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Database: PDB
Entry: 5MBV
LinkDB: 5MBV
Original site: 5MBV 
HEADER    DNA BINDING PROTEIN                     08-NOV-16   5MBV              
TITLE     CRYO-EM STRUCTURE OF LAMBDA PHAGE PROTEIN GAMS BOUND TO RECBCD.       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECBCD ENZYME SUBUNIT RECB;                                
COMPND   3 CHAIN: B;                                                            
COMPND   4 SYNONYM: EXODEOXYRIBONUCLEASE V 135 KDA POLYPEPTIDE,                 
COMPND   5 EXODEOXYRIBONUCLEASE V BETA CHAIN,EXONUCLEASE V SUBUNIT RECB,EXOV    
COMPND   6 SUBUNIT RECB,HELICASE/NUCLEASE RECBCD SUBUNIT RECB;                  
COMPND   7 EC: 3.1.11.5;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RECBCD ENZYME SUBUNIT RECC;                                
COMPND  11 CHAIN: C;                                                            
COMPND  12 SYNONYM: EXODEOXYRIBONUCLEASE V 125 KDA POLYPEPTIDE,                 
COMPND  13 EXODEOXYRIBONUCLEASE V GAMMA CHAIN,EXONUCLEASE V SUBUNIT RECC,EXOV   
COMPND  14 SUBUNIT RECC;                                                        
COMPND  15 EC: 3.1.11.5;                                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: RECBCD ENZYME SUBUNIT RECD;                                
COMPND  19 CHAIN: D;                                                            
COMPND  20 SYNONYM: EXODEOXYRIBONUCLEASE V 67 KDA POLYPEPTIDE,                  
COMPND  21 EXODEOXYRIBONUCLEASE V ALPHA CHAIN,EXONUCLEASE V SUBUNIT RECD,EXOV   
COMPND  22 SUBUNIT RECD,HELICASE/NUCLEASE RECBCD SUBUNIT RECD;                  
COMPND  23 EC: 3.1.11.5;                                                        
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MOL_ID: 4;                                                           
COMPND  26 MOLECULE: HOST-NUCLEASE INHIBITOR PROTEIN GAM;                       
COMPND  27 CHAIN: A, E;                                                         
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MUTATION: YES;                                                       
COMPND  30 OTHER_DETAILS: GAML IS CLEAVED AT POSITION Y44 WHEN EXPRESSED IN     
COMPND  31 E.COLI INTO GAMS (SEE PAPER - PUBMED ID 17544443). WE HAD THE GAMS   
COMPND  32 GENE SYNTHESISED TO START AT M41 FOR THIS PROJECT. IT PURIFIES AS A  
COMPND  33 DIMER.                                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: RECB, IOR, RORA, B2820, JW2788;                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PETDUET-1;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 562;                                                 
SOURCE  12 GENE: RECC, B2822, JW2790;                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1;                               
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  19 ORGANISM_TAXID: 562;                                                 
SOURCE  20 GENE: RECD, HOPE, B2819, JW2787;                                     
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1;                               
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;                    
SOURCE  27 ORGANISM_TAXID: 10710;                                               
SOURCE  28 GENE: GAM, GAMMA;                                                    
SOURCE  29 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  30 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  31 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  32 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    INHIBITOR, COMPLEX, DNA REPAIR, HELICASE/NUCLEASE, DNA BINDING        
KEYWDS   2 PROTEIN                                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    M.WILKINSON,Y.CHABAN,D.B.WIGLEY                                       
REVDAT   3   28-MAR-18 5MBV    1       TITLE                                    
REVDAT   2   23-AUG-17 5MBV    1       REMARK                                   
REVDAT   1   11-JAN-17 5MBV    0                                                
JRNL        AUTH   M.WILKINSON,L.TROMAN,W.A.WAN NUR ISMAH,Y.CHABAN,M.B.AVISON,  
JRNL        AUTH 2 M.S.DILLINGHAM,D.B.WIGLEY                                    
JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF RECBCD BY GAM AND ITS 
JRNL        TITL 2 SYNERGISTIC ANTIBACTERIAL EFFECT WITH QUINOLONES.            
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   28009252                                                     
JRNL        DOI    10.7554/ELIFE.22963                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : GAUTOMATCH, EPU, GCTF, COOT, RELION,      
REMARK   3                            RELION, RELION, RELION, REFMAC, PHENIX    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 5LD2                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
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)  : 3.800                          
REMARK   3   NUMBER OF PARTICLES               : 122796                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING ONLY            
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5MBV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002179.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : RECBCD COMPLEX BOUND TO           
REMARK 245                                    INHIBITORY PROTEIN LAMBDA GAMS;   
REMARK 245                                    RECBCD HELICASE/NUCLEASE          
REMARK 245                                    COMPLEX; LAMBDA GAMS              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 1.40                              
REMARK 245   SAMPLE SUPPORT DETAILS         : GRIDS WERE THINNED BY GLOW        
REMARK 245                                    DISCHARGE IN 30S STEPS WITH 1     
REMARK 245                                    MINUTE WAIT IN BETWEEN            
REMARK 245                                    TREATMENTS. THEN LEFT FOR 1-2     
REMARK 245                                    WEEKS PRIOR TO OVERNIGHT          
REMARK 245                                    TREATMENT WITH 1 MM AMPIPHOL A8-  
REMARK 245                                    35 TO RENDER SURFACE              
REMARK 245                                    HYDROPHILIC. GRIDS WERE WASHED    
REMARK 245                                    WITH 5 DROPS OF WATER PRIOR TO    
REMARK 245                                    USE. EMS                          
REMARK 245   SAMPLE VITRIFICATION DETAILS   : 3 UL SAMPLE APPLIED BLOT FORCE    
REMARK 245                                    OF -4 FOR 1 S                     
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : RECBCD AND GAMS WERE EXPRESSED    
REMARK 245  AND PURIFIED SEPARATELY. THEY WERE MIXED WITH AN EXCESS OF GAMS     
REMARK 245  THEN PASSED THROUGH A SIZE EXCLUSION COLUMN TO SEPARATE OUT FREE    
REMARK 245  GAMS.                                                               
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 334                            
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1200.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2400.00                        
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)  : 1.40                           
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 105000                         
REMARK 245   CALIBRATED MAGNIFICATION          : 37313                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 25710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 129280 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, A, E                         
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     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     SER B   290                                                      
REMARK 465     GLN B   291                                                      
REMARK 465     ARG B   292                                                      
REMARK 465     PHE B   293                                                      
REMARK 465     LEU B   294                                                      
REMARK 465     GLU B   295                                                      
REMARK 465     ASP B   296                                                      
REMARK 465     ARG B   297                                                      
REMARK 465     THR B   298                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     ALA B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     GLU B   303                                                      
REMARK 465     ARG B   912                                                      
REMARK 465     GLY B   913                                                      
REMARK 465     HIS B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     ILE B   916                                                      
REMARK 465     ALA B   917                                                      
REMARK 465     GLN B   918                                                      
REMARK 465     ASP B   919                                                      
REMARK 465     LEU B   920                                                      
REMARK 465     MET B   921                                                      
REMARK 465     PRO B   922                                                      
REMARK 465     ARG B   923                                                      
REMARK 465     LEU B   924                                                      
REMARK 465     ASP B   925                                                      
REMARK 465     VAL B   926                                                      
REMARK 465     ASP B   927                                                      
REMARK 465     ALA B   928                                                      
REMARK 465     ALA B   929                                                      
REMARK 465     GLY B   930                                                      
REMARK 465     VAL B   931                                                      
REMARK 465     ALA B   932                                                      
REMARK 465     SER B   933                                                      
REMARK 465     VAL B   934                                                      
REMARK 465     VAL B   935                                                      
REMARK 465     GLU B   936                                                      
REMARK 465     GLU B   937                                                      
REMARK 465     PRO B   938                                                      
REMARK 465     THR B   939                                                      
REMARK 465     LEU B   940                                                      
REMARK 465     MET B  1175                                                      
REMARK 465     THR B  1176                                                      
REMARK 465     LEU B  1177                                                      
REMARK 465     GLU B  1178                                                      
REMARK 465     GLU B  1179                                                      
REMARK 465     ALA B  1180                                                      
REMARK 465     SER C  1122                                                      
REMARK 465     MET D     0                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     TYR D   359                                                      
REMARK 465     ARG D   360                                                      
REMARK 465     PHE D   361                                                      
REMARK 465     GLY D   362                                                      
REMARK 465     SER D   363                                                      
REMARK 465     ASP D   364                                                      
REMARK 465     SER D   365                                                      
REMARK 465     HIS D   471                                                      
REMARK 465     PRO D   472                                                      
REMARK 465     HIS D   473                                                      
REMARK 465     SER D   474                                                      
REMARK 465     ARG D   475                                                      
REMARK 465     ARG D   607                                                      
REMARK 465     GLU D   608                                                      
REMARK 465     MET E    41                                                      
REMARK 465     ASN E    42                                                      
REMARK 465     ALA E    43                                                      
REMARK 465     TYR E    44                                                      
REMARK 465     TYR E    45                                                      
REMARK 465     ILE E    46                                                      
REMARK 465     GLN E    47                                                      
REMARK 465     ASP E    48                                                      
REMARK 465     ARG E    49                                                      
REMARK 465     LEU E    50                                                      
REMARK 465     GLU E    51                                                      
REMARK 465     ALA E    52                                                      
REMARK 465     GLN E    53                                                      
REMARK 465     SER E    54                                                      
REMARK 465     TRP E    55                                                      
REMARK 465     ALA E    56                                                      
REMARK 465     ARG E    57                                                      
REMARK 465     HIS E    58                                                      
REMARK 465     TYR E    59                                                      
REMARK 465     GLN E    60                                                      
REMARK 465     SER E   136                                                      
REMARK 465     GLU E   137                                                      
REMARK 465     VAL E   138                                                      
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    LEU D    67     OG1  THR D    70              2.17            
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    GLU B  90       -5.09     67.33                                   
REMARK 500    CYS B 172      -59.59   -121.87                                   
REMARK 500    SER B 270       -3.16     70.13                                   
REMARK 500    PRO B 379       48.19    -79.46                                   
REMARK 500    VAL B 380      161.49    176.87                                   
REMARK 500    ILE B 400      -66.70    -91.94                                   
REMARK 500    HIS B 402      -72.81    -56.37                                   
REMARK 500    MET B 469       -7.01     77.70                                   
REMARK 500    LYS B 492       73.75     53.88                                   
REMARK 500    ARG B 547      145.58   -176.94                                   
REMARK 500    ARG B 655      -73.43   -116.41                                   
REMARK 500    SER B 720       -1.39     68.20                                   
REMARK 500    SER B 731       -2.41     72.48                                   
REMARK 500    HIS B 772      -64.00   -107.50                                   
REMARK 500    ASP B 863      -11.05     63.76                                   
REMARK 500    ASP B 864      -64.34   -129.10                                   
REMARK 500    ASN B 875      -73.56   -117.77                                   
REMARK 500    TRP B 878      177.25    177.92                                   
REMARK 500    ASP B 882     -141.44     58.49                                   
REMARK 500    LEU B 909      -63.39    -98.87                                   
REMARK 500    ASN B1003     -142.03     53.77                                   
REMARK 500    GLU B1020       70.03     58.58                                   
REMARK 500    SER B1028      -71.77    -84.17                                   
REMARK 500    LEU B1036      -61.42   -101.63                                   
REMARK 500    CYS B1050      156.86     68.74                                   
REMARK 500    SER B1083      -77.82   -120.59                                   
REMARK 500    ASN B1084     -136.47     46.13                                   
REMARK 500    TRP B1085       71.90     46.79                                   
REMARK 500    ASP B1089      -58.98   -127.99                                   
REMARK 500    SER B1090     -161.65    -73.31                                   
REMARK 500    SER B1091       -0.60    -56.82                                   
REMARK 500    ALA B1162      -12.96     68.67                                   
REMARK 500    LYS C  53      -63.72   -100.17                                   
REMARK 500    GLU C  79       -3.22     79.13                                   
REMARK 500    GLN C  89      -62.99    -91.04                                   
REMARK 500    GLU C 106      -13.98     75.28                                   
REMARK 500    LYS C 121       -3.70     86.68                                   
REMARK 500    ALA C 161       -7.09     80.49                                   
REMARK 500    HIS C 233      -65.70   -121.11                                   
REMARK 500    LYS C 252      -70.66    -83.10                                   
REMARK 500    PHE C 269       -2.75     68.08                                   
REMARK 500    LEU C 276       -1.74     66.65                                   
REMARK 500    PHE C 277     -129.56     63.62                                   
REMARK 500    ASN C 282      -76.15    -61.59                                   
REMARK 500    ALA C 283     -139.59     41.14                                   
REMARK 500    GLN C 285      -70.93    -58.93                                   
REMARK 500    ASN C 288     -140.70     52.78                                   
REMARK 500    GLN C 293      -64.14    -99.77                                   
REMARK 500    ASP C 332      -68.62   -133.90                                   
REMARK 500    HIS C 380      -63.64   -103.57                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      80 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5LD2   RELATED DB: PDB                                   
REMARK 900 5LD2 CONTAINS RECBCD COMPLEXED WITH DNA                              
REMARK 900 RELATED ID: EMD-3460   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF LAMBDA PHAGE PROTEIN GAMS BOUND TO RECBCD       
DBREF  5MBV B    1  1180  UNP    P08394   RECB_ECOLI       1   1180             
DBREF  5MBV C    1  1122  UNP    P07648   RECC_ECOLI       1   1122             
DBREF  5MBV D    2   608  UNP    P04993   RECD_ECOLI       2    608             
DBREF  5MBV A   41   138  UNP    P03702   GAM_LAMBD       41    138             
DBREF  5MBV E   41   138  UNP    P03702   GAM_LAMBD       41    138             
SEQADV 5MBV GLY B    0  UNP  P08394              EXPRESSION TAG                 
SEQADV 5MBV MET D    0  UNP  P04993              INITIATING METHIONINE          
SEQADV 5MBV GLY D    1  UNP  P04993              EXPRESSION TAG                 
SEQADV 5MBV ILE A   79  UNP  P03702    LEU    79 ENGINEERED MUTATION            
SEQADV 5MBV ILE E   79  UNP  P03702    LEU    79 ENGINEERED MUTATION            
SEQRES   1 B 1181  GLY MET SER ASP VAL ALA GLU THR LEU ASP PRO LEU ARG          
SEQRES   2 B 1181  LEU PRO LEU GLN GLY GLU ARG LEU ILE GLU ALA SER ALA          
SEQRES   3 B 1181  GLY THR GLY LYS THR PHE THR ILE ALA ALA LEU TYR LEU          
SEQRES   4 B 1181  ARG LEU LEU LEU GLY LEU GLY GLY SER ALA ALA PHE PRO          
SEQRES   5 B 1181  ARG PRO LEU THR VAL GLU GLU LEU LEU VAL VAL THR PHE          
SEQRES   6 B 1181  THR GLU ALA ALA THR ALA GLU LEU ARG GLY ARG ILE ARG          
SEQRES   7 B 1181  SER ASN ILE HIS GLU LEU ARG ILE ALA CYS LEU ARG GLU          
SEQRES   8 B 1181  THR THR ASP ASN PRO LEU TYR GLU ARG LEU LEU GLU GLU          
SEQRES   9 B 1181  ILE ASP ASP LYS ALA GLN ALA ALA GLN TRP LEU LEU LEU          
SEQRES  10 B 1181  ALA GLU ARG GLN MET ASP GLU ALA ALA VAL PHE THR ILE          
SEQRES  11 B 1181  HIS GLY PHE CYS GLN ARG MET LEU ASN LEU ASN ALA PHE          
SEQRES  12 B 1181  GLU SER GLY MET LEU PHE GLU GLN GLN LEU ILE GLU ASP          
SEQRES  13 B 1181  GLU SER LEU LEU ARG TYR GLN ALA CYS ALA ASP PHE TRP          
SEQRES  14 B 1181  ARG ARG HIS CYS TYR PRO LEU PRO ARG GLU ILE ALA GLN          
SEQRES  15 B 1181  VAL VAL PHE GLU THR TRP LYS GLY PRO GLN ALA LEU LEU          
SEQRES  16 B 1181  ARG ASP ILE ASN ARG TYR LEU GLN GLY GLU ALA PRO VAL          
SEQRES  17 B 1181  ILE LYS ALA PRO PRO PRO ASP ASP GLU THR LEU ALA SER          
SEQRES  18 B 1181  ARG HIS ALA GLN ILE VAL ALA ARG ILE ASP THR VAL LYS          
SEQRES  19 B 1181  GLN GLN TRP ARG ASP ALA VAL GLY GLU LEU ASP ALA LEU          
SEQRES  20 B 1181  ILE GLU SER SER GLY ILE ASP ARG ARG LYS PHE ASN ARG          
SEQRES  21 B 1181  SER ASN GLN ALA LYS TRP ILE ASP LYS ILE SER ALA TRP          
SEQRES  22 B 1181  ALA GLU GLU GLU THR ASN SER TYR GLN LEU PRO GLU SER          
SEQRES  23 B 1181  LEU GLU LYS PHE SER GLN ARG PHE LEU GLU ASP ARG THR          
SEQRES  24 B 1181  LYS ALA GLY GLY GLU THR PRO ARG HIS PRO LEU PHE GLU          
SEQRES  25 B 1181  ALA ILE ASP GLN LEU LEU ALA GLU PRO LEU SER ILE ARG          
SEQRES  26 B 1181  ASP LEU VAL ILE THR ARG ALA LEU ALA GLU ILE ARG GLU          
SEQRES  27 B 1181  THR VAL ALA ARG GLU LYS ARG ARG ARG GLY GLU LEU GLY          
SEQRES  28 B 1181  PHE ASP ASP MET LEU SER ARG LEU ASP SER ALA LEU ARG          
SEQRES  29 B 1181  SER GLU SER GLY GLU VAL LEU ALA ALA ALA ILE ARG THR          
SEQRES  30 B 1181  ARG PHE PRO VAL ALA MET ILE ASP GLU PHE GLN ASP THR          
SEQRES  31 B 1181  ASP PRO GLN GLN TYR ARG ILE PHE ARG ARG ILE TRP HIS          
SEQRES  32 B 1181  HIS GLN PRO GLU THR ALA LEU LEU LEU ILE GLY ASP PRO          
SEQRES  33 B 1181  LYS GLN ALA ILE TYR ALA PHE ARG GLY ALA ASP ILE PHE          
SEQRES  34 B 1181  THR TYR MET LYS ALA ARG SER GLU VAL HIS ALA HIS TYR          
SEQRES  35 B 1181  THR LEU ASP THR ASN TRP ARG SER ALA PRO GLY MET VAL          
SEQRES  36 B 1181  ASN SER VAL ASN LYS LEU PHE SER GLN THR ASP ASP ALA          
SEQRES  37 B 1181  PHE MET PHE ARG GLU ILE PRO PHE ILE PRO VAL LYS SER          
SEQRES  38 B 1181  ALA GLY LYS ASN GLN ALA LEU ARG PHE VAL PHE LYS GLY          
SEQRES  39 B 1181  GLU THR GLN PRO ALA MET LYS MET TRP LEU MET GLU GLY          
SEQRES  40 B 1181  GLU SER CYS GLY VAL GLY ASP TYR GLN SER THR MET ALA          
SEQRES  41 B 1181  GLN VAL CYS ALA ALA GLN ILE ARG ASP TRP LEU GLN ALA          
SEQRES  42 B 1181  GLY GLN ARG GLY GLU ALA LEU LEU MET ASN GLY ASP ASP          
SEQRES  43 B 1181  ALA ARG PRO VAL ARG ALA SER ASP ILE SER VAL LEU VAL          
SEQRES  44 B 1181  ARG SER ARG GLN GLU ALA ALA GLN VAL ARG ASP ALA LEU          
SEQRES  45 B 1181  THR LEU LEU GLU ILE PRO SER VAL TYR LEU SER ASN ARG          
SEQRES  46 B 1181  ASP SER VAL PHE GLU THR LEU GLU ALA GLN GLU MET LEU          
SEQRES  47 B 1181  TRP LEU LEU GLN ALA VAL MET THR PRO GLU ARG GLU ASN          
SEQRES  48 B 1181  THR LEU ARG SER ALA LEU ALA THR SER MET MET GLY LEU          
SEQRES  49 B 1181  ASN ALA LEU ASP ILE GLU THR LEU ASN ASN ASP GLU HIS          
SEQRES  50 B 1181  ALA TRP ASP VAL VAL VAL GLU GLU PHE ASP GLY TYR ARG          
SEQRES  51 B 1181  GLN ILE TRP ARG LYS ARG GLY VAL MET PRO MET LEU ARG          
SEQRES  52 B 1181  ALA LEU MET SER ALA ARG ASN ILE ALA GLU ASN LEU LEU          
SEQRES  53 B 1181  ALA THR ALA GLY GLY GLU ARG ARG LEU THR ASP ILE LEU          
SEQRES  54 B 1181  HIS ILE SER GLU LEU LEU GLN GLU ALA GLY THR GLN LEU          
SEQRES  55 B 1181  GLU SER GLU HIS ALA LEU VAL ARG TRP LEU SER GLN HIS          
SEQRES  56 B 1181  ILE LEU GLU PRO ASP SER ASN ALA SER SER GLN GLN MET          
SEQRES  57 B 1181  ARG LEU GLU SER ASP LYS HIS LEU VAL GLN ILE VAL THR          
SEQRES  58 B 1181  ILE HIS LYS SER LYS GLY LEU GLU TYR PRO LEU VAL TRP          
SEQRES  59 B 1181  LEU PRO PHE ILE THR ASN PHE ARG VAL GLN GLU GLN ALA          
SEQRES  60 B 1181  PHE TYR HIS ASP ARG HIS SER PHE GLU ALA VAL LEU ASP          
SEQRES  61 B 1181  LEU ASN ALA ALA PRO GLU SER VAL ASP LEU ALA GLU ALA          
SEQRES  62 B 1181  GLU ARG LEU ALA GLU ASP LEU ARG LEU LEU TYR VAL ALA          
SEQRES  63 B 1181  LEU THR ARG SER VAL TRP HIS CYS SER LEU GLY VAL ALA          
SEQRES  64 B 1181  PRO LEU VAL ARG ARG ARG GLY ASP LYS LYS GLY ASP THR          
SEQRES  65 B 1181  ASP VAL HIS GLN SER ALA LEU GLY ARG LEU LEU GLN LYS          
SEQRES  66 B 1181  GLY GLU PRO GLN ASP ALA ALA GLY LEU ARG THR CYS ILE          
SEQRES  67 B 1181  GLU ALA LEU CYS ASP ASP ASP ILE ALA TRP GLN THR ALA          
SEQRES  68 B 1181  GLN THR GLY ASP ASN GLN PRO TRP GLN VAL ASN ASP VAL          
SEQRES  69 B 1181  SER THR ALA GLU LEU ASN ALA LYS THR LEU GLN ARG LEU          
SEQRES  70 B 1181  PRO GLY ASP ASN TRP ARG VAL THR SER TYR SER GLY LEU          
SEQRES  71 B 1181  GLN GLN ARG GLY HIS GLY ILE ALA GLN ASP LEU MET PRO          
SEQRES  72 B 1181  ARG LEU ASP VAL ASP ALA ALA GLY VAL ALA SER VAL VAL          
SEQRES  73 B 1181  GLU GLU PRO THR LEU THR PRO HIS GLN PHE PRO ARG GLY          
SEQRES  74 B 1181  ALA SER PRO GLY THR PHE LEU HIS SER LEU PHE GLU ASP          
SEQRES  75 B 1181  LEU ASP PHE THR GLN PRO VAL ASP PRO ASN TRP VAL ARG          
SEQRES  76 B 1181  GLU LYS LEU GLU LEU GLY GLY PHE GLU SER GLN TRP GLU          
SEQRES  77 B 1181  PRO VAL LEU THR GLU TRP ILE THR ALA VAL LEU GLN ALA          
SEQRES  78 B 1181  PRO LEU ASN GLU THR GLY VAL SER LEU SER GLN LEU SER          
SEQRES  79 B 1181  ALA ARG ASN LYS GLN VAL GLU MET GLU PHE TYR LEU PRO          
SEQRES  80 B 1181  ILE SER GLU PRO LEU ILE ALA SER GLN LEU ASP THR LEU          
SEQRES  81 B 1181  ILE ARG GLN PHE ASP PRO LEU SER ALA GLY CYS PRO PRO          
SEQRES  82 B 1181  LEU GLU PHE MET GLN VAL ARG GLY MET LEU LYS GLY PHE          
SEQRES  83 B 1181  ILE ASP LEU VAL PHE ARG HIS GLU GLY ARG TYR TYR LEU          
SEQRES  84 B 1181  LEU ASP TYR LYS SER ASN TRP LEU GLY GLU ASP SER SER          
SEQRES  85 B 1181  ALA TYR THR GLN GLN ALA MET ALA ALA ALA MET GLN ALA          
SEQRES  86 B 1181  HIS ARG TYR ASP LEU GLN TYR GLN LEU TYR THR LEU ALA          
SEQRES  87 B 1181  LEU HIS ARG TYR LEU ARG HIS ARG ILE ALA ASP TYR ASP          
SEQRES  88 B 1181  TYR GLU HIS HIS PHE GLY GLY VAL ILE TYR LEU PHE LEU          
SEQRES  89 B 1181  ARG GLY VAL ASP LYS GLU HIS PRO GLN GLN GLY ILE TYR          
SEQRES  90 B 1181  THR THR ARG PRO ASN ALA GLY LEU ILE ALA LEU MET ASP          
SEQRES  91 B 1181  GLU MET PHE ALA GLY MET THR LEU GLU GLU ALA                  
SEQRES   1 C 1122  MET LEU ARG VAL TYR HIS SER ASN ARG LEU ASP VAL LEU          
SEQRES   2 C 1122  GLU ALA LEU MET GLU PHE ILE VAL GLU ARG GLU ARG LEU          
SEQRES   3 C 1122  ASP ASP PRO PHE GLU PRO GLU MET ILE LEU VAL GLN SER          
SEQRES   4 C 1122  THR GLY MET ALA GLN TRP LEU GLN MET THR LEU SER GLN          
SEQRES   5 C 1122  LYS PHE GLY ILE ALA ALA ASN ILE ASP PHE PRO LEU PRO          
SEQRES   6 C 1122  ALA SER PHE ILE TRP ASP MET PHE VAL ARG VAL LEU PRO          
SEQRES   7 C 1122  GLU ILE PRO LYS GLU SER ALA PHE ASN LYS GLN SER MET          
SEQRES   8 C 1122  SER TRP LYS LEU MET THR LEU LEU PRO GLN LEU LEU GLU          
SEQRES   9 C 1122  ARG GLU ASP PHE THR LEU LEU ARG HIS TYR LEU THR ASP          
SEQRES  10 C 1122  ASP SER ASP LYS ARG LYS LEU PHE GLN LEU SER SER LYS          
SEQRES  11 C 1122  ALA ALA ASP LEU PHE ASP GLN TYR LEU VAL TYR ARG PRO          
SEQRES  12 C 1122  ASP TRP LEU ALA GLN TRP GLU THR GLY HIS LEU VAL GLU          
SEQRES  13 C 1122  GLY LEU GLY GLU ALA GLN ALA TRP GLN ALA PRO LEU TRP          
SEQRES  14 C 1122  LYS ALA LEU VAL GLU TYR THR HIS GLN LEU GLY GLN PRO          
SEQRES  15 C 1122  ARG TRP HIS ARG ALA ASN LEU TYR GLN ARG PHE ILE GLU          
SEQRES  16 C 1122  THR LEU GLU SER ALA THR THR CYS PRO PRO GLY LEU PRO          
SEQRES  17 C 1122  SER ARG VAL PHE ILE CYS GLY ILE SER ALA LEU PRO PRO          
SEQRES  18 C 1122  VAL TYR LEU GLN ALA LEU GLN ALA LEU GLY LYS HIS ILE          
SEQRES  19 C 1122  GLU ILE HIS LEU LEU PHE THR ASN PRO CYS ARG TYR TYR          
SEQRES  20 C 1122  TRP GLY ASP ILE LYS ASP PRO ALA TYR LEU ALA LYS LEU          
SEQRES  21 C 1122  LEU THR ARG GLN ARG ARG HIS SER PHE GLU ASP ARG GLU          
SEQRES  22 C 1122  LEU PRO LEU PHE ARG ASP SER GLU ASN ALA GLY GLN LEU          
SEQRES  23 C 1122  PHE ASN SER ASP GLY GLU GLN ASP VAL GLY ASN PRO LEU          
SEQRES  24 C 1122  LEU ALA SER TRP GLY LYS LEU GLY ARG ASP TYR ILE TYR          
SEQRES  25 C 1122  LEU LEU SER ASP LEU GLU SER SER GLN GLU LEU ASP ALA          
SEQRES  26 C 1122  PHE VAL ASP VAL THR PRO ASP ASN LEU LEU HIS ASN ILE          
SEQRES  27 C 1122  GLN SER ASP ILE LEU GLU LEU GLU ASN ARG ALA VAL ALA          
SEQRES  28 C 1122  GLY VAL ASN ILE GLU GLU PHE SER ARG SER ASP ASN LYS          
SEQRES  29 C 1122  ARG PRO LEU ASP PRO LEU ASP SER SER ILE THR PHE HIS          
SEQRES  30 C 1122  VAL CYS HIS SER PRO GLN ARG GLU VAL GLU VAL LEU HIS          
SEQRES  31 C 1122  ASP ARG LEU LEU ALA MET LEU GLU GLU ASP PRO THR LEU          
SEQRES  32 C 1122  THR PRO ARG ASP ILE ILE VAL MET VAL ALA ASP ILE ASP          
SEQRES  33 C 1122  SER TYR SER PRO PHE ILE GLN ALA VAL PHE GLY SER ALA          
SEQRES  34 C 1122  PRO ALA ASP ARG TYR LEU PRO TYR ALA ILE SER ASP ARG          
SEQRES  35 C 1122  ARG ALA ARG GLN SER HIS PRO VAL LEU GLU ALA PHE ILE          
SEQRES  36 C 1122  SER LEU LEU SER LEU PRO ASP SER ARG PHE VAL SER GLU          
SEQRES  37 C 1122  ASP VAL LEU ALA LEU LEU ASP VAL PRO VAL LEU ALA ALA          
SEQRES  38 C 1122  ARG PHE ASP ILE THR GLU GLU GLY LEU ARG TYR LEU ARG          
SEQRES  39 C 1122  GLN TRP VAL ASN GLU SER GLY ILE ARG TRP GLY ILE ASP          
SEQRES  40 C 1122  ASP ASP ASN VAL ARG GLU LEU GLU LEU PRO ALA THR GLY          
SEQRES  41 C 1122  GLN HIS THR TRP ARG PHE GLY LEU THR ARG MET LEU LEU          
SEQRES  42 C 1122  GLY TYR ALA MET GLU SER ALA GLN GLY GLU TRP GLN SER          
SEQRES  43 C 1122  VAL LEU PRO TYR ASP GLU SER SER GLY LEU ILE ALA GLU          
SEQRES  44 C 1122  LEU VAL GLY HIS LEU ALA SER LEU LEU MET GLN LEU ASN          
SEQRES  45 C 1122  ILE TRP ARG ARG GLY LEU ALA GLN GLU ARG PRO LEU GLU          
SEQRES  46 C 1122  GLU TRP LEU PRO VAL CYS ARG ASP MET LEU ASN ALA PHE          
SEQRES  47 C 1122  PHE LEU PRO ASP ALA GLU THR GLU ALA ALA MET THR LEU          
SEQRES  48 C 1122  ILE GLU GLN GLN TRP GLN ALA ILE ILE ALA GLU GLY LEU          
SEQRES  49 C 1122  GLY ALA GLN TYR GLY ASP ALA VAL PRO LEU SER LEU LEU          
SEQRES  50 C 1122  ARG ASP GLU LEU ALA GLN ARG LEU ASP GLN GLU ARG ILE          
SEQRES  51 C 1122  SER GLN ARG PHE LEU ALA GLY PRO VAL ASN ILE CYS THR          
SEQRES  52 C 1122  LEU MET PRO MET ARG SER ILE PRO PHE LYS VAL VAL CYS          
SEQRES  53 C 1122  LEU LEU GLY MET ASN ASP GLY VAL TYR PRO ARG GLN LEU          
SEQRES  54 C 1122  ALA PRO LEU GLY PHE ASP LEU MET SER GLN LYS PRO LYS          
SEQRES  55 C 1122  ARG GLY ASP ARG SER ARG ARG ASP ASP ASP ARG TYR LEU          
SEQRES  56 C 1122  PHE LEU GLU ALA LEU ILE SER ALA GLN GLN LYS LEU TYR          
SEQRES  57 C 1122  ILE SER TYR ILE GLY ARG SER ILE GLN ASP ASN SER GLU          
SEQRES  58 C 1122  ARG PHE PRO SER VAL LEU VAL GLN GLU LEU ILE ASP TYR          
SEQRES  59 C 1122  ILE GLY GLN SER HIS TYR LEU PRO GLY ASP GLU ALA LEU          
SEQRES  60 C 1122  ASN CYS ASP GLU SER GLU ALA ARG VAL LYS ALA HIS LEU          
SEQRES  61 C 1122  THR CYS LEU HIS THR ARG MET PRO PHE ASP PRO GLN ASN          
SEQRES  62 C 1122  TYR GLN PRO GLY GLU ARG GLN SER TYR ALA ARG GLU TRP          
SEQRES  63 C 1122  LEU PRO ALA ALA SER GLN ALA GLY LYS ALA HIS SER GLU          
SEQRES  64 C 1122  PHE VAL GLN PRO LEU PRO PHE THR LEU PRO GLU THR VAL          
SEQRES  65 C 1122  PRO LEU GLU THR LEU GLN ARG PHE TRP ALA HIS PRO VAL          
SEQRES  66 C 1122  ARG ALA PHE PHE GLN MET ARG LEU GLN VAL ASN PHE ARG          
SEQRES  67 C 1122  THR GLU ASP SER GLU ILE PRO ASP THR GLU PRO PHE ILE          
SEQRES  68 C 1122  LEU GLU GLY LEU SER ARG TYR GLN ILE ASN GLN GLN LEU          
SEQRES  69 C 1122  LEU ASN ALA LEU VAL GLU GLN ASP ASP ALA GLU ARG LEU          
SEQRES  70 C 1122  PHE ARG ARG PHE ARG ALA ALA GLY ASP LEU PRO TYR GLY          
SEQRES  71 C 1122  ALA PHE GLY GLU ILE PHE TRP GLU THR GLN CYS GLN GLU          
SEQRES  72 C 1122  MET GLN GLN LEU ALA ASP ARG VAL ILE ALA CYS ARG GLN          
SEQRES  73 C 1122  PRO GLY GLN SER MET GLU ILE ASP LEU ALA CYS ASN GLY          
SEQRES  74 C 1122  VAL GLN ILE THR GLY TRP LEU PRO GLN VAL GLN PRO ASP          
SEQRES  75 C 1122  GLY LEU LEU ARG TRP ARG PRO SER LEU LEU SER VAL ALA          
SEQRES  76 C 1122  GLN GLY MET GLN LEU TRP LEU GLU HIS LEU VAL TYR CYS          
SEQRES  77 C 1122  ALA SER GLY GLY ASN GLY GLU SER ARG LEU PHE LEU ARG          
SEQRES  78 C 1122  LYS ASP GLY GLU TRP ARG PHE PRO PRO LEU ALA ALA GLU          
SEQRES  79 C 1122  GLN ALA LEU HIS TYR LEU SER GLN LEU ILE GLU GLY TYR          
SEQRES  80 C 1122  ARG GLU GLY MET SER ALA PRO LEU LEU VAL LEU PRO GLU          
SEQRES  81 C 1122  SER GLY GLY ALA TRP LEU LYS THR CYS TYR ASP ALA GLN          
SEQRES  82 C 1122  ASN ASP ALA MET LEU ASP ASP ASP SER THR LEU GLN LYS          
SEQRES  83 C 1122  ALA ARG THR LYS PHE LEU GLN ALA TYR GLU GLY ASN MET          
SEQRES  84 C 1122  MET VAL ARG GLY GLU GLY ASP ASP ILE TRP TYR GLN ARG          
SEQRES  85 C 1122  LEU TRP ARG GLN LEU THR PRO GLU THR MET GLU ALA ILE          
SEQRES  86 C 1122  VAL GLU GLN SER GLN ARG PHE LEU LEU PRO LEU PHE ARG          
SEQRES  87 C 1122  PHE ASN GLN SER                                              
SEQRES   1 D  609  MET GLY LYS LEU GLN LYS GLN LEU LEU GLU ALA VAL GLU          
SEQRES   2 D  609  HIS LYS GLN LEU ARG PRO LEU ASP VAL GLN PHE ALA LEU          
SEQRES   3 D  609  THR VAL ALA GLY ASP GLU HIS PRO ALA VAL THR LEU ALA          
SEQRES   4 D  609  ALA ALA LEU LEU SER HIS ASP ALA GLY GLU GLY HIS VAL          
SEQRES   5 D  609  CYS LEU PRO LEU SER ARG LEU GLU ASN ASN GLU ALA SER          
SEQRES   6 D  609  HIS PRO LEU LEU ALA THR CYS VAL SER GLU ILE GLY GLU          
SEQRES   7 D  609  LEU GLN ASN TRP GLU GLU CYS LEU LEU ALA SER GLN ALA          
SEQRES   8 D  609  VAL SER ARG GLY ASP GLU PRO THR PRO MET ILE LEU CYS          
SEQRES   9 D  609  GLY ASP ARG LEU TYR LEU ASN ARG MET TRP CYS ASN GLU          
SEQRES  10 D  609  ARG THR VAL ALA ARG PHE PHE ASN GLU VAL ASN HIS ALA          
SEQRES  11 D  609  ILE GLU VAL ASP GLU ALA LEU LEU ALA GLN THR LEU ASP          
SEQRES  12 D  609  LYS LEU PHE PRO VAL SER ASP GLU ILE ASN TRP GLN LYS          
SEQRES  13 D  609  VAL ALA ALA ALA VAL ALA LEU THR ARG ARG ILE SER VAL          
SEQRES  14 D  609  ILE SER GLY GLY PRO GLY THR GLY LYS THR THR THR VAL          
SEQRES  15 D  609  ALA LYS LEU LEU ALA ALA LEU ILE GLN MET ALA ASP GLY          
SEQRES  16 D  609  GLU ARG CYS ARG ILE ARG LEU ALA ALA PRO THR GLY LYS          
SEQRES  17 D  609  ALA ALA ALA ARG LEU THR GLU SER LEU GLY LYS ALA LEU          
SEQRES  18 D  609  ARG GLN LEU PRO LEU THR ASP GLU GLN LYS LYS ARG ILE          
SEQRES  19 D  609  PRO GLU ASP ALA SER THR LEU HIS ARG LEU LEU GLY ALA          
SEQRES  20 D  609  GLN PRO GLY SER GLN ARG LEU ARG HIS HIS ALA GLY ASN          
SEQRES  21 D  609  PRO LEU HIS LEU ASP VAL LEU VAL VAL ASP GLU ALA SER          
SEQRES  22 D  609  MET ILE ASP LEU PRO MET MET SER ARG LEU ILE ASP ALA          
SEQRES  23 D  609  LEU PRO ASP HIS ALA ARG VAL ILE PHE LEU GLY ASP ARG          
SEQRES  24 D  609  ASP GLN LEU ALA SER VAL GLU ALA GLY ALA VAL LEU GLY          
SEQRES  25 D  609  ASP ILE CYS ALA TYR ALA ASN ALA GLY PHE THR ALA GLU          
SEQRES  26 D  609  ARG ALA ARG GLN LEU SER ARG LEU THR GLY THR HIS VAL          
SEQRES  27 D  609  PRO ALA GLY THR GLY THR GLU ALA ALA SER LEU ARG ASP          
SEQRES  28 D  609  SER LEU CYS LEU LEU GLN LYS SER TYR ARG PHE GLY SER          
SEQRES  29 D  609  ASP SER GLY ILE GLY GLN LEU ALA ALA ALA ILE ASN ARG          
SEQRES  30 D  609  GLY ASP LYS THR ALA VAL LYS THR VAL PHE GLN GLN ASP          
SEQRES  31 D  609  PHE THR ASP ILE GLU LYS ARG LEU LEU GLN SER GLY GLU          
SEQRES  32 D  609  ASP TYR ILE ALA MET LEU GLU GLU ALA LEU ALA GLY TYR          
SEQRES  33 D  609  GLY ARG TYR LEU ASP LEU LEU GLN ALA ARG ALA GLU PRO          
SEQRES  34 D  609  ASP LEU ILE ILE GLN ALA PHE ASN GLU TYR GLN LEU LEU          
SEQRES  35 D  609  CYS ALA LEU ARG GLU GLY PRO PHE GLY VAL ALA GLY LEU          
SEQRES  36 D  609  ASN GLU ARG ILE GLU GLN PHE MET GLN GLN LYS ARG LYS          
SEQRES  37 D  609  ILE HIS ARG HIS PRO HIS SER ARG TRP TYR GLU GLY ARG          
SEQRES  38 D  609  PRO VAL MET ILE ALA ARG ASN ASP SER ALA LEU GLY LEU          
SEQRES  39 D  609  PHE ASN GLY ASP ILE GLY ILE ALA LEU ASP ARG GLY GLN          
SEQRES  40 D  609  GLY THR ARG VAL TRP PHE ALA MET PRO ASP GLY ASN ILE          
SEQRES  41 D  609  LYS SER VAL GLN PRO SER ARG LEU PRO GLU HIS GLU THR          
SEQRES  42 D  609  THR TRP ALA MET THR VAL HIS LYS SER GLN GLY SER GLU          
SEQRES  43 D  609  PHE ASP HIS ALA ALA LEU ILE LEU PRO SER GLN ARG THR          
SEQRES  44 D  609  PRO VAL VAL THR ARG GLU LEU VAL TYR THR ALA VAL THR          
SEQRES  45 D  609  ARG ALA ARG ARG ARG LEU SER LEU TYR ALA ASP GLU ARG          
SEQRES  46 D  609  ILE LEU SER ALA ALA ILE ALA THR ARG THR GLU ARG ARG          
SEQRES  47 D  609  SER GLY LEU ALA ALA LEU PHE SER SER ARG GLU                  
SEQRES   1 A   98  MET ASN ALA TYR TYR ILE GLN ASP ARG LEU GLU ALA GLN          
SEQRES   2 A   98  SER TRP ALA ARG HIS TYR GLN GLN LEU ALA ARG GLU GLU          
SEQRES   3 A   98  LYS GLU ALA GLU LEU ALA ASP ASP MET GLU LYS GLY ILE          
SEQRES   4 A   98  PRO GLN HIS LEU PHE GLU SER LEU CYS ILE ASP HIS LEU          
SEQRES   5 A   98  GLN ARG HIS GLY ALA SER LYS LYS SER ILE THR ARG ALA          
SEQRES   6 A   98  PHE ASP ASP ASP VAL GLU PHE GLN GLU ARG MET ALA GLU          
SEQRES   7 A   98  HIS ILE ARG TYR MET VAL GLU THR ILE ALA HIS HIS GLN          
SEQRES   8 A   98  VAL ASP ILE ASP SER GLU VAL                                  
SEQRES   1 E   98  MET ASN ALA TYR TYR ILE GLN ASP ARG LEU GLU ALA GLN          
SEQRES   2 E   98  SER TRP ALA ARG HIS TYR GLN GLN LEU ALA ARG GLU GLU          
SEQRES   3 E   98  LYS GLU ALA GLU LEU ALA ASP ASP MET GLU LYS GLY ILE          
SEQRES   4 E   98  PRO GLN HIS LEU PHE GLU SER LEU CYS ILE ASP HIS LEU          
SEQRES   5 E   98  GLN ARG HIS GLY ALA SER LYS LYS SER ILE THR ARG ALA          
SEQRES   6 E   98  PHE ASP ASP ASP VAL GLU PHE GLN GLU ARG MET ALA GLU          
SEQRES   7 E   98  HIS ILE ARG TYR MET VAL GLU THR ILE ALA HIS HIS GLN          
SEQRES   8 E   98  VAL ASP ILE ASP SER GLU VAL                                  
HELIX    1 AA1 GLY B   28  GLY B   43  1                                  16    
HELIX    2 AA2 GLY B   45  ALA B   49  5                                   5    
HELIX    3 AA3 THR B   55  GLU B   58  5                                   4    
HELIX    4 AA4 THR B   65  GLU B   90  1                                  26    
HELIX    5 AA5 ASN B   94  ILE B  104  1                                  11    
HELIX    6 AA6 ASP B  106  GLN B  120  1                                  15    
HELIX    7 AA7 THR B  128  ASN B  138  1                                  11    
HELIX    8 AA8 ASN B  140  GLY B  145  1                                   6    
HELIX    9 AA9 GLU B  156  HIS B  171  1                                  16    
HELIX   10 AB1 PRO B  176  TRP B  187  1                                  12    
HELIX   11 AB2 GLY B  189  GLN B  202  1                                  14    
HELIX   12 AB3 THR B  217  VAL B  240  1                                  24    
HELIX   13 AB4 ARG B  254  ASP B  267  1                                  14    
HELIX   14 AB5 THR B  277  TYR B  280  5                                   4    
HELIX   15 AB6 GLN B  281  PHE B  289  1                                   9    
HELIX   16 AB7 HIS B  307  GLU B  319  1                                  13    
HELIX   17 AB8 ILE B  323  GLY B  347  1                                  25    
HELIX   18 AB9 GLY B  350  SER B  364  1                                  15    
HELIX   19 AC1 SER B  366  PHE B  378  1                                  13    
HELIX   20 AC2 ASP B  390  HIS B  402  1                                  13    
HELIX   21 AC3 ASP B  414  ALA B  418  5                                   5    
HELIX   22 AC4 ILE B  419  GLY B  424  5                                   6    
HELIX   23 AC5 ASP B  426  VAL B  437  1                                  12    
HELIX   24 AC6 ALA B  450  SER B  462  1                                  13    
HELIX   25 AC7 GLY B  510  GLN B  534  1                                  25    
HELIX   26 AC8 SER B  560  LEU B  574  1                                  15    
HELIX   27 AC9 SER B  586  GLU B  589  5                                   4    
HELIX   28 AD1 THR B  590  THR B  605  1                                  16    
HELIX   29 AD2 ARG B  608  ALA B  617  1                                  10    
HELIX   30 AD3 ASN B  624  ASP B  634  1                                  11    
HELIX   31 AD4 ASP B  634  ARG B  655  1                                  22    
HELIX   32 AD5 GLY B  656  ASN B  669  1                                  14    
HELIX   33 AD6 ASN B  669  THR B  677  1                                   9    
HELIX   34 AD7 GLY B  679  LEU B  701  1                                  23    
HELIX   35 AD8 SER B  703  GLU B  717  1                                  15    
HELIX   36 AD9 ASN B  721  GLN B  725  5                                   5    
HELIX   37 AE1 SER B  731  LEU B  735  5                                   5    
HELIX   38 AE2 ALA B  783  ARG B  808  1                                  26    
HELIX   39 AE3 ARG B  823  LYS B  827  5                                   5    
HELIX   40 AE4 THR B  831  GLN B  835  5                                   5    
HELIX   41 AE5 SER B  836  GLN B  843  1                                   8    
HELIX   42 AE6 ASP B  849  LEU B  860  1                                  12    
HELIX   43 AE7 TYR B  906  GLN B  911  1                                   6    
HELIX   44 AE8 THR B  941  PHE B  945  5                                   5    
HELIX   45 AE9 GLY B  948  LEU B  962  1                                  15    
HELIX   46 AF1 ASP B  969  GLY B  981  1                                  13    
HELIX   47 AF2 TRP B  986  GLN B  999  1                                  14    
HELIX   48 AF3 SER B 1008  LEU B 1012  5                                   5    
HELIX   49 AF4 SER B 1013  ARG B 1015  5                                   3    
HELIX   50 AF5 ILE B 1032  ASP B 1044  1                                  13    
HELIX   51 AF6 PRO B 1045  ALA B 1048  5                                   4    
HELIX   52 AF7 THR B 1094  HIS B 1105  1                                  12    
HELIX   53 AF8 ARG B 1106  ILE B 1126  1                                  21    
HELIX   54 AF9 ASP B 1130  HIS B 1134  1                                   5    
HELIX   55 AG1 GLY B 1163  GLY B 1174  1                                  12    
HELIX   56 AG2 ARG C    9  GLU C   24  1                                  16    
HELIX   57 AG3 SER C   39  GLY C   55  1                                  17    
HELIX   58 AG4 LEU C   64  LEU C   77  1                                  14    
HELIX   59 AG5 GLN C   89  LEU C  102  1                                  14    
HELIX   60 AG6 PHE C  108  THR C  116  1                                   9    
HELIX   61 AG7 LYS C  121  ARG C  142  1                                  22    
HELIX   62 AG8 ARG C  142  GLY C  152  1                                  11    
HELIX   63 AG9 ALA C  161  LEU C  179  1                                  19    
HELIX   64 AH1 HIS C  185  SER C  199  1                                  15    
HELIX   65 AH2 PRO C  220  GLY C  231  1                                  12    
HELIX   66 AH3 ALA C  255  THR C  262  5                                   8    
HELIX   67 AH4 ARG C  278  ALA C  283  1                                   6    
HELIX   68 AH5 ASN C  297  GLY C  304  1                                   8    
HELIX   69 AH6 GLY C  304  SER C  315  1                                  12    
HELIX   70 AH7 ASN C  333  LEU C  345  1                                  13    
HELIX   71 AH8 ASN C  354  ARG C  360  1                                   7    
HELIX   72 AH9 SER C  381  ASP C  400  1                                  20    
HELIX   73 AI1 THR C  404  ARG C  406  5                                   3    
HELIX   74 AI2 ASP C  414  SER C  428  1                                  15    
HELIX   75 AI3 SER C  447  LEU C  458  1                                  12    
HELIX   76 AI4 SER C  459  SER C  463  5                                   5    
HELIX   77 AI5 VAL C  466  LEU C  474  1                                   9    
HELIX   78 AI6 VAL C  476  PHE C  483  1                                   8    
HELIX   79 AI7 THR C  486  SER C  500  1                                  15    
HELIX   80 AI8 ASP C  507  LEU C  514  1                                   8    
HELIX   81 AI9 THR C  523  MET C  537  1                                  15    
HELIX   82 AJ1 GLY C  555  ILE C  557  5                                   3    
HELIX   83 AJ2 ALA C  558  LEU C  578  1                                  21    
HELIX   84 AJ3 PRO C  583  GLU C  586  5                                   4    
HELIX   85 AJ4 TRP C  587  PHE C  599  1                                  13    
HELIX   86 AJ5 GLU C  604  ALA C  626  1                                  23    
HELIX   87 AJ6 PRO C  633  GLN C  647  1                                  15    
HELIX   88 AJ7 SER C  707  SER C  722  1                                  16    
HELIX   89 AJ8 SER C  745  SER C  758  1                                  14    
HELIX   90 AJ9 ASN C  768  LEU C  780  1                                  13    
HELIX   91 AK1 ASP C  790  GLN C  795  5                                   6    
HELIX   92 AK2 TRP C  806  GLN C  812  1                                   7    
HELIX   93 AK3 LEU C  834  HIS C  843  1                                  10    
HELIX   94 AK4 HIS C  843  MET C  851  1                                   9    
HELIX   95 AK5 GLY C  874  GLU C  890  1                                  17    
HELIX   96 AK6 ASP C  893  ALA C  904  1                                  12    
HELIX   97 AK7 GLY C  910  ARG C  935  1                                  26    
HELIX   98 AK8 SER C  973  SER C  990  1                                  18    
HELIX   99 AK9 ALA C 1012  ALA C 1033  1                                  22    
HELIX  100 AL1 GLU C 1040  CYS C 1049  1                                  10    
HELIX  101 AL2 ASP C 1060  GLU C 1076  1                                  17    
HELIX  102 AL3 ASP C 1087  TRP C 1094  1                                   8    
HELIX  103 AL4 THR C 1098  LEU C 1113  1                                  16    
HELIX  104 AL5 LEU C 1113  ASN C 1120  1                                   8    
HELIX  105 AL6 LEU D    3  HIS D   13  1                                  11    
HELIX  106 AL7 ARG D   17  GLY D   29  1                                  13    
HELIX  107 AL8 HIS D   32  GLY D   49  1                                  18    
HELIX  108 AL9 LEU D   55  ASN D   60  1                                   6    
HELIX  109 AM1 HIS D   65  CYS D   71  5                                   7    
HELIX  110 AM2 ASN D   80  SER D   88  1                                   9    
HELIX  111 AM3 ASN D  110  GLU D  125  1                                  16    
HELIX  112 AM4 ASP D  133  PHE D  145  1                                  13    
HELIX  113 AM5 ASN D  152  ARG D  164  1                                  13    
HELIX  114 AM6 GLY D  176  ALA D  192  1                                  17    
HELIX  115 AM7 THR D  205  ARG D  221  1                                  17    
HELIX  116 AM8 THR D  226  ARG D  232  1                                   7    
HELIX  117 AM9 LEU D  240  GLY D  245  1                                   6    
HELIX  118 AN1 GLU D  270  ILE D  274  5                                   5    
HELIX  119 AN2 ASP D  275  ASP D  284  1                                  10    
HELIX  120 AN3 GLN D  300  GLU D  305  1                                   6    
HELIX  121 AN4 VAL D  309  CYS D  314  1                                   6    
HELIX  122 AN5 ALA D  315  ALA D  319  5                                   5    
HELIX  123 AN6 THR D  322  GLY D  334  1                                  13    
HELIX  124 AN7 ALA D  345  SER D  351  1                                   7    
HELIX  125 AN8 ILE D  367  ASN D  375  1                                   9    
HELIX  126 AN9 GLY D  377  GLN D  387  1                                  11    
HELIX  127 AO1 SER D  400  TYR D  415  1                                  16    
HELIX  128 AO2 TYR D  415  ALA D  424  1                                  10    
HELIX  129 AO3 GLU D  427  ASN D  436  1                                  10    
HELIX  130 AO4 GLY D  450  LYS D  465  1                                  16    
HELIX  131 AO5 GLN D  523  LEU D  527  5                                   5    
HELIX  132 AO6 THR D  562  THR D  571  1                                  10    
HELIX  133 AO7 ASP D  582  THR D  592  1                                  11    
HELIX  134 AO8 GLY D  599  SER D  605  1                                   7    
HELIX  135 AO9 TYR A   44  LYS A   77  1                                  34    
HELIX  136 AP1 PRO A   80  LEU A   92  1                                  13    
HELIX  137 AP2 GLN A   93  GLY A   96  5                                   4    
HELIX  138 AP3 SER A   98  ASP A  107  1                                  10    
HELIX  139 AP4 ASP A  109  GLU A  137  1                                  29    
HELIX  140 AP5 LEU E   62  ILE E   79  1                                  18    
HELIX  141 AP6 PRO E   80  GLN E   93  1                                  14    
HELIX  142 AP7 SER E   98  ASP E  107  1                                  10    
HELIX  143 AP8 ASP E  109  ASP E  135  1                                  27    
SHEET    1 AA1 7 GLU B   6  THR B   7  0                                        
SHEET    2 AA1 7 TYR B 441  LEU B 443  1  O  THR B 442   N  GLU B   6           
SHEET    3 AA1 7 GLY B  17  ALA B  23  1  N  GLU B  22   O  TYR B 441           
SHEET    4 AA1 7 ALA B 408  ILE B 412  1  O  LEU B 411   N  ILE B  21           
SHEET    5 AA1 7 MET B 382  ILE B 383  1  N  ILE B 383   O  LEU B 410           
SHEET    6 AA1 7 LEU B  60  VAL B  62  1  N  VAL B  62   O  MET B 382           
SHEET    7 AA1 7 ALA B 125  PHE B 127  1  O  PHE B 127   N  VAL B  61           
SHEET    1 AA2 3 VAL B 207  ILE B 208  0                                        
SHEET    2 AA2 3 ALA B 776  LEU B 778  1  O  ALA B 776   N  VAL B 207           
SHEET    3 AA2 3 PHE B 767  HIS B 769 -1  N  TYR B 768   O  VAL B 777           
SHEET    1 AA3 2 THR B 445  ASN B 446  0                                        
SHEET    2 AA3 2 LYS B 479  SER B 480  1  O  LYS B 479   N  ASN B 446           
SHEET    1 AA4 2 LEU B 487  VAL B 490  0                                        
SHEET    2 AA4 2 LEU B 539  ASN B 542 -1  O  MET B 541   N  ARG B 488           
SHEET    1 AA5 7 SER B 578  TYR B 580  0                                        
SHEET    2 AA5 7 VAL B 736  THR B 740  1  O  ILE B 738   N  VAL B 579           
SHEET    3 AA5 7 ILE B 554  VAL B 558  1  N  VAL B 556   O  GLN B 737           
SHEET    4 AA5 7 TYR B 749  LEU B 754  1  O  TRP B 753   N  LEU B 557           
SHEET    5 AA5 7 SER B 809  VAL B 817  1  O  SER B 814   N  LEU B 754           
SHEET    6 AA5 7 MET B 499  MET B 504  1  N  TRP B 502   O  VAL B 817           
SHEET    7 AA5 7 ILE B 865  ALA B 870  1  O  ALA B 870   N  LEU B 503           
SHEET    1 AA6 3 THR B 904  SER B 905  0                                        
SHEET    2 AA6 3 VAL B1058  HIS B1072  1  O  MET B1061   N  THR B 904           
SHEET    3 AA6 3 LYS B1017  LEU B1031 -1  N  ILE B1027   O  GLY B1060           
SHEET    1 AA7 5 THR B 904  SER B 905  0                                        
SHEET    2 AA7 5 VAL B1058  HIS B1072  1  O  MET B1061   N  THR B 904           
SHEET    3 AA7 5 ARG B1075  LYS B1082 -1  O  ARG B1075   N  HIS B1072           
SHEET    4 AA7 5 PHE B1135  PHE B1142  1  O  LEU B1141   N  ASP B1080           
SHEET    5 AA7 5 ILE B1155  THR B1158 -1  O  TYR B1156   N  TYR B1140           
SHEET    1 AA8 7 ILE C  60  ASP C  61  0                                        
SHEET    2 AA8 7 GLU C  33  LEU C  36  1  N  ILE C  35   O  ASP C  61           
SHEET    3 AA8 7 ARG C 210  CYS C 214  1  O  PHE C 212   N  LEU C  36           
SHEET    4 AA8 7 GLU C 235  THR C 241  1  O  LEU C 239   N  ILE C 213           
SHEET    5 AA8 7 ARG C   3  SER C   7  1  N  ARG C   3   O  ILE C 236           
SHEET    6 AA8 7 GLN C 321  ALA C 325  1  O  ALA C 325   N  HIS C   6           
SHEET    7 AA8 7 ARG C 265  ARG C 266  1  N  ARG C 265   O  ASP C 324           
SHEET    1 AA9 2 ARG C 365  PRO C 366  0                                        
SHEET    2 AA9 2 HIS C 759  TYR C 760  1  O  TYR C 760   N  ARG C 365           
SHEET    1 AB1 7 TYR C 437  ILE C 439  0                                        
SHEET    2 AB1 7 VAL C 659  THR C 663  1  O  VAL C 659   N  ALA C 438           
SHEET    3 AB1 7 ILE C 408  VAL C 412  1  N  VAL C 410   O  ASN C 660           
SHEET    4 AB1 7 PHE C 672  LEU C 678  1  O  CYS C 676   N  MET C 411           
SHEET    5 AB1 7 ALA C 723  ILE C 732  1  O  TYR C 728   N  VAL C 675           
SHEET    6 AB1 7 ILE C 374  CYS C 379  1  N  HIS C 377   O  TYR C 731           
SHEET    7 AB1 7 THR C 781  LEU C 783  1  O  CYS C 782   N  VAL C 378           
SHEET    1 AB2 3 THR C 831  PRO C 833  0                                        
SHEET    2 AB2 3 VAL C 950  GLN C 960  1  O  GLN C 951   N  VAL C 832           
SHEET    3 AB2 3 GLN C 939  CYS C 947 -1  N  MET C 941   O  LEU C 956           
SHEET    1 AB3 5 THR C 831  PRO C 833  0                                        
SHEET    2 AB3 5 VAL C 950  GLN C 960  1  O  GLN C 951   N  VAL C 832           
SHEET    3 AB3 5 GLY C 963  TRP C 967 -1  O  GLY C 963   N  GLN C 960           
SHEET    4 AB3 5 GLU C 995  PHE C 999  1  O  ARG C 997   N  LEU C 964           
SHEET    5 AB3 5 GLU C1005  PHE C1008 -1  O  PHE C1008   N  SER C 996           
SHEET    1 AB4 2 TYR C1050  ASP C1051  0                                        
SHEET    2 AB4 2 ALA C1056  MET C1057 -1  O  ALA C1056   N  ASP C1051           
SHEET    1 AB5 4 LEU D  53  PRO D  54  0                                        
SHEET    2 AB5 4 ARG D 106  LEU D 109 -1  O  LEU D 107   N  LEU D  53           
SHEET    3 AB5 4 MET D 100  LEU D 102 -1  N  ILE D 101   O  TYR D 108           
SHEET    4 AB5 4 VAL D  91  SER D  92  1  N  SER D  92   O  LEU D 102           
SHEET    1 AB6 6 ALA D 237  THR D 239  0                                        
SHEET    2 AB6 6 ILE D 199  ALA D 203  1  N  LEU D 201   O  SER D 238           
SHEET    3 AB6 6 VAL D 265  VAL D 268  1  O  VAL D 267   N  ARG D 200           
SHEET    4 AB6 6 ARG D 291  GLY D 296  1  O  ILE D 293   N  VAL D 268           
SHEET    5 AB6 6 ILE D 166  GLY D 171  1  N  ILE D 169   O  PHE D 294           
SHEET    6 AB6 6 LEU D 352  LEU D 355  1  O  CYS D 353   N  SER D 170           
SHEET    1 AB7 5 LYS D 395  ARG D 396  0                                        
SHEET    2 AB7 5 SER D 578  TYR D 580  1  O  LEU D 579   N  ARG D 396           
SHEET    3 AB7 5 HIS D 548  ILE D 552  1  N  ALA D 549   O  SER D 578           
SHEET    4 AB7 5 TYR D 438  CYS D 442  1  N  LEU D 441   O  ILE D 552           
SHEET    5 AB7 5 MET D 536  THR D 537  1  O  MET D 536   N  LEU D 440           
SHEET    1 AB8 5 ILE D 519  VAL D 522  0                                        
SHEET    2 AB8 5 THR D 508  ALA D 513 -1  N  VAL D 510   O  VAL D 522           
SHEET    3 AB8 5 ILE D 498  ASP D 503 -1  N  ILE D 500   O  TRP D 511           
SHEET    4 AB8 5 ARG D 480  MET D 483 -1  N  VAL D 482   O  GLY D 499           
SHEET    5 AB8 5 GLU D 531  THR D 532 -1  O  GLU D 531   N  MET D 483           
CISPEP   1 TYR C  685    PRO C  686          0        -3.33                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004146  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004146  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004146        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system