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Database: PDB
Entry: 3EGG
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HEADER    HYDROLASE                               10-SEP-08   3EGG              
TITLE     CRYSTAL STRUCTURE OF A COMPLEX BETWEEN PROTEIN PHOSPHATASE 1 ALPHA    
TITLE    2 (PP1) AND THE PP1 BINDING AND PDZ DOMAINS OF SPINOPHILIN             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: PP-1A;                                                      
COMPND   6 EC: 3.1.3.16;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SPINOPHILIN;                                               
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: PP1 BINDING AND PDZ DOMAINS;                               
COMPND  12 SYNONYM: NEURABIN-II, NEURABIN-2, PROTEIN PHOSPHATASE 1 REGULATORY   
COMPND  13 SUBUNIT 9B, NEURAL TISSUE-SPECIFIC F-ACTIN-BINDING PROTEIN II, P130, 
COMPND  14 PP1BP134;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CA, PPP1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: RP1B;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  12 ORGANISM_COMMON: RAT;                                                
SOURCE  13 ORGANISM_TAXID: 10116;                                               
SOURCE  14 GENE: PPP1R9B;                                                       
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: RP1B                                      
KEYWDS    PP1, SPINOPHILIN, SERINE/THREONINE PHOSPHATASE, POST SYNAPTIC         
KEYWDS   2 DENSITY, GLUTAMETERGIC RECEPTORS, CARBOHYDRATE METABOLISM, CELL      
KEYWDS   3 CYCLE, CELL DIVISION, GLYCOGEN METABOLISM, HYDROLASE, IRON,          
KEYWDS   4 MANGANESE, METAL-BINDING, PHOSPHOPROTEIN, PROTEIN PHOSPHATASE,       
KEYWDS   5 ACTIN-BINDING, CELL JUNCTION, CELL PROJECTION, CYTOSKELETON,         
KEYWDS   6 DEVELOPMENTAL PROTEIN, DIFFERENTIATION, NEUROGENESIS, NUCLEUS,       
KEYWDS   7 SYNAPSE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.RAGUSA,R.PAGE,W.PETI                                              
REVDAT   4   25-OCT-17 3EGG    1       REMARK                                   
REVDAT   3   13-JUL-11 3EGG    1       VERSN                                    
REVDAT   2   21-APR-10 3EGG    1       JRNL                                     
REVDAT   1   23-MAR-10 3EGG    0                                                
JRNL        AUTH   M.J.RAGUSA,B.DANCHECK,D.A.CRITTON,A.C.NAIRN,R.PAGE,W.PETI    
JRNL        TITL   SPINOPHILIN DIRECTS PROTEIN PHOSPHATASE 1 SPECIFICITY BY     
JRNL        TITL 2 BLOCKING SUBSTRATE BINDING SITES.                            
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   459 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20305656                                                     
JRNL        DOI    10.1038/NSMB.1786                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 87003                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4548                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6136                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 330                          
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6349                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 82                                      
REMARK   3   SOLVENT ATOMS            : 521                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 22.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : 0.51000                                              
REMARK   3    B33 (A**2) : -0.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.98000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.117         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.642         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6641 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8986 ; 1.261 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   822 ; 5.848 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   310 ;35.703 ;24.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1116 ;12.992 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;14.739 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   984 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5036 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3105 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4548 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   485 ; 0.137 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.028 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.170 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.115 ; 0.200       
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):  4198 ; 0.620 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6558 ; 0.974 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2765 ; 1.741 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2422 ; 2.645 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 19                                         
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     7        A    26                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1805 -15.5042 -17.2308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0787 T22:  -0.1144                                     
REMARK   3      T33:  -0.0840 T12:  -0.0721                                     
REMARK   3      T13:   0.0189 T23:   0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9372 L22:   5.4032                                     
REMARK   3      L33:  13.6192 L12:  -4.7940                                     
REMARK   3      L13:   7.2208 L23:  -6.6890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0468 S12:   0.2914 S13:   0.3203                       
REMARK   3      S21:  -0.1827 S22:  -0.0578 S23:  -0.1336                       
REMARK   3      S31:  -0.1914 S32:   0.1713 S33:   0.0110                       
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    27        A    56                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3895 -29.3911  -8.8086              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1579 T22:  -0.1792                                     
REMARK   3      T33:  -0.1335 T12:  -0.0279                                     
REMARK   3      T13:  -0.0201 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4326 L22:   1.4523                                     
REMARK   3      L33:   5.7550 L12:   0.6950                                     
REMARK   3      L13:  -2.7594 L23:  -1.2424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1831 S12:  -0.0764 S13:  -0.2154                       
REMARK   3      S21:  -0.0732 S22:   0.0298 S23:  -0.0638                       
REMARK   3      S31:   0.2922 S32:   0.1525 S33:   0.1533                       
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    57        A   224                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4198 -27.5318 -10.6108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1348 T22:  -0.1105                                     
REMARK   3      T33:  -0.1369 T12:  -0.0274                                     
REMARK   3      T13:  -0.0141 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8860 L22:   0.9534                                     
REMARK   3      L33:   1.5328 L12:   0.1753                                     
REMARK   3      L13:  -0.4339 L23:  -0.1104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0825 S12:   0.1387 S13:  -0.0323                       
REMARK   3      S21:  -0.0511 S22:   0.0362 S23:   0.1192                       
REMARK   3      S31:   0.1288 S32:  -0.2693 S33:   0.0463                       
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   225        A   279                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.6729 -21.3240  -6.5371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1584 T22:   0.0223                                     
REMARK   3      T33:  -0.0279 T12:   0.0055                                     
REMARK   3      T13:  -0.0252 T23:  -0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2651 L22:   2.6104                                     
REMARK   3      L33:   2.4223 L12:   0.4187                                     
REMARK   3      L13:  -0.7214 L23:  -0.6326                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:   0.1869 S13:   0.1759                       
REMARK   3      S21:   0.0034 S22:   0.0423 S23:   0.3376                       
REMARK   3      S31:  -0.0771 S32:  -0.5134 S33:  -0.0195                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   280        A   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0075 -10.2790  -4.0118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0874 T22:  -0.0807                                     
REMARK   3      T33:   0.0582 T12:   0.0621                                     
REMARK   3      T13:  -0.0086 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5053 L22:   2.8436                                     
REMARK   3      L33:  14.3370 L12:  -0.5266                                     
REMARK   3      L13:   2.0193 L23:  -2.4428                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0083 S12:  -0.0125 S13:   0.4514                       
REMARK   3      S21:   0.1370 S22:  -0.0630 S23:   0.1156                       
REMARK   3      S31:  -0.6236 S32:   0.1984 S33:   0.0713                       
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     7        B    20                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8396 -16.1446 -37.0248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0805 T22:  -0.0499                                     
REMARK   3      T33:  -0.0411 T12:   0.0692                                     
REMARK   3      T13:   0.0201 T23:   0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.4304 L22:   3.0293                                     
REMARK   3      L33:   9.3068 L12:   2.0661                                     
REMARK   3      L13:   3.6161 L23:   1.8092                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0331 S12:   0.1405 S13:   0.3263                       
REMARK   3      S21:  -0.0325 S22:   0.0331 S23:   0.4317                       
REMARK   3      S31:  -0.2363 S32:  -0.4695 S33:   0.0000                       
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    21        B   145                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9971 -23.0067 -39.9975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1347 T22:  -0.1499                                     
REMARK   3      T33:  -0.1490 T12:   0.0080                                     
REMARK   3      T13:   0.0013 T23:  -0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5192 L22:   1.4418                                     
REMARK   3      L33:   1.7112 L12:   0.2671                                     
REMARK   3      L13:  -0.7071 L23:  -0.0656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0085 S12:  -0.0401 S13:   0.0813                       
REMARK   3      S21:   0.0175 S22:   0.0247 S23:   0.0776                       
REMARK   3      S31:  -0.0165 S32:  -0.1042 S33:  -0.0162                       
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   146        B   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7806 -33.3973 -48.3273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0887 T22:  -0.1589                                     
REMARK   3      T33:  -0.1356 T12:   0.0146                                     
REMARK   3      T13:  -0.0049 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8374 L22:   1.3700                                     
REMARK   3      L33:   1.7704 L12:   0.1183                                     
REMARK   3      L13:  -0.9028 L23:   0.2201                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0541 S12:   0.0054 S13:  -0.2182                       
REMARK   3      S21:  -0.0366 S22:  -0.0093 S23:  -0.1068                       
REMARK   3      S31:   0.1649 S32:   0.0192 S33:   0.0633                       
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 :   B   217        B   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.3928 -23.1643 -48.1205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1416 T22:  -0.1425                                     
REMARK   3      T33:  -0.1068 T12:   0.0013                                     
REMARK   3      T13:   0.0063 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6445 L22:   2.6496                                     
REMARK   3      L33:   1.9578 L12:  -0.0623                                     
REMARK   3      L13:  -0.2422 L23:   0.5450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:  -0.0715 S13:  -0.0298                       
REMARK   3      S21:  -0.0280 S22:   0.0269 S23:  -0.2191                       
REMARK   3      S31:   0.0020 S32:   0.2272 S33:  -0.0211                       
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 :   B   275        B   300                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8993 -10.7116 -45.3349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1133 T22:  -0.1853                                     
REMARK   3      T33:  -0.0712 T12:  -0.0304                                     
REMARK   3      T13:   0.0308 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8532 L22:   2.3968                                     
REMARK   3      L33:  12.7894 L12:   0.3518                                     
REMARK   3      L13:   0.9605 L23:  -0.1212                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1193 S12:  -0.0828 S13:   0.1496                       
REMARK   3      S21:  -0.0453 S22:  -0.0011 S23:   0.0301                       
REMARK   3      S31:  -0.2456 S32:  -0.1377 S33:  -0.1182                       
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   424        C   440                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.8971  -2.2014 -10.6698              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1074 T22:   0.0239                                     
REMARK   3      T33:   0.2392 T12:   0.1262                                     
REMARK   3      T13:  -0.0863 T23:   0.0610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.3671 L22:   2.9385                                     
REMARK   3      L33:   2.1535 L12:   0.9898                                     
REMARK   3      L13:  -3.8608 L23:   1.0581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2912 S12:  -0.1890 S13:   0.3419                       
REMARK   3      S21:  -0.1799 S22:  -0.2197 S23:  -0.0375                       
REMARK   3      S31:  -0.6255 S32:   0.3116 S33:  -0.0715                       
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   441        C   469                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.7428  -9.5846  -6.2713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1273 T22:  -0.0664                                     
REMARK   3      T33:   0.0835 T12:   0.0641                                     
REMARK   3      T13:  -0.0764 T23:   0.0168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4119 L22:   2.6934                                     
REMARK   3      L33:   4.6305 L12:  -0.3496                                     
REMARK   3      L13:  -1.0499 L23:   0.8051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1081 S12:   0.0660 S13:   0.4403                       
REMARK   3      S21:   0.0417 S22:   0.1209 S23:   0.2661                       
REMARK   3      S31:  -0.2282 S32:  -0.4677 S33:  -0.2290                       
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 :   C   470        C   483                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8275 -31.2383 -30.6222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1434 T22:   0.2377                                     
REMARK   3      T33:  -0.0396 T12:  -0.1095                                     
REMARK   3      T13:  -0.0628 T23:  -0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1922 L22:  17.0053                                     
REMARK   3      L33:   2.9057 L12:  -3.4414                                     
REMARK   3      L13:  -1.8388 L23:   6.0092                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1397 S12:   0.4022 S13:   0.0049                       
REMARK   3      S21:  -0.6216 S22:  -0.0331 S23:   0.4740                       
REMARK   3      S31:  -0.4892 S32:  -0.8219 S33:   0.1729                       
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 :   C   484        C   516                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2723 -49.4945 -37.1442              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1954 T22:   0.0780                                     
REMARK   3      T33:   0.1497 T12:  -0.0392                                     
REMARK   3      T13:  -0.0135 T23:   0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3502 L22:   2.2015                                     
REMARK   3      L33:   1.2550 L12:   0.3112                                     
REMARK   3      L13:  -0.4308 L23:  -0.4667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0670 S12:  -0.2833 S13:  -0.6227                       
REMARK   3      S21:   0.1708 S22:  -0.1486 S23:  -0.0617                       
REMARK   3      S31:   0.0340 S32:   0.2235 S33:   0.2156                       
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 :   C   517        C   583                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5383 -48.2012 -40.8594              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1101 T22:   0.0593                                     
REMARK   3      T33:   0.0392 T12:  -0.0287                                     
REMARK   3      T13:  -0.0263 T23:   0.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8012 L22:   1.1047                                     
REMARK   3      L33:   0.8826 L12:   0.2757                                     
REMARK   3      L13:  -0.5453 L23:   0.0377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0499 S12:   0.0803 S13:  -0.6339                       
REMARK   3      S21:   0.0360 S22:  -0.0155 S23:  -0.2082                       
REMARK   3      S31:   0.1446 S32:   0.2225 S33:   0.0654                       
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   424        D   430                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9218  -1.2639 -29.5577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1570 T22:   0.1511                                     
REMARK   3      T33:   0.1777 T12:   0.0115                                     
REMARK   3      T13:   0.0409 T23:  -0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.5603 L22:  12.4414                                     
REMARK   3      L33:  88.1094 L12:   6.1522                                     
REMARK   3      L13: -31.9143 L23: -17.1776                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3920 S12:  -0.2051 S13:   1.0912                       
REMARK   3      S21:   0.8918 S22:   0.5643 S23:   0.8676                       
REMARK   3      S31:  -1.5249 S32:  -1.0817 S33:  -1.9563                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   431        D   443                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1152  -4.1072 -52.1215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0034 T22:  -0.1091                                     
REMARK   3      T33:  -0.0179 T12:  -0.0408                                     
REMARK   3      T13:  -0.0239 T23:   0.0523                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.3351 L22:  11.5964                                     
REMARK   3      L33:  12.6218 L12:  -2.6670                                     
REMARK   3      L13:  -8.9210 L23:   4.6527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1919 S12:   0.8068 S13:  -0.0683                       
REMARK   3      S21:  -0.5707 S22:  -0.1418 S23:  -0.6739                       
REMARK   3      S31:  -0.1767 S32:  -0.1645 S33:  -0.0501                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   444        D   469                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3247  -8.9820 -45.1727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1196 T22:  -0.1695                                     
REMARK   3      T33:  -0.0502 T12:  -0.0029                                     
REMARK   3      T13:  -0.0142 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2535 L22:   1.8137                                     
REMARK   3      L33:   5.0216 L12:   0.7703                                     
REMARK   3      L13:  -1.7935 L23:  -1.5972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1470 S12:   0.0349 S13:   0.2087                       
REMARK   3      S21:   0.0760 S22:   0.0423 S23:  -0.0232                       
REMARK   3      S31:  -0.0330 S32:   0.0195 S33:  -0.1893                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   470        D   489                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6220 -36.6330 -24.5171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1575 T22:   0.1265                                     
REMARK   3      T33:  -0.0161 T12:   0.0431                                     
REMARK   3      T13:  -0.0770 T23:   0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8000 L22:  25.3960                                     
REMARK   3      L33:   2.1430 L12:   1.9694                                     
REMARK   3      L13:  -1.9527 L23:  -2.8933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0249 S12:  -0.2166 S13:  -0.2641                       
REMARK   3      S21:   0.8593 S22:  -0.1773 S23:  -0.0351                       
REMARK   3      S31:   0.3843 S32:   0.1774 S33:   0.1524                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3EGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000049291.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111) CHANNEL CUT                
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : DOUBLE CRYSTAL CHANNEL CUT,        
REMARK 200                                   SI(111), 1M LONG RH COATED         
REMARK 200                                   TOROIDAL MIRROR FOR VERTICAL AND   
REMARK 200                                   HORIZONTAL FOCUSING                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91570                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.59600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.980                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 3E7A AND 2G5M                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NACL, 0.1M MES, 10% PEG 4000, PH    
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       59.83750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.20900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.83750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.20900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 476  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ASN A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     TYR A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     ARG A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     ILE A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     ARG A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     LYS A   330                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     MET B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     ASN B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     GLY B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     TYR B   306                                                      
REMARK 465     GLY B   307                                                      
REMARK 465     GLN B   308                                                      
REMARK 465     PHE B   309                                                      
REMARK 465     SER B   310                                                      
REMARK 465     GLY B   311                                                      
REMARK 465     LEU B   312                                                      
REMARK 465     ASN B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     GLY B   316                                                      
REMARK 465     ARG B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     ILE B   319                                                      
REMARK 465     THR B   320                                                      
REMARK 465     PRO B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     ARG B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     SER B   325                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     LYS B   327                                                      
REMARK 465     ALA B   328                                                      
REMARK 465     LYS B   329                                                      
REMARK 465     LYS B   330                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     MET C     0                                                      
REMARK 465     ASP C   417                                                      
REMARK 465     GLU C   418                                                      
REMARK 465     GLU C   419                                                      
REMARK 465     ASP C   420                                                      
REMARK 465     GLY C   421                                                      
REMARK 465     GLU C   422                                                      
REMARK 465     PRO C   423                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     ASP D   417                                                      
REMARK 465     GLU D   418                                                      
REMARK 465     GLU D   419                                                      
REMARK 465     ASP D   420                                                      
REMARK 465     GLY D   421                                                      
REMARK 465     GLU D   422                                                      
REMARK 465     PRO D   423                                                      
REMARK 465     GLU D   490                                                      
REMARK 465     ARG D   491                                                      
REMARK 465     LEU D   492                                                      
REMARK 465     GLU D   493                                                      
REMARK 465     LEU D   494                                                      
REMARK 465     PHE D   495                                                      
REMARK 465     PRO D   496                                                      
REMARK 465     VAL D   497                                                      
REMARK 465     GLU D   498                                                      
REMARK 465     LEU D   499                                                      
REMARK 465     GLU D   500                                                      
REMARK 465     LYS D   501                                                      
REMARK 465     ASP D   502                                                      
REMARK 465     SER D   503                                                      
REMARK 465     GLU D   504                                                      
REMARK 465     GLY D   505                                                      
REMARK 465     LEU D   506                                                      
REMARK 465     GLY D   507                                                      
REMARK 465     ILE D   508                                                      
REMARK 465     SER D   509                                                      
REMARK 465     ILE D   510                                                      
REMARK 465     ILE D   511                                                      
REMARK 465     GLY D   512                                                      
REMARK 465     MET D   513                                                      
REMARK 465     GLY D   514                                                      
REMARK 465     ALA D   515                                                      
REMARK 465     GLY D   516                                                      
REMARK 465     ALA D   517                                                      
REMARK 465     ASP D   518                                                      
REMARK 465     MET D   519                                                      
REMARK 465     GLY D   520                                                      
REMARK 465     LEU D   521                                                      
REMARK 465     GLU D   522                                                      
REMARK 465     LYS D   523                                                      
REMARK 465     LEU D   524                                                      
REMARK 465     GLY D   525                                                      
REMARK 465     ILE D   526                                                      
REMARK 465     PHE D   527                                                      
REMARK 465     VAL D   528                                                      
REMARK 465     LYS D   529                                                      
REMARK 465     THR D   530                                                      
REMARK 465     VAL D   531                                                      
REMARK 465     THR D   532                                                      
REMARK 465     GLU D   533                                                      
REMARK 465     GLY D   534                                                      
REMARK 465     GLY D   535                                                      
REMARK 465     ALA D   536                                                      
REMARK 465     ALA D   537                                                      
REMARK 465     HIS D   538                                                      
REMARK 465     ARG D   539                                                      
REMARK 465     ASP D   540                                                      
REMARK 465     GLY D   541                                                      
REMARK 465     ARG D   542                                                      
REMARK 465     ILE D   543                                                      
REMARK 465     GLN D   544                                                      
REMARK 465     VAL D   545                                                      
REMARK 465     ASN D   546                                                      
REMARK 465     ASP D   547                                                      
REMARK 465     LEU D   548                                                      
REMARK 465     LEU D   549                                                      
REMARK 465     VAL D   550                                                      
REMARK 465     GLU D   551                                                      
REMARK 465     VAL D   552                                                      
REMARK 465     ASP D   553                                                      
REMARK 465     GLY D   554                                                      
REMARK 465     THR D   555                                                      
REMARK 465     SER D   556                                                      
REMARK 465     LEU D   557                                                      
REMARK 465     VAL D   558                                                      
REMARK 465     GLY D   559                                                      
REMARK 465     VAL D   560                                                      
REMARK 465     THR D   561                                                      
REMARK 465     GLN D   562                                                      
REMARK 465     SER D   563                                                      
REMARK 465     PHE D   564                                                      
REMARK 465     ALA D   565                                                      
REMARK 465     ALA D   566                                                      
REMARK 465     SER D   567                                                      
REMARK 465     VAL D   568                                                      
REMARK 465     LEU D   569                                                      
REMARK 465     ARG D   570                                                      
REMARK 465     ASN D   571                                                      
REMARK 465     THR D   572                                                      
REMARK 465     LYS D   573                                                      
REMARK 465     GLY D   574                                                      
REMARK 465     ARG D   575                                                      
REMARK 465     VAL D   576                                                      
REMARK 465     ARG D   577                                                      
REMARK 465     PHE D   578                                                      
REMARK 465     MET D   579                                                      
REMARK 465     ILE D   580                                                      
REMARK 465     GLY D   581                                                      
REMARK 465     ARG D   582                                                      
REMARK 465     GLU D   583                                                      
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     ARG A  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  98    CE   NZ                                             
REMARK 470     LYS A 141    CE   NZ                                             
REMARK 470     LYS A 147    CE   NZ                                             
REMARK 470     LYS A 211    CD   CE   NZ                                        
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 234    CD   CE   NZ                                        
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     ASP A 300    CG   OD1  OD2                                       
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 211    CD   CE   NZ                                        
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 234    CD   CE   NZ                                        
REMARK 470     LYS B 260    CE   NZ                                             
REMARK 470     ASP B 300    CG   OD1  OD2                                       
REMARK 470     GLU C 426    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 441    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 442    CG   OD1  OD2                                       
REMARK 470     GLU C 465    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 470    CZ   NH1  NH2                                       
REMARK 470     GLU C 472    CG   CD   OE1  OE2                                  
REMARK 470     MET C 477    CG   SD   CE                                        
REMARK 470     ARG C 491    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 493    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 504    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 533    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 553    CG   OD1  OD2                                       
REMARK 470     GLU C 583    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 426    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 428    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 441    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 442    CG   OD1  OD2                                       
REMARK 470     GLU D 465    CD   OE1  OE2                                       
REMARK 470     GLU D 472    CG   CD   OE1  OE2                                  
REMARK 470     MET D 477    SD   CE                                             
REMARK 470     ARG D 488    CG   CD   NE   CZ   NH1  NH2                        
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    ASP A  95      149.45     79.02                                   
REMARK 500    ARG A  96      -50.53     80.05                                   
REMARK 500    TYR A 144     -112.06   -134.41                                   
REMARK 500    GLU A 167       17.57     56.86                                   
REMARK 500    SER A 224     -148.86     64.03                                   
REMARK 500    ALA A 247     -131.25   -134.42                                   
REMARK 500    HIS A 248      -15.31     80.35                                   
REMARK 500    LYS A 260     -107.00     60.56                                   
REMARK 500    ASP B  95      153.19     79.99                                   
REMARK 500    ARG B  96      -53.67     76.63                                   
REMARK 500    TYR B 144     -109.03   -134.54                                   
REMARK 500    SER B 224     -147.82     66.13                                   
REMARK 500    ALA B 247     -128.69   -133.06                                   
REMARK 500    HIS B 248      -20.75     79.99                                   
REMARK 500    LYS B 260     -109.44     64.28                                   
REMARK 500    ASN B 271       52.38     39.37                                   
REMARK 500    CYS B 273       33.82     39.08                                   
REMARK 500    ASP C 442       81.65     33.21                                   
REMARK 500    ASP C 502     -164.86   -102.80                                   
REMARK 500    ASP C 553       46.89     39.43                                   
REMARK 500    ASP D 442       71.07     42.14                                   
REMARK 500    LYS D 487       14.50    -67.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     MES B   405                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 331                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 331                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3E7A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1S70   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FJM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2G5M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EGH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HVQ   RELATED DB: PDB                                   
DBREF  3EGG A    7   330  UNP    P62136   PP1A_HUMAN       7    330             
DBREF  3EGG B    7   330  UNP    P62136   PP1A_HUMAN       7    330             
DBREF  3EGG C  417   583  UNP    O35274   NEB2_RAT       417    583             
DBREF  3EGG D  417   583  UNP    O35274   NEB2_RAT       417    583             
SEQADV 3EGG GLY A   -4  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG HIS A   -3  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG MET A   -2  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG GLY A   -1  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG SER A    0  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG GLY B   -4  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG HIS B   -3  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG MET B   -2  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG GLY B   -1  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG SER B    0  UNP  P62136              EXPRESSION TAG                 
SEQADV 3EGG GLY C   -2  UNP  O35274              EXPRESSION TAG                 
SEQADV 3EGG HIS C   -1  UNP  O35274              EXPRESSION TAG                 
SEQADV 3EGG MET C    0  UNP  O35274              EXPRESSION TAG                 
SEQADV 3EGG GLY D   -2  UNP  O35274              EXPRESSION TAG                 
SEQADV 3EGG HIS D   -1  UNP  O35274              EXPRESSION TAG                 
SEQADV 3EGG MET D    0  UNP  O35274              EXPRESSION TAG                 
SEQRES   1 A  329  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 A  329  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 A  329  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 A  329  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 A  329  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 A  329  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 A  329  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 A  329  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 A  329  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 A  329  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 A  329  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 A  329  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 A  329  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 A  329  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 A  329  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 A  329  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 A  329  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 A  329  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 A  329  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 A  329  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 A  329  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 A  329  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 A  329  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES  24 A  329  LYS ASN LYS GLY LYS TYR GLY GLN PHE SER GLY LEU ASN          
SEQRES  25 A  329  PRO GLY GLY ARG PRO ILE THR PRO PRO ARG ASN SER ALA          
SEQRES  26 A  329  LYS ALA LYS LYS                                              
SEQRES   1 B  329  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 B  329  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 B  329  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 B  329  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 B  329  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 B  329  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 B  329  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 B  329  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 B  329  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 B  329  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 B  329  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 B  329  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 B  329  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 B  329  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 B  329  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 B  329  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 B  329  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 B  329  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 B  329  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 B  329  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 B  329  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 B  329  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 B  329  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES  24 B  329  LYS ASN LYS GLY LYS TYR GLY GLN PHE SER GLY LEU ASN          
SEQRES  25 B  329  PRO GLY GLY ARG PRO ILE THR PRO PRO ARG ASN SER ALA          
SEQRES  26 B  329  LYS ALA LYS LYS                                              
SEQRES   1 C  170  GLY HIS MET ASP GLU GLU ASP GLY GLU PRO PRO TYR GLU          
SEQRES   2 C  170  PRO GLU SER GLY CYS VAL GLU ILE PRO GLY LEU SER GLU          
SEQRES   3 C  170  GLU GLU ASP PRO ALA PRO SER ARG LYS ILE HIS PHE SER          
SEQRES   4 C  170  THR ALA PRO ILE GLN VAL PHE SER THR TYR SER ASN GLU          
SEQRES   5 C  170  ASP TYR ASP ARG ARG ASN GLU ASP VAL ASP PRO MET ALA          
SEQRES   6 C  170  ALA SER ALA GLU TYR GLU LEU GLU LYS ARG VAL GLU ARG          
SEQRES   7 C  170  LEU GLU LEU PHE PRO VAL GLU LEU GLU LYS ASP SER GLU          
SEQRES   8 C  170  GLY LEU GLY ILE SER ILE ILE GLY MET GLY ALA GLY ALA          
SEQRES   9 C  170  ASP MET GLY LEU GLU LYS LEU GLY ILE PHE VAL LYS THR          
SEQRES  10 C  170  VAL THR GLU GLY GLY ALA ALA HIS ARG ASP GLY ARG ILE          
SEQRES  11 C  170  GLN VAL ASN ASP LEU LEU VAL GLU VAL ASP GLY THR SER          
SEQRES  12 C  170  LEU VAL GLY VAL THR GLN SER PHE ALA ALA SER VAL LEU          
SEQRES  13 C  170  ARG ASN THR LYS GLY ARG VAL ARG PHE MET ILE GLY ARG          
SEQRES  14 C  170  GLU                                                          
SEQRES   1 D  170  GLY HIS MET ASP GLU GLU ASP GLY GLU PRO PRO TYR GLU          
SEQRES   2 D  170  PRO GLU SER GLY CYS VAL GLU ILE PRO GLY LEU SER GLU          
SEQRES   3 D  170  GLU GLU ASP PRO ALA PRO SER ARG LYS ILE HIS PHE SER          
SEQRES   4 D  170  THR ALA PRO ILE GLN VAL PHE SER THR TYR SER ASN GLU          
SEQRES   5 D  170  ASP TYR ASP ARG ARG ASN GLU ASP VAL ASP PRO MET ALA          
SEQRES   6 D  170  ALA SER ALA GLU TYR GLU LEU GLU LYS ARG VAL GLU ARG          
SEQRES   7 D  170  LEU GLU LEU PHE PRO VAL GLU LEU GLU LYS ASP SER GLU          
SEQRES   8 D  170  GLY LEU GLY ILE SER ILE ILE GLY MET GLY ALA GLY ALA          
SEQRES   9 D  170  ASP MET GLY LEU GLU LYS LEU GLY ILE PHE VAL LYS THR          
SEQRES  10 D  170  VAL THR GLU GLY GLY ALA ALA HIS ARG ASP GLY ARG ILE          
SEQRES  11 D  170  GLN VAL ASN ASP LEU LEU VAL GLU VAL ASP GLY THR SER          
SEQRES  12 D  170  LEU VAL GLY VAL THR GLN SER PHE ALA ALA SER VAL LEU          
SEQRES  13 D  170  ARG ASN THR LYS GLY ARG VAL ARG PHE MET ILE GLY ARG          
SEQRES  14 D  170  GLU                                                          
HET    GOL  A 331       6                                                       
HET    GOL  A 332       6                                                       
HET    GOL  A 333       6                                                       
HET     MN  A 400       1                                                       
HET     MN  A 402       1                                                       
HET    MES  A 403      12                                                       
HET    GOL  B 331       6                                                       
HET    GOL  B 332       6                                                       
HET     MN  B 401       1                                                       
HET     MN  B 403       1                                                       
HET    MES  B 404      12                                                       
HET    MES  B 405      12                                                       
HET    GOL  C   1       6                                                       
HET    GOL  D   1       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  GOL    7(C3 H8 O3)                                                  
FORMUL   8   MN    4(MN 2+)                                                     
FORMUL  10  MES    3(C6 H13 N O4 S)                                             
FORMUL  19  HOH   *521(H2 O)                                                    
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 VAL A   19  SER A   22  5                                   4    
HELIX    3   3 THR A   31  GLN A   49  1                                  19    
HELIX    4   4 GLN A   68  GLY A   80  1                                  13    
HELIX    5   5 GLN A   99  TYR A  114  1                                  16    
HELIX    6   6 CYS A  127  ARG A  132  1                                   6    
HELIX    7   7 GLY A  135  TYR A  144  1                                  10    
HELIX    8   8 ASN A  145  ASN A  157  1                                  13    
HELIX    9   9 MET A  183  ARG A  188  1                                   6    
HELIX   10  10 GLY A  199  SER A  207  1                                   9    
HELIX   11  11 GLY A  228  ASP A  240  1                                  13    
HELIX   12  12 ASN A  271  GLU A  275  5                                   5    
HELIX   13  13 ASN B    8  GLU B   18  1                                  11    
HELIX   14  14 VAL B   19  SER B   22  5                                   4    
HELIX   15  15 THR B   31  GLN B   49  1                                  19    
HELIX   16  16 GLN B   68  GLY B   80  1                                  13    
HELIX   17  17 GLN B   99  TYR B  114  1                                  16    
HELIX   18  18 CYS B  127  ARG B  132  1                                   6    
HELIX   19  19 GLY B  135  TYR B  144  1                                  10    
HELIX   20  20 ASN B  145  ASN B  157  1                                  13    
HELIX   21  21 MET B  183  ARG B  188  1                                   6    
HELIX   22  22 GLY B  199  SER B  207  1                                   9    
HELIX   23  23 GLY B  228  ASP B  240  1                                  13    
HELIX   24  24 ASN B  271  GLU B  275  5                                   5    
HELIX   25  25 ASP C  475  GLU C  490  1                                  16    
HELIX   26  26 GLY C  535  GLY C  541  1                                   7    
HELIX   27  27 THR C  561  THR C  572  1                                  12    
HELIX   28  28 ASP D  475  LYS D  487  1                                  13    
SHEET    1   A 6 LEU A  52  LEU A  55  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ILE A 164   N  LEU A  53           
SHEET    3   A 6 ILE A 169  CYS A 172 -1  O  CYS A 171   N  ALA A 163           
SHEET    4   A 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5   A 6 LEU A 263  LEU A 266  1  O  VAL A 264   N  ILE A 244           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  PHE A 258   O  LEU A 263           
SHEET    1   B 7 PHE A 118  LEU A 120  0                                        
SHEET    2   B 7 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   B 7 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4   B 7 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   B 7 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6   B 7 ILE C 456  THR C 461  1  O  PHE C 459   N  ILE A 295           
SHEET    7   B 7 CYS C 431  ILE C 434 -1  N  VAL C 432   O  VAL C 458           
SHEET    1   C 6 PHE A 118  LEU A 120  0                                        
SHEET    2   C 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3   C 6 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4   C 6 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   C 6 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6   C 6 HIS C 450  PHE C 451  1  O  HIS C 450   N  CYS A 291           
SHEET    1   D 3 ASP A 208  PRO A 209  0                                        
SHEET    2   D 3 PHE A 225  PHE A 227  1  O  PHE A 225   N  ASP A 208           
SHEET    3   D 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1   E 6 LEU B  52  LEU B  55  0                                        
SHEET    2   E 6 ALA B 162  VAL B 165  1  O  ILE B 164   N  LEU B  55           
SHEET    3   E 6 ILE B 169  CYS B 172 -1  O  CYS B 171   N  ALA B 163           
SHEET    4   E 6 LEU B 243  ARG B 246  1  O  CYS B 245   N  PHE B 170           
SHEET    5   E 6 LEU B 263  LEU B 266  1  O  LEU B 266   N  ARG B 246           
SHEET    6   E 6 TYR B 255  PHE B 258 -1  N  PHE B 258   O  LEU B 263           
SHEET    1   F 7 PHE B 118  LEU B 120  0                                        
SHEET    2   F 7 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3   F 7 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4   F 7 GLY B 280  VAL B 285 -1  O  MET B 283   N  ILE B  61           
SHEET    5   F 7 MET B 290  PRO B 298 -1  O  LEU B 296   N  GLY B 280           
SHEET    6   F 7 ILE D 456  THR D 461  1  O  PHE D 459   N  ILE B 295           
SHEET    7   F 7 CYS D 431  ILE D 434 -1  N  VAL D 432   O  VAL D 458           
SHEET    1   G 6 PHE B 118  LEU B 120  0                                        
SHEET    2   G 6 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3   G 6 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4   G 6 GLY B 280  VAL B 285 -1  O  MET B 283   N  ILE B  61           
SHEET    5   G 6 MET B 290  PRO B 298 -1  O  LEU B 296   N  GLY B 280           
SHEET    6   G 6 HIS D 450  PHE D 451  1  O  HIS D 450   N  CYS B 291           
SHEET    1   H 3 ASP B 208  PRO B 209  0                                        
SHEET    2   H 3 PHE B 225  PHE B 227  1  O  PHE B 227   N  ASP B 208           
SHEET    3   H 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
SHEET    1   I 4 GLU C 493  GLU C 500  0                                        
SHEET    2   I 4 ARG C 575  ARG C 582 -1  O  PHE C 578   N  VAL C 497           
SHEET    3   I 4 LEU C 548  VAL C 552 -1  N  LEU C 548   O  GLY C 581           
SHEET    4   I 4 THR C 555  SER C 556 -1  O  THR C 555   N  VAL C 552           
SHEET    1   J 2 ILE C 508  MET C 513  0                                        
SHEET    2   J 2 GLY C 525  VAL C 531 -1  O  GLY C 525   N  MET C 513           
CISPEP   1 ALA A   57    PRO A   58          0         1.37                     
CISPEP   2 PRO A   82    PRO A   83          0         6.47                     
CISPEP   3 ARG A  191    PRO A  192          0         1.60                     
CISPEP   4 ALA B   57    PRO B   58          0         2.85                     
CISPEP   5 PRO B   82    PRO B   83          0         1.66                     
CISPEP   6 ARG B  191    PRO B  192          0        -0.01                     
SITE     1 AC1  1 GLN A  20                                                     
SITE     1 AC2  8 PRO A  58  LEU A  59  LYS A  60  SER A  85                    
SITE     2 AC2  8 ASN A  86  VAL A 285  HOH A 533  HOH C 636                    
SITE     1 AC3  6 LYS A  41  SER A  48  GLN A  49  PRO A  50                    
SITE     2 AC3  6 GLU A 116  HOH B 495                                          
SITE     1 AC4  7 ASP A  64  HIS A  66  ASP A  92   MN A 402                    
SITE     2 AC4  7 MES A 403  HOH A 457  HOH A 458                               
SITE     1 AC5  7 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC5  7  MN A 400  MES A 403  HOH A 457                               
SITE     1 AC6 14 HIS A  66  ASP A  92  ARG A  96  ASN A 124                    
SITE     2 AC6 14 HIS A 125  TYR A 134  TRP A 206  ARG A 221                    
SITE     3 AC6 14 HIS A 248  TYR A 272   MN A 400   MN A 402                    
SITE     4 AC6 14 HOH A 457  HOH A 458                                          
SITE     1 AC7  3 LEU B  17  GLN B  20  PHE B  81                               
SITE     1 AC8  8 PRO B  58  LEU B  59  LYS B  60  SER B  85                    
SITE     2 AC8  8 ASN B  86  VAL B 285  HOH B 638  HOH B 639                    
SITE     1 AC9  7 ASP B  64  HIS B  66  ASP B  92   MN B 403                    
SITE     2 AC9  7 MES B 404  HOH B 653  HOH B 654                               
SITE     1 BC1  7 ASP B  92  ASN B 124  HIS B 173  HIS B 248                    
SITE     2 BC1  7  MN B 401  MES B 404  HOH B 653                               
SITE     1 BC2 12 HIS B  66  ASP B  92  ARG B  96  ASN B 124                    
SITE     2 BC2 12 HIS B 125  TYR B 134  ARG B 221  HIS B 248                    
SITE     3 BC2 12  MN B 401   MN B 403  HOH B 653  HOH B 654                    
SITE     1 BC3  3 SER B 129  VAL B 195  TRP B 206                               
SITE     1 BC4  8 ASP B 253  HOH B 597  HOH B 601  HOH B 602                    
SITE     2 BC4  8 MET C 513  GLY C 514  GLY C 520  HOH C 595                    
SITE     1 BC5  3 HOH B 514  HOH B 640  HIS D 450                               
CRYST1  119.675   84.418  109.164  90.00  93.50  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008356  0.000000  0.000512        0.00000                         
SCALE2      0.000000  0.011846  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009178        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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