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Database: PDB
Entry: 3J5Y
LinkDB: 3J5Y
Original site: 3J5Y 
HEADER    TRANSLATION/RNA                         21-NOV-13   3J5Y              
TITLE     STRUCTURE OF THE MAMMALIAN RIBOSOMAL PRE-TERMINATION COMPLEX          
TITLE    2 ASSOCIATED WITH ERF1-ERF3-GDPNP                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1;         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 7-420;                                        
COMPND   5 SYNONYM: EUKARYOTIC RELEASE FACTOR 1, ERF1, PROTEIN CL1, TB3-1;      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR GTP-BINDING SUBUNIT
COMPND   9 ERF3A;                                                               
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 69-496;                                       
COMPND  12 SYNONYM: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 3A, ERF3A,  
COMPND  13 G1 TO S PHASE TRANSITION PROTEIN 1 HOMOLOG;                          
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: 5'-R(*AP*UP*UP*GP*UP*AP*AP*AP*AP*A)-3';                    
COMPND  17 CHAIN: C;                                                            
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: MESSENGER RNA;                                        
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: TRNA-LEU;                                                  
COMPND  22 CHAIN: D                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ETF1, ERF1, RF1, SUP45L1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: GSPT1, ERF3A;                                                  
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE  25 ORGANISM_COMMON: RABBIT;                                             
SOURCE  26 ORGANISM_TAXID: 9986                                                 
KEYWDS    TRANSLATION TERMINATION, ERF1, ERF3, TRNALEU, RIBOSOME, MAMMALIAN,    
KEYWDS   2 TRANSLATION-RNA COMPLEX                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.DES GEORGES,Y.HASHEM,A.UNBEHAUN,R.A.GRASSUCCI,D.TAYLOR,             
AUTHOR   2 C.U.T.HELLEN,T.V.PESTOVA,J.FRANK                                     
REVDAT   3   18-JUL-18 3J5Y    1       REMARK                                   
REVDAT   2   26-MAR-14 3J5Y    1       JRNL                                     
REVDAT   1   25-DEC-13 3J5Y    0                                                
SPRSDE     25-DEC-13 3J5Y      3J2K                                             
JRNL        AUTH   A.DES GEORGES,Y.HASHEM,A.UNBEHAUN,R.A.GRASSUCCI,D.TAYLOR,    
JRNL        AUTH 2 C.U.HELLEN,T.V.PESTOVA,J.FRANK                               
JRNL        TITL   STRUCTURE OF THE MAMMALIAN RIBOSOMAL PRE-TERMINATION COMPLEX 
JRNL        TITL 2 ASSOCIATED WITH ERF1*ERF3*GDPNP.                             
JRNL        REF    NUCLEIC ACIDS RES.            V.  42  3409 2014              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   24335085                                                     
JRNL        DOI    10.1093/NAR/GKT1279                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    9.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSF CHIMERA, RELION                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3E1Y                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS CORRELATION                   
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : REFINEMENT PROTOCOL--RIGID BODY DETAILS-         
REMARK   3  -DOMAINS WERE FITTED AS RIGID BODIES USING CHIMERA. INDIVIDUAL      
REMARK   3  DOMAINS WERE THEN REFINED MANUALLY USING HINGE POINTS AS POINTS     
REMARK   3  OF FLEXIBILITY.                                                     
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)  : 9.700                          
REMARK   3   NUMBER OF PARTICLES               : 48973                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: (SINGLE PARTICLE DETAILS: IMAGES WERE CLASSIFIED      
REMARK   3  AND REFINED WITH RELION) (SINGLE PARTICLE--APPLIED SYMMETRY: C1)    
REMARK   4                                                                      
REMARK   4 3J5Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000160292.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : ERF1-ERF3-GDPNP-BOUND MAMMALIAN   
REMARK 245                                    RIBOSOMAL PRE-TERMINATION         
REMARK 245                                    COMPLEX; 80S RIBOSOME;            
REMARK 245                                    EUKARYOTIC RELEASE FACTOR 1;      
REMARK 245                                    EUKARYOTIC RELEASE FACTOR 3;      
REMARK 245                                    TRANSFER-MESSENGER RNA LEU;       
REMARK 245                                    MESSENGER RNA                     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : QUANTIFOIL GRIDS, GLOW            
REMARK 245                                    DISCHARGED                        
REMARK 245   SAMPLE VITRIFICATION DETAILS   : PLUNGED INTO LIQUID ETHANE (FEI   
REMARK 245                                    VITROBOT MARK IV)                 
REMARK 245   SAMPLE BUFFER                  : 20 MM TRIS, 100 MM KOAC, 2.5 MM   
REMARK 245                                    MGCL2, 2 MM DTT, 0.25 MM          
REMARK 245                                    SPERMIDINE SUPPLEMENTED WITH      
REMARK 245                                    200 UNITS RNASIN, 0.4 MM ATP, 3   
REMARK 245                                    MM MG-GMPPNP                      
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 01-JAN-10                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 81.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI POLARA 300                 
REMARK 245   DETECTOR TYPE                     : TVIPS TEMCAM-F415 (4K X 4K)    
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.10                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 25.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   N3     U C    91     N1     A D    39              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A 125   CA    TYR A 125   CB      0.137                       
REMARK 500    SER A 154   CB    SER A 154   OG      0.080                       
REMARK 500    ARG A 192   CD    ARG A 192   NE      0.103                       
REMARK 500    GLU A 235   CG    GLU A 235   CD     -0.092                       
REMARK 500    SER A 248   CA    SER A 248   CB      0.099                       
REMARK 500    TYR B 260   CG    TYR B 260   CD2     0.080                       
REMARK 500    HIS B 300   CG    HIS B 300   CD2     0.054                       
REMARK 500    GLY B 404   N     GLY B 404   CA     -0.104                       
REMARK 500    HIS B 477   CG    HIS B 477   CD2     0.063                       
REMARK 500    SER B 527   CA    SER B 527   CB      0.094                       
REMARK 500    GLU B 559   CD    GLU B 559   OE2     0.074                       
REMARK 500    CYS B 591   CB    CYS B 591   SG      0.118                       
REMARK 500      A C  90   O4'     A C  90   C1'    -0.091                       
REMARK 500      A C  90   N3      A C  90   C4      0.044                       
REMARK 500      A C  90   C6      A C  90   N1      0.050                       
REMARK 500      A C  90   N9      A C  90   C4      0.050                       
REMARK 500      U C  91   O4'     U C  91   C4'    -0.094                       
REMARK 500      U C  91   C2      U C  91   N3      0.047                       
REMARK 500      U C  91   O3'     U C  92   P      -0.094                       
REMARK 500      G C  93   N3      G C  93   C4     -0.074                       
REMARK 500      G C  93   C6      G C  93   N1      0.072                       
REMARK 500      G C  93   O3'     U C  94   P      -0.075                       
REMARK 500      A C  95   C2'     A C  95   C1'    -0.110                       
REMARK 500      A C  95   N3      A C  95   C4      0.042                       
REMARK 500      A C  95   C5      A C  95   N7      0.042                       
REMARK 500      A C  95   N9      A C  95   C4      0.043                       
REMARK 500      A C  96   C5'     A C  96   C4'     0.072                       
REMARK 500      A C  97   N3      A C  97   C4     -0.036                       
REMARK 500      A C  97   N7      A C  97   C8     -0.047                       
REMARK 500      A C  99   P       A C  99   O5'    -0.075                       
REMARK 500      A C  99   C3'     A C  99   C2'     0.122                       
REMARK 500      A C  99   O4'     A C  99   C4'     0.073                       
REMARK 500      A C  99   C6      A C  99   N6     -0.049                       
REMARK 500      G D   1   C5      G D   1   N7      0.041                       
REMARK 500      G D   1   N7      G D   1   C8     -0.052                       
REMARK 500      C D   2   O4'     C D   2   C1'    -0.082                       
REMARK 500      G D   3   C2'     G D   3   C1'    -0.054                       
REMARK 500      G D   3   C2      G D   3   N3      0.053                       
REMARK 500      G D   3   N3      G D   3   C4     -0.043                       
REMARK 500      G D   3   C6      G D   3   N1     -0.055                       
REMARK 500      G D   4   N3      G D   4   C4     -0.054                       
REMARK 500      G D   5   C4'     G D   5   C3'     0.074                       
REMARK 500      G D   5   N3      G D   5   C4      0.072                       
REMARK 500      G D   5   N9      G D   5   C4     -0.071                       
REMARK 500      G D   6   P       G D   6   O5'     0.071                       
REMARK 500      G D   6   C6      G D   6   N1      0.082                       
REMARK 500      G D   6   C5      G D   6   N7      0.037                       
REMARK 500      G D   6   N7      G D   6   C8     -0.040                       
REMARK 500      G D   7   C5'     G D   7   C4'     0.090                       
REMARK 500      G D   7   C2'     G D   7   C1'    -0.050                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     193 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    GLY A  29   C   -  N   -  CA  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    LEU A  37   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    GLU A  55   OE1 -  CD  -  OE2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PHE A  56   CB  -  CG  -  CD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    PHE A  56   CB  -  CG  -  CD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    VAL A  66   CA  -  CB  -  CG2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ALA A  74   CB  -  CA  -  C   ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ARG A  81   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ARG A  81   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    TYR A  85   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR A  85   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    PHE A 131   CB  -  CG  -  CD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    THR A 137   N   -  CA  -  CB  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    PHE A 148   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    PHE A 148   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    PHE A 158   CB  -  CG  -  CD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    PHE A 158   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 166   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG A 166   NE  -  CZ  -  NH2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    VAL A 174   CG1 -  CB  -  CG2 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    ARG A 182   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 198   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TYR A 201   CB  -  CG  -  CD1 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG A 203   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500    ARG A 203   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    VAL A 219   CG1 -  CB  -  CG2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD1 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    PHE A 242   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 255   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    SER A 257   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    TYR A 258   CB  -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    PHE A 264   CB  -  CG  -  CD1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 289   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    PHE A 291   CB  -  CG  -  CD2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    PHE A 303   CB  -  CG  -  CD2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    PHE A 303   CB  -  CG  -  CD1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    LEU A 309   CB  -  CG  -  CD1 ANGL. DEV. =  10.3 DEGREES          
REMARK 500    MET A 314   CG  -  SD  -  CE  ANGL. DEV. = -11.2 DEGREES          
REMARK 500    CYS A 335   CA  -  CB  -  SG  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PHE A 357   CB  -  CG  -  CD1 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    PHE A 402   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     398 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  23       25.78    -77.11                                   
REMARK 500    SER A  33       22.00    -75.35                                   
REMARK 500    PRO A  41      126.28    -35.82                                   
REMARK 500    ASP A  43     -160.00    -64.34                                   
REMARK 500    ASN A  61      -93.87   -112.34                                   
REMARK 500    ILE A  62      -31.65     68.35                                   
REMARK 500    LYS A  63      129.39     76.86                                   
REMARK 500    SER A  64       73.55     81.88                                   
REMARK 500    ARG A  65      -91.16     21.03                                   
REMARK 500    ARG A  68      -73.46    -50.37                                   
REMARK 500    GLU A 104       13.53     80.79                                   
REMARK 500    PRO A 116      135.09    -38.34                                   
REMARK 500    LEU A 124      124.47   -179.81                                   
REMARK 500    ASP A 128     -152.99    -99.08                                   
REMARK 500    SER A 141     -168.01     52.77                                   
REMARK 500    SER A 144     -150.94    -63.82                                   
REMARK 500    LYS A 145       83.06    138.20                                   
REMARK 500    HIS A 170      142.92    178.92                                   
REMARK 500    ARG A 182       51.79   -140.22                                   
REMARK 500    PHE A 190      -72.96    -53.33                                   
REMARK 500    ASP A 217       12.38     83.49                                   
REMARK 500    ASP A 231      -26.52     75.11                                   
REMARK 500    ASP A 243      162.84    -48.75                                   
REMARK 500    GLN A 244     -136.22     75.76                                   
REMARK 500    THR A 272      -56.27    -25.96                                   
REMARK 500    LEU A 326       81.55    174.07                                   
REMARK 500    THR A 338      154.67     55.35                                   
REMARK 500    PRO A 373      126.69    -27.92                                   
REMARK 500    ASN A 381       -4.53   -144.91                                   
REMARK 500    PRO B 208      117.25    -21.34                                   
REMARK 500    THR B 277      156.32    -38.25                                   
REMARK 500    VAL B 278      -31.93   -139.25                                   
REMARK 500    PRO B 298      133.41    -15.24                                   
REMARK 500    ASP B 315      -62.56     49.34                                   
REMARK 500    ARG B 324      132.41    -39.07                                   
REMARK 500    ASN B 366       40.70   -109.02                                   
REMARK 500    LYS B 408      -38.15   -134.39                                   
REMARK 500    ASN B 431       61.44    -65.45                                   
REMARK 500    TYR B 448      153.22    179.51                                   
REMARK 500    ASP B 450      -99.94   -149.01                                   
REMARK 500    SER B 461      125.70    168.72                                   
REMARK 500    GLN B 469      137.86    -36.83                                   
REMARK 500    PRO B 474      -27.56    -38.96                                   
REMARK 500    ASN B 475      -55.64    -23.74                                   
REMARK 500    LYS B 476       35.71     72.58                                   
REMARK 500    ASP B 487      -99.92     33.60                                   
REMARK 500    GLU B 509       -4.38   -165.55                                   
REMARK 500    ASN B 522     -158.01     45.93                                   
REMARK 500    GLU B 539       78.42   -172.05                                   
REMARK 500    ILE B 543      123.43    -23.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 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  141     ASP A  142                 -147.84                    
REMARK 500 ASP A  142     ASP A  143                  116.64                    
REMARK 500 SER A  144     LYS A  145                  -67.68                    
REMARK 500 LEU A  275     SER A  276                 -108.94                    
REMARK 500 SER A  276     ASN A  277                   53.92                    
REMARK 500 VAL A  278     LYS A  279                  -40.18                    
REMARK 500 ASN A  325     LEU A  326                 -126.90                    
REMARK 500 PHE B  292     THR B  293                  149.61                    
REMARK 500 ALA B  314     ASP B  315                 -138.26                    
REMARK 500 PRO B  439     ILE B  440                 -138.30                    
REMARK 500 GLN B  469     LEU B  470                  133.54                    
REMARK 500 MET B  473     PRO B  474                  -47.11                    
REMARK 500 ILE B  517     LEU B  518                  136.87                    
REMARK 500 PRO B  521     ASN B  522                   55.08                    
REMARK 500 LEU B  524     CYS B  525                 -134.29                    
REMARK 500 GLY B  528     ARG B  529                   80.49                    
REMARK 500 VAL B  536     ILE B  537                 -136.48                    
REMARK 500 GLU B  539     HIS B  540                  142.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  28         0.14    SIDE CHAIN                              
REMARK 500    ARG A  81         0.11    SIDE CHAIN                              
REMARK 500    HIS A 132         0.08    SIDE CHAIN                              
REMARK 500    ARG A 194         0.09    SIDE CHAIN                              
REMARK 500    TYR A 301         0.08    SIDE CHAIN                              
REMARK 500    TYR A 323         0.09    SIDE CHAIN                              
REMARK 500    TYR A 331         0.10    SIDE CHAIN                              
REMARK 500    HIS A 356         0.08    SIDE CHAIN                              
REMARK 500    PHE A 402         0.08    SIDE CHAIN                              
REMARK 500    PHE A 419         0.17    SIDE CHAIN                              
REMARK 500    TYR B 247         0.07    SIDE CHAIN                              
REMARK 500    ARG B 272         0.12    SIDE CHAIN                              
REMARK 500    PHE B 303         0.07    SIDE CHAIN                              
REMARK 500    PHE B 328         0.08    SIDE CHAIN                              
REMARK 500    ARG B 371         0.11    SIDE CHAIN                              
REMARK 500    TYR B 372         0.12    SIDE CHAIN                              
REMARK 500    TYR B 448         0.08    SIDE CHAIN                              
REMARK 500    ARG B 503         0.08    SIDE CHAIN                              
REMARK 500    HIS B 553         0.10    SIDE CHAIN                              
REMARK 500    ARG B 581         0.08    SIDE CHAIN                              
REMARK 500    ARG B 583         0.07    SIDE CHAIN                              
REMARK 500      A C  90         0.08    SIDE CHAIN                              
REMARK 500      U C  91         0.18    SIDE CHAIN                              
REMARK 500      U C  92         0.09    SIDE CHAIN                              
REMARK 500      G C  93         0.16    SIDE CHAIN                              
REMARK 500      A C  95         0.07    SIDE CHAIN                              
REMARK 500      A C  97         0.07    SIDE CHAIN                              
REMARK 500      A C  98         0.07    SIDE CHAIN                              
REMARK 500      G D   1         0.09    SIDE CHAIN                              
REMARK 500      G D   4         0.11    SIDE CHAIN                              
REMARK 500      G D   5         0.11    SIDE CHAIN                              
REMARK 500      U D   8         0.12    SIDE CHAIN                              
REMARK 500      U D   9         0.07    SIDE CHAIN                              
REMARK 500      G D  10         0.11    SIDE CHAIN                              
REMARK 500      C D  12         0.09    SIDE CHAIN                              
REMARK 500      A D  14         0.08    SIDE CHAIN                              
REMARK 500      G D  15         0.08    SIDE CHAIN                              
REMARK 500      U D  18         0.10    SIDE CHAIN                              
REMARK 500      G D  19         0.09    SIDE CHAIN                              
REMARK 500      G D  20         0.18    SIDE CHAIN                              
REMARK 500      U D  21         0.06    SIDE CHAIN                              
REMARK 500      A D  23         0.08    SIDE CHAIN                              
REMARK 500      A D  24         0.07    SIDE CHAIN                              
REMARK 500      G D  26         0.11    SIDE CHAIN                              
REMARK 500      C D  28         0.06    SIDE CHAIN                              
REMARK 500      G D  29         0.08    SIDE CHAIN                              
REMARK 500      G D  30         0.06    SIDE CHAIN                              
REMARK 500      U D  36         0.13    SIDE CHAIN                              
REMARK 500      C D  37         0.13    SIDE CHAIN                              
REMARK 500      A D  38         0.20    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE B 232        -11.04                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-5801   RELATED DB: EMDB                              
DBREF  3J5Y A    7   420  UNP    P62495   ERF1_HUMAN       7    420             
DBREF  3J5Y B  207   634  UNP    P15170   ERF3A_HUMAN     69    496             
DBREF  3J5Y C   90    99  PDB    3J5Y     3J5Y            90     99             
DBREF  3J5Y D    1    88  PDB    3J5Y     3J5Y             1     88             
SEQADV 3J5Y ILE B  369  UNP  P15170    ASN   231 CONFLICT                       
SEQADV 3J5Y SER B  389  UNP  P15170    ASN   251 CONFLICT                       
SEQADV 3J5Y ILE B  407  UNP  P15170    LEU   269 CONFLICT                       
SEQADV 3J5Y THR B  418  UNP  P15170    ILE   280 CONFLICT                       
SEQADV 3J5Y ILE B  436  UNP  P15170    VAL   298 CONFLICT                       
SEQRES   1 A  414  ALA ALA ASP ARG ASN VAL GLU ILE TRP LYS ILE LYS LYS          
SEQRES   2 A  414  LEU ILE LYS SER LEU GLU ALA ALA ARG GLY ASN GLY THR          
SEQRES   3 A  414  SER MET ILE SER LEU ILE ILE PRO PRO LYS ASP GLN ILE          
SEQRES   4 A  414  SER ARG VAL ALA LYS MET LEU ALA ASP GLU PHE GLY THR          
SEQRES   5 A  414  ALA SER ASN ILE LYS SER ARG VAL ASN ARG LEU SER VAL          
SEQRES   6 A  414  LEU GLY ALA ILE THR SER VAL GLN GLN ARG LEU LYS LEU          
SEQRES   7 A  414  TYR ASN LYS VAL PRO PRO ASN GLY LEU VAL VAL TYR CYS          
SEQRES   8 A  414  GLY THR ILE VAL THR GLU GLU GLY LYS GLU LYS LYS VAL          
SEQRES   9 A  414  ASN ILE ASP PHE GLU PRO PHE LYS PRO ILE ASN THR SER          
SEQRES  10 A  414  LEU TYR LEU CYS ASP ASN LYS PHE HIS THR GLU ALA LEU          
SEQRES  11 A  414  THR ALA LEU LEU SER ASP ASP SER LYS PHE GLY PHE ILE          
SEQRES  12 A  414  VAL ILE ASP GLY SER GLY ALA LEU PHE GLY THR LEU GLN          
SEQRES  13 A  414  GLY ASN THR ARG GLU VAL LEU HIS LYS PHE THR VAL ASP          
SEQRES  14 A  414  LEU PRO LYS LYS HIS GLY ARG GLY GLY GLN SER ALA LEU          
SEQRES  15 A  414  ARG PHE ALA ARG LEU ARG MET GLU LYS ARG HIS ASN TYR          
SEQRES  16 A  414  VAL ARG LYS VAL ALA GLU THR ALA VAL GLN LEU PHE ILE          
SEQRES  17 A  414  SER GLY ASP LYS VAL ASN VAL ALA GLY LEU VAL LEU ALA          
SEQRES  18 A  414  GLY SER ALA ASP PHE LYS THR GLU LEU SER GLN SER ASP          
SEQRES  19 A  414  MET PHE ASP GLN ARG LEU GLN SER LYS VAL LEU LYS LEU          
SEQRES  20 A  414  VAL ASP ILE SER TYR GLY GLY GLU ASN GLY PHE ASN GLN          
SEQRES  21 A  414  ALA ILE GLU LEU SER THR GLU VAL LEU SER ASN VAL LYS          
SEQRES  22 A  414  PHE ILE GLN GLU LYS LYS LEU ILE GLY ARG TYR PHE ASP          
SEQRES  23 A  414  GLU ILE SER GLN ASP THR GLY LYS TYR CYS PHE GLY VAL          
SEQRES  24 A  414  GLU ASP THR LEU LYS ALA LEU GLU MET GLY ALA VAL GLU          
SEQRES  25 A  414  ILE LEU ILE VAL TYR GLU ASN LEU ASP ILE MET ARG TYR          
SEQRES  26 A  414  VAL LEU HIS CYS GLN GLY THR GLU GLU GLU LYS ILE LEU          
SEQRES  27 A  414  TYR LEU THR PRO GLU GLN GLU LYS ASP LYS SER HIS PHE          
SEQRES  28 A  414  THR ASP LYS GLU THR GLY GLN GLU HIS GLU LEU ILE GLU          
SEQRES  29 A  414  SER MET PRO LEU LEU GLU TRP PHE ALA ASN ASN TYR LYS          
SEQRES  30 A  414  LYS PHE GLY ALA THR LEU GLU ILE VAL THR ASP LYS SER          
SEQRES  31 A  414  GLN GLU GLY SER GLN PHE VAL LYS GLY PHE GLY GLY ILE          
SEQRES  32 A  414  GLY GLY ILE LEU ARG TYR ARG VAL ASP PHE GLN                  
SEQRES   1 B  428  ALA PRO LYS LYS GLU HIS VAL ASN VAL VAL PHE ILE GLY          
SEQRES   2 B  428  HIS VAL ASP ALA GLY LYS SER THR ILE GLY GLY GLN ILE          
SEQRES   3 B  428  MET TYR LEU THR GLY MET VAL ASP LYS ARG THR LEU GLU          
SEQRES   4 B  428  LYS TYR GLU ARG GLU ALA LYS GLU LYS ASN ARG GLU THR          
SEQRES   5 B  428  TRP TYR LEU SER TRP ALA LEU ASP THR ASN GLN GLU GLU          
SEQRES   6 B  428  ARG ASP LYS GLY LYS THR VAL GLU VAL GLY ARG ALA TYR          
SEQRES   7 B  428  PHE GLU THR GLU LYS LYS HIS PHE THR ILE LEU ASP ALA          
SEQRES   8 B  428  PRO GLY HIS LYS SER PHE VAL PRO ASN MET ILE GLY GLY          
SEQRES   9 B  428  ALA SER GLN ALA ASP LEU ALA VAL LEU VAL ILE SER ALA          
SEQRES  10 B  428  ARG LYS GLY GLU PHE GLU THR GLY PHE GLU LYS GLY GLY          
SEQRES  11 B  428  GLN THR ARG GLU HIS ALA MET LEU ALA LYS THR ALA GLY          
SEQRES  12 B  428  VAL LYS HIS LEU ILE VAL LEU ILE ASN LYS MET ASP ASP          
SEQRES  13 B  428  PRO THR VAL ASN TRP SER ILE GLU ARG TYR GLU GLU CYS          
SEQRES  14 B  428  LYS GLU LYS LEU VAL PRO PHE LEU LYS LYS VAL GLY PHE          
SEQRES  15 B  428  SER PRO LYS LYS ASP ILE HIS PHE MET PRO CYS SER GLY          
SEQRES  16 B  428  LEU THR GLY ALA ASN ILE LYS GLU GLN SER ASP PHE CYS          
SEQRES  17 B  428  PRO TRP TYR THR GLY LEU PRO PHE ILE PRO TYR LEU ASP          
SEQRES  18 B  428  ASN LEU PRO ASN PHE ASN ARG SER ILE ASP GLY PRO ILE          
SEQRES  19 B  428  ARG LEU PRO ILE VAL ASP LYS TYR LYS ASP MET GLY THR          
SEQRES  20 B  428  VAL VAL LEU GLY LYS LEU GLU SER GLY SER ILE CYS LYS          
SEQRES  21 B  428  GLY GLN GLN LEU VAL MET MET PRO ASN LYS HIS ASN VAL          
SEQRES  22 B  428  GLU VAL LEU GLY ILE LEU SER ASP ASP VAL GLU THR ASP          
SEQRES  23 B  428  THR VAL ALA PRO GLY GLU ASN LEU LYS ILE ARG LEU LYS          
SEQRES  24 B  428  GLY ILE GLU GLU GLU GLU ILE LEU PRO GLY PHE ILE LEU          
SEQRES  25 B  428  CYS ASP PRO ASN ASN LEU CYS HIS SER GLY ARG THR PHE          
SEQRES  26 B  428  ASP ALA GLN ILE VAL ILE ILE GLU HIS LYS SER ILE ILE          
SEQRES  27 B  428  CYS PRO GLY TYR ASN ALA VAL LEU HIS ILE HIS THR CYS          
SEQRES  28 B  428  ILE GLU GLU VAL GLU ILE THR ALA LEU ILE CYS LEU VAL          
SEQRES  29 B  428  ASP LYS LYS SER GLY GLU LYS SER LYS THR ARG PRO ARG          
SEQRES  30 B  428  PHE VAL LYS GLN ASP GLN VAL CYS ILE ALA ARG LEU ARG          
SEQRES  31 B  428  THR ALA GLY THR ILE CYS LEU GLU THR PHE LYS ASP PHE          
SEQRES  32 B  428  PRO GLN MET GLY ARG PHE THR LEU ARG ASP GLU GLY LYS          
SEQRES  33 B  428  THR ILE ALA ILE GLY LYS VAL LEU LYS LEU VAL PRO              
SEQRES   1 C   10    A   U   U   G   U   A   A   A   A   A                      
SEQRES   1 D   88    G   C   G   G   G   G   G   U   U   G   C   C   G          
SEQRES   2 D   88    A   G   C   C   U   G   G   U   C   A   A   A   G          
SEQRES   3 D   88    G   C   G   G   G   G   G   A   C   U   C   A   A          
SEQRES   4 D   88    G   A   U   C   C   C   C   U   C   C   C   G   U          
SEQRES   5 D   88    A   G   G   G   G   U   U   C   C   G   G   G   G          
SEQRES   6 D   88    U   U   C   G   A   A   U   C   C   C   C   G   C          
SEQRES   7 D   88    C   C   C   C   G   C   A   C   C   A                      
HELIX    1   1 ALA A    7  ALA A   26  1                                  20    
HELIX    2   2 GLN A   44  ALA A   59  1                                  16    
HELIX    3   3 SER A   64  LYS A   83  1                                  20    
HELIX    4   4 GLU A  103  GLY A  105  5                                   3    
HELIX    5   5 THR A  133  SER A  141  1                                   9    
HELIX    6   6 SER A  186  PHE A  213  1                                  28    
HELIX    7   7 LYS A  233  GLN A  238  1                                   6    
HELIX    8   8 ARG A  245  SER A  248  5                                   4    
HELIX    9   9 GLU A  261  LEU A  270  1                                  10    
HELIX   10  10 SER A  271  LEU A  275  5                                   5    
HELIX   11  11 PHE A  280  SER A  295  1                                  16    
HELIX   12  12 VAL A  305  MET A  314  1                                  10    
HELIX   13  13 THR A  347  ASP A  353  1                                   7    
HELIX   14  14 LEU A  374  ASN A  380  1                                   7    
HELIX   15  15 SER A  396  PHE A  406  1                                  11    
HELIX   16  16 GLY B  224  LEU B  235  1                                  12    
HELIX   17  17 ASP B  240  LYS B  254  1                                  15    
HELIX   18  18 ARG B  256  TYR B  260  5                                   5    
HELIX   19  19 LEU B  261  LEU B  265  5                                   5    
HELIX   20  20 ASN B  268  GLY B  275  1                                   8    
HELIX   21  21 PHE B  303  GLN B  313  1                                  11    
HELIX   22  22 GLY B  326  PHE B  332  1                                   7    
HELIX   23  23 GLN B  337  ALA B  348  1                                  12    
HELIX   24  24 SER B  368  PHE B  388  1                                  21    
HELIX   25  25 PRO B  421  LEU B  429  1                                   9    
HELIX   26  26 PHE B  609  MET B  612  5                                   4    
SHEET    1   A 4 LYS A 106  PHE A 114  0                                        
SHEET    2   A 4 LEU A  93  THR A 102 -1  N  TYR A  96   O  ILE A 112           
SHEET    3   A 4 MET A  34  ILE A  39 -1  N  LEU A  37   O  VAL A  95           
SHEET    4   A 4 LEU A 124  ASP A 128 -1  O  LEU A 126   N  SER A  36           
SHEET    1   B 5 THR A 165  THR A 173  0                                        
SHEET    2   B 5 GLY A 155  GLN A 162 -1  N  THR A 160   O  GLU A 167           
SHEET    3   B 5 LYS A 145  ILE A 151 -1  N  VAL A 150   O  LEU A 157           
SHEET    4   B 5 LEU A 224  GLY A 228  1  O  ALA A 227   N  ILE A 149           
SHEET    5   B 5 VAL A 250  ASP A 255  1  O  LEU A 251   N  LEU A 224           
SHEET    1   C 2 ILE A 214  SER A 215  0                                        
SHEET    2   C 2 LYS A 218  VAL A 219 -1  O  LYS A 218   N  SER A 215           
SHEET    1   D 4 TYR A 301  PHE A 303  0                                        
SHEET    2   D 4 ILE A 409  LEU A 413 -1  O  GLY A 411   N  CYS A 302           
SHEET    3   D 4 VAL A 317  TYR A 323 -1  N  ILE A 319   O  ILE A 412           
SHEET    4   D 4 GLY A 386  VAL A 392  1  O  GLU A 390   N  LEU A 320           
SHEET    1   E 3 GLU A 341  LEU A 346  0                                        
SHEET    2   E 3 MET A 329  HIS A 334 -1  N  LEU A 333   O  LYS A 342           
SHEET    3   E 3 GLU A 367  PRO A 373 -1  O  GLU A 367   N  HIS A 334           
SHEET    1   F 6 GLY B 281  GLU B 286  0                                        
SHEET    2   F 6 LYS B 290  ASP B 296 -1  O  ILE B 294   N  ALA B 283           
SHEET    3   F 6 GLU B 211  GLY B 219  1  N  PHE B 217   O  LEU B 295           
SHEET    4   F 6 LEU B 316  SER B 322  1  O  VAL B 320   N  ILE B 218           
SHEET    5   F 6 LEU B 353  ASN B 358  1  O  ILE B 354   N  LEU B 319           
SHEET    6   F 6 ILE B 394  PRO B 398  1  O  HIS B 395   N  VAL B 355           
SHEET    1   G 8 VAL B 489  THR B 491  0                                        
SHEET    2   G 8 ASN B 478  SER B 486 -1  N  SER B 486   O  VAL B 489           
SHEET    3   G 8 ASN B 499  LYS B 505 -1  O  ARG B 503   N  GLY B 483           
SHEET    4   G 8 THR B 453  LYS B 458 -1  N  VAL B 455   O  ILE B 502           
SHEET    5   G 8 ARG B 441  LYS B 449 -1  N  VAL B 445   O  LEU B 456           
SHEET    6   G 8 ILE B 517  CYS B 519 -1  O  LEU B 518   N  LEU B 442           
SHEET    7   G 8 GLN B 469  MET B 472 -1  N  VAL B 471   O  CYS B 519           
SHEET    8   G 8 ASN B 478  SER B 486 -1  O  VAL B 479   N  LEU B 470           
SHEET    1   H 7 THR B 530  VAL B 536  0                                        
SHEET    2   H 7 VAL B 590  THR B 597 -1  O  LEU B 595   N  PHE B 531           
SHEET    3   H 7 CYS B 557  VAL B 570 -1  N  GLU B 562   O  ARG B 596           
SHEET    4   H 7 ASN B 549  ILE B 554 -1  N  LEU B 552   O  GLU B 559           
SHEET    5   H 7 ARG B 614  ARG B 618 -1  O  ARG B 618   N  VAL B 551           
SHEET    6   H 7 ALA B 625  VAL B 633 -1  O  GLY B 627   N  PHE B 615           
SHEET    7   H 7 THR B 530  VAL B 536 -1  N  ASP B 532   O  LYS B 631           
SSBOND   1 CYS B  519    CYS B  525                          1555   1555  2.04  
CISPEP   1 HIS B  540    LYS B  541          0         6.29                     
CISPEP   2 VAL B  633    PRO B  634          0       -14.43                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system