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Database: PDB
Entry: 5FKW
LinkDB: 5FKW
Original site: 5FKW 
HEADER    TRANSFERASE                             20-OCT-15   5FKW              
TITLE     CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX   
TITLE    2 BOUND TO DNA (DNA POLYMERASE III ALPHA, BETA, EPSILON)               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA POLYMERASE III ALPHA;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.7.7;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA POLYMERASE III BETA;                                   
COMPND   9 CHAIN: B, C;                                                         
COMPND  10 EC: 2.7.7.7;                                                         
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: DNA POLYMERASE III EPSILON;                                
COMPND  14 CHAIN: D;                                                            
COMPND  15 EC: 2.7.7.7;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MUTATION: YES;                                                       
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: PRIMER-TEMPLATE DUPLEX DNA;                                
COMPND  20 CHAIN: P;                                                            
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 OTHER_DETAILS: TEMPLATE STRAND TCAGGAGTCCTTCGTCCTAGTACTACTCC PRIMER  
COMPND  23 STRAND GGAGTAGTACTAGGACGAAGGACTC;                                    
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: PRIMER-TEMPLATE DUPLEX DNA;                                
COMPND  26 CHAIN: T;                                                            
COMPND  27 ENGINEERED: YES;                                                     
COMPND  28 OTHER_DETAILS: TEMPLATE STRAND TCAGGAGTCCTTCGTCCTAGTACTACTCC PRIMER  
COMPND  29 STRAND GGAGTAGTACTAGGACGAAGGACTC                                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 ATCC: 10798;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3D;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  12 ORGANISM_TAXID: 83333;                                               
SOURCE  13 ATCC: 10798;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET3D;                                    
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  21 ORGANISM_TAXID: 83333;                                               
SOURCE  22 ATCC: 10798;                                                         
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  25 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PET3D;                                    
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 SYNTHETIC: YES;                                                      
SOURCE  30 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  31 ORGANISM_TAXID: 32630;                                               
SOURCE  32 MOL_ID: 5;                                                           
SOURCE  33 SYNTHETIC: YES;                                                      
SOURCE  34 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  35 ORGANISM_TAXID: 32630                                                
KEYWDS    TRANSFERASE, DNA REPLICATION, DNA POLYMERASE III ALPHA, DNA           
KEYWDS   2 POLYMERASE III BETA, DNA POLYMERASE III EPSILON                      
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    R.FERNANDEZ-LEIRO,J.CONRAD,S.H.W.SCHERES,M.H.LAMERS                   
REVDAT   4   27-FEB-19 5FKW    1       JRNL                                     
REVDAT   3   19-APR-17 5FKW    1       REMARK                                   
REVDAT   2   21-DEC-16 5FKW    1       JRNL                                     
REVDAT   1   25-NOV-15 5FKW    0                                                
JRNL        AUTH   R.FERNANDEZ-LEIRO,J.CONRAD,S.H.SCHERES,M.H.LAMERS            
JRNL        TITL   CRYO-EM STRUCTURES OF THEE. COLIREPLICATIVE DNA POLYMERASE   
JRNL        TITL 2 REVEAL ITS DYNAMIC INTERACTIONS WITH THE DNA SLIDING CLAMP,  
JRNL        TITL 3 EXONUCLEASE ANDTAU.                                          
JRNL        REF    ELIFE                         V.   4       2015              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   26499492                                                     
JRNL        DOI    10.7554/ELIFE.11134                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    7.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
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)  : 7.300                          
REMARK   3   NUMBER OF PARTICLES               : 40582                          
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 5FKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290065339.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : DNA POLYMERASE III CATALYTIC      
REMARK 245                                    COMPLEX (ALPHA, EPSILON, BETA,    
REMARK 245                                    TAU)                              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 1.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : LIQUID ETHANE                     
REMARK 245   SAMPLE BUFFER                  : 25 MM HEPES PH 7.5, 150 MM        
REMARK 245                                    NACL, AND 2 MM DTT                
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 12-MAY-14                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 85.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 QUANTUM (4K X 4K)     
REMARK 245   MINIMUM DEFOCUS (NM)              : 2000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 40.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 64000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 28409                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
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 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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, P, T                      
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     ALA A   928                                                      
REMARK 465     GLU A   929                                                      
REMARK 465     GLU A   930                                                      
REMARK 465     PRO A   931                                                      
REMARK 465     GLU A   932                                                      
REMARK 465     GLN A   933                                                      
REMARK 465     ILE A   934                                                      
REMARK 465     GLU A   935                                                      
REMARK 465     GLN A   936                                                      
REMARK 465     SER A   937                                                      
REMARK 465     TYR A   938                                                      
REMARK 465     ALA A   939                                                      
REMARK 465     SER A   940                                                      
REMARK 465     CYS A   941                                                      
REMARK 465     GLN A   942                                                      
REMARK 465     PRO A   943                                                      
REMARK 465     TRP A   944                                                      
REMARK 465     PRO A   945                                                      
REMARK 465     GLU A   946                                                      
REMARK 465     GLN A   947                                                      
REMARK 465     VAL A   948                                                      
REMARK 465     VAL A   949                                                      
REMARK 465     LEU A   950                                                      
REMARK 465     ASP A   951                                                      
REMARK 465     GLY A   952                                                      
REMARK 465     GLU A   953                                                      
REMARK 465     ARG A   954                                                      
REMARK 465     GLU A   955                                                      
REMARK 465     THR A   956                                                      
REMARK 465     LEU A   957                                                      
REMARK 465     GLY A   958                                                      
REMARK 465     LEU A   959                                                      
REMARK 465     TYR A   960                                                      
REMARK 465     LEU A   961                                                      
REMARK 465     THR A   962                                                      
REMARK 465     GLY A   963                                                      
REMARK 465     HIS A   964                                                      
REMARK 465     PRO A   965                                                      
REMARK 465     ILE A   966                                                      
REMARK 465     ASN A   967                                                      
REMARK 465     GLN A   968                                                      
REMARK 465     TYR A   969                                                      
REMARK 465     LEU A   970                                                      
REMARK 465     LYS A   971                                                      
REMARK 465     GLU A   972                                                      
REMARK 465     ILE A   973                                                      
REMARK 465     GLU A   974                                                      
REMARK 465     ARG A   975                                                      
REMARK 465     TYR A   976                                                      
REMARK 465     VAL A   977                                                      
REMARK 465     GLY A   978                                                      
REMARK 465     GLY A   979                                                      
REMARK 465     VAL A   980                                                      
REMARK 465     ARG A   981                                                      
REMARK 465     LEU A   982                                                      
REMARK 465     LYS A   983                                                      
REMARK 465     ASP A   984                                                      
REMARK 465     MET A   985                                                      
REMARK 465     HIS A   986                                                      
REMARK 465     PRO A   987                                                      
REMARK 465     THR A   988                                                      
REMARK 465     GLU A   989                                                      
REMARK 465     ARG A   990                                                      
REMARK 465     GLY A   991                                                      
REMARK 465     LYS A   992                                                      
REMARK 465     VAL A   993                                                      
REMARK 465     ILE A   994                                                      
REMARK 465     THR A   995                                                      
REMARK 465     ALA A   996                                                      
REMARK 465     ALA A   997                                                      
REMARK 465     GLY A   998                                                      
REMARK 465     LEU A   999                                                      
REMARK 465     VAL A  1000                                                      
REMARK 465     VAL A  1001                                                      
REMARK 465     ALA A  1002                                                      
REMARK 465     ALA A  1003                                                      
REMARK 465     ARG A  1004                                                      
REMARK 465     VAL A  1005                                                      
REMARK 465     MET A  1006                                                      
REMARK 465     VAL A  1007                                                      
REMARK 465     THR A  1008                                                      
REMARK 465     LYS A  1009                                                      
REMARK 465     ARG A  1010                                                      
REMARK 465     GLY A  1011                                                      
REMARK 465     ASN A  1012                                                      
REMARK 465     ARG A  1013                                                      
REMARK 465     ILE A  1014                                                      
REMARK 465     GLY A  1015                                                      
REMARK 465     ILE A  1016                                                      
REMARK 465     CYS A  1017                                                      
REMARK 465     THR A  1018                                                      
REMARK 465     LEU A  1019                                                      
REMARK 465     ASP A  1020                                                      
REMARK 465     ASP A  1021                                                      
REMARK 465     ARG A  1022                                                      
REMARK 465     SER A  1023                                                      
REMARK 465     GLY A  1024                                                      
REMARK 465     ARG A  1025                                                      
REMARK 465     LEU A  1026                                                      
REMARK 465     GLU A  1027                                                      
REMARK 465     VAL A  1028                                                      
REMARK 465     MET A  1029                                                      
REMARK 465     LEU A  1030                                                      
REMARK 465     PHE A  1031                                                      
REMARK 465     THR A  1032                                                      
REMARK 465     ASP A  1033                                                      
REMARK 465     ALA A  1034                                                      
REMARK 465     LEU A  1035                                                      
REMARK 465     ASP A  1036                                                      
REMARK 465     LYS A  1037                                                      
REMARK 465     TYR A  1038                                                      
REMARK 465     GLN A  1039                                                      
REMARK 465     GLN A  1040                                                      
REMARK 465     LEU A  1041                                                      
REMARK 465     LEU A  1042                                                      
REMARK 465     GLU A  1043                                                      
REMARK 465     LYS A  1044                                                      
REMARK 465     ASP A  1045                                                      
REMARK 465     ARG A  1046                                                      
REMARK 465     ILE A  1047                                                      
REMARK 465     LEU A  1048                                                      
REMARK 465     ILE A  1049                                                      
REMARK 465     VAL A  1050                                                      
REMARK 465     SER A  1051                                                      
REMARK 465     GLY A  1052                                                      
REMARK 465     GLN A  1053                                                      
REMARK 465     VAL A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     PHE A  1056                                                      
REMARK 465     ASP A  1057                                                      
REMARK 465     ASP A  1058                                                      
REMARK 465     PHE A  1059                                                      
REMARK 465     SER A  1060                                                      
REMARK 465     GLY A  1061                                                      
REMARK 465     GLY A  1062                                                      
REMARK 465     LEU A  1063                                                      
REMARK 465     LYS A  1064                                                      
REMARK 465     MET A  1065                                                      
REMARK 465     THR A  1066                                                      
REMARK 465     ALA A  1067                                                      
REMARK 465     ARG A  1068                                                      
REMARK 465     GLU A  1069                                                      
REMARK 465     VAL A  1070                                                      
REMARK 465     MET A  1071                                                      
REMARK 465     ASP A  1072                                                      
REMARK 465     ILE A  1073                                                      
REMARK 465     ASP A  1074                                                      
REMARK 465     GLU A  1075                                                      
REMARK 465     ALA A  1076                                                      
REMARK 465     ARG A  1077                                                      
REMARK 465     GLU A  1078                                                      
REMARK 465     LYS A  1079                                                      
REMARK 465     TYR A  1080                                                      
REMARK 465     ALA A  1081                                                      
REMARK 465     ARG A  1082                                                      
REMARK 465     GLY A  1083                                                      
REMARK 465     LEU A  1084                                                      
REMARK 465     ALA A  1085                                                      
REMARK 465     ILE A  1086                                                      
REMARK 465     SER A  1087                                                      
REMARK 465     LEU A  1088                                                      
REMARK 465     THR A  1089                                                      
REMARK 465     ASP A  1090                                                      
REMARK 465     ARG A  1091                                                      
REMARK 465     GLN A  1092                                                      
REMARK 465     ILE A  1093                                                      
REMARK 465     ASP A  1094                                                      
REMARK 465     ASP A  1095                                                      
REMARK 465     GLN A  1096                                                      
REMARK 465     LEU A  1097                                                      
REMARK 465     LEU A  1098                                                      
REMARK 465     ASN A  1099                                                      
REMARK 465     ARG A  1100                                                      
REMARK 465     LEU A  1101                                                      
REMARK 465     ARG A  1102                                                      
REMARK 465     GLN A  1103                                                      
REMARK 465     SER A  1104                                                      
REMARK 465     LEU A  1105                                                      
REMARK 465     GLU A  1106                                                      
REMARK 465     PRO A  1107                                                      
REMARK 465     HIS A  1108                                                      
REMARK 465     ARG A  1109                                                      
REMARK 465     SER A  1110                                                      
REMARK 465     GLY A  1111                                                      
REMARK 465     THR A  1112                                                      
REMARK 465     ILE A  1113                                                      
REMARK 465     PRO A  1114                                                      
REMARK 465     VAL A  1115                                                      
REMARK 465     HIS A  1116                                                      
REMARK 465     LEU A  1117                                                      
REMARK 465     TYR A  1118                                                      
REMARK 465     TYR A  1119                                                      
REMARK 465     GLN A  1120                                                      
REMARK 465     ARG A  1121                                                      
REMARK 465     ALA A  1122                                                      
REMARK 465     ASP A  1123                                                      
REMARK 465     ALA A  1124                                                      
REMARK 465     ARG A  1125                                                      
REMARK 465     ALA A  1126                                                      
REMARK 465     ARG A  1127                                                      
REMARK 465     LEU A  1128                                                      
REMARK 465     ARG A  1129                                                      
REMARK 465     PHE A  1130                                                      
REMARK 465     GLY A  1131                                                      
REMARK 465     ALA A  1132                                                      
REMARK 465     THR A  1133                                                      
REMARK 465     TRP A  1134                                                      
REMARK 465     ARG A  1135                                                      
REMARK 465     VAL A  1136                                                      
REMARK 465     SER A  1137                                                      
REMARK 465     PRO A  1138                                                      
REMARK 465     SER A  1139                                                      
REMARK 465     ASP A  1140                                                      
REMARK 465     ARG A  1141                                                      
REMARK 465     LEU A  1142                                                      
REMARK 465     LEU A  1143                                                      
REMARK 465     ASN A  1144                                                      
REMARK 465     ASP A  1145                                                      
REMARK 465     LEU A  1146                                                      
REMARK 465     ARG A  1147                                                      
REMARK 465     GLY A  1148                                                      
REMARK 465     LEU A  1149                                                      
REMARK 465     ILE A  1150                                                      
REMARK 465     GLY A  1151                                                      
REMARK 465     SER A  1152                                                      
REMARK 465     GLU A  1153                                                      
REMARK 465     GLN A  1154                                                      
REMARK 465     VAL A  1155                                                      
REMARK 465     GLU A  1156                                                      
REMARK 465     LEU A  1157                                                      
REMARK 465     GLU A  1158                                                      
REMARK 465     PHE A  1159                                                      
REMARK 465     ASP A  1160                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     THR D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     GLU D   190                                                      
REMARK 465     GLY D   191                                                      
REMARK 465     GLU D   192                                                      
REMARK 465     THR D   193                                                      
REMARK 465     GLN D   194                                                      
REMARK 465     GLN D   195                                                      
REMARK 465     GLN D   196                                                      
REMARK 465     GLN D   197                                                      
REMARK 465     GLY D   198                                                      
REMARK 465     GLU D   199                                                      
REMARK 465     ALA D   200                                                      
REMARK 465     THR D   201                                                      
REMARK 465     ILE D   202                                                      
REMARK 465     GLN D   203                                                      
REMARK 465     ARG D   204                                                      
REMARK 465     ILE D   205                                                      
REMARK 465     VAL D   206                                                      
REMARK 465     ARG D   207                                                      
REMARK 465      DT T     9                                                      
REMARK 465      DC T    10                                                      
REMARK 465      DA T    11                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG A   560     N    LEU A   562              1.87            
REMARK 500   O    GLY A   558     N    ARG A   560              1.94            
REMARK 500   N3    DC P    25     O6    DG T    13              2.09            
REMARK 500   NH2  ARG A   639     O    TYR A   754              2.18            
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    GLN A 687   CD    GLN A 687   NE2     0.241                       
REMARK 500    GLU D 110   CD    GLU D 110   OE2     0.074                       
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    ARG A 614   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    PHE A 924   N   -  CA  -  CB  ANGL. DEV. = -11.1 DEGREES          
REMARK 500    PHE A 924   N   -  CA  -  C   ANGL. DEV. =  19.3 DEGREES          
REMARK 500    ARG C  73   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    LEU D 212   CB  -  CA  -  C   ANGL. DEV. = -11.5 DEGREES          
REMARK 500    LEU D 212   N   -  CA  -  CB  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    LEU D 212   N   -  CA  -  C   ANGL. DEV. =  18.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   2      -75.86    -57.47                                   
REMARK 500    MET A  17      -42.67     68.19                                   
REMARK 500    ASP A  19     -158.32   -158.60                                   
REMARK 500    LEU A  21      -56.62   -136.32                                   
REMARK 500    LEU A  39      125.46   -173.36                                   
REMARK 500    ASN A 125      -57.06   -133.65                                   
REMARK 500    PHE A 162       52.60   -140.85                                   
REMARK 500    ASP A 164       16.03     56.64                                   
REMARK 500    ARG A 232       68.22   -118.20                                   
REMARK 500    GLN A 238       46.18    -78.68                                   
REMARK 500    PHE A 281      145.59   -176.20                                   
REMARK 500    THR A 283     -139.86   -128.45                                   
REMARK 500    SER A 287      154.78    -47.03                                   
REMARK 500    MET A 399      122.10    -38.45                                   
REMARK 500    ASP A 403       62.38     39.23                                   
REMARK 500    ASN A 507     -174.96    162.39                                   
REMARK 500    HIS A 511     -154.40   -138.87                                   
REMARK 500    LYS A 521      132.13    -33.74                                   
REMARK 500    ASP A 531     -170.48    -69.32                                   
REMARK 500    LEU A 559       42.61    -42.42                                   
REMARK 500    THR A 561      -36.14     29.75                                   
REMARK 500    ARG A 575        2.82    -57.71                                   
REMARK 500    ASN A 579       39.01   -150.72                                   
REMARK 500    GLN A 610       -9.77     83.45                                   
REMARK 500    TYR A 778       71.20   -172.51                                   
REMARK 500    PRO A 779       69.44    -63.47                                   
REMARK 500    ALA A 780      -14.16   -153.92                                   
REMARK 500    GLU A 781      -39.82   -131.81                                   
REMARK 500    PHE A 782      -54.72    -29.82                                   
REMARK 500    ASP A 790       51.59   -109.30                                   
REMARK 500    LEU A 809      175.30    -54.37                                   
REMARK 500    LYS A 810      138.09     92.19                                   
REMARK 500    ILE A 811      136.75    175.31                                   
REMARK 500    HIS A 822     -152.15   -119.60                                   
REMARK 500    ARG A 895       19.42    -51.51                                   
REMARK 500    ALA A 896      -35.22   -158.44                                   
REMARK 500    GLN A 920      139.72   -171.52                                   
REMARK 500    ASP A 922     -169.63   -107.38                                   
REMARK 500    PHE A 924     -177.58     -1.57                                   
REMARK 500    VAL A 926      156.43    172.75                                   
REMARK 500    ARG B  24       60.46     38.68                                   
REMARK 500    ASP B  39     -148.92     68.20                                   
REMARK 500    LEU B  49      -24.94     73.43                                   
REMARK 500    GLU B 125      -42.52   -132.80                                   
REMARK 500    HIS B 148      -62.59    -96.42                                   
REMARK 500    GLU B 163      121.96   -175.11                                   
REMARK 500    HIS B 175      -53.10   -121.87                                   
REMARK 500    ARG B 240       63.07     67.66                                   
REMARK 500    ASN B 251       72.27     54.64                                   
REMARK 500    ASN B 288       12.41     59.42                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      72 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 SER A    2     GLU A    3                  125.53                    
REMARK 500 PRO A  400     ASP A  401                 -132.42                    
REMARK 500 PHE A  433     GLY A  434                  148.76                    
REMARK 500 GLY A  509     LYS A  510                 -138.32                    
REMARK 500 LEU A  559     ARG A  560                 -141.36                    
REMARK 500 ARG A  895     ALA A  896                 -149.83                    
REMARK 500 LEU A  923     PHE A  924                 -134.82                    
REMARK 500 LEU B   21     GLY B   22                  134.79                    
REMARK 500 GLY D   67     ILE D   68                 -145.94                    
REMARK 500 LYS D  211     LEU D  212                 -125.94                    
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 559         12.40                                           
REMARK 500    ARG A 576        -10.88                                           
REMARK 500    LEU A 923        -13.37                                           
REMARK 500    PHE A 924         12.28                                           
REMARK 500    GLY D  67        -10.64                                           
REMARK 500    LYS D 211        -12.85                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FKU   RELATED DB: PDB                                   
REMARK 900 CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX  
REMARK 900 IN DNA FREE STATE (DNA POLYMERASE III ALPHA, BETA, EPSILON, TAU      
REMARK 900 COMPLEX)                                                             
REMARK 900 RELATED ID: 5FKV   RELATED DB: PDB                                   
REMARK 900 CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX  
REMARK 900 BOUND TO DNA (DNA POLYMERASE III ALPHA, BETA, EPSILON, TAU COMPLEX)  
REMARK 900 RELATED ID: EMD-3202   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF THE E. COLI REPLICATIVE DNA POLYMERASE COMPLEX  
REMARK 900 BOUND TO DNA (DNA POLYMERASE III ALPHA, BETA, AND EPSILON SUBUNITS)  
DBREF  5FKW A    1  1160  UNP    P10443   DPO3A_ECOLI      1   1160             
DBREF  5FKW B    1   366  UNP    P0A988   DPO3B_ECOLI      1    366             
DBREF  5FKW C    1   366  UNP    P0A988   DPO3B_ECOLI      1    366             
DBREF  5FKW D    1   243  UNP    P03007   DPO3E_ECOLI      1    243             
DBREF  5FKW T   12    37  PDB    5FKW     5FKW            12     37             
DBREF  5FKW P    1    25  PDB    5FKW     5FKW             1     25             
SEQADV 5FKW LEU A  921  UNP  P10443    ALA   921 ENGINEERED MUTATION            
SEQADV 5FKW LEU A  923  UNP  P10443    MET   923 ENGINEERED MUTATION            
SEQADV 5FKW LEU D  183  UNP  P03007    THR   183 ENGINEERED MUTATION            
SEQADV 5FKW LEU D  185  UNP  P03007    MET   185 ENGINEERED MUTATION            
SEQADV 5FKW PRO D  186  UNP  P03007    ALA   186 ENGINEERED MUTATION            
SEQADV 5FKW LEU D  187  UNP  P03007    PHE   187 ENGINEERED MUTATION            
SEQRES   1 A 1160  MET SER GLU PRO ARG PHE VAL HIS LEU ARG VAL HIS SER          
SEQRES   2 A 1160  ASP TYR SER MET ILE ASP GLY LEU ALA LYS THR ALA PRO          
SEQRES   3 A 1160  LEU VAL LYS LYS ALA ALA ALA LEU GLY MET PRO ALA LEU          
SEQRES   4 A 1160  ALA ILE THR ASP PHE THR ASN LEU CYS GLY LEU VAL LYS          
SEQRES   5 A 1160  PHE TYR GLY ALA GLY HIS GLY ALA GLY ILE LYS PRO ILE          
SEQRES   6 A 1160  VAL GLY ALA ASP PHE ASN VAL GLN CYS ASP LEU LEU GLY          
SEQRES   7 A 1160  ASP GLU LEU THR HIS LEU THR VAL LEU ALA ALA ASN ASN          
SEQRES   8 A 1160  THR GLY TYR GLN ASN LEU THR LEU LEU ILE SER LYS ALA          
SEQRES   9 A 1160  TYR GLN ARG GLY TYR GLY ALA ALA GLY PRO ILE ILE ASP          
SEQRES  10 A 1160  ARG ASP TRP LEU ILE GLU LEU ASN GLU GLY LEU ILE LEU          
SEQRES  11 A 1160  LEU SER GLY GLY ARG MET GLY ASP VAL GLY ARG SER LEU          
SEQRES  12 A 1160  LEU ARG GLY ASN SER ALA LEU VAL ASP GLU CYS VAL ALA          
SEQRES  13 A 1160  PHE TYR GLU GLU HIS PHE PRO ASP ARG TYR PHE LEU GLU          
SEQRES  14 A 1160  LEU ILE ARG THR GLY ARG PRO ASP GLU GLU SER TYR LEU          
SEQRES  15 A 1160  HIS ALA ALA VAL GLU LEU ALA GLU ALA ARG GLY LEU PRO          
SEQRES  16 A 1160  VAL VAL ALA THR ASN ASP VAL ARG PHE ILE ASP SER SER          
SEQRES  17 A 1160  ASP PHE ASP ALA HIS GLU ILE ARG VAL ALA ILE HIS ASP          
SEQRES  18 A 1160  GLY PHE THR LEU ASP ASP PRO LYS ARG PRO ARG ASN TYR          
SEQRES  19 A 1160  SER PRO GLN GLN TYR MET ARG SER GLU GLU GLU MET CYS          
SEQRES  20 A 1160  GLU LEU PHE ALA ASP ILE PRO GLU ALA LEU ALA ASN THR          
SEQRES  21 A 1160  VAL GLU ILE ALA LYS ARG CYS ASN VAL THR VAL ARG LEU          
SEQRES  22 A 1160  GLY GLU TYR PHE LEU PRO GLN PHE PRO THR GLY ASP MET          
SEQRES  23 A 1160  SER THR GLU ASP TYR LEU VAL LYS ARG ALA LYS GLU GLY          
SEQRES  24 A 1160  LEU GLU GLU ARG LEU ALA PHE LEU PHE PRO ASP GLU GLU          
SEQRES  25 A 1160  GLU ARG LEU LYS ARG ARG PRO GLU TYR ASP GLU ARG LEU          
SEQRES  26 A 1160  GLU THR GLU LEU GLN VAL ILE ASN GLN MET GLY PHE PRO          
SEQRES  27 A 1160  GLY TYR PHE LEU ILE VAL MET GLU PHE ILE GLN TRP SER          
SEQRES  28 A 1160  LYS ASP ASN GLY VAL PRO VAL GLY PRO GLY ARG GLY SER          
SEQRES  29 A 1160  GLY ALA GLY SER LEU VAL ALA TYR ALA LEU LYS ILE THR          
SEQRES  30 A 1160  ASP LEU ASP PRO LEU GLU PHE ASP LEU LEU PHE GLU ARG          
SEQRES  31 A 1160  PHE LEU ASN PRO GLU ARG VAL SER MET PRO ASP PHE ASP          
SEQRES  32 A 1160  VAL ASP PHE CYS MET GLU LYS ARG ASP GLN VAL ILE GLU          
SEQRES  33 A 1160  HIS VAL ALA ASP MET TYR GLY ARG ASP ALA VAL SER GLN          
SEQRES  34 A 1160  ILE ILE THR PHE GLY THR MET ALA ALA LYS ALA VAL ILE          
SEQRES  35 A 1160  ARG ASP VAL GLY ARG VAL LEU GLY HIS PRO TYR GLY PHE          
SEQRES  36 A 1160  VAL ASP ARG ILE SER LYS LEU ILE PRO PRO ASP PRO GLY          
SEQRES  37 A 1160  MET THR LEU ALA LYS ALA PHE GLU ALA GLU PRO GLN LEU          
SEQRES  38 A 1160  PRO GLU ILE TYR GLU ALA ASP GLU GLU VAL LYS ALA LEU          
SEQRES  39 A 1160  ILE ASP MET ALA ARG LYS LEU GLU GLY VAL THR ARG ASN          
SEQRES  40 A 1160  ALA GLY LYS HIS ALA GLY GLY VAL VAL ILE ALA PRO THR          
SEQRES  41 A 1160  LYS ILE THR ASP PHE ALA PRO LEU TYR CYS ASP GLU GLU          
SEQRES  42 A 1160  GLY LYS HIS PRO VAL THR GLN PHE ASP LYS SER ASP VAL          
SEQRES  43 A 1160  GLU TYR ALA GLY LEU VAL LYS PHE ASP PHE LEU GLY LEU          
SEQRES  44 A 1160  ARG THR LEU THR ILE ILE ASN TRP ALA LEU GLU MET ILE          
SEQRES  45 A 1160  ASN LYS ARG ARG ALA LYS ASN GLY GLU PRO PRO LEU ASP          
SEQRES  46 A 1160  ILE ALA ALA ILE PRO LEU ASP ASP LYS LYS SER PHE ASP          
SEQRES  47 A 1160  MET LEU GLN ARG SER GLU THR THR ALA VAL PHE GLN LEU          
SEQRES  48 A 1160  GLU SER ARG GLY MET LYS ASP LEU ILE LYS ARG LEU GLN          
SEQRES  49 A 1160  PRO ASP CYS PHE GLU ASP MET ILE ALA LEU VAL ALA LEU          
SEQRES  50 A 1160  PHE ARG PRO GLY PRO LEU GLN SER GLY MET VAL ASP ASN          
SEQRES  51 A 1160  PHE ILE ASP ARG LYS HIS GLY ARG GLU GLU ILE SER TYR          
SEQRES  52 A 1160  PRO ASP VAL GLN TRP GLN HIS GLU SER LEU LYS PRO VAL          
SEQRES  53 A 1160  LEU GLU PRO THR TYR GLY ILE ILE LEU TYR GLN GLU GLN          
SEQRES  54 A 1160  VAL MET GLN ILE ALA GLN VAL LEU SER GLY TYR THR LEU          
SEQRES  55 A 1160  GLY GLY ALA ASP MET LEU ARG ARG ALA MET GLY LYS LYS          
SEQRES  56 A 1160  LYS PRO GLU GLU MET ALA LYS GLN ARG SER VAL PHE ALA          
SEQRES  57 A 1160  GLU GLY ALA GLU LYS ASN GLY ILE ASN ALA GLU LEU ALA          
SEQRES  58 A 1160  MET LYS ILE PHE ASP LEU VAL GLU LYS PHE ALA GLY TYR          
SEQRES  59 A 1160  GLY PHE ASN LYS SER HIS SER ALA ALA TYR ALA LEU VAL          
SEQRES  60 A 1160  SER TYR GLN THR LEU TRP LEU LYS ALA HIS TYR PRO ALA          
SEQRES  61 A 1160  GLU PHE MET ALA ALA VAL MET THR ALA ASP MET ASP ASN          
SEQRES  62 A 1160  THR GLU LYS VAL VAL GLY LEU VAL ASP GLU CYS TRP ARG          
SEQRES  63 A 1160  MET GLY LEU LYS ILE LEU PRO PRO ASP ILE ASN SER GLY          
SEQRES  64 A 1160  LEU TYR HIS PHE HIS VAL ASN ASP ASP GLY GLU ILE VAL          
SEQRES  65 A 1160  TYR GLY ILE GLY ALA ILE LYS GLY VAL GLY GLU GLY PRO          
SEQRES  66 A 1160  ILE GLU ALA ILE ILE GLU ALA ARG ASN LYS GLY GLY TYR          
SEQRES  67 A 1160  PHE ARG GLU LEU PHE ASP LEU CYS ALA ARG THR ASP THR          
SEQRES  68 A 1160  LYS LYS LEU ASN ARG ARG VAL LEU GLU LYS LEU ILE MET          
SEQRES  69 A 1160  SER GLY ALA PHE ASP ARG LEU GLY PRO HIS ARG ALA ALA          
SEQRES  70 A 1160  LEU MET ASN SER LEU GLY ASP ALA LEU LYS ALA ALA ASP          
SEQRES  71 A 1160  GLN HIS ALA LYS ALA GLU ALA ILE GLY GLN LEU ASP LEU          
SEQRES  72 A 1160  PHE GLY VAL LEU ALA GLU GLU PRO GLU GLN ILE GLU GLN          
SEQRES  73 A 1160  SER TYR ALA SER CYS GLN PRO TRP PRO GLU GLN VAL VAL          
SEQRES  74 A 1160  LEU ASP GLY GLU ARG GLU THR LEU GLY LEU TYR LEU THR          
SEQRES  75 A 1160  GLY HIS PRO ILE ASN GLN TYR LEU LYS GLU ILE GLU ARG          
SEQRES  76 A 1160  TYR VAL GLY GLY VAL ARG LEU LYS ASP MET HIS PRO THR          
SEQRES  77 A 1160  GLU ARG GLY LYS VAL ILE THR ALA ALA GLY LEU VAL VAL          
SEQRES  78 A 1160  ALA ALA ARG VAL MET VAL THR LYS ARG GLY ASN ARG ILE          
SEQRES  79 A 1160  GLY ILE CYS THR LEU ASP ASP ARG SER GLY ARG LEU GLU          
SEQRES  80 A 1160  VAL MET LEU PHE THR ASP ALA LEU ASP LYS TYR GLN GLN          
SEQRES  81 A 1160  LEU LEU GLU LYS ASP ARG ILE LEU ILE VAL SER GLY GLN          
SEQRES  82 A 1160  VAL SER PHE ASP ASP PHE SER GLY GLY LEU LYS MET THR          
SEQRES  83 A 1160  ALA ARG GLU VAL MET ASP ILE ASP GLU ALA ARG GLU LYS          
SEQRES  84 A 1160  TYR ALA ARG GLY LEU ALA ILE SER LEU THR ASP ARG GLN          
SEQRES  85 A 1160  ILE ASP ASP GLN LEU LEU ASN ARG LEU ARG GLN SER LEU          
SEQRES  86 A 1160  GLU PRO HIS ARG SER GLY THR ILE PRO VAL HIS LEU TYR          
SEQRES  87 A 1160  TYR GLN ARG ALA ASP ALA ARG ALA ARG LEU ARG PHE GLY          
SEQRES  88 A 1160  ALA THR TRP ARG VAL SER PRO SER ASP ARG LEU LEU ASN          
SEQRES  89 A 1160  ASP LEU ARG GLY LEU ILE GLY SER GLU GLN VAL GLU LEU          
SEQRES  90 A 1160  GLU PHE ASP                                                  
SEQRES   1 B  366  MET LYS PHE THR VAL GLU ARG GLU HIS LEU LEU LYS PRO          
SEQRES   2 B  366  LEU GLN GLN VAL SER GLY PRO LEU GLY GLY ARG PRO THR          
SEQRES   3 B  366  LEU PRO ILE LEU GLY ASN LEU LEU LEU GLN VAL ALA ASP          
SEQRES   4 B  366  GLY THR LEU SER LEU THR GLY THR ASP LEU GLU MET GLU          
SEQRES   5 B  366  MET VAL ALA ARG VAL ALA LEU VAL GLN PRO HIS GLU PRO          
SEQRES   6 B  366  GLY ALA THR THR VAL PRO ALA ARG LYS PHE PHE ASP ILE          
SEQRES   7 B  366  CYS ARG GLY LEU PRO GLU GLY ALA GLU ILE ALA VAL GLN          
SEQRES   8 B  366  LEU GLU GLY GLU ARG MET LEU VAL ARG SER GLY ARG SER          
SEQRES   9 B  366  ARG PHE SER LEU SER THR LEU PRO ALA ALA ASP PHE PRO          
SEQRES  10 B  366  ASN LEU ASP ASP TRP GLN SER GLU VAL GLU PHE THR LEU          
SEQRES  11 B  366  PRO GLN ALA THR MET LYS ARG LEU ILE GLU ALA THR GLN          
SEQRES  12 B  366  PHE SER MET ALA HIS GLN ASP VAL ARG TYR TYR LEU ASN          
SEQRES  13 B  366  GLY MET LEU PHE GLU THR GLU GLY GLU GLU LEU ARG THR          
SEQRES  14 B  366  VAL ALA THR ASP GLY HIS ARG LEU ALA VAL CYS SER MET          
SEQRES  15 B  366  PRO ILE GLY GLN SER LEU PRO SER HIS SER VAL ILE VAL          
SEQRES  16 B  366  PRO ARG LYS GLY VAL ILE GLU LEU MET ARG MET LEU ASP          
SEQRES  17 B  366  GLY GLY ASP ASN PRO LEU ARG VAL GLN ILE GLY SER ASN          
SEQRES  18 B  366  ASN ILE ARG ALA HIS VAL GLY ASP PHE ILE PHE THR SER          
SEQRES  19 B  366  LYS LEU VAL ASP GLY ARG PHE PRO ASP TYR ARG ARG VAL          
SEQRES  20 B  366  LEU PRO LYS ASN PRO ASP LYS HIS LEU GLU ALA GLY CYS          
SEQRES  21 B  366  ASP LEU LEU LYS GLN ALA PHE ALA ARG ALA ALA ILE LEU          
SEQRES  22 B  366  SER ASN GLU LYS PHE ARG GLY VAL ARG LEU TYR VAL SER          
SEQRES  23 B  366  GLU ASN GLN LEU LYS ILE THR ALA ASN ASN PRO GLU GLN          
SEQRES  24 B  366  GLU GLU ALA GLU GLU ILE LEU ASP VAL THR TYR SER GLY          
SEQRES  25 B  366  ALA GLU MET GLU ILE GLY PHE ASN VAL SER TYR VAL LEU          
SEQRES  26 B  366  ASP VAL LEU ASN ALA LEU LYS CYS GLU ASN VAL ARG MET          
SEQRES  27 B  366  MET LEU THR ASP SER VAL SER SER VAL GLN ILE GLU ASP          
SEQRES  28 B  366  ALA ALA SER GLN SER ALA ALA TYR VAL VAL MET PRO MET          
SEQRES  29 B  366  ARG LEU                                                      
SEQRES   1 C  366  MET LYS PHE THR VAL GLU ARG GLU HIS LEU LEU LYS PRO          
SEQRES   2 C  366  LEU GLN GLN VAL SER GLY PRO LEU GLY GLY ARG PRO THR          
SEQRES   3 C  366  LEU PRO ILE LEU GLY ASN LEU LEU LEU GLN VAL ALA ASP          
SEQRES   4 C  366  GLY THR LEU SER LEU THR GLY THR ASP LEU GLU MET GLU          
SEQRES   5 C  366  MET VAL ALA ARG VAL ALA LEU VAL GLN PRO HIS GLU PRO          
SEQRES   6 C  366  GLY ALA THR THR VAL PRO ALA ARG LYS PHE PHE ASP ILE          
SEQRES   7 C  366  CYS ARG GLY LEU PRO GLU GLY ALA GLU ILE ALA VAL GLN          
SEQRES   8 C  366  LEU GLU GLY GLU ARG MET LEU VAL ARG SER GLY ARG SER          
SEQRES   9 C  366  ARG PHE SER LEU SER THR LEU PRO ALA ALA ASP PHE PRO          
SEQRES  10 C  366  ASN LEU ASP ASP TRP GLN SER GLU VAL GLU PHE THR LEU          
SEQRES  11 C  366  PRO GLN ALA THR MET LYS ARG LEU ILE GLU ALA THR GLN          
SEQRES  12 C  366  PHE SER MET ALA HIS GLN ASP VAL ARG TYR TYR LEU ASN          
SEQRES  13 C  366  GLY MET LEU PHE GLU THR GLU GLY GLU GLU LEU ARG THR          
SEQRES  14 C  366  VAL ALA THR ASP GLY HIS ARG LEU ALA VAL CYS SER MET          
SEQRES  15 C  366  PRO ILE GLY GLN SER LEU PRO SER HIS SER VAL ILE VAL          
SEQRES  16 C  366  PRO ARG LYS GLY VAL ILE GLU LEU MET ARG MET LEU ASP          
SEQRES  17 C  366  GLY GLY ASP ASN PRO LEU ARG VAL GLN ILE GLY SER ASN          
SEQRES  18 C  366  ASN ILE ARG ALA HIS VAL GLY ASP PHE ILE PHE THR SER          
SEQRES  19 C  366  LYS LEU VAL ASP GLY ARG PHE PRO ASP TYR ARG ARG VAL          
SEQRES  20 C  366  LEU PRO LYS ASN PRO ASP LYS HIS LEU GLU ALA GLY CYS          
SEQRES  21 C  366  ASP LEU LEU LYS GLN ALA PHE ALA ARG ALA ALA ILE LEU          
SEQRES  22 C  366  SER ASN GLU LYS PHE ARG GLY VAL ARG LEU TYR VAL SER          
SEQRES  23 C  366  GLU ASN GLN LEU LYS ILE THR ALA ASN ASN PRO GLU GLN          
SEQRES  24 C  366  GLU GLU ALA GLU GLU ILE LEU ASP VAL THR TYR SER GLY          
SEQRES  25 C  366  ALA GLU MET GLU ILE GLY PHE ASN VAL SER TYR VAL LEU          
SEQRES  26 C  366  ASP VAL LEU ASN ALA LEU LYS CYS GLU ASN VAL ARG MET          
SEQRES  27 C  366  MET LEU THR ASP SER VAL SER SER VAL GLN ILE GLU ASP          
SEQRES  28 C  366  ALA ALA SER GLN SER ALA ALA TYR VAL VAL MET PRO MET          
SEQRES  29 C  366  ARG LEU                                                      
SEQRES   1 D  243  MET SER THR ALA ILE THR ARG GLN ILE VAL LEU ASP THR          
SEQRES   2 D  243  GLU THR THR GLY MET ASN GLN ILE GLY ALA HIS TYR GLU          
SEQRES   3 D  243  GLY HIS LYS ILE ILE GLU ILE GLY ALA VAL GLU VAL VAL          
SEQRES   4 D  243  ASN ARG ARG LEU THR GLY ASN ASN PHE HIS VAL TYR LEU          
SEQRES   5 D  243  LYS PRO ASP ARG LEU VAL ASP PRO GLU ALA PHE GLY VAL          
SEQRES   6 D  243  HIS GLY ILE ALA ASP GLU PHE LEU LEU ASP LYS PRO THR          
SEQRES   7 D  243  PHE ALA GLU VAL ALA ASP GLU PHE MET ASP TYR ILE ARG          
SEQRES   8 D  243  GLY ALA GLU LEU VAL ILE HIS ASN ALA ALA PHE ASP ILE          
SEQRES   9 D  243  GLY PHE MET ASP TYR GLU PHE SER LEU LEU LYS ARG ASP          
SEQRES  10 D  243  ILE PRO LYS THR ASN THR PHE CYS LYS VAL THR ASP SER          
SEQRES  11 D  243  LEU ALA VAL ALA ARG LYS MET PHE PRO GLY LYS ARG ASN          
SEQRES  12 D  243  SER LEU ASP ALA LEU CYS ALA ARG TYR GLU ILE ASP ASN          
SEQRES  13 D  243  SER LYS ARG THR LEU HIS GLY ALA LEU LEU ASP ALA GLN          
SEQRES  14 D  243  ILE LEU ALA GLU VAL TYR LEU ALA MET THR GLY GLY GLN          
SEQRES  15 D  243  LEU SER LEU PRO LEU ALA MET GLU GLY GLU THR GLN GLN          
SEQRES  16 D  243  GLN GLN GLY GLU ALA THR ILE GLN ARG ILE VAL ARG GLN          
SEQRES  17 D  243  ALA SER LYS LEU ARG VAL VAL PHE ALA THR ASP GLU GLU          
SEQRES  18 D  243  ILE ALA ALA HIS GLU ALA ARG LEU ASP LEU VAL GLN LYS          
SEQRES  19 D  243  LYS GLY GLY SER CYS LEU TRP ARG ALA                          
SEQRES   1 P   25   DG  DG  DA  DG  DT  DA  DG  DT  DA  DC  DT  DA  DG          
SEQRES   2 P   25   DG  DA  DC  DG  DA  DA  DG  DG  DA  DC  DT  DC              
SEQRES   1 T   29   DT  DC  DA  DG  DG  DA  DG  DT  DC  DC  DT  DT  DC          
SEQRES   2 T   29   DG  DT  DC  DC  DT  DA  DG  DT  DA  DC  DT  DA  DC          
SEQRES   3 T   29   DT  DC  DC                                                  
HELIX    1   1 SER A   13  MET A   17  5                                   5    
HELIX    2   2 LYS A   23  LEU A   34  1                                  12    
HELIX    3   3 GLY A   49  GLY A   61  1                                  13    
HELIX    4   4 ASN A   90  GLY A  108  1                                  19    
HELIX    5   5 ASP A  119  LEU A  124  1                                   6    
HELIX    6   6 GLY A  133  MET A  136  5                                   4    
HELIX    7   7 GLY A  137  GLY A  146  1                                  10    
HELIX    8   8 ASN A  147  PHE A  162  1                                  16    
HELIX    9   9 ASP A  177  GLY A  193  1                                  17    
HELIX   10  10 ASP A  206  SER A  208  5                                   3    
HELIX   11  11 ASP A  209  GLY A  222  1                                  14    
HELIX   12  12 SER A  242  PHE A  250  1                                   9    
HELIX   13  13 ILE A  253  CYS A  267  1                                  15    
HELIX   14  14 SER A  287  PHE A  308  1                                  22    
HELIX   15  15 ASP A  310  ARG A  318  1                                   9    
HELIX   16  16 ARG A  318  GLY A  336  1                                  19    
HELIX   17  17 PHE A  337  ASN A  354  1                                  18    
HELIX   18  18 SER A  364  GLY A  367  5                                   4    
HELIX   19  19 SER A  368  LEU A  374  1                                   7    
HELIX   20  20 LEU A  387  PHE A  391  5                                   5    
HELIX   21  21 CYS A  407  GLU A  409  5                                   3    
HELIX   22  22 LYS A  410  GLY A  423  1                                  14    
HELIX   23  23 ALA A  437  LEU A  449  1                                  13    
HELIX   24  24 PRO A  452  LYS A  461  1                                  10    
HELIX   25  25 THR A  470  GLU A  478  1                                   9    
HELIX   26  26 PRO A  479  ASP A  488  1                                  10    
HELIX   27  27 ASP A  488  GLU A  502  1                                  15    
HELIX   28  28 LYS A  521  PHE A  525  5                                   5    
HELIX   29  29 LYS A  543  ALA A  549  1                                   7    
HELIX   30  30 THR A  561  ASN A  579  1                                  19    
HELIX   31  31 ASP A  585  ILE A  589  5                                   5    
HELIX   32  32 ASP A  593  ARG A  602  1                                  10    
HELIX   33  33 SER A  613  GLN A  624  1                                  12    
HELIX   34  34 CYS A  627  PHE A  638  1                                  12    
HELIX   35  35 ARG A  639  GLN A  644  1                                   6    
HELIX   36  36 GLY A  646  HIS A  656  1                                  11    
HELIX   37  37 HIS A  670  SER A  672  5                                   3    
HELIX   38  38 LEU A  673  GLU A  678  1                                   6    
HELIX   39  39 PRO A  679  TYR A  681  5                                   3    
HELIX   40  40 TYR A  686  LEU A  697  1                                  12    
HELIX   41  41 THR A  701  LYS A  715  1                                  15    
HELIX   42  42 LYS A  716  ASN A  734  1                                  19    
HELIX   43  43 ASN A  737  GLY A  753  1                                  17    
HELIX   44  44 ASN A  757  HIS A  777  1                                  21    
HELIX   45  45 GLU A  781  ASP A  790  1                                  10    
HELIX   46  46 ASN A  793  GLY A  808  1                                  16    
HELIX   47  47 GLY A  842  GLY A  856  1                                  15    
HELIX   48  48 GLU A  861  THR A  869  1                                   9    
HELIX   49  49 ASN A  875  GLY A  886  1                                  12    
HELIX   50  50 ALA A  896  ILE A  918  1                                  23    
HELIX   51  51 ARG B    7  SER B   18  1                                  12    
HELIX   52  52 LEU B   27  LEU B   30  5                                   4    
HELIX   53  53 ALA B   72  LEU B   82  1                                  11    
HELIX   54  54 PRO B  112  PHE B  116  5                                   5    
HELIX   55  55 GLN B  132  ALA B  141  1                                  10    
HELIX   56  56 THR B  142  MET B  146  5                                   5    
HELIX   57  57 ARG B  152  LEU B  155  5                                   4    
HELIX   58  58 ARG B  197  LEU B  207  1                                  11    
HELIX   59  59 ASP B  243  LEU B  248  1                                   6    
HELIX   60  60 CYS B  260  ILE B  272  1                                  13    
HELIX   61  61 VAL B  321  LEU B  331  1                                  11    
HELIX   62  62 ARG C    7  GLY C   19  1                                  13    
HELIX   63  63 LEU C   27  LEU C   30  5                                   4    
HELIX   64  64 ALA C   72  GLY C   81  1                                  10    
HELIX   65  65 PRO C  112  PHE C  116  5                                   5    
HELIX   66  66 GLN C  132  ALA C  141  1                                  10    
HELIX   67  67 THR C  142  MET C  146  5                                   5    
HELIX   68  68 ARG C  197  LEU C  207  1                                  11    
HELIX   69  69 ASP C  243  LEU C  248  1                                   6    
HELIX   70  70 CYS C  260  LEU C  273  1                                  14    
HELIX   71  71 VAL C  321  LEU C  331  1                                  11    
HELIX   72  72 ASP D   59  GLY D   67  1                                   9    
HELIX   73  73 ALA D   69  LEU D   73  5                                   5    
HELIX   74  74 VAL D   82  ARG D   91  1                                  10    
HELIX   75  75 ASN D   99  LYS D  115  1                                  17    
HELIX   76  76 LYS D  120  PHE D  124  5                                   5    
HELIX   77  77 SER D  130  PHE D  138  1                                   9    
HELIX   78  78 SER D  144  TYR D  152  1                                   9    
HELIX   79  79 GLY D  163  THR D  179  1                                  17    
HELIX   80  80 THR D  218  GLY D  237  1                                  20    
HELIX   81  81 CYS D  239  ALA D  243  5                                   5    
SHEET    1  AA 2 ALA A  38  ILE A  41  0                                        
SHEET    2  AA 2 LYS A  63  GLN A  73  1  O  LYS A  63   N  LEU A  39           
SHEET    1  AB 2 ILE A 116  ASP A 117  0                                        
SHEET    2  AB 2 LYS A  63  GLN A  73 -1  O  ASN A  71   N  ILE A 116           
SHEET    1  AC 6 VAL A 196  ALA A 198  0                                        
SHEET    2  AC 6 TYR A 166  LEU A 170  1  O  LEU A 168   N  VAL A 197           
SHEET    3  AC 6 LEU A 128  LEU A 131  1  O  LEU A 130   N  PHE A 167           
SHEET    4  AC 6 THR A  82  ALA A  88 -1  O  THR A  85   N  LEU A 131           
SHEET    5  AC 6 LYS A  63  GLN A  73 -1  O  VAL A  66   N  ALA A  88           
SHEET    6  AC 6 ILE A 116  ASP A 117 -1  O  ILE A 116   N  GLN A  73           
SHEET    1  AD 6 VAL A 196  ALA A 198  0                                        
SHEET    2  AD 6 TYR A 166  LEU A 170  1  O  LEU A 168   N  VAL A 197           
SHEET    3  AD 6 LEU A 128  LEU A 131  1  O  LEU A 130   N  PHE A 167           
SHEET    4  AD 6 THR A  82  ALA A  88 -1  O  THR A  85   N  LEU A 131           
SHEET    5  AD 6 LYS A  63  GLN A  73 -1  O  VAL A  66   N  ALA A  88           
SHEET    6  AD 6 ALA A  38  ILE A  41  1  O  LEU A  39   N  ILE A  65           
SHEET    1  AE 6 ASP A 405  PHE A 406  0                                        
SHEET    2  AE 6 VAL A 552  PHE A 556  1  O  ASP A 555   N  PHE A 406           
SHEET    3  AE 6 GLY A 514  ILE A 517 -1  O  VAL A 515   N  PHE A 554           
SHEET    4  AE 6 VAL A 427  ILE A 431 -1  O  SER A 428   N  VAL A 516           
SHEET    5  AE 6 VAL A 538  ASP A 542  1  O  THR A 539   N  ILE A 431           
SHEET    6  AE 6 LEU A 528  TYR A 529 -1  O  TYR A 529   N  VAL A 538           
SHEET    1  AF 2 GLY A 434  THR A 435  0                                        
SHEET    2  AF 2 THR A 505  ASN A 507 -1  N  ARG A 506   O  GLY A 434           
SHEET    1  BA 8 LYS B   2  GLU B   6  0                                        
SHEET    2  BA 8 GLU B  87  GLU B  93 -1  O  ILE B  88   N  VAL B   5           
SHEET    3  BA 8 ARG B  96  SER B 101 -1  O  ARG B  96   N  GLU B  93           
SHEET    4  BA 8 SER B 104  SER B 109 -1  O  SER B 104   N  SER B 101           
SHEET    5  BA 8 GLU C 301  ASP C 307 -1  O  GLU C 301   N  SER B 107           
SHEET    6  BA 8 GLN C 289  ASN C 295 -1  O  LEU C 290   N  LEU C 306           
SHEET    7  BA 8 GLY C 280  SER C 286 -1  O  GLY C 280   N  ASN C 295           
SHEET    8  BA 8 MET C 315  ASN C 320 -1  O  MET C 315   N  VAL C 285           
SHEET    1  BB 8 GLY B  66  PRO B  71  0                                        
SHEET    2  BB 8 ASN B  32  ALA B  38 -1  O  LEU B  33   N  VAL B  70           
SHEET    3  BB 8 THR B  41  THR B  47 -1  O  THR B  41   N  ALA B  38           
SHEET    4  BB 8 MET B  51  ALA B  58 -1  O  MET B  53   N  GLY B  46           
SHEET    5  BB 8 PHE B 230  LYS B 235 -1  O  ILE B 231   N  VAL B  54           
SHEET    6  BB 8 ASN B 222  VAL B 227 -1  O  ILE B 223   N  SER B 234           
SHEET    7  BB 8 PRO B 213  GLY B 219 -1  O  ARG B 215   N  HIS B 226           
SHEET    8  BB 8 SER B 124  PRO B 131 -1  N  GLU B 125   O  ILE B 218           
SHEET    1  BC 3 GLY B 157  THR B 172  0                                        
SHEET    2  BC 3 ARG B 176  PRO B 196 -1  O  ALA B 178   N  ALA B 171           
SHEET    3  BC 3 ALA B 357  VAL B 361 -1  O  ALA B 358   N  VAL B 179           
SHEET    1  BD 4 THR B 309  SER B 311  0                                        
SHEET    2  BD 4 LYS B 254  GLY B 259 -1  O  HIS B 255   N  SER B 311           
SHEET    3  BD 4 ASN B 335  LEU B 340 -1  O  VAL B 336   N  ALA B 258           
SHEET    4  BD 4 GLN B 348  ASP B 351 -1  O  GLN B 348   N  MET B 339           
SHEET    1  BE 8 MET B 315  ASN B 320  0                                        
SHEET    2  BE 8 GLY B 280  SER B 286 -1  O  VAL B 281   N  PHE B 319           
SHEET    3  BE 8 GLN B 289  ALA B 294 -1  O  GLN B 289   N  SER B 286           
SHEET    4  BE 8 GLU B 301  ASP B 307 -1  O  ALA B 302   N  ALA B 294           
SHEET    5  BE 8 SER C 104  SER C 109 -1  O  ARG C 105   N  GLU B 303           
SHEET    6  BE 8 ARG C  96  SER C 101 -1  O  MET C  97   N  LEU C 108           
SHEET    7  BE 8 GLU C  87  GLU C  93 -1  O  ALA C  89   N  ARG C 100           
SHEET    8  BE 8 LYS C   2  GLU C   6 -1  O  PHE C   3   N  VAL C  90           
SHEET    1  CA 8 GLY C  66  PRO C  71  0                                        
SHEET    2  CA 8 ASN C  32  ALA C  38 -1  O  LEU C  33   N  VAL C  70           
SHEET    3  CA 8 THR C  41  THR C  47 -1  O  THR C  41   N  ALA C  38           
SHEET    4  CA 8 MET C  51  ALA C  58 -1  O  MET C  53   N  GLY C  46           
SHEET    5  CA 8 PHE C 230  LYS C 235 -1  O  ILE C 231   N  VAL C  54           
SHEET    6  CA 8 ASN C 222  VAL C 227 -1  O  ILE C 223   N  SER C 234           
SHEET    7  CA 8 PRO C 213  ILE C 218 -1  O  ARG C 215   N  HIS C 226           
SHEET    8  CA 8 VAL C 126  PRO C 131 -1  O  VAL C 126   N  ILE C 218           
SHEET    1  CB 9 HIS C 191  PRO C 196  0                                        
SHEET    2  CB 9 GLY C 157  GLU C 163 -1  O  MET C 158   N  VAL C 195           
SHEET    3  CB 9 GLU C 166  THR C 172 -1  O  GLU C 166   N  GLU C 163           
SHEET    4  CB 9 ARG C 176  PRO C 183 -1  O  ALA C 178   N  ALA C 171           
SHEET    5  CB 9 ALA C 357  VAL C 361 -1  O  ALA C 358   N  VAL C 179           
SHEET    6  CB 9 VAL C 347  ASP C 351 -1  O  VAL C 347   N  VAL C 361           
SHEET    7  CB 9 ASN C 335  LEU C 340 -1  O  ARG C 337   N  GLU C 350           
SHEET    8  CB 9 LYS C 254  GLY C 259 -1  O  LYS C 254   N  LEU C 340           
SHEET    9  CB 9 THR C 309  SER C 311 -1  O  THR C 309   N  GLU C 257           
SHEET    1  DA 2 GLN D   8  THR D  15  0                                        
SHEET    2  DA 2 ILE D  30  VAL D  39 -1  N  ILE D  31   O  GLU D  14           
SHEET    1  DB 2 ARG D  42  LEU D  43  0                                        
SHEET    2  DB 2 ILE D  30  VAL D  39  1  O  VAL D  39   N  ARG D  42           
SHEET    1  DC 2 PHE D  48  TYR D  51  0                                        
SHEET    2  DC 2 ILE D  30  VAL D  39 -1  O  ILE D  33   N  VAL D  50           
SHEET    1  DD 2 GLU D  94  ILE D  97  0                                        
SHEET    2  DD 2 LYS D 126  ASP D 129  1  O  LYS D 126   N  LEU D  95           
CISPEP   1 TYR A  663    PRO A  664          0         5.19                     
CISPEP   2 LYS A  810    ILE A  811          0       -26.45                     
CISPEP   3 ILE A  918    GLY A  919          0       -27.84                     
CISPEP   4 GLY A  919    GLN A  920          0        -1.34                     
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                                                                             
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