3      L13:   0.0496 L23:   0.2424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:  -0.0541 S13:  -0.2653                       
REMARK   3      S21:  -0.1086 S22:   0.0416 S23:   0.2170                       
REMARK   3      S31:   0.1970 S32:  -0.1280 S33:  -0.0318                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   118        A   212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9100   0.2670  67.2020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1946 T22:   0.2008                                     
REMARK   3      T33:   0.2045 T12:   0.0052                                     
REMARK   3      T13:   0.0120 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8419 L22:   1.0458                                     
REMARK   3      L33:   1.4182 L12:  -0.8911                                     
REMARK   3      L13:   0.9590 L23:  -0.9739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0306 S12:  -0.0385 S13:   0.0339                       
REMARK   3      S21:   0.0086 S22:   0.0705 S23:  -0.0075                       
REMARK   3      S31:  -0.2829 S32:  -0.0688 S33:  -0.0399                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   213        A   375                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9480   8.1020  52.7490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3102 T22:   0.2040                                     
REMARK   3      T33:   0.2164 T12:   0.0283                                     
REMARK   3      T13:   0.0199 T23:   0.0561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1363 L22:   1.5180                                     
REMARK   3      L33:   2.5448 L12:   0.2272                                     
REMARK   3      L13:   0.7656 L23:   0.9757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0959 S12:  -0.3932 S13:   0.0158                       
REMARK   3      S21:   0.1064 S22:  -0.1362 S23:   0.0571                       
REMARK   3      S31:  -0.0962 S32:  -0.2697 S33:   0.0403                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   376        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3720   1.4060  39.7500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3751 T22:   0.7171                                     
REMARK   3      T33:   0.4625 T12:   0.0822                                     
REMARK   3      T13:  -0.1302 T23:   0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.2549 L22:   6.4960                                     
REMARK   3      L33:   6.4183 L12:  -2.7142                                     
REMARK   3      L13:  -1.6772 L23:   0.5875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1224 S12:   0.2362 S13:  -0.5908                       
REMARK   3      S21:   0.0434 S22:  -0.3602 S23:   0.5222                       
REMARK   3      S31:  -0.5046 S32:  -1.2613 S33:   0.2378                       
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 :   B     3        B   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0290  50.4660  34.8190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2314 T22:   0.1266                                     
REMARK   3      T33:   0.1257 T12:  -0.0063                                     
REMARK   3      T13:  -0.0200 T23:   0.0550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5156 L22:   2.6809                                     
REMARK   3      L33:   2.3984 L12:   0.7250                                     
REMARK   3      L13:  -0.3336 L23:   0.2213                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0093 S12:   0.0410 S13:   0.2552                       
REMARK   3      S21:  -0.0046 S22:  -0.0364 S23:   0.0419                       
REMARK   3      S31:  -0.1326 S32:   0.0407 S33:   0.0270                       
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   118        B   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.8490  45.8940   6.5830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1235 T22:   0.2617                                     
REMARK   3      T33:   0.2709 T12:   0.0324                                     
REMARK   3      T13:   0.0069 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6866 L22:   1.6376                                     
REMARK   3      L33:   1.6591 L12:   0.9763                                     
REMARK   3      L13:  -0.6997 L23:  -0.8788                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0135 S12:  -0.0056 S13:  -0.0502                       
REMARK   3      S21:   0.0750 S22:   0.1027 S23:   0.1083                       
REMARK   3      S31:   0.1836 S32:  -0.0377 S33:  -0.1162                       
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 :   B   192        B   326                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8470  32.5800  19.0480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4641 T22:   0.3733                                     
REMARK   3      T33:   0.3032 T12:   0.0752                                     
REMARK   3      T13:  -0.0437 T23:   0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6769 L22:   1.3242                                     
REMARK   3      L33:   2.6688 L12:   0.4051                                     
REMARK   3      L13:  -0.9263 L23:   1.5347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2192 S12:   0.7101 S13:  -0.1226                       
REMARK   3      S21:  -0.1087 S22:  -0.1288 S23:  -0.0056                       
REMARK   3      S31:   0.1148 S32:  -0.1340 S33:  -0.0904                       
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 :   B   327        B   399                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2180  37.4990  36.6460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4041 T22:   0.2814                                     
REMARK   3      T33:   0.2060 T12:  -0.1041                                     
REMARK   3      T13:   0.0359 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5585 L22:   3.2704                                     
REMARK   3      L33:   4.1069 L12:   0.1227                                     
REMARK   3      L13:   1.1141 L23:  -0.0313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.3787 S13:  -0.1030                       
REMARK   3      S21:  -0.0172 S22:  -0.0588 S23:   0.6898                       
REMARK   3      S31:   0.3359 S32:  -0.8418 S33:   0.0039                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   132                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4540  12.5050  95.8150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1543 T22:   0.0871                                     
REMARK   3      T33:   0.1624 T12:  -0.0004                                     
REMARK   3      T13:   0.0207 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8686 L22:   1.7191                                     
REMARK   3      L33:   3.4098 L12:  -0.5355                                     
REMARK   3      L13:   1.5662 L23:   0.0816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1158 S12:   0.1020 S13:   0.2662                       
REMARK   3      S21:   0.1159 S22:   0.1101 S23:  -0.2146                       
REMARK   3      S31:  -0.2238 S32:   0.3213 S33:   0.0058                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   141        C   180                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9020  -8.9460  73.0560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0170 T22:   0.1042                                     
REMARK   3      T33:   0.1583 T12:   0.0003                                     
REMARK   3      T13:  -0.0433 T23:  -0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1491 L22:   6.1820                                     
REMARK   3      L33:   8.1689 L12:   1.4644                                     
REMARK   3      L13:  -1.2703 L23:  -4.3364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0107 S12:  -0.0256 S13:   0.2774                       
REMARK   3      S21:  -0.0426 S22:  -0.1271 S23:   0.0263                       
REMARK   3      S31:  -0.1038 S32:   0.0998 S33:   0.1164                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   181        C   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.6520  -9.5860  79.6030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0479 T22:   0.0379                                     
REMARK   3      T33:   0.1275 T12:  -0.0065                                     
REMARK   3      T13:  -0.0068 T23:  -0.0226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6274 L22:   2.6566                                     
REMARK   3      L33:   3.9672 L12:  -0.7555                                     
REMARK   3      L13:   2.1182 L23:  -0.9350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1219 S12:   0.1871 S13:  -0.2057                       
REMARK   3      S21:  -0.2466 S22:  -0.0405 S23:   0.1135                       
REMARK   3      S31:   0.2001 S32:  -0.2002 S33:  -0.0815                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   265        C   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3890  14.1050  88.7560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1039 T22:   0.1341                                     
REMARK   3      T33:   0.1696 T12:  -0.0122                                     
REMARK   3      T13:  -0.0005 T23:   0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4284 L22:   5.8141                                     
REMARK   3      L33:   1.2689 L12:  -1.7496                                     
REMARK   3      L13:   1.2858 L23:  -1.5325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0393 S12:   0.1022 S13:   0.0740                       
REMARK   3      S21:  -0.0209 S22:   0.0782 S23:   0.1211                       
REMARK   3      S31:  -0.0265 S32:   0.0297 S33:  -0.0389                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.6880  29.2910 -20.2440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1350 T22:   0.0967                                     
REMARK   3      T33:   0.1583 T12:  -0.0123                                     
REMARK   3      T13:   0.0157 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6509 L22:   2.3641                                     
REMARK   3      L33:   3.1500 L12:   0.3670                                     
REMARK   3      L13:  -1.3781 L23:   0.1971                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1019 S12:  -0.1615 S13:  -0.2841                       
REMARK   3      S21:  -0.1474 S22:   0.1312 S23:  -0.2831                       
REMARK   3      S31:   0.1978 S32:   0.3839 S33:  -0.0293                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   125        D   241                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4490  51.8270  -1.9840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1399 T22:   0.1531                                     
REMARK   3      T33:   0.1412 T12:   0.0136                                     
REMARK   3      T13:   0.0361 T23:  -0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5242 L22:   0.4111                                     
REMARK   3      L33:   1.0000 L12:   1.1428                                     
REMARK   3      L13:   1.5545 L23:   0.3104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0767 S12:  -0.3661 S13:  -0.0560                       
REMARK   3      S21:   0.0885 S22:   0.0216 S23:  -0.0629                       
REMARK   3      S31:   0.1235 S32:  -0.1340 S33:  -0.0982                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   242        D   326                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8860  40.7160  -2.8420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1296 T22:   0.2942                                     
REMARK   3      T33:   0.2116 T12:   0.0332                                     
REMARK   3      T13:   0.0288 T23:   0.0545                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6884 L22:   3.4741                                     
REMARK   3      L33:   5.5667 L12:   0.8705                                     
REMARK   3      L13:  -0.6974 L23:   2.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0232 S12:  -0.2877 S13:  -0.2387                       
REMARK   3      S21:   0.4828 S22:  -0.0381 S23:  -0.3975                       
REMARK   3      S31:   0.4768 S32:   0.3287 S33:   0.0150                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   327        D   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.9650  24.2760 -13.8100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0674 T22:   0.1106                                     
REMARK   3      T33:   0.1521 T12:  -0.0253                                     
REMARK   3      T13:  -0.0027 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7029 L22:   7.4380                                     
REMARK   3      L33:   3.7509 L12:   1.1725                                     
REMARK   3      L13:  -1.1573 L23:  -3.9773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0686 S12:  -0.0675 S13:  -0.0932                       
REMARK   3      S21:  -0.0446 S22:   0.2747 S23:   0.4639                       
REMARK   3      S31:   0.0576 S32:  -0.2948 S33:  -0.2062                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4AOY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-51913.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0052                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.4                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.60                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTIONS OF 9-11%             
REMARK 280  (W/V) POLYETHYLENE GLYCOL (PEG) PEG3350, AND 0.15 M                 
REMARK 280  AMMONIUM DIHYDROGEN CITRATE AT 37 DEG. C. PROTEIN AT 9.5            
REMARK 280  MG/ML                                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       53.42000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     TYR A   135                                                      
REMARK 465     GLY A   136                                                      
REMARK 465     ASP A   137                                                      
REMARK 465     VAL A   138                                                      
REMARK 465     TYR A   139                                                      
REMARK 465     TYR A   270                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     THR A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     THR A   310                                                      
REMARK 465     ARG A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     TYR A   313                                                      
REMARK 465     TYR A   314                                                      
REMARK 465     LYS A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     LEU A   317                                                      
REMARK 465     LYS A   318                                                      
REMARK 465     GLY A   319                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     ALA A   402                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     TYR B   135                                                      
REMARK 465     GLY B   136                                                      
REMARK 465     ASP B   137                                                      
REMARK 465     VAL B   138                                                      
REMARK 465     TYR B   139                                                      
REMARK 465     LYS B   210                                                      
REMARK 465     ASP B   211                                                      
REMARK 465     THR B   212                                                      
REMARK 465     ILE B   213                                                      
REMARK 465     SER B   214                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     GLY B   307                                                      
REMARK 465     THR B   308                                                      
REMARK 465     VAL B   309                                                      
REMARK 465     THR B   310                                                      
REMARK 465     ARG B   311                                                      
REMARK 465     HIS B   312                                                      
REMARK 465     TYR B   313                                                      
REMARK 465     TYR B   314                                                      
REMARK 465     LYS B   315                                                      
REMARK 465     HIS B   316                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     LYS B   318                                                      
REMARK 465     GLY B   319                                                      
REMARK 465     GLU B   320                                                      
REMARK 465     GLU B   321                                                      
REMARK 465     ALA B   402                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C   134                                                      
REMARK 465     TYR C   135                                                      
REMARK 465     GLY C   136                                                      
REMARK 465     ASP C   137                                                      
REMARK 465     VAL C   138                                                      
REMARK 465     TYR C   139                                                      
REMARK 465     LYS C   140                                                      
REMARK 465     TYR C   270                                                      
REMARK 465     ASP C   271                                                      
REMARK 465     GLY C   272                                                      
REMARK 465     HIS C   306                                                      
REMARK 465     GLY C   307                                                      
REMARK 465     THR C   308                                                      
REMARK 465     VAL C   309                                                      
REMARK 465     THR C   310                                                      
REMARK 465     ARG C   311                                                      
REMARK 465     HIS C   312                                                      
REMARK 465     TYR C   313                                                      
REMARK 465     TYR C   314                                                      
REMARK 465     LYS C   315                                                      
REMARK 465     HIS C   316                                                      
REMARK 465     LEU C   317                                                      
REMARK 465     LYS C   318                                                      
REMARK 465     GLY C   319                                                      
REMARK 465     GLU C   320                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     THR C   322                                                      
REMARK 465     SER C   323                                                      
REMARK 465     THR C   324                                                      
REMARK 465     ALA C   402                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D   138                                                      
REMARK 465     TYR D   139                                                      
REMARK 465     LYS D   140                                                      
REMARK 465     TYR D   270                                                      
REMARK 465     ASP D   271                                                      
REMARK 465     GLY D   272                                                      
REMARK 465     HIS D   306                                                      
REMARK 465     GLY D   307                                                      
REMARK 465     THR D   308                                                      
REMARK 465     VAL D   309                                                      
REMARK 465     THR D   310                                                      
REMARK 465     ARG D   311                                                      
REMARK 465     HIS D   312                                                      
REMARK 465     TYR D   313                                                      
REMARK 465     TYR D   314                                                      
REMARK 465     LYS D   315                                                      
REMARK 465     HIS D   316                                                      
REMARK 465     LEU D   317                                                      
REMARK 465     LYS D   318                                                      
REMARK 465     GLY D   319                                                      
REMARK 465     GLU D   320                                                      
REMARK 465     GLU D   321                                                      
REMARK 465     THR D   322                                                      
REMARK 465     SER D   323                                                      
REMARK 465     THR D   324                                                      
REMARK 465     ALA D   402                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  36    CD   OE1  OE2                                       
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  51    CE   NZ                                             
REMARK 470     LYS A  93    CD   CE   NZ                                        
REMARK 470     LYS A 122    CG   CD   CE   NZ                                   
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     LYS A 185    CD   CE   NZ                                        
REMARK 470     LYS A 215    CD   CE   NZ                                        
REMARK 470     TYR A 217    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     GLU A 227    CD   OE1  OE2                                       
REMARK 470     LYS A 234    CD   CE   NZ                                        
REMARK 470     GLU A 235    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 249    CD1                                                 
REMARK 470     GLU A 260    CD   OE1  OE2                                       
REMARK 470     LYS A 268    CD   CE   NZ                                        
REMARK 470     ASP A 271    CB   CG   OD1  OD2                                  
REMARK 470     MET A 278    CG   SD   CE                                        
REMARK 470     LEU A 286    CB   CG   CD1  CD2                                  
REMARK 470     GLU A 365    CD   OE1  OE2                                       
REMARK 470     LYS A 371    CG   CD   CE   NZ                                   
REMARK 470     LEU A 376    CG   CD1  CD2                                       
REMARK 470     GLU A 381    CD   OE1  OE2                                       
REMARK 470     LYS A 383    CB   CG   CD   CE   NZ                              
REMARK 470     THR A 387    CB   OG1  CG2                                       
REMARK 470     LYS A 396    CD   CE   NZ                                        
REMARK 470     LYS B   7    CG   CD   CE   NZ                                   
REMARK 470     GLU B  36    CD   OE1  OE2                                       
REMARK 470     LYS B  93    CD   CE   NZ                                        
REMARK 470     ARG B 100    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 118    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 122    CE   NZ                                             
REMARK 470     LYS B 125    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 140    CD   CE   NZ                                        
REMARK 470     LYS B 185    CD   CE   NZ                                        
REMARK 470     ILE B 187    CD1                                                 
REMARK 470     ARG B 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 234    CD   CE   NZ                                        
REMARK 470     GLU B 235    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN B 241    CB   CG   OD1  ND2                                  
REMARK 470     LEU B 248    CB   CG   CD1  CD2                                  
REMARK 470     ILE B 249    CD1                                                 
REMARK 470     GLU B 260    CG   CD   OE1  OE2                                  
REMARK 470     CYS B 267    CB   SG                                             
REMARK 470     LYS B 268    CG   CD   CE   NZ                                   
REMARK 470     TYR B 270    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR B 270    OH                                                  
REMARK 470     MET B 278    SD   CE                                             
REMARK 470     LEU B 286    CB   CG   CD1  CD2                                  
REMARK 470     GLU B 303    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 371    CD   CE   NZ                                        
REMARK 470     LEU B 376    CB   CG   CD1  CD2                                  
REMARK 470     GLU B 378    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU B 381    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B 382    CE   NZ                                             
REMARK 470     LYS B 383    CG   CD   CE   NZ                                   
REMARK 470     ASP B 389    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 396    CD   CE   NZ                                        
REMARK 470     LYS C   5    CD   CE   NZ                                        
REMARK 470     LYS C   7    CE   NZ                                             
REMARK 470     GLN C  81    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG C  82    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     VAL C  83    CB   CG1  CG2                                       
REMARK 470     GLU C  84    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU C  85    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS C  90    CD   CE   NZ                                        
REMARK 470     LYS C  93    CD   CE   NZ                                        
REMARK 470     ARG C 109    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C 118    CD   CE   NZ                                        
REMARK 470     LYS C 122    CG   CD   CE   NZ                                   
REMARK 470     ASN C 141    CG   OD1  ND2                                       
REMARK 470     GLU C 159    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 213    CG1  CD1                                            
REMARK 470     LYS C 215    CD   CE   NZ                                        
REMARK 470     VAL C 274    CB   CG1  CG2                                       
REMARK 470     MET C 275    CG   SD   CE                                        
REMARK 470     MET C 278    SD   CE                                             
REMARK 470     LEU C 286    CG   CD1  CD2                                       
REMARK 470     GLU C 342    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 347    CG   CD   CE   NZ                                   
REMARK 470     GLU C 348    CD   OE1  OE2                                       
REMARK 470     LYS D   5    CD   CE   NZ                                        
REMARK 470     GLU D  36    CD   OE1  OE2                                       
REMARK 470     GLU D  47    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  85    CB   CG   CD   OE1  OE2                             
REMARK 470     ARG D 109    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 122    CB   CG   CD   CE   NZ                              
REMARK 470     LYS D 125    CD   CE   NZ                                        
REMARK 470     LYS D 126    CE   NZ                                             
REMARK 470     ASP D 137    CB   CG   OD1  OD2                                  
REMARK 470     GLU D 159    CD   OE1  OE2                                       
REMARK 470     LYS D 210    CG   CD   CE   NZ                                   
REMARK 470     LYS D 215    CB   CG   CD   CE   NZ                              
REMARK 470     ASP D 250    CG   OD1  OD2                                       
REMARK 470     ASN D 269    CB   CG   OD1  ND2                                  
REMARK 470     MET D 275    CB   CG   SD   CE                                   
REMARK 470     MET D 278    CG   SD   CE                                        
REMARK 470     LYS D 371    CE   NZ                                             
REMARK 470     LYS D 396    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA B   149     O    PHE B   171              1.93            
REMARK 500   OD1  ASN A   202     NZ   LYS A   240              1.95            
REMARK 500   OG   SER B   158     ND2  ASN B   160              2.07            
REMARK 500   O    LYS B   215     ND1  HIS B   219              2.14            
REMARK 500   NE2  GLN A   362     OD1  ASN A   366              2.15            
REMARK 500   OD2  ASP D   200     NZ   LYS D   339              2.17            
REMARK 500   O    VAL D    83     N    ASN D    87              2.19            
REMARK 500   NE2  GLN D   203     O    HOH D  2014              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS C 267   CB    CYS C 267   SG     -0.114                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 380   C   -  N   -  CA  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    MET B  13   CG  -  SD  -  CE  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ALA B 149   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    GLY B 150   N   -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500    PRO B 380   C   -  N   -  CA  ANGL. DEV. = -27.0 DEGREES          
REMARK 500    PRO B 380   C   -  N   -  CD  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    GLY B 400   N   -  CA  -  C   ANGL. DEV. = -15.6 DEGREES          
REMARK 500    ASP C 297   CB  -  CG  -  OD1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    PRO C 380   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500    PRO D  78   C   -  N   -  CA  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    PRO D  78   C   -  N   -  CD  ANGL. DEV. = -13.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   7      -91.37   -116.40                                   
REMARK 500    GLU A  17     -131.73     65.28                                   
REMARK 500    ASN A  79     -169.86   -124.54                                   
REMARK 500    TRP A  92      132.48    -35.64                                   
REMARK 500    SER A  94      126.20    -38.72                                   
REMARK 500    SER A 148       21.70    178.05                                   
REMARK 500    ALA A 149      129.84    105.96                                   
REMARK 500    HIS A 169      145.46   -179.25                                   
REMARK 500    ASP A 211      -14.18    -49.18                                   
REMARK 500    TYR A 233      -12.18   -144.19                                   
REMARK 500    THR A 247     -179.65   -170.60                                   
REMARK 500    MET A 288       47.33   -100.81                                   
REMARK 500    ILE A 346       73.55   -113.18                                   
REMARK 500    VAL A 379      -47.84   -143.42                                   
REMARK 500    PRO A 380     -114.35   -168.98                                   
REMARK 500    GLU A 399       64.19    -65.15                                   
REMARK 500    LYS B   7      -84.20   -107.67                                   
REMARK 500    GLU B  17     -114.49     58.24                                   
REMARK 500    ASN B  79     -167.76   -112.10                                   
REMARK 500    LYS B 122      -80.16    -10.28                                   
REMARK 500    SER B 148     -176.29   -176.58                                   
REMARK 500    HIS B 169      143.35   -177.64                                   
REMARK 500    ASP B 200      -31.65    -39.07                                   
REMARK 500    TYR B 233      -38.72   -133.15                                   
REMARK 500    LYS B 234      -54.44    -26.68                                   
REMARK 500    THR B 247     -175.39   -174.21                                   
REMARK 500    SER B 259     -169.74   -105.65                                   
REMARK 500    ASN B 269      179.57    -55.27                                   
REMARK 500    TYR B 270      -43.29     70.97                                   
REMARK 500    VAL B 274      -72.22    -68.21                                   
REMARK 500    SER B 285      118.55    113.80                                   
REMARK 500    MET B 288       44.60    -90.79                                   
REMARK 500    LEU B 376      -71.87    -91.49                                   
REMARK 500    GLU B 378     -106.32    -82.35                                   
REMARK 500    VAL B 379       76.80     33.26                                   
REMARK 500    PRO B 380     -176.48    159.58                                   
REMARK 500    GLU B 399       91.61    -59.03                                   
REMARK 500    LYS C   7      -69.59   -106.16                                   
REMARK 500    GLU C  17     -124.52     51.53                                   
REMARK 500    LEU C  31      -64.44   -108.58                                   
REMARK 500    ASP C  54        3.60     80.63                                   
REMARK 500    ASN C  79     -156.93   -119.03                                   
REMARK 500    ASN C  87       78.78     33.74                                   
REMARK 500    THR C 216      -51.56   -130.75                                   
REMARK 500    SER C 259     -166.97   -104.82                                   
REMARK 500    VAL C 274      -20.23    135.87                                   
REMARK 500    SER C 285      122.48    144.07                                   
REMARK 500    ASP C 297      -28.36    -36.63                                   
REMARK 500    LYS D   7      -91.75   -120.30                                   
REMARK 500    GLU D  17     -133.59     43.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  379     PRO A  380                 -146.01                    
REMARK 500 PRO B  380     GLU B  381                  138.74                    
REMARK 500 ASP C  273     VAL C  274                 -143.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A 211        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ALA B 149        20.3      L          L   OUTSIDE RANGE           
REMARK 500    THR B 329        22.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4AOU   RELATED DB: PDB                                   
REMARK 900  CTIDH BOUND TO NADP. THE COMPLEX STRUCTURES OF                      
REMARK 900  ISOCITRATE DEHYDROGENASE FROM CLOSTRIDIUM THERMOCELLUM AND          
REMARK 900  DESULFOTALEA PSYCHROPHILA, SUPPORT A NEW ACTIVE SITE                
REMARK 900  LOCKING MECHANISM                                                   
REMARK 900 RELATED ID: 4AOV   RELATED DB: PDB                                   
REMARK 900  DPIDH-NADP. THE COMPLEX STRUCTURES OF ISOCITRATE                    
REMARK 900  DEHYDROGENASE FROM CLOSTRIDIUM THERMOCELLUM AND DESULFOTALEA        
REMARK 900   PSYCHROPHILA, SUPPORT A NEW ACTIVE SITE LOCKING                    
REMARK 900  MECHANISM                                                           
DBREF  4AOY A    1   402  UNP    D1NLE9   D1NLE9_CLOTM     1    402             
DBREF  4AOY B    1   402  UNP    D1NLE9   D1NLE9_CLOTM     1    402             
DBREF  4AOY C    1   402  UNP    D1NLE9   D1NLE9_CLOTM     1    402             
DBREF  4AOY D    1   402  UNP    D1NLE9   D1NLE9_CLOTM     1    402             
SEQRES   1 A  402  MET SER LYS ILE LYS MET LYS VAL PRO LEU VAL GLU MET          
SEQRES   2 A  402  ASP GLY ASP GLU MET THR ARG ILE ILE TRP ARG LEU ILE          
SEQRES   3 A  402  LYS GLU ASN LEU LEU GLU PRO TYR ILE GLU LEU ASN THR          
SEQRES   4 A  402  GLU TYR TYR ASP LEU GLY LEU GLU ASN ARG ASP LYS THR          
SEQRES   5 A  402  GLU ASP GLN VAL THR ILE ASP ALA ALA ARG ALA ILE GLN          
SEQRES   6 A  402  LYS TYR GLY VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 A  402  ASN ALA GLN ARG VAL GLU GLU TYR ASN LEU LYS LYS MET          
SEQRES   8 A  402  TRP LYS SER PRO ASN GLY THR ILE ARG ALA ILE LEU ASP          
SEQRES   9 A  402  GLY THR VAL PHE ARG ALA PRO ILE VAL VAL ASN SER ILE          
SEQRES  10 A  402  LYS PRO PHE VAL LYS GLY TRP LYS LYS PRO ILE SER ILE          
SEQRES  11 A  402  ALA ARG HIS ALA TYR GLY ASP VAL TYR LYS ASN VAL GLU          
SEQRES  12 A  402  TYR TYR VAL PRO SER ALA GLY LYS ALA GLU LEU VAL PHE          
SEQRES  13 A  402  THR SER GLU ASN GLY GLU VAL SER ARG GLN THR ILE HIS          
SEQRES  14 A  402  GLU PHE ASP GLY PRO GLY VAL ILE MET GLY MET HIS ASN          
SEQRES  15 A  402  THR ASP LYS SER ILE ARG SER PHE ALA ARG ALA CYS PHE          
SEQRES  16 A  402  ASN TYR ALA LEU ASP MET ASN GLN ASP LEU TRP PHE SER          
SEQRES  17 A  402  THR LYS ASP THR ILE SER LYS THR TYR ASP HIS ARG PHE          
SEQRES  18 A  402  LYS ASP ILE PHE GLN GLU ILE TYR GLU ASN GLU TYR LYS          
SEQRES  19 A  402  GLU LYS PHE GLU ALA LYS ASN LEU GLN TYR PHE TYR THR          
SEQRES  20 A  402  LEU ILE ASP ASP ALA VAL ALA ARG ILE ILE ARG SER GLU          
SEQRES  21 A  402  GLY GLY MET VAL TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 A  402  VAL MET SER ASP MET VAL ALA SER ALA PHE GLY SER LEU          
SEQRES  23 A  402  ALA MET MET THR SER VAL LEU VAL SER PRO ASP GLY LYS          
SEQRES  24 A  402  TYR GLU PHE GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 A  402  TYR TYR LYS HIS LEU LYS GLY GLU GLU THR SER THR ASN          
SEQRES  26 A  402  SER MET ALA THR ILE PHE ALA TRP THR GLY ALA LEU LYS          
SEQRES  27 A  402  LYS ARG GLY GLU LEU ASP GLY ILE LYS GLU LEU VAL ASP          
SEQRES  28 A  402  PHE ALA THR LYS LEU GLU GLN ALA SER VAL GLN THR ILE          
SEQRES  29 A  402  GLU ASN GLY VAL MET THR LYS ASP LEU ALA SER LEU SER          
SEQRES  30 A  402  GLU VAL PRO GLU LYS LYS ILE VAL ASN THR GLU ASP PHE          
SEQRES  31 A  402  LEU LYS GLU ILE ARG LYS THR PHE GLU GLY MET ALA              
SEQRES   1 B  402  MET SER LYS ILE LYS MET LYS VAL PRO LEU VAL GLU MET          
SEQRES   2 B  402  ASP GLY ASP GLU MET THR ARG ILE ILE TRP ARG LEU ILE          
SEQRES   3 B  402  LYS GLU ASN LEU LEU GLU PRO TYR ILE GLU LEU ASN THR          
SEQRES   4 B  402  GLU TYR TYR ASP LEU GLY LEU GLU ASN ARG ASP LYS THR          
SEQRES   5 B  402  GLU ASP GLN VAL THR ILE ASP ALA ALA ARG ALA ILE GLN          
SEQRES   6 B  402  LYS TYR GLY VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 B  402  ASN ALA GLN ARG VAL GLU GLU TYR ASN LEU LYS LYS MET          
SEQRES   8 B  402  TRP LYS SER PRO ASN GLY THR ILE ARG ALA ILE LEU ASP          
SEQRES   9 B  402  GLY THR VAL PHE ARG ALA PRO ILE VAL VAL ASN SER ILE          
SEQRES  10 B  402  LYS PRO PHE VAL LYS GLY TRP LYS LYS PRO ILE SER ILE          
SEQRES  11 B  402  ALA ARG HIS ALA TYR GLY ASP VAL TYR LYS ASN VAL GLU          
SEQRES  12 B  402  TYR TYR VAL PRO SER ALA GLY LYS ALA GLU LEU VAL PHE          
SEQRES  13 B  402  THR SER GLU ASN GLY GLU VAL SER ARG GLN THR ILE HIS          
SEQRES  14 B  402  GLU PHE ASP GLY PRO GLY VAL ILE MET GLY MET HIS ASN          
SEQRES  15 B  402  THR ASP LYS SER ILE ARG SER PHE ALA ARG ALA CYS PHE          
SEQRES  16 B  402  ASN TYR ALA LEU ASP MET ASN GLN ASP LEU TRP PHE SER          
SEQRES  17 B  402  THR LYS ASP THR ILE SER LYS THR TYR ASP HIS ARG PHE          
SEQRES  18 B  402  LYS ASP ILE PHE GLN GLU ILE TYR GLU ASN GLU TYR LYS          
SEQRES  19 B  402  GLU LYS PHE GLU ALA LYS ASN LEU GLN TYR PHE TYR THR          
SEQRES  20 B  402  LEU ILE ASP ASP ALA VAL ALA ARG ILE ILE ARG SER GLU          
SEQRES  21 B  402  GLY GLY MET VAL TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 B  402  VAL MET SER ASP MET VAL ALA SER ALA PHE GLY SER LEU          
SEQRES  23 B  402  ALA MET MET THR SER VAL LEU VAL SER PRO ASP GLY LYS          
SEQRES  24 B  402  TYR GLU PHE GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 B  402  TYR TYR LYS HIS LEU LYS GLY GLU GLU THR SER THR ASN          
SEQRES  26 B  402  SER MET ALA THR ILE PHE ALA TRP THR GLY ALA LEU LYS          
SEQRES  27 B  402  LYS ARG GLY GLU LEU ASP GLY ILE LYS GLU LEU VAL ASP          
SEQRES  28 B  402  PHE ALA THR LYS LEU GLU GLN ALA SER VAL GLN THR ILE          
SEQRES  29 B  402  GLU ASN GLY VAL MET THR LYS ASP LEU ALA SER LEU SER          
SEQRES  30 B  402  GLU VAL PRO GLU LYS LYS ILE VAL ASN THR GLU ASP PHE          
SEQRES  31 B  402  LEU LYS GLU ILE ARG LYS THR PHE GLU GLY MET ALA              
SEQRES   1 C  402  MET SER LYS ILE LYS MET LYS VAL PRO LEU VAL GLU MET          
SEQRES   2 C  402  ASP GLY ASP GLU MET THR ARG ILE ILE TRP ARG LEU ILE          
SEQRES   3 C  402  LYS GLU ASN LEU LEU GLU PRO TYR ILE GLU LEU ASN THR          
SEQRES   4 C  402  GLU TYR TYR ASP LEU GLY LEU GLU ASN ARG ASP LYS THR          
SEQRES   5 C  402  GLU ASP GLN VAL THR ILE ASP ALA ALA ARG ALA ILE GLN          
SEQRES   6 C  402  LYS TYR GLY VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 C  402  ASN ALA GLN ARG VAL GLU GLU TYR ASN LEU LYS LYS MET          
SEQRES   8 C  402  TRP LYS SER PRO ASN GLY THR ILE ARG ALA ILE LEU ASP          
SEQRES   9 C  402  GLY THR VAL PHE ARG ALA PRO ILE VAL VAL ASN SER ILE          
SEQRES  10 C  402  LYS PRO PHE VAL LYS GLY TRP LYS LYS PRO ILE SER ILE          
SEQRES  11 C  402  ALA ARG HIS ALA TYR GLY ASP VAL TYR LYS ASN VAL GLU          
SEQRES  12 C  402  TYR TYR VAL PRO SER ALA GLY LYS ALA GLU LEU VAL PHE          
SEQRES  13 C  402  THR SER GLU ASN GLY GLU VAL SER ARG GLN THR ILE HIS          
SEQRES  14 C  402  GLU PHE ASP GLY PRO GLY VAL ILE MET GLY MET HIS ASN          
SEQRES  15 C  402  THR ASP LYS SER ILE ARG SER PHE ALA ARG ALA CYS PHE          
SEQRES  16 C  402  ASN TYR ALA LEU ASP MET ASN GLN ASP LEU TRP PHE SER          
SEQRES  17 C  402  THR LYS ASP THR ILE SER LYS THR TYR ASP HIS ARG PHE          
SEQRES  18 C  402  LYS ASP ILE PHE GLN GLU ILE TYR GLU ASN GLU TYR LYS          
SEQRES  19 C  402  GLU LYS PHE GLU ALA LYS ASN LEU GLN TYR PHE TYR THR          
SEQRES  20 C  402  LEU ILE ASP ASP ALA VAL ALA ARG ILE ILE ARG SER GLU          
SEQRES  21 C  402  GLY GLY MET VAL TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 C  402  VAL MET SER ASP MET VAL ALA SER ALA PHE GLY SER LEU          
SEQRES  23 C  402  ALA MET MET THR SER VAL LEU VAL SER PRO ASP GLY LYS          
SEQRES  24 C  402  TYR GLU PHE GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 C  402  TYR TYR LYS HIS LEU LYS GLY GLU GLU THR SER THR ASN          
SEQRES  26 C  402  SER MET ALA THR ILE PHE ALA TRP THR GLY ALA LEU LYS          
SEQRES  27 C  402  LYS ARG GLY GLU LEU ASP GLY ILE LYS GLU LEU VAL ASP          
SEQRES  28 C  402  PHE ALA THR LYS LEU GLU GLN ALA SER VAL GLN THR ILE          
SEQRES  29 C  402  GLU ASN GLY VAL MET THR LYS ASP LEU ALA SER LEU SER          
SEQRES  30 C  402  GLU VAL PRO GLU LYS LYS ILE VAL ASN THR GLU ASP PHE          
SEQRES  31 C  402  LEU LYS GLU ILE ARG LYS THR PHE GLU GLY MET ALA              
SEQRES   1 D  402  MET SER LYS ILE LYS MET LYS VAL PRO LEU VAL GLU MET          
SEQRES   2 D  402  ASP GLY ASP GLU MET THR ARG ILE ILE TRP ARG LEU ILE          
SEQRES   3 D  402  LYS GLU ASN LEU LEU GLU PRO TYR ILE GLU LEU ASN THR          
SEQRES   4 D  402  GLU TYR TYR ASP LEU GLY LEU GLU ASN ARG ASP LYS THR          
SEQRES   5 D  402  GLU ASP GLN VAL THR ILE ASP ALA ALA ARG ALA ILE GLN          
SEQRES   6 D  402  LYS TYR GLY VAL GLY VAL LYS CYS ALA THR ILE THR PRO          
SEQRES   7 D  402  ASN ALA GLN ARG VAL GLU GLU TYR ASN LEU LYS LYS MET          
SEQRES   8 D  402  TRP LYS SER PRO ASN GLY THR ILE ARG ALA ILE LEU ASP          
SEQRES   9 D  402  GLY THR VAL PHE ARG ALA PRO ILE VAL VAL ASN SER ILE          
SEQRES  10 D  402  LYS PRO PHE VAL LYS GLY TRP LYS LYS PRO ILE SER ILE          
SEQRES  11 D  402  ALA ARG HIS ALA TYR GLY ASP VAL TYR LYS ASN VAL GLU          
SEQRES  12 D  402  TYR TYR VAL PRO SER ALA GLY LYS ALA GLU LEU VAL PHE          
SEQRES  13 D  402  THR SER GLU ASN GLY GLU VAL SER ARG GLN THR ILE HIS          
SEQRES  14 D  402  GLU PHE ASP GLY PRO GLY VAL ILE MET GLY MET HIS ASN          
SEQRES  15 D  402  THR ASP LYS SER ILE ARG SER PHE ALA ARG ALA CYS PHE          
SEQRES  16 D  402  ASN TYR ALA LEU ASP MET ASN GLN ASP LEU TRP PHE SER          
SEQRES  17 D  402  THR LYS ASP THR ILE SER LYS THR TYR ASP HIS ARG PHE          
SEQRES  18 D  402  LYS ASP ILE PHE GLN GLU ILE TYR GLU ASN GLU TYR LYS          
SEQRES  19 D  402  GLU LYS PHE GLU ALA LYS ASN LEU GLN TYR PHE TYR THR          
SEQRES  20 D  402  LEU ILE ASP ASP ALA VAL ALA ARG ILE ILE ARG SER GLU          
SEQRES  21 D  402  GLY GLY MET VAL TRP ALA CYS LYS ASN TYR ASP GLY ASP          
SEQRES  22 D  402  VAL MET SER ASP MET VAL ALA SER ALA PHE GLY SER LEU          
SEQRES  23 D  402  ALA MET MET THR SER VAL LEU VAL SER PRO ASP GLY LYS          
SEQRES  24 D  402  TYR GLU PHE GLU ALA ALA HIS GLY THR VAL THR ARG HIS          
SEQRES  25 D  402  TYR TYR LYS HIS LEU LYS GLY GLU GLU THR SER THR ASN          
SEQRES  26 D  402  SER MET ALA THR ILE PHE ALA TRP THR GLY ALA LEU LYS          
SEQRES  27 D  402  LYS ARG GLY GLU LEU ASP GLY ILE LYS GLU LEU VAL ASP          
SEQRES  28 D  402  PHE ALA THR LYS LEU GLU GLN ALA SER VAL GLN THR ILE          
SEQRES  29 D  402  GLU ASN GLY VAL MET THR LYS ASP LEU ALA SER LEU SER          
SEQRES  30 D  402  GLU VAL PRO GLU LYS LYS ILE VAL ASN THR GLU ASP PHE          
SEQRES  31 D  402  LEU LYS GLU ILE ARG LYS THR PHE GLU GLY MET ALA              
FORMUL   5  HOH   *88(H2 O)                                                     
HELIX    1   1 ASP A   16  LEU A   31  1                                  16    
HELIX    2   2 GLY A   45  GLU A   53  1                                   9    
HELIX    3   3 ASP A   54  GLY A   68  1                                  15    
HELIX    4   4 ASN A   79  TYR A   86  1                                   8    
HELIX    5   5 SER A   94  ASP A  104  1                                  11    
HELIX    6   6 ASP A  184  MET A  201  1                                  18    
HELIX    7   7 SER A  214  TYR A  233  1                                  20    
HELIX    8   8 TYR A  233  LYS A  240  1                                   8    
HELIX    9   9 ILE A  249  ARG A  258  1                                  10    
HELIX   10  10 ASP A  271  GLY A  284  1                                  14    
HELIX   11  11 SER A  326  ASP A  344  1                                  19    
HELIX   12  12 ILE A  346  ASN A  366  1                                  21    
HELIX   13  13 LYS A  371  SER A  375  1                                   5    
HELIX   14  14 ASN A  386  GLU A  399  1                                  14    
HELIX   15  15 ASP B   16  LEU B   31  1                                  16    
HELIX   16  16 GLY B   45  THR B   52  1                                   8    
HELIX   17  17 ASP B   54  GLY B   68  1                                  15    
HELIX   18  18 ASN B   79  ASN B   87  1                                   9    
HELIX   19  19 SER B   94  ASP B  104  1                                  11    
HELIX   20  20 ASP B  184  MET B  201  1                                  18    
HELIX   21  21 THR B  216  TYR B  233  1                                  18    
HELIX   22  22 TYR B  233  ALA B  239  1                                   7    
HELIX   23  23 ILE B  249  ARG B  258  1                                  10    
HELIX   24  24 TYR B  270  GLY B  284  1                                  15    
HELIX   25  25 SER B  326  ASP B  344  1                                  19    
HELIX   26  26 ILE B  346  ASN B  366  1                                  21    
HELIX   27  27 LYS B  371  SER B  375  1                                   5    
HELIX   28  28 ASN B  386  GLU B  399  1                                  14    
HELIX   29  29 ASP C   16  LEU C   31  1                                  16    
HELIX   30  30 GLY C   45  THR C   52  1                                   8    
HELIX   31  31 ASP C   54  GLY C   68  1                                  15    
HELIX   32  32 GLN C   81  TYR C   86  1                                   6    
HELIX   33  33 SER C   94  ASP C  104  1                                  11    
HELIX   34  34 ASP C  184  ASN C  202  1                                  19    
HELIX   35  35 THR C  216  TYR C  233  1                                  18    
HELIX   36  36 TYR C  233  LYS C  240  1                                   8    
HELIX   37  37 ILE C  249  ARG C  258  1                                  10    
HELIX   38  38 VAL C  274  GLY C  284  1                                  11    
HELIX   39  39 ASN C  325  GLY C  345  1                                  21    
HELIX   40  40 ILE C  346  ASN C  366  1                                  21    
HELIX   41  41 THR C  370  SER C  375  1                                   6    
HELIX   42  42 ASN C  386  MET C  401  1                                  16    
HELIX   43  43 ASP D   16  LEU D   31  1                                  16    
HELIX   44  44 GLY D   45  THR D   52  1                                   8    
HELIX   45  45 ASP D   54  GLY D   68  1                                  15    
HELIX   46  46 ASN D   79  ASN D   87  1                                   9    
HELIX   47  47 SER D   94  LEU D  103  1                                  10    
HELIX   48  48 ASP D  184  ASN D  202  1                                  19    
HELIX   49  49 THR D  216  TYR D  233  1                                  18    
HELIX   50  50 TYR D  233  LYS D  240  1                                   8    
HELIX   51  51 ILE D  249  ARG D  258  1                                  10    
HELIX   52  52 VAL D  274  GLY D  284  1                                  11    
HELIX   53  53 ASN D  325  GLY D  345  1                                  21    
HELIX   54  54 ILE D  346  ASN D  366  1                                  21    
HELIX   55  55 THR D  370  SER D  377  1                                   8    
HELIX   56  56 ASN D  386  MET D  401  1                                  16    
SHEET    1  AA 2 ILE A   4  LYS A   5  0                                        
SHEET    2  AA 2 ILE A  35  GLU A  36  1  N  GLU A  36   O  ILE A   4           
SHEET    1  AB10 THR A  39  ASP A  43  0                                        
SHEET    2  AB10 LEU A  10  ASP A  14  1  O  LEU A  10   N  GLU A  40           
SHEET    3  AB10 VAL A  69  LYS A  72  1  O  VAL A  69   N  VAL A  11           
SHEET    4  AB10 TYR A 300  GLU A 303  1  O  TYR A 300   N  GLY A  70           
SHEET    5  AB10 MET A 289  VAL A 294 -1  O  SER A 291   N  GLU A 303           
SHEET    6  AB10 THR A 106  PRO A 111 -1  O  THR A 106   N  VAL A 294           
SHEET    7  AB10 SER A 129  ARG A 132 -1  O  ILE A 130   N  ARG A 109           
SHEET    8  AB10 VAL A 264  ALA A 266  1  O  TRP A 265   N  ALA A 131           
SHEET    9  AB10 LEU A 205  THR A 209  1  O  TRP A 206   N  ALA A 266           
SHEET   10  AB10 TYR A 244  LEU A 248  1  O  PHE A 245   N  PHE A 207           
SHEET    1  AC 4 VAL A 142  VAL A 146  0                                        
SHEET    2  AC 4 GLY A 175  THR A 183 -1  O  GLY A 175   N  VAL A 146           
SHEET    3  AC 4 GLY C 175  THR C 183 -1  O  VAL C 176   N  ASN A 182           
SHEET    4  AC 4 VAL C 142  VAL C 146 -1  O  VAL C 142   N  GLY C 179           
SHEET    1  AD 4 VAL A 163  PHE A 171  0                                        
SHEET    2  AD 4 GLY A 150  SER A 158 -1  O  GLY A 150   N  PHE A 171           
SHEET    3  AD 4 GLY C 150  SER C 158 -1  O  LYS C 151   N  THR A 157           
SHEET    4  AD 4 VAL C 163  PHE C 171 -1  O  SER C 164   N  PHE C 156           
SHEET    1  AE 2 VAL A 368  THR A 370  0                                        
SHEET    2  AE 2 LYS A 383  VAL A 385  1  O  LYS A 383   N  MET A 369           
SHEET    1  BA10 THR B  39  ASP B  43  0                                        
SHEET    2  BA10 LEU B  10  ASP B  14  1  O  LEU B  10   N  GLU B  40           
SHEET    3  BA10 VAL B  69  LYS B  72  1  O  VAL B  69   N  VAL B  11           
SHEET    4  BA10 TYR B 300  ALA B 304  1  O  TYR B 300   N  GLY B  70           
SHEET    5  BA10 MET B 289  VAL B 294 -1  O  SER B 291   N  GLU B 303           
SHEET    6  BA10 THR B 106  PRO B 111 -1  O  THR B 106   N  VAL B 294           
SHEET    7  BA10 SER B 129  ARG B 132 -1  O  ILE B 130   N  ARG B 109           
SHEET    8  BA10 VAL B 264  ALA B 266  1  O  TRP B 265   N  ALA B 131           
SHEET    9  BA10 LEU B 205  THR B 209  1  O  TRP B 206   N  ALA B 266           
SHEET   10  BA10 TYR B 244  LEU B 248  1  O  PHE B 245   N  PHE B 207           
SHEET    1  BB 4 VAL B 142  VAL B 146  0                                        
SHEET    2  BB 4 GLY B 175  THR B 183 -1  O  GLY B 175   N  VAL B 146           
SHEET    3  BB 4 GLY D 175  THR D 183 -1  O  VAL D 176   N  ASN B 182           
SHEET    4  BB 4 VAL D 142  VAL D 146 -1  O  VAL D 142   N  GLY D 179           
SHEET    1  BC 4 VAL B 163  GLU B 170  0                                        
SHEET    2  BC 4 LYS B 151  SER B 158 -1  O  ALA B 152   N  ILE B 168           
SHEET    3  BC 4 GLY D 150  THR D 157 -1  O  LYS D 151   N  THR B 157           
SHEET    4  BC 4 VAL D 163  PHE D 171 -1  O  SER D 164   N  PHE D 156           
SHEET    1  BD 2 VAL B 368  THR B 370  0                                        
SHEET    2  BD 2 LYS B 383  VAL B 385  1  O  LYS B 383   N  MET B 369           
SHEET    1  CA 2 ILE C   4  LYS C   5  0                                        
SHEET    2  CA 2 ILE C  35  GLU C  36  1  N  GLU C  36   O  ILE C   4           
SHEET    1  CB10 THR C  39  ASP C  43  0                                        
SHEET    2  CB10 LEU C  10  ASP C  14  1  O  LEU C  10   N  GLU C  40           
SHEET    3  CB10 VAL C  69  LYS C  72  1  O  VAL C  69   N  VAL C  11           
SHEET    4  CB10 TYR C 300  ALA C 304  1  O  TYR C 300   N  GLY C  70           
SHEET    5  CB10 MET C 289  VAL C 294 -1  O  SER C 291   N  GLU C 303           
SHEET    6  CB10 THR C 106  PRO C 111 -1  O  THR C 106   N  VAL C 294           
SHEET    7  CB10 SER C 129  ARG C 132 -1  O  ILE C 130   N  ARG C 109           
SHEET    8  CB10 VAL C 264  ALA C 266  1  O  TRP C 265   N  ALA C 131           
SHEET    9  CB10 LEU C 205  THR C 209  1  O  TRP C 206   N  ALA C 266           
SHEET   10  CB10 TYR C 244  LEU C 248  1  O  PHE C 245   N  PHE C 207           
SHEET    1  CC 2 VAL C 368  MET C 369  0                                        
SHEET    2  CC 2 LYS C 383  ILE C 384  1  O  LYS C 383   N  MET C 369           
SHEET    1  DA 2 ILE D   4  LYS D   5  0                                        
SHEET    2  DA 2 ILE D  35  GLU D  36  1  N  GLU D  36   O  ILE D   4           
SHEET    1  DB10 THR D  39  ASP D  43  0                                        
SHEET    2  DB10 LEU D  10  ASP D  14  1  O  LEU D  10   N  GLU D  40           
SHEET    3  DB10 VAL D  69  LYS D  72  1  O  VAL D  69   N  VAL D  11           
SHEET    4  DB10 TYR D 300  ALA D 304  1  O  TYR D 300   N  GLY D  70           
SHEET    5  DB10 MET D 289  VAL D 294 -1  O  SER D 291   N  GLU D 303           
SHEET    6  DB10 THR D 106  PRO D 111 -1  O  THR D 106   N  VAL D 294           
SHEET    7  DB10 SER D 129  ARG D 132 -1  O  ILE D 130   N  ARG D 109           
SHEET    8  DB10 VAL D 264  CYS D 267  1  O  TRP D 265   N  ALA D 131           
SHEET    9  DB10 LEU D 205  THR D 209  1  O  TRP D 206   N  ALA D 266           
SHEET   10  DB10 TYR D 244  LEU D 248  1  O  PHE D 245   N  PHE D 207           
SHEET    1  DC 2 VAL D 368  MET D 369  0                                        
SHEET    2  DC 2 LYS D 383  ILE D 384  1  O  LYS D 383   N  MET D 369           
CRYST1   56.130  106.840  154.500  90.00  93.63  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017816  0.000000  0.001130        0.00000                         
SCALE2      0.000000  0.009360  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006486        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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