GenomeNet

Database: PDB
Entry: 3J16
LinkDB: 3J16
Original site: 3J16 
HEADER    RIBOSOME                                12-DEC-11   3J16              
TITLE     MODELS OF RIBOSOME-BOUND DOM34P AND RLI1P AND THEIR RIBOSOMAL BINDING 
TITLE    2 PARTNERS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DOM34P;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: RLI1P;                                                     
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 28S RIBOSOMAL RNA;                                         
COMPND   9 CHAIN: J;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: 18S RIBOSOMAL RNA;                                         
COMPND  12 CHAIN: K;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: P-SITE TRNA;                                               
COMPND  15 CHAIN: L;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 60S RIBOSOMAL PROTEIN L6;                                  
COMPND  18 CHAIN: F;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 40S RIBOSOMAL PROTEIN S30E;                                
COMPND  21 CHAIN: E;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 60S RIBOSOMAL PROTEIN L10;                                 
COMPND  24 CHAIN: G;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 40S RIBOSOMAL PROTEIN S6E;                                 
COMPND  27 CHAIN: C;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 60S RIBOSOMAL PROTEIN L11;                                 
COMPND  30 CHAIN: H;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 40S RIBOSOMAL PROTEIN S24E;                                
COMPND  33 CHAIN: I;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 40S RIBOSOMAL PROTEIN S24-A;                               
COMPND  36 CHAIN: D                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_TAXID: 4932;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   6 ORGANISM_TAXID: 4932;                                                
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   9 ORGANISM_TAXID: 4932;                                                
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  12 ORGANISM_TAXID: 4932;                                                
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  15 ORGANISM_TAXID: 4932;                                                
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  18 ORGANISM_TAXID: 4932;                                                
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  21 ORGANISM_TAXID: 4932;                                                
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  24 ORGANISM_TAXID: 4932;                                                
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  27 ORGANISM_TAXID: 4932;                                                
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  30 ORGANISM_TAXID: 4932;                                                
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  33 ORGANISM_TAXID: 4932;                                                
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  36 ORGANISM_TAXID: 4932                                                 
KEYWDS    RIBOSOME RECYCLING, TRANSLATION, EUKARYA, RIBOSOME                    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    T.BECKER,S.FRANCKENBERG,S.WICKLES,C.J.SHOEMAKER,A.M.ANGER,J.-         
AUTHOR   2 P.ARMACHE,H.SIEBER,C.UNGEWICKELL,O.BERNINGHAUSEN,I.DABERKOW,         
AUTHOR   3 A.KARCHER,M.THOMM,K.-P.HOPFNER,R.GREEN,R.BECKMANN                    
REVDAT   5   30-MAY-12 3J16    1       COMPND REMARK                            
REVDAT   4   18-APR-12 3J16    1       JRNL                                     
REVDAT   3   28-MAR-12 3J16    1       JRNL                                     
REVDAT   2   29-FEB-12 3J16    1       JRNL                                     
REVDAT   1   22-FEB-12 3J16    0                                                
JRNL        AUTH   T.BECKER,S.FRANCKENBERG,S.WICKLES,C.J.SHOEMAKER,A.M.ANGER,   
JRNL        AUTH 2 J.-P.ARMACHE,H.SIEBER,C.UNGEWICKELL,O.BERNINGHAUSEN,         
JRNL        AUTH 3 I.DABERKOW,A.KARCHER,M.THOMM,K.P.HOPFNER,R.GREEN,R.BECKMANN  
JRNL        TITL   STRUCTURAL BASIS OF HIGHLY CONSERVED RIBOSOME RECYCLING IN   
JRNL        TITL 2 EUKARYOTES AND ARCHAEA.                                      
JRNL        REF    NATURE                        V. 482   501 2012              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   22358840                                                     
JRNL        DOI    10.1038/NATURE10829                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    7.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : SINGLE PARTICLE                           
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 7.200                          
REMARK   3   NUMBER OF PARTICLES               : NULL                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 3J16 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB160120.                                      
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : ASYMMETRIC                        
REMARK 245   NAME OF SAMPLE                 : DOM34P-RLI1P COMPLEX              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : ETHANE (VITROBOT)                 
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : NULL                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : NULL                           
REMARK 245   DETECTOR TYPE                     : NULL                           
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : NULL                           
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : NULL                           
REMARK 245   ILLUMINATION MODE                 : NULL                           
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : NULL                           
REMARK 245   ACCELERATION VOLTAGE (KV)         : NULL                           
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, J, K, L, F, E, G, C,            
REMARK 350                    AND CHAINS: H, I, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     LYS E     3                                                      
REMARK 465     VAL E     4                                                      
REMARK 465     HIS E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     VAL E    62                                                      
REMARK 465     GLN E    63                                                      
REMARK 465     SER G   200                                                      
REMARK 465     ILE G   201                                                      
REMARK 465     LEU G   202                                                      
REMARK 465     ASP G   203                                                      
REMARK 465     ILE G   204                                                      
REMARK 465     THR G   205                                                      
REMARK 465     ASP G   206                                                      
REMARK 465     GLU G   207                                                      
REMARK 465     GLU G   208                                                      
REMARK 465     LEU G   209                                                      
REMARK 465     VAL G   210                                                      
REMARK 465     SER G   211                                                      
REMARK 465     HIS G   212                                                      
REMARK 465     PHE G   213                                                      
REMARK 465     VAL G   214                                                      
REMARK 465     SER G   215                                                      
REMARK 465     ALA G   216                                                      
REMARK 465     VAL G   217                                                      
REMARK 465     SER G   218                                                      
REMARK 465     THR G   219                                                      
REMARK 465     ILE G   220                                                      
REMARK 465     ALA G   221                                                      
REMARK 465     SER G   222                                                      
REMARK 465     ILE G   223                                                      
REMARK 465     SER G   224                                                      
REMARK 465     LEU G   225                                                      
REMARK 465     ALA G   226                                                      
REMARK 465     ILE G   227                                                      
REMARK 465     GLY G   228                                                      
REMARK 465     TYR G   229                                                      
REMARK 465     PRO G   230                                                      
REMARK 465     THR G   231                                                      
REMARK 465     LEU G   232                                                      
REMARK 465     PRO G   233                                                      
REMARK 465     SER G   234                                                      
REMARK 465     VAL G   235                                                      
REMARK 465     GLY G   236                                                      
REMARK 465     HIS G   237                                                      
REMARK 465     THR G   238                                                      
REMARK 465     LEU G   239                                                      
REMARK 465     ILE G   240                                                      
REMARK 465     ASN G   241                                                      
REMARK 465     ASN G   242                                                      
REMARK 465     TYR G   243                                                      
REMARK 465     LYS G   244                                                      
REMARK 465     ASP G   245                                                      
REMARK 465     LEU G   246                                                      
REMARK 465     LEU G   247                                                      
REMARK 465     ALA G   248                                                      
REMARK 465     VAL G   249                                                      
REMARK 465     ALA G   250                                                      
REMARK 465     ILE G   251                                                      
REMARK 465     ALA G   252                                                      
REMARK 465     ALA G   253                                                      
REMARK 465     SER G   254                                                      
REMARK 465     TYR G   255                                                      
REMARK 465     HIS G   256                                                      
REMARK 465     TYR G   257                                                      
REMARK 465     PRO G   258                                                      
REMARK 465     GLU G   259                                                      
REMARK 465     ILE G   260                                                      
REMARK 465     GLU G   261                                                      
REMARK 465     ASP G   262                                                      
REMARK 465     LEU G   263                                                      
REMARK 465     VAL G   264                                                      
REMARK 465     ASP G   265                                                      
REMARK 465     ARG G   266                                                      
REMARK 465     ILE G   267                                                      
REMARK 465     GLU G   268                                                      
REMARK 465     ASN G   269                                                      
REMARK 465     PRO G   270                                                      
REMARK 465     GLU G   271                                                      
REMARK 465     LYS G   272                                                      
REMARK 465     TYR G   273                                                      
REMARK 465     ALA G   274                                                      
REMARK 465     ALA G   275                                                      
REMARK 465     ALA G   276                                                      
REMARK 465     ALA G   277                                                      
REMARK 465     PRO G   278                                                      
REMARK 465     ALA G   279                                                      
REMARK 465     ALA G   280                                                      
REMARK 465     THR G   281                                                      
REMARK 465     SER G   282                                                      
REMARK 465     ALA G   283                                                      
REMARK 465     ALA G   284                                                      
REMARK 465     SER G   285                                                      
REMARK 465     GLY G   286                                                      
REMARK 465     ASP G   287                                                      
REMARK 465     ALA G   288                                                      
REMARK 465     ALA G   289                                                      
REMARK 465     PRO G   290                                                      
REMARK 465     ALA G   291                                                      
REMARK 465     GLU G   292                                                      
REMARK 465     GLU G   293                                                      
REMARK 465     ALA G   294                                                      
REMARK 465     ALA G   295                                                      
REMARK 465     ALA G   296                                                      
REMARK 465     GLU G   297                                                      
REMARK 465     GLU G   298                                                      
REMARK 465     GLU G   299                                                      
REMARK 465     GLU G   300                                                      
REMARK 465     GLU G   301                                                      
REMARK 465     SER G   302                                                      
REMARK 465     ASP G   303                                                      
REMARK 465     ASP G   304                                                      
REMARK 465     ASP G   305                                                      
REMARK 465     MET G   306                                                      
REMARK 465     GLY G   307                                                      
REMARK 465     PHE G   308                                                      
REMARK 465     GLY G   309                                                      
REMARK 465     LEU G   310                                                      
REMARK 465     PHE G   311                                                      
REMARK 465     ASP G   312                                                      
REMARK 465     ARG C   227                                                      
REMARK 465     LYS C   228                                                      
REMARK 465     ARG C   229                                                      
REMARK 465     ARG C   230                                                      
REMARK 465     ALA C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     SER C   233                                                      
REMARK 465     LEU C   234                                                      
REMARK 465     LYS C   235                                                      
REMARK 465     ALA C   236                                                      
REMARK 465     MET H     1                                                      
REMARK 465     PRO H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     LYS H     4                                                      
REMARK 465     PHE H     5                                                      
REMARK 465     ASP H     6                                                      
REMARK 465     PHE H   145                                                      
REMARK 465     LYS H   146                                                      
REMARK 465     ASN H   147                                                      
REMARK 465     PRO H   148                                                      
REMARK 465     HIS H   149                                                      
REMARK 465     ASP H   150                                                      
REMARK 465     ILE H   151                                                      
REMARK 465     ILE H   152                                                      
REMARK 465     GLU H   153                                                      
REMARK 465     GLY H   154                                                      
REMARK 465     ILE H   155                                                      
REMARK 465     ASN H   156                                                      
REMARK 465     ALA H   157                                                      
REMARK 465     GLY H   158                                                      
REMARK 465     GLU H   159                                                      
REMARK 465     ILE H   160                                                      
REMARK 465     GLU H   161                                                      
REMARK 465     ILE H   162                                                      
REMARK 465     PRO H   163                                                      
REMARK 465     GLU H   164                                                      
REMARK 465     ASN H   165                                                      
REMARK 465     MET I     1                                                      
REMARK 465     MET D     1                                                      
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       U J 152    P    OP1  OP2                                       
REMARK 470       A J 412    P    OP1  OP2                                       
REMARK 470       A J 425    P    OP1  OP2                                       
REMARK 470       G J 548    P    OP1  OP2                                       
REMARK 470       U J1175    P    OP1  OP2                                       
REMARK 470       U J1266    P    OP1  OP2                                       
REMARK 470       A J1427    P    OP1  OP2                                       
REMARK 470       A J1631    P    OP1  OP2                                       
REMARK 470       A J1750    P    OP1  OP2                                       
REMARK 470       G K2250    P    OP1  OP2                                       
REMARK 470       G K2283    P    OP1  OP2                                       
REMARK 470       A K2833    P    OP1  OP2                                       
REMARK 470       G K2918    P    OP1  OP2                                       
REMARK 470       G K3015    P    OP1  OP2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B    21    FE2   SF4 B   704              1.11            
REMARK 500   OG   SER B   117    MG     MG B   701              1.12            
REMARK 500   OE2  GLU A   386     CG   GLU B    24              1.33            
REMARK 500   CB   GLN B   589     CD   LYS C    58              1.33            
REMARK 500   O    ARG G     5     N    GLU G     6              1.36            
REMARK 500   O    LEU H    80     CG2  THR H    83              1.40            
REMARK 500   OE1  GLN B   589     CA   LYS C    58              1.41            
REMARK 500   O    ASP G    72     N    PHE G    73              1.49            
REMARK 500   CG   GLN B   589     CD   LYS C    58              1.52            
REMARK 500   SG   CYS B    58    FE4   SF4 B   703              1.52            
REMARK 500   SG   CYS B    29    FE1   SF4 B   703              1.52            
REMARK 500   OE1  GLU A   386     OG   SER B    28              1.56            
REMARK 500   O2'    G J   418     NH2  ARG C    72              1.60            
REMARK 500   CE   LYS A   187     OP1    C L    66              1.63            
REMARK 500   OG   SER H   101     CA   GLY H   140              1.64            
REMARK 500   CD1  ILE H   109     OG1  THR H   129              1.66            
REMARK 500   CB   CYS B    21    FE2   SF4 B   704              1.66            
REMARK 500   NZ   LYS B   116     O3G  ATP B   702              1.68            
REMARK 500   NZ   LYS B   518     CD   ARG F   115              1.69            
REMARK 500   CE   LYS B   116     O3G  ATP B   702              1.71            
REMARK 500   CB   GLN B   589     CE   LYS C    58              1.78            
REMARK 500   O2'    G K  3022     OP2    U K  3023              1.78            
REMARK 500   CD2  LEU H    85     N    GLU H    87              1.80            
REMARK 500   NE2  GLN B   589     CB   LYS C    58              1.82            
REMARK 500   NZ   LYS A    84     OP2    G J   564              1.82            
REMARK 500   O2'    C K  1239     O    ASN H    97              1.84            
REMARK 500   CD   GLN B   589     CB   LYS C    58              1.84            
REMARK 500   O2     C K  2287     O4'    U K  2298              1.85            
REMARK 500   CE   LYS B   116     O3B  ATP B   702              1.86            
REMARK 500   CD   LYS B   116     PB   ATP B   702              1.87            
REMARK 500   OG   SER H   120     CG2  VAL H   128              1.88            
REMARK 500   O3'    G J   419     OG   SER C    96              1.89            
REMARK 500   OD2  ASP A    52     OP1    C J   575              1.89            
REMARK 500   N    GLY B   115     O2B  ATP B   702              1.91            
REMARK 500   OP1    A J   420     N    SER C    96              1.92            
REMARK 500   O5'    C K  1279     CE   MET G     1              1.93            
REMARK 500   CG1  ILE H   109     OG1  THR H   129              1.93            
REMARK 500   C1'    G K  1234     OE1  GLU H   131              1.95            
REMARK 500   OP2    C J  1274     OP1    G J  1428              1.96            
REMARK 500   OE1  GLU A   385     NH1  ARG B    27              1.96            
REMARK 500   O4'    U J   152     CG   GLN C    13              1.96            
REMARK 500   O    LEU H   125     CG2  THR H   129              1.99            
REMARK 500   P      A J   420     OG   SER C    96              1.99            
REMARK 500   O2'    A K  2930     CB   ALA I    38              1.99            
REMARK 500   OP1    A J   420     OG   SER C    96              1.99            
REMARK 500   CE   LYS A   237     O2'    G K  2839              2.00            
REMARK 500   SG   CYS B    21     S1   SF4 B   704              2.00            
REMARK 500   O2'    U J   152     OD1  ASN C     4              2.00            
REMARK 500   OG   SER H   101     N    GLY H   140              2.01            
REMARK 500   NE   ARG B   574     O    PHE B   602              2.01            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      93 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 113   CE1   TYR A 113   CZ      0.087                       
REMARK 500    SER A 171   CA    SER A 171   CB      0.098                       
REMARK 500    SER A 315   CB    SER A 315   OG      0.080                       
REMARK 500    SER A 326   CA    SER A 326   CB      0.098                       
REMARK 500    SER A 357   CA    SER A 357   CB      0.097                       
REMARK 500    GLU A 361   CD    GLU A 361   OE1     0.084                       
REMARK 500    ARG B 311   CD    ARG B 311   NE      0.121                       
REMARK 500    HIS B 516   CB    HIS B 516   CG     -0.100                       
REMARK 500    PHE B 572   N     PHE B 572   CA     -0.122                       
REMARK 500    ILE B 608   C     ILE B 608   O      -0.229                       
REMARK 500    ILE B 608   C     ILE B 608   OXT    -0.229                       
REMARK 500      G J 153   P       G J 153   O5'    -0.061                       
REMARK 500      G J 154   N1      G J 154   C2      0.050                       
REMARK 500      G J 154   C4      G J 154   C5      0.046                       
REMARK 500      U J 155   C4'     U J 155   C3'    -0.078                       
REMARK 500      U J 155   O4'     U J 155   C4'     0.071                       
REMARK 500      A J 156   C6      A J 156   N1      0.061                       
REMARK 500      A J 156   N7      A J 156   C8     -0.045                       
REMARK 500      A J 156   N9      A J 156   C4     -0.036                       
REMARK 500      A J 156   C6      A J 156   N6      0.053                       
REMARK 500      U J 158   N3      U J 158   C4      0.063                       
REMARK 500      U J 159   C2      U J 159   N3      0.056                       
REMARK 500      C J 160   C4'     C J 160   C3'     0.097                       
REMARK 500      U J 159   O3'     C J 160   P      -0.082                       
REMARK 500      A J 417   P       A J 417   O5'    -0.070                       
REMARK 500      A J 417   C5      A J 417   N7     -0.042                       
REMARK 500      A J 417   N9      A J 417   C4     -0.063                       
REMARK 500      G J 457   C2'     G J 457   C1'    -0.083                       
REMARK 500      G J 458   C2      G J 458   N3      0.055                       
REMARK 500      G J 458   C8      G J 458   N9      0.055                       
REMARK 500      G J 459   N1      G J 459   C2      0.060                       
REMARK 500      A J 556   P       A J 556   O5'     0.082                       
REMARK 500      A J 556   C6      A J 556   N6      0.049                       
REMARK 500      A J 555   O3'     A J 556   P      -0.106                       
REMARK 500      U J 558   C2      U J 558   N3      0.042                       
REMARK 500      C J 559   C3'     C J 559   C2'     0.069                       
REMARK 500      C J 559   N1      C J 559   C6      0.038                       
REMARK 500      G J 576   C2'     G J 576   C1'    -0.053                       
REMARK 500      G J 576   C2      G J 576   N3      0.055                       
REMARK 500      G J 577   C2'     G J 577   C1'    -0.058                       
REMARK 500      G J 577   N3      G J 577   C4      0.063                       
REMARK 500      G J 577   C6      G J 577   N1      0.044                       
REMARK 500      G J 576   O3'     G J 577   P      -0.084                       
REMARK 500      U J 578   C2'     U J 578   C1'    -0.074                       
REMARK 500      U J 578   O4'     U J 578   C4'    -0.158                       
REMARK 500      U J 578   C1'     U J 578   N1      0.169                       
REMARK 500      U J 578   O3'     A J 579   P      -0.101                       
REMARK 500      U J1181   O4'     U J1181   C4'    -0.084                       
REMARK 500      C J1180   O3'     U J1181   P      -0.081                       
REMARK 500      A J1183   N9      A J1183   C4     -0.064                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     278 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE A  11   CB  -  CG  -  CD2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    PHE A  11   CB  -  CG  -  CD1 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP A  38   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    PHE A  47   CB  -  CG  -  CD2 ANGL. DEV. = -10.1 DEGREES          
REMARK 500    PHE A  47   CB  -  CG  -  CD1 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    SER A  49   CB  -  CA  -  C   ANGL. DEV. =  27.6 DEGREES          
REMARK 500    LYS A  50   C   -  N   -  CA  ANGL. DEV. =  20.5 DEGREES          
REMARK 500    PHE A  74   CB  -  CG  -  CD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    PHE A  74   CB  -  CG  -  CD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    TYR A  83   CZ  -  CE2 -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    PHE A 122   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ALA A 133   N   -  CA  -  CB  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ASP A 141   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    LEU A 147   CB  -  CG  -  CD1 ANGL. DEV. =  12.5 DEGREES          
REMARK 500    VAL A 157   CB  -  CA  -  C   ANGL. DEV. =  11.8 DEGREES          
REMARK 500    THR A 158   N   -  CA  -  CB  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    SER A 160   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    TYR A 170   CB  -  CG  -  CD2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    TYR A 170   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    MET A 172   CG  -  SD  -  CE  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ASP A 180   N   -  CA  -  CB  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ASN A 204   N   -  CA  -  C   ANGL. DEV. = -26.3 DEGREES          
REMARK 500    PHE A 205   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    PHE A 205   CB  -  CG  -  CD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    LEU A 208   CB  -  CG  -  CD2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    MET A 224   CG  -  SD  -  CE  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    LYS A 226   N   -  CA  -  CB  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    MET A 245   CG  -  SD  -  CE  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    PHE A 246   N   -  CA  -  CB  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ALA A 249   CB  -  CA  -  C   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    TYR A 255   CB  -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TYR A 255   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    TYR A 255   O   -  C   -  N   ANGL. DEV. = -10.1 DEGREES          
REMARK 500    TYR A 268   CG  -  CD2 -  CE2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    SER A 270   N   -  CA  -  CB  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    GLN A 273   N   -  CA  -  C   ANGL. DEV. =  18.5 DEGREES          
REMARK 500    LEU A 272   CA  -  C   -  N   ANGL. DEV. = -14.0 DEGREES          
REMARK 500    LEU A 272   O   -  C   -  N   ANGL. DEV. = -25.9 DEGREES          
REMARK 500    ASP A 274   N   -  CA  -  CB  ANGL. DEV. =  12.4 DEGREES          
REMARK 500    THR A 275   CA  -  CB  -  CG2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LYS A 276   N   -  CA  -  CB  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    LYS A 276   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    TYR A 277   C   -  N   -  CA  ANGL. DEV. =  26.4 DEGREES          
REMARK 500    TYR A 300   CB  -  CG  -  CD2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    TYR A 300   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    TYR A 300   CZ  -  CE2 -  CD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    GLU A 304   CB  -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    TYR A 311   CB  -  CG  -  CD2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    LEU A 318   CB  -  CA  -  C   ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LEU A 324   CB  -  CG  -  CD2 ANGL. DEV. =  13.7 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     749 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A   6      106.33    178.89                                   
REMARK 500    ASP A   9      166.44    -41.52                                   
REMARK 500    ASP A  38      -19.36     88.88                                   
REMARK 500    LYS A  45      -87.56   -141.92                                   
REMARK 500    LYS A  46       67.34    141.57                                   
REMARK 500    THR A  48       57.17    168.94                                   
REMARK 500    LYS A  50     -154.32    -71.71                                   
REMARK 500    LEU A  51     -167.07   -102.37                                   
REMARK 500    ASP A  52       89.22   -179.63                                   
REMARK 500    GLU A  53      170.40     77.07                                   
REMARK 500    LYS A  56      -75.86    -10.61                                   
REMARK 500    LYS A  58     -148.94   -158.28                                   
REMARK 500    SER A  59      -65.16   -155.91                                   
REMARK 500    THR A  60     -131.29    123.92                                   
REMARK 500    ASP A  61     -115.47    113.68                                   
REMARK 500    LEU A  62       74.32    147.34                                   
REMARK 500    THR A  89       82.43     51.77                                   
REMARK 500    ASN A  96      -11.18     57.89                                   
REMARK 500    VAL A  97      124.58    -33.59                                   
REMARK 500    ASP A  98      -20.19    101.25                                   
REMARK 500    LYS A 103      111.13    161.52                                   
REMARK 500    TYR A 104      157.76    -47.06                                   
REMARK 500    ASN A 131       22.72   -142.15                                   
REMARK 500    GLU A 132      -29.11   -141.99                                   
REMARK 500    ALA A 133      -57.59    144.53                                   
REMARK 500    CYS A 134       31.38     85.10                                   
REMARK 500    ILE A 136       20.04    -67.12                                   
REMARK 500    TYR A 138      112.91     68.08                                   
REMARK 500    SER A 140     -141.87   -106.85                                   
REMARK 500    ASP A 141       31.28    153.06                                   
REMARK 500    GLN A 148     -164.15    -71.86                                   
REMARK 500    CYS A 155     -163.45   -117.42                                   
REMARK 500    LEU A 156      142.58    157.90                                   
REMARK 500    SER A 159      -51.19    -16.76                                   
REMARK 500    THR A 162       49.81    -73.69                                   
REMARK 500    GLN A 166      107.61   -175.95                                   
REMARK 500    ILE A 168     -178.32    -52.59                                   
REMARK 500    GLU A 169      137.67    163.59                                   
REMARK 500    TYR A 170     -164.33   -122.70                                   
REMARK 500    LYS A 175       72.93     67.61                                   
REMARK 500    THR A 178      176.70    -48.49                                   
REMARK 500    THR A 179       -6.59    -47.36                                   
REMARK 500    ASP A 180       48.26    124.97                                   
REMARK 500    VAL A 181      105.06      2.27                                   
REMARK 500    LEU A 182      -31.28    -36.53                                   
REMARK 500    LYS A 183      -34.35    -33.62                                   
REMARK 500    PHE A 205       39.75    -63.58                                   
REMARK 500    ASP A 206       20.83   -142.86                                   
REMARK 500    LYS A 207      -44.60   -133.18                                   
REMARK 500    TYR A 255     -158.07    -37.78                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     263 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   48     SER A   49                 -147.37                    
REMARK 500 THR A  158     SER A  159                  130.55                    
REMARK 500 SER A  215     PRO A  216                  142.04                    
REMARK 500 ASP A  241     ASN A  242                 -145.81                    
REMARK 500 GLY A  244     MET A  245                  145.06                    
REMARK 500 THR A  253     GLY A  254                 -147.46                    
REMARK 500 GLY A  254     TYR A  255                  147.07                    
REMARK 500 ASP A  274     THR A  275                  -94.53                    
REMARK 500 LYS A  276     TYR A  277                  110.62                    
REMARK 500 LYS F   21     SER F   22                 -146.91                    
REMARK 500 LEU E    8     ALA E    9                 -144.73                    
REMARK 500 ARG G    5     GLU G    6                  -42.25                    
REMARK 500 VAL G   30     ASP G   31                 -149.04                    
REMARK 500 ALA G   49     VAL G   50                 -135.28                    
REMARK 500 LEU G   52     MET G   53                 -134.33                    
REMARK 500 LYS G   55     ASN G   56                  136.42                    
REMARK 500 ASP G   72     PHE G   73                   79.95                    
REMARK 500 ARG H   16     ALA H   17                 -118.41                    
REMARK 500 LEU H   28     ALA H   29                  143.81                    
REMARK 500 ALA H   29     PRO H   30                  149.28                    
REMARK 500 PRO H   30     LYS H   31                 -119.30                    
REMARK 500 GLY H   33     PRO H   34                  104.76                    
REMARK 500 LYS H   40     LYS H   41                   48.79                    
REMARK 500 VAL H   42     GLY H   43                   46.18                    
REMARK 500 GLY H   43     GLU H   44                  141.84                    
REMARK 500 ALA H   71     SER H   72                 -135.57                    
REMARK 500 ALA H   77     SER H   78                 -136.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 104         0.07    SIDE CHAIN                              
REMARK 500    TYR A 113         0.08    SIDE CHAIN                              
REMARK 500    TYR A 170         0.07    SIDE CHAIN                              
REMARK 500    PHE A 191         0.09    SIDE CHAIN                              
REMARK 500    TYR A 268         0.12    SIDE CHAIN                              
REMARK 500    TYR A 311         0.08    SIDE CHAIN                              
REMARK 500    TYR A 374         0.15    SIDE CHAIN                              
REMARK 500    HIS B 516         0.12    SIDE CHAIN                              
REMARK 500    ARG B 580         0.12    SIDE CHAIN                              
REMARK 500    ARG B 582         0.10    SIDE CHAIN                              
REMARK 500      A J 156         0.08    SIDE CHAIN                              
REMARK 500      C J 415         0.08    SIDE CHAIN                              
REMARK 500      A J 416         0.09    SIDE CHAIN                              
REMARK 500      A J 417         0.10    SIDE CHAIN                              
REMARK 500      A J 556         0.15    SIDE CHAIN                              
REMARK 500      C J 559         0.12    SIDE CHAIN                              
REMARK 500      G J 576         0.07    SIDE CHAIN                              
REMARK 500      G J 577         0.14    SIDE CHAIN                              
REMARK 500      U J 578         0.11    SIDE CHAIN                              
REMARK 500      U J 588         0.07    SIDE CHAIN                              
REMARK 500      U J1181         0.11    SIDE CHAIN                              
REMARK 500      U J1182         0.07    SIDE CHAIN                              
REMARK 500      A J1184         0.10    SIDE CHAIN                              
REMARK 500      U J1185         0.10    SIDE CHAIN                              
REMARK 500      C J1632         0.07    SIDE CHAIN                              
REMARK 500      A J1633         0.08    SIDE CHAIN                              
REMARK 500      A J1635         0.06    SIDE CHAIN                              
REMARK 500      G J1642         0.12    SIDE CHAIN                              
REMARK 500      C J1644         0.08    SIDE CHAIN                              
REMARK 500      U J1650         0.11    SIDE CHAIN                              
REMARK 500      A J1750         0.08    SIDE CHAIN                              
REMARK 500      U J1752         0.08    SIDE CHAIN                              
REMARK 500      G J1760         0.08    SIDE CHAIN                              
REMARK 500      U J1761         0.09    SIDE CHAIN                              
REMARK 500      A J1766         0.06    SIDE CHAIN                              
REMARK 500      G K1236         0.11    SIDE CHAIN                              
REMARK 500      G K1237         0.12    SIDE CHAIN                              
REMARK 500      G K1242         0.15    SIDE CHAIN                              
REMARK 500      G K1243         0.05    SIDE CHAIN                              
REMARK 500      A K1245         0.08    SIDE CHAIN                              
REMARK 500      G K2250         0.06    SIDE CHAIN                              
REMARK 500      G K2251         0.06    SIDE CHAIN                              
REMARK 500      U K2254         0.07    SIDE CHAIN                              
REMARK 500      C K2257         0.12    SIDE CHAIN                              
REMARK 500      U K2258         0.10    SIDE CHAIN                              
REMARK 500      U K2260         0.07    SIDE CHAIN                              
REMARK 500      G K2261         0.12    SIDE CHAIN                              
REMARK 500      A K2262         0.10    SIDE CHAIN                              
REMARK 500      U K2264         0.07    SIDE CHAIN                              
REMARK 500      U K2266         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      69 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU A 272         33.64                                           
REMARK 500    TYR A 277         12.61                                           
REMARK 500    PHE B 572         16.39                                           
REMARK 500    ARG E  10         10.30                                           
REMARK 500    ARG G   5         70.44                                           
REMARK 500    ASP G  72        -79.80                                           
REMARK 500    PRO H  39         11.71                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500      U L  11       -46.7      D          D   OUTSIDE RANGE           
REMARK 500      G L  22       -19.7      D          D   OUTSIDE RANGE           
REMARK 500      G L  26       -23.8      D          D   OUTSIDE RANGE           
REMARK 500      G L  41       -19.7      D          D   OUTSIDE RANGE           
REMARK 500      C L  43       -23.2      D          D   OUTSIDE RANGE           
REMARK 500      U L  47       -46.3      D          D   OUTSIDE RANGE           
REMARK 500      A L  75       -45.2      D          D   OUTSIDE RANGE           
REMARK 500    LYS A  56        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 133        17.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 141        11.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 147        24.5      L          L   OUTSIDE RANGE           
REMARK 500    THR A 158        21.1      L          L   OUTSIDE RANGE           
REMARK 500    SER A 159        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 168        20.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 181        23.1      L          L   OUTSIDE RANGE           
REMARK 500    THR A 188        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 204        46.8      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 208        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 226        21.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 263        24.1      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 273        21.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 274        20.4      L          L   OUTSIDE RANGE           
REMARK 500    TYR A 277        19.4      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 293        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 295        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 296        20.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 304        21.2      L          L   OUTSIDE RANGE           
REMARK 500    THR A 366        15.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 376        22.1      L          L   OUTSIDE RANGE           
REMARK 500    PRO B 183        46.3      L          L   OUTSIDE RANGE           
REMARK 500    ILE F   4        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ILE F  41        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASN F 116        22.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS F 121        20.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE F 172        23.6      L          L   OUTSIDE RANGE           
REMARK 500    ALA E   9        22.4      L          L   OUTSIDE RANGE           
REMARK 500    ARG E  10        46.6      L          L   OUTSIDE RANGE           
REMARK 500    ASN E  57        21.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR G  18        22.1      L          L   OUTSIDE RANGE           
REMARK 500    SER G  35        11.0      L          L   OUTSIDE RANGE           
REMARK 500    HIS G  39        20.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP G  72        55.8      L          L   OUTSIDE RANGE           
REMARK 500    PHE G  73        16.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL H  18        15.7      L          L   OUTSIDE RANGE           
REMARK 500    ALA H  29        18.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL H  42        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE H  56        21.9      L          L   OUTSIDE RANGE           
REMARK 500    THR H  59        24.0      L          L   OUTSIDE RANGE           
REMARK 500    LYS H  63        21.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE H  64        19.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 CHIRALITY DEVIATIONS.                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 703  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  55   SG                                                     
REMARK 620 2 SF4 B 703   S1  101.0                                              
REMARK 620 3 SF4 B 703   S3  122.9  95.8                                        
REMARK 620 4 SF4 B 703   S4  120.5 101.8 108.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP B 702   O1B                                                    
REMARK 620 2 ATP B 702   O2G  78.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 703  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  61   SG                                                     
REMARK 620 2 SF4 B 703   S1  101.4                                              
REMARK 620 3 SF4 B 703   S2  120.9  99.9                                        
REMARK 620 4 SF4 B 703   S4  121.6 100.6 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 704  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  16   SG                                                     
REMARK 620 2 SF4 B 704   S1  149.6                                              
REMARK 620 3 SF4 B 704   S2   79.6 108.5                                        
REMARK 620 4 SF4 B 704   S3   99.8 106.1 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 704  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 SF4 B 704   S1  146.2                                              
REMARK 620 3 SF4 B 704   S2   90.8 100.1                                        
REMARK 620 4 SF4 B 704   S4  106.2 101.0 107.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 704                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3J15   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EMD-2010   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-2008   RELATED DB: EMDB                              
DBREF  3J16 A    1   386  UNP    P33309   DOM34_YEAST      1    386             
DBREF  3J16 B    1   608  UNP    Q03195   RLI1_YEAST       1    608             
DBREF  3J16 F    1   191  UNP    P05738   RL9A_YEAST       1    191             
DBREF  3J16 E    1    63  UNP    P0CX33   RS30A_YEAST      1     63             
DBREF  3J16 G    1   312  UNP    P05317   RLA0_YEAST       1    312             
DBREF  3J16 C    1   236  UNP    P0CX37   RS6A_YEAST       1    236             
DBREF  3J16 H    1   165  UNP    P0CX53   RL12A_YEAST      1    165             
DBREF  3J16 I    1   137  UNP    P0CX41   RL23A_YEAST      1    137             
DBREF  3J16 D    1   135  UNP    P0CX31   RS24A_YEAST      1    135             
DBREF  3J16 J   36  1769  PDB    3J16     3J16            36   1769             
DBREF  3J16 K 1227  3039  PDB    3J16     3J16          1227   3039             
DBREF  3J16 L    1    75  PDB    3J16     3J16             1     75             
SEQRES   1 A  386  MET LYS VAL ILE SER LEU LYS LYS ASP SER PHE ASN LYS          
SEQRES   2 A  386  GLY GLY ALA VAL ILE THR LEU LEU PRO GLU ASP LYS GLU          
SEQRES   3 A  386  ASP LEU PHE THR VAL TYR GLN ILE VAL ASP LYS ASP ASP          
SEQRES   4 A  386  GLU LEU ILE PHE LYS LYS LYS PHE THR SER LYS LEU ASP          
SEQRES   5 A  386  GLU ALA GLY LYS LYS LYS SER THR ASP LEU VAL LYS LEU          
SEQRES   6 A  386  LYS ILE LYS VAL ILE SER GLU ASP PHE ASP MET LYS ASP          
SEQRES   7 A  386  GLU TYR LEU LYS TYR LYS GLY VAL THR VAL THR ASP GLU          
SEQRES   8 A  386  SER GLY ALA SER ASN VAL ASP ILE PRO VAL GLY LYS TYR          
SEQRES   9 A  386  LEU SER PHE THR LEU ASP TYR VAL TYR PRO PHE THR ILE          
SEQRES  10 A  386  ILE LYS GLN ASN PHE ASN LYS PHE MET GLN LYS LEU LEU          
SEQRES  11 A  386  ASN GLU ALA CYS ASN ILE GLU TYR LYS SER ASP THR ALA          
SEQRES  12 A  386  ALA VAL VAL LEU GLN GLU GLY ILE ALA HIS VAL CYS LEU          
SEQRES  13 A  386  VAL THR SER SER SER THR ILE LEU LYS GLN LYS ILE GLU          
SEQRES  14 A  386  TYR SER MET PRO LYS LYS LYS ARG THR THR ASP VAL LEU          
SEQRES  15 A  386  LYS PHE ASP GLU LYS THR GLU LYS PHE TYR LYS ALA ILE          
SEQRES  16 A  386  TYR SER ALA MET LYS LYS ASP LEU ASN PHE ASP LYS LEU          
SEQRES  17 A  386  LYS THR ILE ILE LEU CYS SER PRO GLY PHE TYR ALA LYS          
SEQRES  18 A  386  ILE LEU MET ASP LYS ILE PHE GLN TYR ALA GLU GLU GLU          
SEQRES  19 A  386  HIS ASN LYS LYS ILE LEU ASP ASN LYS GLY MET PHE PHE          
SEQRES  20 A  386  ILE ALA HIS CYS SER THR GLY TYR LEU GLN GLY ILE ASN          
SEQRES  21 A  386  GLU VAL LEU LYS ASN PRO LEU TYR ALA SER LYS LEU GLN          
SEQRES  22 A  386  ASP THR LYS TYR SER LYS GLU ILE MET VAL MET ASP GLU          
SEQRES  23 A  386  PHE LEU LEU HIS LEU ASN LYS ASP ASP ASP LYS ALA TRP          
SEQRES  24 A  386  TYR GLY GLU LYS GLU VAL VAL LYS ALA ALA GLU TYR GLY          
SEQRES  25 A  386  ALA ILE SER TYR LEU LEU LEU THR ASP LYS VAL LEU HIS          
SEQRES  26 A  386  SER ASP ASN ILE ALA GLN ARG GLU GLU TYR LEU LYS LEU          
SEQRES  27 A  386  MET ASP SER VAL GLU SER ASN GLY GLY LYS ALA LEU VAL          
SEQRES  28 A  386  LEU SER THR LEU HIS SER LEU GLY GLU GLU LEU ASP GLN          
SEQRES  29 A  386  LEU THR GLY ILE ALA CYS ILE LEU LYS TYR PRO LEU PRO          
SEQRES  30 A  386  ASP LEU ASP GLU ASP ASP GLY GLU GLU                          
SEQRES   1 B  608  MET SER ASP LYS ASN SER ARG ILE ALA ILE VAL SER ALA          
SEQRES   2 B  608  ASP LYS CYS LYS PRO LYS LYS CYS ARG GLN GLU CYS LYS          
SEQRES   3 B  608  ARG SER CYS PRO VAL VAL LYS THR GLY LYS LEU CYS ILE          
SEQRES   4 B  608  GLU VAL THR PRO THR SER LYS ILE ALA PHE ILE SER GLU          
SEQRES   5 B  608  ILE LEU CYS ILE GLY CYS GLY ILE CYS VAL LYS LYS CYS          
SEQRES   6 B  608  PRO PHE ASP ALA ILE GLN ILE ILE ASN LEU PRO THR ASN          
SEQRES   7 B  608  LEU GLU ALA HIS VAL THR HIS ARG TYR SER ALA ASN SER          
SEQRES   8 B  608  PHE LYS LEU HIS ARG LEU PRO THR PRO ARG PRO GLY GLN          
SEQRES   9 B  608  VAL LEU GLY LEU VAL GLY THR ASN GLY ILE GLY LYS SER          
SEQRES  10 B  608  THR ALA LEU LYS ILE LEU ALA GLY LYS GLN LYS PRO ASN          
SEQRES  11 B  608  LEU GLY ARG PHE ASP ASP PRO PRO GLU TRP GLN GLU ILE          
SEQRES  12 B  608  ILE LYS TYR PHE ARG GLY SER GLU LEU GLN ASN TYR PHE          
SEQRES  13 B  608  THR LYS MET LEU GLU ASP ASP ILE LYS ALA ILE ILE LYS          
SEQRES  14 B  608  PRO GLN TYR VAL ASP ASN ILE PRO ARG ALA ILE LYS GLY          
SEQRES  15 B  608  PRO VAL GLN LYS VAL GLY GLU LEU LEU LYS LEU ARG MET          
SEQRES  16 B  608  GLU LYS SER PRO GLU ASP VAL LYS ARG TYR ILE LYS ILE          
SEQRES  17 B  608  LEU GLN LEU GLU ASN VAL LEU LYS ARG ASP ILE GLU LYS          
SEQRES  18 B  608  LEU SER GLY GLY GLU LEU GLN ARG PHE ALA ILE GLY MET          
SEQRES  19 B  608  SER CYS VAL GLN GLU ALA ASP VAL TYR MET PHE ASP GLU          
SEQRES  20 B  608  PRO SER SER TYR LEU ASP VAL LYS GLN ARG LEU ASN ALA          
SEQRES  21 B  608  ALA GLN ILE ILE ARG SER LEU LEU ALA PRO THR LYS TYR          
SEQRES  22 B  608  VAL ILE CYS VAL GLU HIS ASP LEU SER VAL LEU ASP TYR          
SEQRES  23 B  608  LEU SER ASP PHE VAL CYS ILE ILE TYR GLY VAL PRO SER          
SEQRES  24 B  608  VAL TYR GLY VAL VAL THR LEU PRO ALA SER VAL ARG GLU          
SEQRES  25 B  608  GLY ILE ASN ILE PHE LEU ASP GLY HIS ILE PRO ALA GLU          
SEQRES  26 B  608  ASN LEU ARG PHE ARG THR GLU ALA LEU GLN PHE ARG ILE          
SEQRES  27 B  608  ALA ASP ALA THR GLU ASP LEU GLN ASN ASP SER ALA SER          
SEQRES  28 B  608  ARG ALA PHE SER TYR PRO SER LEU LYS LYS THR GLN GLY          
SEQRES  29 B  608  ASP PHE VAL LEU ASN VAL GLU GLU GLY GLU PHE SER ASP          
SEQRES  30 B  608  SER GLU ILE LEU VAL MET MET GLY GLU ASN GLY THR GLY          
SEQRES  31 B  608  LYS THR THR LEU ILE LYS LEU LEU ALA GLY ALA LEU LYS          
SEQRES  32 B  608  PRO ASP GLU GLY GLN ASP ILE PRO LYS LEU ASN VAL SER          
SEQRES  33 B  608  MET LYS PRO GLN LYS ILE ALA PRO LYS PHE PRO GLY THR          
SEQRES  34 B  608  VAL ARG GLN LEU PHE PHE LYS LYS ILE ARG GLY GLN PHE          
SEQRES  35 B  608  LEU ASN PRO GLN PHE GLN THR ASP VAL VAL LYS PRO LEU          
SEQRES  36 B  608  ARG ILE ASP ASP ILE ILE ASP GLN GLU VAL GLN HIS LEU          
SEQRES  37 B  608  SER GLY GLY GLU LEU GLN ARG VAL ALA ILE VAL LEU ALA          
SEQRES  38 B  608  LEU GLY ILE PRO ALA ASP ILE TYR LEU ILE ASP GLU PRO          
SEQRES  39 B  608  SER ALA TYR LEU ASP SER GLU GLN ARG ILE ILE CYS SER          
SEQRES  40 B  608  LYS VAL ILE ARG ARG PHE ILE LEU HIS ASN LYS LYS THR          
SEQRES  41 B  608  ALA PHE ILE VAL GLU HIS ASP PHE ILE MET ALA THR TYR          
SEQRES  42 B  608  LEU ALA ASP LYS VAL ILE VAL PHE GLU GLY ILE PRO SER          
SEQRES  43 B  608  LYS ASN ALA HIS ALA ARG ALA PRO GLU SER LEU LEU THR          
SEQRES  44 B  608  GLY CYS ASN ARG PHE LEU LYS ASN LEU ASN VAL THR PHE          
SEQRES  45 B  608  ARG ARG ASP PRO ASN SER PHE ARG PRO ARG ILE ASN LYS          
SEQRES  46 B  608  LEU ASP SER GLN MET ASP LYS GLU GLN LYS SER SER GLY          
SEQRES  47 B  608  ASN TYR PHE PHE LEU ASP ASN THR GLY ILE                      
SEQRES   1 J  233    C   U   C   A   A   A   G   A   U   U   A   A   G          
SEQRES   2 J  233    C   C   A   U   G   U   G   G   U   A   A   U   U          
SEQRES   3 J  233    C   U   A   A   U   C   C   A   A   G   G   A   A          
SEQRES   4 J  233    A   G   C   A   G   G   C   G   C   G   C   A   A          
SEQRES   5 J  233    A   U   U   A   C   C   C   A   A   U   C   C   U          
SEQRES   6 J  233    A   A   U   U   C   A   G   G   G   A   G   G   U          
SEQRES   7 J  233    A   G   U   G   A   G   G   A   G   G   G   C   A          
SEQRES   8 J  233    A   G   U   C   U   G   G   U   G   C   C   A   G          
SEQRES   9 J  233    C   A   G   C   C   G   C   G   G   U   A   A   U          
SEQRES  10 J  233    U   C   C   A   G   C   U   C   C   U   G   C   G          
SEQRES  11 J  233    G   C   U   U   A   A   U   U   U   G   A   C   U          
SEQRES  12 J  233    C   A   A   C   A   C   G   G   G   G   A   A   A          
SEQRES  13 J  233    C   U   C   A   C   C   U   G   G   U   G   G   U          
SEQRES  14 J  233    G   C   A   U   G   G   C   A   G   G   U   C   U          
SEQRES  15 J  233    G   U   G   A   U   G   C   C   C   U   U   A   C          
SEQRES  16 J  233    A   C   A   C   C   G   C   C   C   G   U   C   G          
SEQRES  17 J  233    C   U   A   G   U   A   C   U   A   A   A   A   G          
SEQRES  18 J  233    U   C   G   U   A   A   C   A   A   G   G   U              
SEQRES   1 K  155    C   C   G   G   A   C   G   G   U   G   G   C   C          
SEQRES   2 K  155    A   U   G   G   A   A   G   U   C   G   G   A   A          
SEQRES   3 K  155    U   C   C   G   C   U   A   A   G   G   A   G   U          
SEQRES   4 K  155    G   U   G   U   A   A   C   A   A   C   U   C   A          
SEQRES   5 K  155    C   C   G   G   C   G   G   A   G   U   A   A   C          
SEQRES   6 K  155    U   A   U   G   A   C   U   C   U   C   G   C   C          
SEQRES   7 K  155    U   C   G   U   C   A   U   C   U   A   A   U   U          
SEQRES   8 K  155    A   A   G   U   C   A   A   G   C   G   U   U   C          
SEQRES   9 K  155    A   U   A   G   C   G   A   C   A   U   U   G   A          
SEQRES  10 K  155    U   U   G   U   U   C   A   C   C   C   A   C   U          
SEQRES  11 K  155    G   A   A   C   U   U   A   G   U   A   C   G   A          
SEQRES  12 K  155    G   A   G   G   A   A   C   A   G   U   U   C              
SEQRES   1 L   75    U   C   C   G   U   G   A   U   A   G   U   U   U          
SEQRES   2 L   75    A   A   U   G   G   U   C   A   G   A   A   U   G          
SEQRES   3 L   75    G   G   C   G   C   U   U   G   U   C   G   C   G          
SEQRES   4 L   75    U   G   C   C   A   G   A   U   C   G   G   G   G          
SEQRES   5 L   75    U   U   C   A   A   U   U   C   C   C   C   G   U          
SEQRES   6 L   75    C   G   C   G   G   A   G   C   C   A                      
SEQRES   1 F  191  MET LYS TYR ILE GLN THR GLU GLN GLN ILE GLU VAL PRO          
SEQRES   2 F  191  GLU GLY VAL THR VAL SER ILE LYS SER ARG ILE VAL LYS          
SEQRES   3 F  191  VAL VAL GLY PRO ARG GLY THR LEU THR LYS ASN LEU LYS          
SEQRES   4 F  191  HIS ILE ASP VAL THR PHE THR LYS VAL ASN ASN GLN LEU          
SEQRES   5 F  191  ILE LYS VAL ALA VAL HIS ASN GLY GLY ARG LYS HIS VAL          
SEQRES   6 F  191  ALA ALA LEU ARG THR VAL LYS SER LEU VAL ASP ASN MET          
SEQRES   7 F  191  ILE THR GLY VAL THR LYS GLY TYR LYS TYR LYS MET ARG          
SEQRES   8 F  191  TYR VAL TYR ALA HIS PHE PRO ILE ASN VAL ASN ILE VAL          
SEQRES   9 F  191  GLU LYS ASP GLY ALA LYS PHE ILE GLU VAL ARG ASN PHE          
SEQRES  10 F  191  LEU GLY ASP LYS LYS ILE ARG ASN VAL PRO VAL ARG ASP          
SEQRES  11 F  191  GLY VAL THR ILE GLU PHE SER THR ASN VAL LYS ASP GLU          
SEQRES  12 F  191  ILE VAL LEU SER GLY ASN SER VAL GLU ASP VAL SER GLN          
SEQRES  13 F  191  ASN ALA ALA ASP LEU GLN GLN ILE CYS ARG VAL ARG ASN          
SEQRES  14 F  191  LYS ASP ILE ARG LYS PHE LEU ASP GLY ILE TYR VAL SER          
SEQRES  15 F  191  HIS LYS GLY PHE ILE THR GLU ASP LEU                          
SEQRES   1 E   63  MET ALA LYS VAL HIS GLY SER LEU ALA ARG ALA GLY LYS          
SEQRES   2 E   63  VAL LYS SER GLN THR PRO LYS VAL GLU LYS THR GLU LYS          
SEQRES   3 E   63  PRO LYS LYS PRO LYS GLY ARG ALA TYR LYS ARG LEU LEU          
SEQRES   4 E   63  TYR THR ARG ARG PHE VAL ASN VAL THR LEU VAL ASN GLY          
SEQRES   5 E   63  LYS ARG ARG MET ASN PRO GLY PRO SER VAL GLN                  
SEQRES   1 G  312  MET GLY GLY ILE ARG GLU LYS LYS ALA GLU TYR PHE ALA          
SEQRES   2 G  312  LYS LEU ARG GLU TYR LEU GLU GLU TYR LYS SER LEU PHE          
SEQRES   3 G  312  VAL VAL GLY VAL ASP ASN VAL SER SER GLN GLN MET HIS          
SEQRES   4 G  312  GLU VAL ARG LYS GLU LEU ARG GLY ARG ALA VAL VAL LEU          
SEQRES   5 G  312  MET GLY LYS ASN THR MET VAL ARG ARG ALA ILE ARG GLY          
SEQRES   6 G  312  PHE LEU SER ASP LEU PRO ASP PHE GLU LYS LEU LEU PRO          
SEQRES   7 G  312  PHE VAL LYS GLY ASN VAL GLY PHE VAL PHE THR ASN GLU          
SEQRES   8 G  312  PRO LEU THR GLU ILE LYS ASN VAL ILE VAL SER ASN ARG          
SEQRES   9 G  312  VAL ALA ALA PRO ALA ARG ALA GLY ALA VAL ALA PRO GLU          
SEQRES  10 G  312  ASP ILE TRP VAL ARG ALA VAL ASN THR GLY MET GLU PRO          
SEQRES  11 G  312  GLY LYS THR SER PHE PHE GLN ALA LEU GLY VAL PRO THR          
SEQRES  12 G  312  LYS ILE ALA ARG GLY THR ILE GLU ILE VAL SER ASP VAL          
SEQRES  13 G  312  LYS VAL VAL ASP ALA GLY ASN LYS VAL GLY GLN SER GLU          
SEQRES  14 G  312  ALA SER LEU LEU ASN LEU LEU ASN ILE SER PRO PHE THR          
SEQRES  15 G  312  PHE GLY LEU THR VAL VAL GLN VAL TYR ASP ASN GLY GLN          
SEQRES  16 G  312  VAL PHE PRO SER SER ILE LEU ASP ILE THR ASP GLU GLU          
SEQRES  17 G  312  LEU VAL SER HIS PHE VAL SER ALA VAL SER THR ILE ALA          
SEQRES  18 G  312  SER ILE SER LEU ALA ILE GLY TYR PRO THR LEU PRO SER          
SEQRES  19 G  312  VAL GLY HIS THR LEU ILE ASN ASN TYR LYS ASP LEU LEU          
SEQRES  20 G  312  ALA VAL ALA ILE ALA ALA SER TYR HIS TYR PRO GLU ILE          
SEQRES  21 G  312  GLU ASP LEU VAL ASP ARG ILE GLU ASN PRO GLU LYS TYR          
SEQRES  22 G  312  ALA ALA ALA ALA PRO ALA ALA THR SER ALA ALA SER GLY          
SEQRES  23 G  312  ASP ALA ALA PRO ALA GLU GLU ALA ALA ALA GLU GLU GLU          
SEQRES  24 G  312  GLU GLU SER ASP ASP ASP MET GLY PHE GLY LEU PHE ASP          
SEQRES   1 C  236  MET LYS LEU ASN ILE SER TYR PRO VAL ASN GLY SER GLN          
SEQRES   2 C  236  LYS THR PHE GLU ILE ASP ASP GLU HIS ARG ILE ARG VAL          
SEQRES   3 C  236  PHE PHE ASP LYS ARG ILE GLY GLN GLU VAL ASP GLY GLU          
SEQRES   4 C  236  ALA VAL GLY ASP GLU PHE LYS GLY TYR VAL PHE LYS ILE          
SEQRES   5 C  236  SER GLY GLY ASN ASP LYS GLN GLY PHE PRO MET LYS GLN          
SEQRES   6 C  236  GLY VAL LEU LEU PRO THR ARG ILE LYS LEU LEU LEU THR          
SEQRES   7 C  236  LYS ASN VAL SER CYS TYR ARG PRO ARG ARG ASP GLY GLU          
SEQRES   8 C  236  ARG LYS ARG LYS SER VAL ARG GLY ALA ILE VAL GLY PRO          
SEQRES   9 C  236  ASP LEU ALA VAL LEU ALA LEU VAL ILE VAL LYS LYS GLY          
SEQRES  10 C  236  GLU GLN GLU LEU GLU GLY LEU THR ASP THR THR VAL PRO          
SEQRES  11 C  236  LYS ARG LEU GLY PRO LYS ARG ALA ASN ASN ILE ARG LYS          
SEQRES  12 C  236  PHE PHE GLY LEU SER LYS GLU ASP ASP VAL ARG ASP PHE          
SEQRES  13 C  236  VAL ILE ARG ARG GLU VAL THR LYS GLY GLU LYS THR TYR          
SEQRES  14 C  236  THR LYS ALA PRO LYS ILE GLN ARG LEU VAL THR PRO GLN          
SEQRES  15 C  236  ARG LEU GLN ARG LYS ARG HIS GLN ARG ALA LEU LYS VAL          
SEQRES  16 C  236  ARG ASN ALA GLN ALA GLN ARG GLU ALA ALA ALA GLU TYR          
SEQRES  17 C  236  ALA GLN LEU LEU ALA LYS ARG LEU SER GLU ARG LYS ALA          
SEQRES  18 C  236  GLU LYS ALA GLU ILE ARG LYS ARG ARG ALA SER SER LEU          
SEQRES  19 C  236  LYS ALA                                                      
SEQRES   1 H  165  MET PRO PRO LYS PHE ASP PRO ASN GLU VAL LYS TYR LEU          
SEQRES   2 H  165  TYR LEU ARG ALA VAL GLY GLY GLU VAL GLY ALA SER ALA          
SEQRES   3 H  165  ALA LEU ALA PRO LYS ILE GLY PRO LEU GLY LEU SER PRO          
SEQRES   4 H  165  LYS LYS VAL GLY GLU ASP ILE ALA LYS ALA THR LYS GLU          
SEQRES   5 H  165  PHE LYS GLY ILE LYS VAL THR VAL GLN LEU LYS ILE GLN          
SEQRES   6 H  165  ASN ARG GLN ALA ALA ALA SER VAL VAL PRO SER ALA SER          
SEQRES   7 H  165  SER LEU VAL ILE THR ALA LEU LYS GLU PRO PRO ARG ASP          
SEQRES   8 H  165  ARG LYS LYS ASP LYS ASN VAL LYS HIS SER GLY ASN ILE          
SEQRES   9 H  165  GLN LEU ASP GLU ILE ILE GLU ILE ALA ARG GLN MET ARG          
SEQRES  10 H  165  ASP LYS SER PHE GLY ARG THR LEU ALA SER VAL THR LYS          
SEQRES  11 H  165  GLU ILE LEU GLY THR ALA GLN SER VAL GLY CYS ARG VAL          
SEQRES  12 H  165  ASP PHE LYS ASN PRO HIS ASP ILE ILE GLU GLY ILE ASN          
SEQRES  13 H  165  ALA GLY GLU ILE GLU ILE PRO GLU ASN                          
SEQRES   1 I  137  MET SER GLY ASN GLY ALA GLN GLY THR LYS PHE ARG ILE          
SEQRES   2 I  137  SER LEU GLY LEU PRO VAL GLY ALA ILE MET ASN CYS ALA          
SEQRES   3 I  137  ASP ASN SER GLY ALA ARG ASN LEU TYR ILE ILE ALA VAL          
SEQRES   4 I  137  LYS GLY SER GLY SER ARG LEU ASN ARG LEU PRO ALA ALA          
SEQRES   5 I  137  SER LEU GLY ASP MET VAL MET ALA THR VAL LYS LYS GLY          
SEQRES   6 I  137  LYS PRO GLU LEU ARG LYS LYS VAL MET PRO ALA ILE VAL          
SEQRES   7 I  137  VAL ARG GLN ALA LYS SER TRP ARG ARG ARG ASP GLY VAL          
SEQRES   8 I  137  PHE LEU TYR PHE GLU ASP ASN ALA GLY VAL ILE ALA ASN          
SEQRES   9 I  137  PRO LYS GLY GLU MET LYS GLY SER ALA ILE THR GLY PRO          
SEQRES  10 I  137  VAL GLY LYS GLU CYS ALA ASP LEU TRP PRO ARG VAL ALA          
SEQRES  11 I  137  SER ASN SER GLY VAL VAL VAL                                  
SEQRES   1 D  135  MET SER ASP ALA VAL THR ILE ARG THR ARG LYS VAL ILE          
SEQRES   2 D  135  SER ASN PRO LEU LEU ALA ARG LYS GLN PHE VAL VAL ASP          
SEQRES   3 D  135  VAL LEU HIS PRO ASN ARG ALA ASN VAL SER LYS ASP GLU          
SEQRES   4 D  135  LEU ARG GLU LYS LEU ALA GLU VAL TYR LYS ALA GLU LYS          
SEQRES   5 D  135  ASP ALA VAL SER VAL PHE GLY PHE ARG THR GLN PHE GLY          
SEQRES   6 D  135  GLY GLY LYS SER VAL GLY PHE GLY LEU VAL TYR ASN SER          
SEQRES   7 D  135  VAL ALA GLU ALA LYS LYS PHE GLU PRO THR TYR ARG LEU          
SEQRES   8 D  135  VAL ARG TYR GLY LEU ALA GLU LYS VAL GLU LYS ALA SER          
SEQRES   9 D  135  ARG GLN GLN ARG LYS GLN LYS LYS ASN ARG ASP LYS LYS          
SEQRES  10 D  135  ILE PHE GLY THR GLY LYS ARG LEU ALA LYS LYS VAL ALA          
SEQRES  11 D  135  ARG ARG ASN ALA ASP                                          
HET     MG  B 701       1                                                       
HET    ATP  B 702      31                                                       
HET    SF4  B 703       8                                                       
HET    SF4  B 704       8                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
FORMUL  13   MG    MG 2+                                                        
FORMUL  14  ATP    C10 H16 N5 O13 P3                                            
FORMUL  15  SF4    2(FE4 S4)                                                    
FORMUL  17  HOH   *(H2 O)                                                       
HELIX    1   1 ASP A   24  GLN A   33  1                                  10    
HELIX    2   2 ASN A  123  LEU A  129  1                                   7    
HELIX    3   3 LEU A  182  LEU A  203  1                                  22    
HELIX    4   4 PHE A  218  HIS A  235  1                                  18    
HELIX    5   5 ASN A  236  ASP A  241  1                                   6    
HELIX    6   6 GLN A  257  ASN A  265  1                                   9    
HELIX    7   7 SER A  278  LYS A  293  1                                  16    
HELIX    8   8 GLY A  301  TYR A  311  1                                  11    
HELIX    9   9 ASP A  321  SER A  326  1                                   6    
HELIX   10  10 GLN A  331  SER A  344  1                                  14    
HELIX   11  11 HIS A  356  GLN A  364  1                                   9    
HELIX   12  12 LYS B   17  ARG B   22  1                                   6    
HELIX   13  13 GLN B   23  CYS B   29  1                                   7    
HELIX   14  14 CYS B   29  GLY B   35  1                                   7    
HELIX   15  15 GLY B   59  CYS B   65  1                                   7    
HELIX   16  16 GLY B  115  GLY B  125  1                                  11    
HELIX   17  17 GLU B  139  PHE B  147  1                                   9    
HELIX   18  18 GLU B  151  ASP B  162  1                                  12    
HELIX   19  19 ASN B  175  ILE B  180  1                                   6    
HELIX   20  20 GLN B  185  MET B  195  1                                  11    
HELIX   21  21 SER B  198  GLN B  210  1                                  13    
HELIX   22  22 GLU B  212  ARG B  217  5                                   6    
HELIX   23  23 SER B  223  GLN B  238  1                                  16    
HELIX   24  24 ASP B  253  SER B  266  1                                  14    
HELIX   25  25 LEU B  267  ALA B  269  5                                   3    
HELIX   26  26 ASP B  280  SER B  288  1                                   9    
HELIX   27  27 VAL B  310  GLY B  320  1                                  11    
HELIX   28  28 GLY B  390  GLY B  400  1                                  11    
HELIX   29  29 THR B  429  ILE B  438  1                                  10    
HELIX   30  30 ASN B  444  VAL B  451  1                                   8    
HELIX   31  31 VAL B  451  ARG B  456  1                                   6    
HELIX   32  32 SER B  469  LEU B  482  1                                  14    
HELIX   33  33 ASP B  499  LYS B  518  1                                  20    
HELIX   34  34 ASP B  527  ALA B  535  1                                   9    
HELIX   35  35 LEU B  557  ASN B  569  1                                  13    
HELIX   36  36 GLN B  589  SER B  596  1                                   8    
HELIX   37  37 GLY F   61  LYS F   84  1                                  24    
HELIX   38  38 ASN F  116  ASP F  120  5                                   5    
HELIX   39  39 SER F  150  ILE F  164  1                                  15    
HELIX   40  40 GLY E   12  THR E   18  1                                   7    
HELIX   41  41 GLY E   32  VAL E   45  1                                  14    
HELIX   42  42 ALA G    9  TYR G   22  1                                  14    
HELIX   43  43 SER G   34  ALA G   49  1                                  16    
HELIX   44  44 ARG G   60  SER G   68  1                                   9    
HELIX   45  45 PRO G   92  ASN G  103  1                                  12    
HELIX   46  46 THR G  133  LEU G  139  1                                   7    
HELIX   47  47 GLY G  166  ASN G  177  1                                  12    
HELIX   48  48 ASP C   20  ARG C   25  1                                   6    
HELIX   49  49 VAL C   26  PHE C   28  5                                   3    
HELIX   50  50 GLU C   39  GLY C   42  5                                   4    
HELIX   51  51 GLN C   59  PHE C   61  5                                   3    
HELIX   52  52 LEU C  121  ASP C  126  1                                   6    
HELIX   53  53 ARG C  137  GLY C  146  1                                  10    
HELIX   54  54 THR C  180  ILE C  226  1                                  47    
HELIX   55  55 ALA H   49  LYS H   54  1                                   6    
HELIX   56  56 SER H   78  THR H   83  1                                   6    
HELIX   57  57 SER H  127  ALA H  136  1                                  10    
HELIX   58  58 GLY I  119  ASP I  124  1                                   6    
HELIX   59  59 TRP I  126  ASN I  132  1                                   7    
HELIX   60  60 PRO D   16  LEU D   18  5                                   3    
HELIX   61  61 SER D   36  GLU D   46  1                                  11    
HELIX   62  62 GLU D   51  ASP D   53  5                                   3    
HELIX   63  63 SER D   78  GLU D   86  1                                   9    
HELIX   64  64 PRO D   87  GLY D   95  1                                   9    
HELIX   65  65 SER D  104  LYS D  117  1                                  14    
HELIX   66  66 GLY D  122  ASN D  133  1                                  12    
SHEET    1   A 7 LYS A   2  LYS A   7  0                                        
SHEET    2   A 7 ALA A  16  LEU A  21 -1  O  LEU A  21   N  LYS A   2           
SHEET    3   A 7 PHE A 115  LYS A 119 -1  O  ILE A 117   N  ILE A  18           
SHEET    4   A 7 GLU A  40  ILE A  42 -1  N  GLU A  40   O  ILE A 118           
SHEET    5   A 7 LYS A  66  ASP A  75 -1  O  ILE A  67   N  LEU A  41           
SHEET    6   A 7 TYR A  80  THR A  87 -1  O  TYR A  80   N  ASP A  75           
SHEET    7   A 7 PHE A 107  THR A 108 -1  O  PHE A 107   N  TYR A  83           
SHEET    1   B 4 ALA A 152  VAL A 154  0                                        
SHEET    2   B 4 ALA A 144  LEU A 147 -1  N  VAL A 146   O  HIS A 153           
SHEET    3   B 4 ILE A 211  CYS A 214  1  O  CYS A 214   N  VAL A 145           
SHEET    4   B 4 PHE A 246  ILE A 248  1  O  PHE A 247   N  LEU A 213           
SHEET    1   C 4 ALA A 298  TYR A 300  0                                        
SHEET    2   C 4 ALA A 369  ILE A 371 -1  O  CYS A 370   N  TRP A 299           
SHEET    3   C 4 LEU A 317  THR A 320 -1  N  LEU A 318   O  ALA A 369           
SHEET    4   C 4 ALA A 349  LEU A 352  1  O  LEU A 350   N  LEU A 319           
SHEET    1   D 2 SER B   6  VAL B  11  0                                        
SHEET    2   D 2 ILE B  70  LEU B  75 -1  O  LEU B  75   N  SER B   6           
SHEET    1   E 2 ILE B  39  VAL B  41  0                                        
SHEET    2   E 2 ALA B  48  ILE B  50 -1  O  PHE B  49   N  GLU B  40           
SHEET    1   F 8 VAL B  83  ARG B  86  0                                        
SHEET    2   F 8 LYS B  93  HIS B  95 -1  O  LEU B  94   N  HIS B  85           
SHEET    3   F 8 TYR B 301  VAL B 304  1  O  GLY B 302   N  HIS B  95           
SHEET    4   F 8 PHE B 290  TYR B 295 -1  N  TYR B 295   O  VAL B 303           
SHEET    5   F 8 VAL B 105  VAL B 109  1  N  GLY B 107   O  PHE B 290           
SHEET    6   F 8 TYR B 273  VAL B 277  1  O  CYS B 276   N  LEU B 106           
SHEET    7   F 8 VAL B 242  ASP B 246  1  N  TYR B 243   O  TYR B 273           
SHEET    8   F 8 ILE B 167  LYS B 169  1  N  ILE B 167   O  MET B 244           
SHEET    1   G 5 VAL B  83  ARG B  86  0                                        
SHEET    2   G 5 LYS B  93  HIS B  95 -1  O  LEU B  94   N  HIS B  85           
SHEET    3   G 5 TYR B 301  VAL B 304  1  O  GLY B 302   N  HIS B  95           
SHEET    4   G 5 PHE B 290  TYR B 295 -1  N  TYR B 295   O  VAL B 303           
SHEET    5   G 5 ALA B 308  SER B 309 -1  O  ALA B 308   N  VAL B 291           
SHEET    1   H 2 HIS B 321  ILE B 322  0                                        
SHEET    2   H 2 LEU B 327  ARG B 328 -1  O  LEU B 327   N  ILE B 322           
SHEET    1   I 2 SER B 355  TYR B 356  0                                        
SHEET    2   I 2 GLY B 373  GLU B 374 -1  O  GLY B 373   N  TYR B 356           
SHEET    1   J 4 LEU B 359  THR B 362  0                                        
SHEET    2   J 4 VAL B 367  VAL B 370 -1  O  LEU B 368   N  LYS B 361           
SHEET    3   J 4 ASN B 548  HIS B 550  1  O  ALA B 549   N  VAL B 367           
SHEET    4   J 4 GLU B 542  ILE B 544 -1  N  GLU B 542   O  HIS B 550           
SHEET    1   K 6 VAL B 415  LYS B 418  0                                        
SHEET    2   K 6 ILE B 488  ILE B 491  1  O  LEU B 490   N  LYS B 418           
SHEET    3   K 6 THR B 520  VAL B 524  1  O  PHE B 522   N  ILE B 491           
SHEET    4   K 6 ILE B 380  MET B 384  1  N  LEU B 381   O  ILE B 523           
SHEET    5   K 6 LYS B 537  VAL B 540  1  O  ILE B 539   N  VAL B 382           
SHEET    6   K 6 GLU B 555  SER B 556 -1  O  GLU B 555   N  VAL B 538           
SHEET    1   L 3 TYR F   3  GLU F  11  0                                        
SHEET    2   L 3 LEU F  52  GLY F  60 -1  O  VAL F  55   N  GLN F   8           
SHEET    3   L 3 THR F  44  ASN F  49 -1  N  THR F  46   O  LYS F  54           
SHEET    1   M 3 THR F  17  LYS F  21  0                                        
SHEET    2   M 3 ILE F  24  GLY F  29 -1  O  LYS F  26   N  SER F  19           
SHEET    3   M 3 GLY F  32  ASN F  37 -1  O  LEU F  34   N  VAL F  27           
SHEET    1   N 4 VAL F 132  PHE F 136  0                                        
SHEET    2   N 4 GLU F 143  GLY F 148 -1  O  SER F 147   N  THR F 133           
SHEET    3   N 4 TYR F  86  VAL F  93 -1  N  TYR F  88   O  LEU F 146           
SHEET    4   N 4 GLY F 178  PHE F 186 -1  O  SER F 182   N  LYS F  89           
SHEET    1   O 3 ASN F 100  VAL F 104  0                                        
SHEET    2   O 3 PHE F 111  ARG F 115 -1  O  ARG F 115   N  ASN F 100           
SHEET    3   O 3 ARG F 124  PRO F 127 -1  O  VAL F 126   N  ILE F 112           
SHEET    1   P 5 VAL G  51  LEU G  52  0                                        
SHEET    2   P 5 VAL G  84  THR G  89 -1  O  PHE G  86   N  LEU G  52           
SHEET    3   P 5 SER G  24  GLY G  29 -1  N  SER G  24   O  THR G  89           
SHEET    4   P 5 THR G 186  ASP G 192 -1  O  VAL G 188   N  VAL G  27           
SHEET    5   P 5 GLN G 195  PHE G 197 -1  O  PHE G 197   N  VAL G 190           
SHEET    1   Q 2 ILE G 119  VAL G 121  0                                        
SHEET    2   Q 2 VAL G 156  VAL G 159 -1  O  VAL G 159   N  ILE G 119           
SHEET    1   R 3 VAL G 124  ASN G 125  0                                        
SHEET    2   R 3 THR G 149  ILE G 152 -1  O  ILE G 152   N  VAL G 124           
SHEET    3   R 3 THR G 143  ALA G 146 -1  N  LYS G 144   O  GLU G 151           
SHEET    1   S 5 SER C  12  GLU C  17  0                                        
SHEET    2   S 5 LYS C   2  TYR C   7 -1  N  LEU C   3   O  PHE C  16           
SHEET    3   S 5 LEU C 106  LYS C 115  1  O  LEU C 109   N  ASN C   4           
SHEET    4   S 5 VAL C  49  ASP C  57 -1  N  SER C  53   O  ALA C 110           
SHEET    5   S 5 GLU C  35  ASP C  37 -1  N  VAL C  36   O  PHE C  50           
SHEET    1   T 2 ARG C  72  LEU C  77  0                                        
SHEET    2   T 2 LYS C  93  ARG C  98 -1  O  LYS C  95   N  LEU C  75           
SHEET    1   U 2 ARG C 160  THR C 163  0                                        
SHEET    2   U 2 THR C 168  LYS C 171 -1  O  TYR C 169   N  VAL C 162           
SHEET    1   V 2 LEU I  17  PRO I  18  0                                        
SHEET    2   V 2 ALA I  51  ALA I  52 -1  O  ALA I  52   N  LEU I  17           
SHEET    1   W 6 ILE I  22  CYS I  25  0                                        
SHEET    2   W 6 ASN I  33  VAL I  39 -1  O  LEU I  34   N  MET I  23           
SHEET    3   W 6 MET I  57  THR I  61 -1  O  MET I  59   N  ILE I  37           
SHEET    4   W 6 MET I  74  ARG I  80 -1  O  MET I  74   N  ALA I  60           
SHEET    5   W 6 ALA I  99  ILE I 102 -1  O  ALA I  99   N  VAL I  79           
SHEET    6   W 6 ILE I  22  CYS I  25  1  N  ASN I  24   O  GLY I 100           
SHEET    1   X 2 TRP I  85  ARG I  86  0                                        
SHEET    2   X 2 PHE I  92  LEU I  93 -1  O  LEU I  93   N  TRP I  85           
SHEET    1   Y 4 ILE D   7  ASN D  15  0                                        
SHEET    2   Y 4 ARG D  20  LEU D  28 -1  O  ARG D  20   N  ASN D  15           
SHEET    3   Y 4 LYS D  68  TYR D  76 -1  O  GLY D  73   N  PHE D  23           
SHEET    4   Y 4 VAL D  55  THR D  62 -1  N  PHE D  58   O  PHE D  72           
LINK         SG  CYS B  55                FE2  SF4 B 703     1555   1555  1.98  
LINK        MG    MG B 701                 O1B ATP B 702     1555   1555  2.20  
LINK         SG  CYS B  61                FE3  SF4 B 703     1555   1555  2.47  
LINK         SG  CYS B  16                FE4  SF4 B 704     1555   1555  2.48  
LINK         SG  CYS B  65                FE3  SF4 B 704     1555   1555  2.58  
LINK        MG    MG B 701                 O2G ATP B 702     1555   1555  2.67  
CISPEP   1 ASP A   52    GLU A   53          0        -3.63                     
CISPEP   2 LYS A   56    LYS A   57          0         4.82                     
SITE     1 AC1  5 LYS B 116  SER B 117  GLN B 171  GLU B 247                    
SITE     2 AC1  5 ATP B 702                                                     
SITE     1 AC2 12 TYR B  87  PHE B  92  ASN B 112  GLY B 113                    
SITE     2 AC2 12 ILE B 114  GLY B 115  LYS B 116  SER B 117                    
SITE     3 AC2 12 THR B 118  SER B 299   MG B 701  HOH B 801                    
SITE     1 AC3 11 CYS B  29  PRO B  30  CYS B  38  ILE B  39                    
SITE     2 AC3 11 ILE B  50  CYS B  55  ILE B  56  CYS B  58                    
SITE     3 AC3 11 GLY B  59  ILE B  60  CYS B  61                               
SITE     1 AC4 10 CYS B  16  LYS B  17  PRO B  18  CYS B  21                    
SITE     2 AC4 10 ARG B  22  CYS B  25  CYS B  65  PRO B  66                    
SITE     3 AC4 10 PHE B  67  ALA B  69                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system