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Database: PDB
Entry: 3JS4
LinkDB: 3JS4
Original site: 3JS4 
HEADER    OXIDOREDUCTASE                          09-SEP-09   3JS4              
TITLE     CRYSTAL STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM ANAPLASMA         
TITLE    2 PHAGOCYTOPHILUM                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ANAPLASMA PHAGOCYTOPHILUM;                      
SOURCE   3 ORGANISM_TAXID: 212042;                                              
SOURCE   4 STRAIN: HZ;                                                          
SOURCE   5 GENE: SODB, APH_0371;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    NIAID, SSGCID, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS      
KEYWDS   2 DISEASE, GRAM-NEGATIVE BACTERIA, HUMAN GRANULOCYTIC ANAPLASMOSIS,    
KEYWDS   3 FE, METALLOENZYME, OXIDOREDUCTASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   2   13-JUL-11 3JS4    1       VERSN                                    
REVDAT   1   22-SEP-09 3JS4    0                                                
JRNL        AUTH   T.E.EDWARDS,B.L.STAKER,                                      
JRNL        AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE    
JRNL        AUTH 3 (SSGCID)                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM          
JRNL        TITL 2 ANAPLASMA PHAGOCYTOPHILUM                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 63217                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3182                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4048                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.16                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 233                          
REMARK   3   BIN FREE R VALUE                    : 0.2690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6509                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 643                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.65                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.17000                                             
REMARK   3    B22 (A**2) : 1.02000                                              
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : -0.02000                                             
REMARK   3    B13 (A**2) : -0.13000                                             
REMARK   3    B23 (A**2) : 0.45000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.164         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.998         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6725 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9167 ; 1.222 ; 1.932       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   830 ; 5.447 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   336 ;36.295 ;24.762       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1009 ;14.071 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.704 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   967 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5294 ; 0.006 ; 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):  4093 ; 0.552 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6521 ; 1.017 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2632 ; 1.784 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2643 ; 2.853 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     206      4                      
REMARK   3           1     B      1       B     206      4                      
REMARK   3           1     C      1       C     206      4                      
REMARK   3           1     D      1       D     206      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1581 ; 0.250 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1581 ; 0.280 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1581 ; 0.250 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1581 ; 0.270 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1581 ; 0.670 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1581 ; 0.670 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1581 ; 0.720 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1581 ; 0.780 ; 2.000           
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     1        A    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0128   1.7569  11.6805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0693 T22:   0.0591                                     
REMARK   3      T33:   0.0299 T12:   0.0163                                     
REMARK   3      T13:   0.0103 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7241 L22:   0.7024                                     
REMARK   3      L33:   1.1470 L12:   0.7718                                     
REMARK   3      L13:   0.3156 L23:  -0.0784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0544 S12:  -0.2783 S13:   0.2034                       
REMARK   3      S21:   0.1030 S22:   0.0207 S23:   0.0318                       
REMARK   3      S31:  -0.0718 S32:  -0.0810 S33:   0.0337                       
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    50        A    98                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0724   3.8110   0.4034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0640 T22:   0.0354                                     
REMARK   3      T33:   0.0598 T12:   0.0094                                     
REMARK   3      T13:   0.0148 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6632 L22:   0.1760                                     
REMARK   3      L33:   0.7631 L12:   0.3072                                     
REMARK   3      L13:   0.5485 L23:  -0.1589                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0150 S12:   0.0199 S13:   0.2012                       
REMARK   3      S21:   0.0302 S22:  -0.0223 S23:   0.0383                       
REMARK   3      S31:  -0.1155 S32:  -0.0019 S33:   0.0073                       
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    99        A   124                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2841  -3.1348 -12.5642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0783 T22:   0.1780                                     
REMARK   3      T33:   0.0270 T12:  -0.0265                                     
REMARK   3      T13:  -0.0293 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0522 L22:   2.8473                                     
REMARK   3      L33:   2.3978 L12:  -2.1048                                     
REMARK   3      L13:   1.3592 L23:  -0.6582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1041 S12:   0.3790 S13:   0.0349                       
REMARK   3      S21:  -0.0854 S22:   0.0324 S23:   0.1571                       
REMARK   3      S31:   0.0585 S32:  -0.2031 S33:   0.0718                       
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   125        A   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0824  -1.8246  -4.2713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0594 T22:   0.0905                                     
REMARK   3      T33:   0.0250 T12:   0.0060                                     
REMARK   3      T13:   0.0107 T23:   0.0324                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5574 L22:   0.6729                                     
REMARK   3      L33:   0.8218 L12:  -0.3145                                     
REMARK   3      L13:   0.3429 L23:  -0.0269                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0205 S12:   0.1807 S13:   0.0982                       
REMARK   3      S21:  -0.0846 S22:   0.0130 S23:  -0.0025                       
REMARK   3      S31:  -0.0336 S32:  -0.0831 S33:  -0.0335                       
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     1        B    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6946 -14.5093 -51.7544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0732 T22:   0.0617                                     
REMARK   3      T33:   0.0591 T12:  -0.0108                                     
REMARK   3      T13:   0.0075 T23:   0.0522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8794 L22:   0.8716                                     
REMARK   3      L33:   0.9714 L12:  -1.2906                                     
REMARK   3      L13:   0.0540 L23:   0.0688                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0463 S12:   0.3620 S13:   0.2508                       
REMARK   3      S21:  -0.0924 S22:  -0.0571 S23:  -0.0053                       
REMARK   3      S31:  -0.0392 S32:   0.0758 S33:   0.0108                       
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    50        B    98                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3622 -12.6141 -40.4649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0673 T22:   0.0169                                     
REMARK   3      T33:   0.1141 T12:  -0.0100                                     
REMARK   3      T13:   0.0080 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6398 L22:   0.0584                                     
REMARK   3      L33:   0.6532 L12:  -0.2157                                     
REMARK   3      L13:   0.5394 L23:   0.1262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0172 S12:  -0.0334 S13:   0.3648                       
REMARK   3      S21:  -0.0355 S22:  -0.0030 S23:  -0.0383                       
REMARK   3      S31:  -0.1169 S32:  -0.0070 S33:   0.0203                       
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    99        B   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4754 -20.0664 -27.3903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0421 T22:   0.1193                                     
REMARK   3      T33:   0.0153 T12:   0.0242                                     
REMARK   3      T13:  -0.0068 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7053 L22:   1.5909                                     
REMARK   3      L33:   2.7227 L12:   1.3371                                     
REMARK   3      L13:   1.8503 L23:   1.1527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0594 S12:  -0.4043 S13:   0.1192                       
REMARK   3      S21:   0.0442 S22:   0.0943 S23:  -0.0335                       
REMARK   3      S31:   0.1441 S32:   0.0647 S33:  -0.0350                       
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   125        B   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5210 -18.5131 -35.9660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0587 T22:   0.0395                                     
REMARK   3      T33:   0.0559 T12:  -0.0076                                     
REMARK   3      T13:   0.0036 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9297 L22:   0.8453                                     
REMARK   3      L33:   0.7513 L12:   0.0782                                     
REMARK   3      L13:  -0.1813 L23:   0.2998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0179 S12:  -0.1449 S13:   0.2110                       
REMARK   3      S21:   0.0487 S22:   0.0084 S23:   0.0009                       
REMARK   3      S31:  -0.0213 S32:   0.0547 S33:  -0.0263                       
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     1        C    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9781 -46.8269 -42.2259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0385 T22:   0.0307                                     
REMARK   3      T33:   0.0907 T12:   0.0124                                     
REMARK   3      T13:  -0.0057 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6969 L22:   1.2864                                     
REMARK   3      L33:   3.5162 L12:   0.5200                                     
REMARK   3      L13:   1.4812 L23:   0.0101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1054 S12:   0.0746 S13:  -0.3074                       
REMARK   3      S21:   0.0613 S22:   0.0141 S23:  -0.2251                       
REMARK   3      S31:   0.1809 S32:   0.3027 S33:  -0.1195                       
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    50        C    98                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8693 -45.6511 -38.8651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0753 T22:   0.0302                                     
REMARK   3      T33:   0.0616 T12:  -0.0313                                     
REMARK   3      T13:   0.0096 T23:   0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7405 L22:   0.7135                                     
REMARK   3      L33:   1.0881 L12:  -0.0111                                     
REMARK   3      L13:   0.7054 L23:  -0.1822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0362 S12:  -0.1345 S13:  -0.1572                       
REMARK   3      S21:   0.0976 S22:  -0.0171 S23:  -0.0166                       
REMARK   3      S31:   0.1034 S32:  -0.0321 S33:  -0.0191                       
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    99        C   124                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7417 -38.3012 -51.0800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0384 T22:   0.1318                                     
REMARK   3      T33:   0.1588 T12:   0.0029                                     
REMARK   3      T13:  -0.0495 T23:   0.0682                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0667 L22:   5.6171                                     
REMARK   3      L33:   1.4044 L12:   2.8510                                     
REMARK   3      L13:   0.1115 L23:   1.0140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1543 S12:   0.1736 S13:   0.3597                       
REMARK   3      S21:  -0.4255 S22:   0.0882 S23:   0.5010                       
REMARK   3      S31:  -0.1345 S32:  -0.3417 S33:   0.0661                       
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   125        C   206                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5694 -40.8815 -45.7546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0448 T22:   0.0473                                     
REMARK   3      T33:   0.0630 T12:  -0.0196                                     
REMARK   3      T13:   0.0007 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2719 L22:   0.9527                                     
REMARK   3      L33:   0.6036 L12:   0.4792                                     
REMARK   3      L13:  -0.0532 L23:  -0.0536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0209 S12:   0.0373 S13:   0.0347                       
REMARK   3      S21:  -0.0456 S22:   0.0085 S23:   0.1501                       
REMARK   3      S31:  -0.0110 S32:  -0.0746 S33:   0.0124                       
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     1        D    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4293 -30.2268   0.7926              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0705 T22:   0.0504                                     
REMARK   3      T33:   0.1734 T12:  -0.0245                                     
REMARK   3      T13:  -0.0316 T23:  -0.0535                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9296 L22:   0.8529                                     
REMARK   3      L33:   2.2678 L12:  -0.6250                                     
REMARK   3      L13:   0.5581 L23:  -0.1593                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1334 S12:   0.1242 S13:  -0.5139                       
REMARK   3      S21:  -0.1006 S22:  -0.0996 S23:   0.2517                       
REMARK   3      S31:   0.2569 S32:  -0.2218 S33:  -0.0338                       
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    50        D    98                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2991 -28.8528  -1.9563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0902 T22:   0.1028                                     
REMARK   3      T33:   0.2077 T12:   0.0250                                     
REMARK   3      T13:  -0.0204 T23:  -0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4957 L22:   0.5695                                     
REMARK   3      L33:   2.4039 L12:  -0.6549                                     
REMARK   3      L13:   1.0738 L23:  -0.3286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1241 S12:   0.2449 S13:  -0.4205                       
REMARK   3      S21:  -0.0535 S22:  -0.1380 S23:   0.1254                       
REMARK   3      S31:   0.0884 S32:   0.0704 S33:   0.0139                       
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    99        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9243 -22.4172  11.5666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0325 T22:   0.1006                                     
REMARK   3      T33:   0.0600 T12:  -0.0275                                     
REMARK   3      T13:  -0.0025 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4828 L22:   4.1447                                     
REMARK   3      L33:   2.3523 L12:  -3.2243                                     
REMARK   3      L13:   0.9813 L23:  -1.5766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0422 S12:  -0.1061 S13:  -0.1100                       
REMARK   3      S21:   0.2095 S22:   0.0427 S23:   0.1495                       
REMARK   3      S31:  -0.1329 S32:   0.2782 S33:  -0.0006                       
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   125        D   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5474 -24.7084   5.8863              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0500 T22:   0.0563                                     
REMARK   3      T33:   0.0749 T12:   0.0052                                     
REMARK   3      T13:  -0.0067 T23:  -0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5561 L22:   0.9059                                     
REMARK   3      L33:   0.5813 L12:  -0.5061                                     
REMARK   3      L13:   0.1023 L23:   0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0707 S12:   0.0705 S13:  -0.1871                       
REMARK   3      S21:   0.0086 S22:  -0.0430 S23:  -0.0301                       
REMARK   3      S31:   0.0356 S32:   0.0565 S33:  -0.0277                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. THE FRIEDEL PAIRS WERE USED IN         
REMARK   3  PHASING. 2. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 3.   
REMARK   3  U VALUES: RESIDUAL ONLY.                                            
REMARK   4                                                                      
REMARK   4 3JS4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055089.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63217                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.03600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1UNF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PACT SCREEN CONDITION E1, 20% PEG        
REMARK 280  3350, 0.2 M NAF. 0.4/0.4 MICROLITER DROPS. 30.0 MG/ML PROTEIN IN    
REMARK 280  25 MM HEPES PH 7.0, 0.3 M NACL, 10% GLYCEROL, 2 MM DTT. CRYSTAL     
REMARK 280  TRACKING ID 204869E1, EXPRESSION TAG NOT REMOVED PRIOR TO           
REMARK 280  CRYSTALLIZATION, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     ALA B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     MET B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     THR B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     THR B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     MET C   -20                                                      
REMARK 465     ALA C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     MET C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     THR C   -10                                                      
REMARK 465     LEU C    -9                                                      
REMARK 465     GLU C    -8                                                      
REMARK 465     ALA C    -7                                                      
REMARK 465     GLN C    -6                                                      
REMARK 465     THR C    -5                                                      
REMARK 465     GLN C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     PRO C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET D   -20                                                      
REMARK 465     ALA D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     MET D   -12                                                      
REMARK 465     GLY D   -11                                                      
REMARK 465     THR D   -10                                                      
REMARK 465     LEU D    -9                                                      
REMARK 465     GLU D    -8                                                      
REMARK 465     ALA D    -7                                                      
REMARK 465     GLN D    -6                                                      
REMARK 465     THR D    -5                                                      
REMARK 465     GLN D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     PRO D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
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  97    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     GLN A 156    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 136    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 156    CG   CD   OE1  NE2                                  
REMARK 470     LYS C  59    CG   CD   CE   NZ                                   
REMARK 470     GLU C  97    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 156    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 181    CG   CD   CE   NZ                                   
REMARK 470     GLU D  97    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  98    CG   CD   CE   NZ                                   
REMARK 470     ARG D 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 137    CG   OD1  OD2                                       
REMARK 470     LYS D 142    CG   CD   CE   NZ                                   
REMARK 470     GLN D 156    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 181    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER D   106     O    HOH D   254              2.08            
REMARK 500   OH   TYR C    32     O    HOH C   300              2.08            
REMARK 500   OE2  GLU A   101     O    HOH A   374              2.08            
REMARK 500   O    HOH A   395     O    HOH A   567              2.09            
REMARK 500   OD1  ASP D   184     O    HOH D   261              2.13            
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    ASN A 148     -108.19     55.68                                   
REMARK 500    LEU A 176     -137.58     52.02                                   
REMARK 500    ASN B 148     -106.04     56.35                                   
REMARK 500    LEU B 176     -134.55     52.99                                   
REMARK 500    ASN C 148     -105.07     64.84                                   
REMARK 500    LEU C 176     -132.69     52.77                                   
REMARK 500    ASN D 148     -109.72     58.27                                   
REMARK 500    LEU D 176     -135.89     55.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 329        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A 593        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH C 396        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH D 628        DISTANCE =  5.02 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 207  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  24   NE2                                                    
REMARK 620 2 HIS A  80   NE2  90.4                                              
REMARK 620 3 ASP A 165   OD2  82.7 112.6                                        
REMARK 620 4 HIS A 169   NE2  95.7 125.6 121.7                                  
REMARK 620 5 HOH A 209   O   173.4  88.5  91.7  90.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 208  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO A 152   O                                                      
REMARK 620 2 THR A 155   O    82.0                                              
REMARK 620 3 GLN A 158   O   101.8 112.2                                        
REMARK 620 4 HOH A 235   O   100.5 162.1  84.9                                  
REMARK 620 5 HOH A 407   O   167.0  86.4  88.0  88.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 207  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  24   NE2                                                    
REMARK 620 2 HIS B  80   NE2  91.3                                              
REMARK 620 3 ASP B 165   OD2  91.1 110.4                                        
REMARK 620 4 HIS B 169   NE2  95.5 126.9 122.0                                  
REMARK 620 5 HOH B 209   O   170.5  88.3  80.2  92.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 208  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO B 152   O                                                      
REMARK 620 2 THR B 155   O    78.1                                              
REMARK 620 3 GLN B 158   O    97.1 102.4                                        
REMARK 620 4 HOH B 222   O    88.4  70.7 170.2                                  
REMARK 620 5 HOH B 408   O    94.5 172.6  78.6 109.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 207  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  24   NE2                                                    
REMARK 620 2 HIS C  80   NE2  93.8                                              
REMARK 620 3 ASP C 165   OD2  87.1 111.0                                        
REMARK 620 4 HIS C 169   NE2  98.3 127.7 120.2                                  
REMARK 620 5 HOH C 214   O   176.7  88.4  89.9  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 208  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO C 152   O                                                      
REMARK 620 2 THR C 155   O    82.8                                              
REMARK 620 3 GLN C 158   O    98.2 109.0                                        
REMARK 620 4 HOH C 274   O   173.8  91.0  83.3                                  
REMARK 620 5 HOH C 268   O    95.0 157.5  93.5  90.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 207  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  24   NE2                                                    
REMARK 620 2 HIS D  80   NE2  94.1                                              
REMARK 620 3 ASP D 165   OD2  86.0 110.9                                        
REMARK 620 4 HIS D 169   NE2  92.2 128.9 120.0                                  
REMARK 620 5 HOH D 209   O   175.5  88.9  89.8  88.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 208  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PRO D 152   O                                                      
REMARK 620 2 THR D 155   O    82.0                                              
REMARK 620 3 GLN D 158   O    96.2 103.0                                        
REMARK 620 4 HOH D 390   O   100.4  98.4 154.5                                  
REMARK 620 5 HOH D 268   O    92.1 167.1  89.0  71.3                            
REMARK 620 6 HOH D 217   O   172.1  90.6  82.6  83.4  95.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 208                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: ANPHA.01360.A   RELATED DB: TARGETDB                     
DBREF  3JS4 A    1   206  UNP    Q2GKX4   Q2GKX4_ANAPZ     1    206             
DBREF  3JS4 B    1   206  UNP    Q2GKX4   Q2GKX4_ANAPZ     1    206             
DBREF  3JS4 C    1   206  UNP    Q2GKX4   Q2GKX4_ANAPZ     1    206             
DBREF  3JS4 D    1   206  UNP    Q2GKX4   Q2GKX4_ANAPZ     1    206             
SEQADV 3JS4 MET A  -20  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA A  -19  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS A  -18  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS A  -17  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS A  -16  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS A  -15  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS A  -14  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS A  -13  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET A  -12  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY A  -11  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR A  -10  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 LEU A   -9  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLU A   -8  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA A   -7  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN A   -6  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR A   -5  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN A   -4  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY A   -3  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 PRO A   -2  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY A   -1  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 SER A    0  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET B  -20  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA B  -19  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS B  -18  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS B  -17  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS B  -16  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS B  -15  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS B  -14  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS B  -13  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET B  -12  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY B  -11  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR B  -10  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 LEU B   -9  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLU B   -8  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA B   -7  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN B   -6  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR B   -5  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN B   -4  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY B   -3  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 PRO B   -2  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY B   -1  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 SER B    0  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET C  -20  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA C  -19  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS C  -18  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS C  -17  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS C  -16  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS C  -15  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS C  -14  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS C  -13  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET C  -12  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY C  -11  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR C  -10  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 LEU C   -9  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLU C   -8  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA C   -7  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN C   -6  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR C   -5  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN C   -4  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY C   -3  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 PRO C   -2  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY C   -1  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 SER C    0  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET D  -20  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA D  -19  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS D  -18  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS D  -17  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS D  -16  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS D  -15  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS D  -14  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 HIS D  -13  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 MET D  -12  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY D  -11  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR D  -10  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 LEU D   -9  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLU D   -8  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 ALA D   -7  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN D   -6  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 THR D   -5  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLN D   -4  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY D   -3  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 PRO D   -2  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 GLY D   -1  UNP  Q2GKX4              EXPRESSION TAG                 
SEQADV 3JS4 SER D    0  UNP  Q2GKX4              EXPRESSION TAG                 
SEQRES   1 A  227  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 A  227  ALA GLN THR GLN GLY PRO GLY SER MET PHE GLU LEU SER          
SEQRES   3 A  227  ASP LEU PRO TYR GLU GLY LEU GLU PRO TYR ILE SER SER          
SEQRES   4 A  227  HIS LEU LEU ASP ARG HIS TYR ASN GLY HIS HIS LYS THR          
SEQRES   5 A  227  TYR VAL ASP VAL LEU ASN LYS LEU VAL VAL GLY THR GLU          
SEQRES   6 A  227  PHE GLU GLY LEU GLY ASN GLU SER LEU GLY ASP ILE VAL          
SEQRES   7 A  227  VAL LYS ALA HIS ASN SER GLY SER ALA GLY ARG ALA ILE          
SEQRES   8 A  227  PHE ASN ASN ALA ALA GLN ILE TRP ASN HIS ASP PHE TYR          
SEQRES   9 A  227  TRP GLN SER MET LYS PRO ASN GLY GLY GLY ASN PRO PRO          
SEQRES  10 A  227  GLU LYS LEU ARG GLU MET ILE GLU HIS SER PHE GLY SER          
SEQRES  11 A  227  VAL GLU GLY PHE ASN ASN ALA PHE THR THR SER GLY LEU          
SEQRES  12 A  227  GLY GLN PHE GLY SER GLY TRP VAL TRP LEU VAL TYR ASP          
SEQRES  13 A  227  GLU ASP ALA LYS ALA LEU LYS VAL VAL SER THR ALA ASN          
SEQRES  14 A  227  ALA ASP SER PRO LEU LEU THR GLN GLY GLN LEU PRO LEU          
SEQRES  15 A  227  ALA THR MET ASP VAL TRP GLU HIS ALA TYR TYR LEU ASP          
SEQRES  16 A  227  TYR LEU ASN LEU ARG LYS LYS TYR ILE ASP VAL PHE LEU          
SEQRES  17 A  227  GLU HIS LEU LEU ASN TRP ASP PHE VAL LEU GLY ARG LEU          
SEQRES  18 A  227  GLU ASP ALA GLY VAL LEU                                      
SEQRES   1 B  227  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 B  227  ALA GLN THR GLN GLY PRO GLY SER MET PHE GLU LEU SER          
SEQRES   3 B  227  ASP LEU PRO TYR GLU GLY LEU GLU PRO TYR ILE SER SER          
SEQRES   4 B  227  HIS LEU LEU ASP ARG HIS TYR ASN GLY HIS HIS LYS THR          
SEQRES   5 B  227  TYR VAL ASP VAL LEU ASN LYS LEU VAL VAL GLY THR GLU          
SEQRES   6 B  227  PHE GLU GLY LEU GLY ASN GLU SER LEU GLY ASP ILE VAL          
SEQRES   7 B  227  VAL LYS ALA HIS ASN SER GLY SER ALA GLY ARG ALA ILE          
SEQRES   8 B  227  PHE ASN ASN ALA ALA GLN ILE TRP ASN HIS ASP PHE TYR          
SEQRES   9 B  227  TRP GLN SER MET LYS PRO ASN GLY GLY GLY ASN PRO PRO          
SEQRES  10 B  227  GLU LYS LEU ARG GLU MET ILE GLU HIS SER PHE GLY SER          
SEQRES  11 B  227  VAL GLU GLY PHE ASN ASN ALA PHE THR THR SER GLY LEU          
SEQRES  12 B  227  GLY GLN PHE GLY SER GLY TRP VAL TRP LEU VAL TYR ASP          
SEQRES  13 B  227  GLU ASP ALA LYS ALA LEU LYS VAL VAL SER THR ALA ASN          
SEQRES  14 B  227  ALA ASP SER PRO LEU LEU THR GLN GLY GLN LEU PRO LEU          
SEQRES  15 B  227  ALA THR MET ASP VAL TRP GLU HIS ALA TYR TYR LEU ASP          
SEQRES  16 B  227  TYR LEU ASN LEU ARG LYS LYS TYR ILE ASP VAL PHE LEU          
SEQRES  17 B  227  GLU HIS LEU LEU ASN TRP ASP PHE VAL LEU GLY ARG LEU          
SEQRES  18 B  227  GLU ASP ALA GLY VAL LEU                                      
SEQRES   1 C  227  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 C  227  ALA GLN THR GLN GLY PRO GLY SER MET PHE GLU LEU SER          
SEQRES   3 C  227  ASP LEU PRO TYR GLU GLY LEU GLU PRO TYR ILE SER SER          
SEQRES   4 C  227  HIS LEU LEU ASP ARG HIS TYR ASN GLY HIS HIS LYS THR          
SEQRES   5 C  227  TYR VAL ASP VAL LEU ASN LYS LEU VAL VAL GLY THR GLU          
SEQRES   6 C  227  PHE GLU GLY LEU GLY ASN GLU SER LEU GLY ASP ILE VAL          
SEQRES   7 C  227  VAL LYS ALA HIS ASN SER GLY SER ALA GLY ARG ALA ILE          
SEQRES   8 C  227  PHE ASN ASN ALA ALA GLN ILE TRP ASN HIS ASP PHE TYR          
SEQRES   9 C  227  TRP GLN SER MET LYS PRO ASN GLY GLY GLY ASN PRO PRO          
SEQRES  10 C  227  GLU LYS LEU ARG GLU MET ILE GLU HIS SER PHE GLY SER          
SEQRES  11 C  227  VAL GLU GLY PHE ASN ASN ALA PHE THR THR SER GLY LEU          
SEQRES  12 C  227  GLY GLN PHE GLY SER GLY TRP VAL TRP LEU VAL TYR ASP          
SEQRES  13 C  227  GLU ASP ALA LYS ALA LEU LYS VAL VAL SER THR ALA ASN          
SEQRES  14 C  227  ALA ASP SER PRO LEU LEU THR GLN GLY GLN LEU PRO LEU          
SEQRES  15 C  227  ALA THR MET ASP VAL TRP GLU HIS ALA TYR TYR LEU ASP          
SEQRES  16 C  227  TYR LEU ASN LEU ARG LYS LYS TYR ILE ASP VAL PHE LEU          
SEQRES  17 C  227  GLU HIS LEU LEU ASN TRP ASP PHE VAL LEU GLY ARG LEU          
SEQRES  18 C  227  GLU ASP ALA GLY VAL LEU                                      
SEQRES   1 D  227  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 D  227  ALA GLN THR GLN GLY PRO GLY SER MET PHE GLU LEU SER          
SEQRES   3 D  227  ASP LEU PRO TYR GLU GLY LEU GLU PRO TYR ILE SER SER          
SEQRES   4 D  227  HIS LEU LEU ASP ARG HIS TYR ASN GLY HIS HIS LYS THR          
SEQRES   5 D  227  TYR VAL ASP VAL LEU ASN LYS LEU VAL VAL GLY THR GLU          
SEQRES   6 D  227  PHE GLU GLY LEU GLY ASN GLU SER LEU GLY ASP ILE VAL          
SEQRES   7 D  227  VAL LYS ALA HIS ASN SER GLY SER ALA GLY ARG ALA ILE          
SEQRES   8 D  227  PHE ASN ASN ALA ALA GLN ILE TRP ASN HIS ASP PHE TYR          
SEQRES   9 D  227  TRP GLN SER MET LYS PRO ASN GLY GLY GLY ASN PRO PRO          
SEQRES  10 D  227  GLU LYS LEU ARG GLU MET ILE GLU HIS SER PHE GLY SER          
SEQRES  11 D  227  VAL GLU GLY PHE ASN ASN ALA PHE THR THR SER GLY LEU          
SEQRES  12 D  227  GLY GLN PHE GLY SER GLY TRP VAL TRP LEU VAL TYR ASP          
SEQRES  13 D  227  GLU ASP ALA LYS ALA LEU LYS VAL VAL SER THR ALA ASN          
SEQRES  14 D  227  ALA ASP SER PRO LEU LEU THR GLN GLY GLN LEU PRO LEU          
SEQRES  15 D  227  ALA THR MET ASP VAL TRP GLU HIS ALA TYR TYR LEU ASP          
SEQRES  16 D  227  TYR LEU ASN LEU ARG LYS LYS TYR ILE ASP VAL PHE LEU          
SEQRES  17 D  227  GLU HIS LEU LEU ASN TRP ASP PHE VAL LEU GLY ARG LEU          
SEQRES  18 D  227  GLU ASP ALA GLY VAL LEU                                      
HET     FE  A 207       1                                                       
HET     NA  A 208       1                                                       
HET     FE  B 207       1                                                       
HET     NA  B 208       1                                                       
HET     FE  C 207       1                                                       
HET     NA  C 208       1                                                       
HET     FE  D 207       1                                                       
HET     NA  D 208       1                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM      NA SODIUM ION                                                       
FORMUL   5   FE    4(FE 3+)                                                     
FORMUL   6   NA    4(NA 1+)                                                     
FORMUL  13  HOH   *643(H2 O)                                                    
HELIX    1   1 SER A   17  GLY A   27  1                                  11    
HELIX    2   2 GLY A   27  VAL A   40  1                                  14    
HELIX    3   3 GLY A   49  GLU A   51  5                                   3    
HELIX    4   4 SER A   52  SER A   63  1                                  12    
HELIX    5   5 GLY A   64  ALA A   66  5                                   3    
HELIX    6   6 GLY A   67  SER A   86  1                                  20    
HELIX    7   7 PRO A   96  LYS A   98  5                                   3    
HELIX    8   8 LEU A   99  GLY A  108  1                                  10    
HELIX    9   9 SER A  109  GLN A  124  1                                  16    
HELIX   10  10 SER A  151  THR A  155  5                                   5    
HELIX   11  11 TRP A  167  ALA A  170  5                                   4    
HELIX   12  12 TYR A  171  LEU A  176  1                                   6    
HELIX   13  13 LEU A  178  LEU A  190  1                                  13    
HELIX   14  14 ASN A  192  ALA A  203  1                                  12    
HELIX   15  15 SER B   17  GLY B   27  1                                  11    
HELIX   16  16 GLY B   27  VAL B   40  1                                  14    
HELIX   17  17 GLY B   49  GLU B   51  5                                   3    
HELIX   18  18 SER B   52  SER B   63  1                                  12    
HELIX   19  19 GLY B   64  ALA B   66  5                                   3    
HELIX   20  20 GLY B   67  SER B   86  1                                  20    
HELIX   21  21 PRO B   96  GLY B  108  1                                  13    
HELIX   22  22 SER B  109  GLN B  124  1                                  16    
HELIX   23  23 SER B  151  THR B  155  5                                   5    
HELIX   24  24 TRP B  167  ALA B  170  5                                   4    
HELIX   25  25 TYR B  171  LEU B  176  1                                   6    
HELIX   26  26 LEU B  178  LEU B  190  1                                  13    
HELIX   27  27 ASN B  192  ALA B  203  1                                  12    
HELIX   28  28 SER C   17  GLY C   27  1                                  11    
HELIX   29  29 GLY C   27  VAL C   40  1                                  14    
HELIX   30  30 GLY C   49  GLU C   51  5                                   3    
HELIX   31  31 SER C   52  ASN C   62  1                                  11    
HELIX   32  32 SER C   63  ALA C   66  5                                   4    
HELIX   33  33 GLY C   67  SER C   86  1                                  20    
HELIX   34  34 PRO C   96  GLY C  108  1                                  13    
HELIX   35  35 SER C  109  GLN C  124  1                                  16    
HELIX   36  36 SER C  151  THR C  155  5                                   5    
HELIX   37  37 TRP C  167  ALA C  170  5                                   4    
HELIX   38  38 TYR C  171  LEU C  176  1                                   6    
HELIX   39  39 LEU C  178  LEU C  190  1                                  13    
HELIX   40  40 ASN C  192  ALA C  203  1                                  12    
HELIX   41  41 SER D   17  GLY D   27  1                                  11    
HELIX   42  42 GLY D   27  VAL D   41  1                                  15    
HELIX   43  43 GLY D   49  GLU D   51  5                                   3    
HELIX   44  44 SER D   52  ASN D   62  1                                  11    
HELIX   45  45 SER D   63  ALA D   66  5                                   4    
HELIX   46  46 GLY D   67  SER D   86  1                                  20    
HELIX   47  47 PRO D   96  LYS D   98  5                                   3    
HELIX   48  48 LEU D   99  GLY D  108  1                                  10    
HELIX   49  49 SER D  109  GLN D  124  1                                  16    
HELIX   50  50 SER D  151  THR D  155  5                                   5    
HELIX   51  51 TRP D  167  ALA D  170  5                                   4    
HELIX   52  52 TYR D  171  LEU D  176  1                                   6    
HELIX   53  53 LEU D  178  LEU D  190  1                                  13    
HELIX   54  54 ASN D  192  ALA D  203  1                                  12    
SHEET    1   A 3 ALA A 140  ALA A 147  0                                        
SHEET    2   A 3 GLY A 128  ASP A 135 -1  N  TRP A 131   O  VAL A 144           
SHEET    3   A 3 GLN A 158  ASP A 165 -1  O  LEU A 159   N  TYR A 134           
SHEET    1   B 3 ALA B 140  ALA B 147  0                                        
SHEET    2   B 3 GLY B 128  ASP B 135 -1  N  TRP B 131   O  VAL B 144           
SHEET    3   B 3 GLN B 158  ASP B 165 -1  O  LEU B 161   N  LEU B 132           
SHEET    1   C 3 ALA C 140  ALA C 147  0                                        
SHEET    2   C 3 GLY C 128  ASP C 135 -1  N  TRP C 131   O  VAL C 144           
SHEET    3   C 3 GLN C 158  ASP C 165 -1  O  LEU C 161   N  LEU C 132           
SHEET    1   D 3 ALA D 140  ALA D 147  0                                        
SHEET    2   D 3 GLY D 128  ASP D 135 -1  N  TRP D 131   O  VAL D 144           
SHEET    3   D 3 GLN D 158  ASP D 165 -1  O  LEU D 159   N  TYR D 134           
LINK         NE2 HIS A  24                FE    FE A 207     1555   1555  2.30  
LINK         NE2 HIS A  80                FE    FE A 207     1555   1555  2.21  
LINK         O   PRO A 152                NA    NA A 208     1555   1555  2.38  
LINK         O   THR A 155                NA    NA A 208     1555   1555  2.35  
LINK         O   GLN A 158                NA    NA A 208     1555   1555  2.55  
LINK         OD2 ASP A 165                FE    FE A 207     1555   1555  2.04  
LINK         NE2 HIS A 169                FE    FE A 207     1555   1555  2.23  
LINK         NE2 HIS B  24                FE    FE B 207     1555   1555  2.22  
LINK         NE2 HIS B  80                FE    FE B 207     1555   1555  2.30  
LINK         O   PRO B 152                NA    NA B 208     1555   1555  2.53  
LINK         O   THR B 155                NA    NA B 208     1555   1555  2.52  
LINK         O   GLN B 158                NA    NA B 208     1555   1555  2.88  
LINK         OD2 ASP B 165                FE    FE B 207     1555   1555  2.01  
LINK         NE2 HIS B 169                FE    FE B 207     1555   1555  2.14  
LINK         NE2 HIS C  24                FE    FE C 207     1555   1555  2.23  
LINK         NE2 HIS C  80                FE    FE C 207     1555   1555  2.15  
LINK         O   PRO C 152                NA    NA C 208     1555   1555  2.43  
LINK         O   THR C 155                NA    NA C 208     1555   1555  2.29  
LINK         O   GLN C 158                NA    NA C 208     1555   1555  2.51  
LINK         OD2 ASP C 165                FE    FE C 207     1555   1555  2.01  
LINK         NE2 HIS C 169                FE    FE C 207     1555   1555  2.21  
LINK         NE2 HIS D  24                FE    FE D 207     1555   1555  2.27  
LINK         NE2 HIS D  80                FE    FE D 207     1555   1555  2.18  
LINK         O   PRO D 152                NA    NA D 208     1555   1555  2.49  
LINK         O   THR D 155                NA    NA D 208     1555   1555  2.45  
LINK         O   GLN D 158                NA    NA D 208     1555   1555  2.52  
LINK         OD2 ASP D 165                FE    FE D 207     1555   1555  2.02  
LINK         NE2 HIS D 169                FE    FE D 207     1555   1555  2.07  
LINK        FE    FE A 207                 O   HOH A 209     1555   1555  2.25  
LINK        NA    NA A 208                 O   HOH A 235     1555   1555  2.31  
LINK        NA    NA A 208                 O   HOH A 407     1555   1555  2.29  
LINK        FE    FE B 207                 O   HOH B 209     1555   1555  2.27  
LINK        NA    NA B 208                 O   HOH B 222     1555   1555  2.21  
LINK        NA    NA B 208                 O   HOH B 408     1555   1555  2.32  
LINK        FE    FE C 207                 O   HOH C 214     1555   1555  2.23  
LINK        NA    NA C 208                 O   HOH C 274     1555   1555  2.48  
LINK        NA    NA C 208                 O   HOH C 268     1555   1555  2.26  
LINK        FE    FE D 207                 O   HOH D 209     1555   1555  2.25  
LINK        NA    NA D 208                 O   HOH D 390     1555   1555  2.34  
LINK        NA    NA D 208                 O   HOH D 268     1555   1555  2.49  
LINK        NA    NA D 208                 O   HOH D 217     1555   1555  2.28  
CISPEP   1 GLU A   13    PRO A   14          0        -0.51                     
CISPEP   2 GLU B   13    PRO B   14          0         2.99                     
CISPEP   3 GLU C   13    PRO C   14          0         2.26                     
CISPEP   4 GLU D   13    PRO D   14          0        -0.19                     
SITE     1 AC1  5 HIS A  24  HIS A  80  ASP A 165  HIS A 169                    
SITE     2 AC1  5 HOH A 209                                                     
SITE     1 AC2  5 PRO A 152  THR A 155  GLN A 158  HOH A 235                    
SITE     2 AC2  5 HOH A 407                                                     
SITE     1 AC3  5 HIS B  24  HIS B  80  ASP B 165  HIS B 169                    
SITE     2 AC3  5 HOH B 209                                                     
SITE     1 AC4  5 PRO B 152  THR B 155  GLN B 158  HOH B 222                    
SITE     2 AC4  5 HOH B 408                                                     
SITE     1 AC5  5 HIS C  24  HIS C  80  ASP C 165  HIS C 169                    
SITE     2 AC5  5 HOH C 214                                                     
SITE     1 AC6  5 PRO C 152  THR C 155  GLN C 158  HOH C 268                    
SITE     2 AC6  5 HOH C 274                                                     
SITE     1 AC7  5 HIS D  24  HIS D  80  ASP D 165  HIS D 169                    
SITE     2 AC7  5 HOH D 209                                                     
SITE     1 AC8  6 PRO D 152  THR D 155  GLN D 158  HOH D 217                    
SITE     2 AC8  6 HOH D 268  HOH D 390                                          
CRYST1   45.660   66.600   85.440 102.09 104.83  88.58 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021901 -0.000542  0.005816        0.00000                         
SCALE2      0.000000  0.015020  0.003228        0.00000                         
SCALE3      0.000000  0.000000  0.012384        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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