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Database: PDB
Entry: 4CRM
LinkDB: 4CRM
Original site: 4CRM 
HEADER    TRANSLATION                             28-FEB-14   4CRM              
TITLE     CRYO-EM OF A PRE-RECYCLING COMPLEX WITH ERF1 AND ABCE1                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSLATION INITIATION FACTOR RLI1;                        
COMPND   3 CHAIN: P;                                                            
COMPND   4 SYNONYM: ATP-BINDING CASSETTE SUB-FAMILY E MEMBER RLI1, RNASE L      
COMPND   5 INHIBITOR, ABCE1 IN RIBOSOME BOUND ERF1-ABCE1-ADPNP COMPLEX;         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1;         
COMPND   9 CHAIN: X;                                                            
COMPND  10 SYNONYM: EUKARYOTIC RELEASE FACTOR 1, ERF1, OMNIPOTENT SUPPRESSOR    
COMPND  11 PROTEIN 1, ERF1 IN RIBOSOME-BOUND ERF1-ABCE1-ADPNP COMPLEX;          
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PYES2;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  12 ORGANISM_TAXID: 4932;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSLATION, TERMINATION, RECYCLING                                   
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.PREIS,A.HEUER,C.BARRIO-GARCIA,A.HAUSER,D.EYLER,O.BERNINGHAUSEN,     
AUTHOR   2 R.GREEN,T.BECKER,R.BECKMANN                                          
REVDAT   3   30-AUG-17 4CRM    1       REMARK                                   
REVDAT   2   11-MAY-16 4CRM    1       AUTHOR                                   
REVDAT   1   23-JUL-14 4CRM    0                                                
JRNL        AUTH   A.PREIS,A.HEUER,C.BARRIO-GARCIA,A.HAUSER,D.E.EYLER,          
JRNL        AUTH 2 O.BERNINGHAUSEN,R.GREEN,T.BECKER,R.BECKMANN                  
JRNL        TITL   CRYOELECTRON MICROSCOPIC STRUCTURES OF EUKARYOTIC            
JRNL        TITL 2 TRANSLATION TERMINATION COMPLEXES CONTAINING ERF1-ERF3 OR    
JRNL        TITL 3 ERF1-ABCE1.                                                  
JRNL        REF    CELL REP.                     V.   8    59 2014              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   25001285                                                     
JRNL        DOI    10.1016/J.CELREP.2014.04.058                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    8.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : COOT, MDFF, UCSF CHIMERA, STARFISH,       
REMARK   3                            SPIDER                                    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 1DT9                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--RIGID BODY                               
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)  : 8.750                          
REMARK   3   NUMBER OF PARTICLES               : 39309                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD   
REMARK   3  -2598.                                                              
REMARK   4                                                                      
REMARK   4 4CRM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290059858.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : CMV-STALLED WHEAT GERM 80S-RNC    
REMARK 245                                    BOUND TO ERF1 AND ABCE1-ADPNP     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : CARBON                            
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 -CRYOGEN-         
REMARK 245                                    ETHANE, HUMIDITY- 100,            
REMARK 245                                    INSTRUMENT- FEI VITROBOT MARK     
REMARK 245                                    IV, METHOD- BLOT FOR 3 SECONDS    
REMARK 245                                    BEFORE PLUNGING                   
REMARK 245   SAMPLE BUFFER                  : 20 MM HEPES PH 7.5, 200 MM KCL,   
REMARK 245                                    1.5 MGCL2, 2 MM DTT, 0.01 MG/ML   
REMARK 245                                    CYCLOHEXIMIDE, 0.05 % NIKKOL,     
REMARK 245                                    0.03 % DBC, 0.5 MM ADPNP).        
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 20-FEB-13                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI MORGAGNI                   
REMARK 245   DETECTOR TYPE                     : TVIPS TEMCAM-F416 (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                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : 147136                         
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, X                                  
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   CD1  ILE P    72     S1   SF4 P  1610              0.96            
REMARK 500   SG   CYS P    61    FE3   SF4 P  1610              0.96            
REMARK 500   CB   LEU X   323     CD1  ILE X   370              1.33            
REMARK 500   CG2  ILE X   302     CE   LYS X   340              1.53            
REMARK 500   CB   LEU X   173     NH1  ARG X   191              1.57            
REMARK 500   OH   TYR X   287     CD1  ILE X   318              1.71            
REMARK 500   CG2  ILE X   302     NZ   LYS X   340              1.75            
REMARK 500   C    ILE X   302     NZ   LYS X   340              1.75            
REMARK 500   CG   LEU X   323     CG1  ILE X   370              1.79            
REMARK 500   CG2  ILE X   302     CD   LYS X   340              1.83            
REMARK 500   CB   LEU X   323     CG1  ILE X   370              1.84            
REMARK 500   CD1  LEU X   323     CG1  ILE X   370              1.94            
REMARK 500   N    GLY P   115     O1B  ATP P  1609              1.96            
REMARK 500   OD1  ASP X   310     CE1  PHE X   380              1.98            
REMARK 500   O    ILE X   302     NZ   LYS X   340              2.06            
REMARK 500   CG   LEU X   173     NH1  ARG X   191              2.13            
REMARK 500   CD1  ILE X   302     CB   THR X   325              2.14            
REMARK 500   N    LYS P   116     O1B  ATP P  1609              2.14            
REMARK 500   N    GLY P   388     O3B  ADP P  1612              2.17            
REMARK 500   CG   LEU X   323     CD1  ILE X   370              2.18            
REMARK 500   O    GLY X   301     OG1  THR X   305              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    SER P 309   CA    SER P 309   CB     -0.155                       
REMARK 500    GLN P 589   CA    GLN P 589   CB      0.177                       
REMARK 500    GLN P 589   CB    GLN P 589   CG      0.209                       
REMARK 500    GLN P 589   CA    GLN P 589   C       0.245                       
REMARK 500    ILE P 608   C     ILE P 608   O      -0.229                       
REMARK 500    ILE P 608   C     ILE P 608   OXT    -0.229                       
REMARK 500    GLY X 150   N     GLY X 150   CA      0.117                       
REMARK 500    GLY X 150   CA    GLY X 150   C       0.115                       
REMARK 500    GLY X 181   CA    GLY X 181   C      -0.105                       
REMARK 500    ARG X 186   CD    ARG X 186   NE      0.177                       
REMARK 500    ARG X 186   NE    ARG X 186   CZ      0.117                       
REMARK 500    ILE X 302   C     ASP X 303   N       0.147                       
REMARK 500    SER X 421   C     SER X 421   O      -0.229                       
REMARK 500    SER X 421   C     SER X 421   OXT    -0.229                       
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 P 573   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASN P 584   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    LYS P 585   CB  -  CA  -  C   ANGL. DEV. =  16.4 DEGREES          
REMARK 500    LEU P 586   CB  -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    LEU P 586   CB  -  CG  -  CD2 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ASP P 587   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    SER P 588   N   -  CA  -  CB  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    SER P 588   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    GLN P 589   CB  -  CA  -  C   ANGL. DEV. =  21.2 DEGREES          
REMARK 500    GLN P 589   N   -  CA  -  CB  ANGL. DEV. = -20.4 DEGREES          
REMARK 500    GLN P 589   CA  -  CB  -  CG  ANGL. DEV. =  28.3 DEGREES          
REMARK 500    GLN P 589   CB  -  CG  -  CD  ANGL. DEV. =  29.5 DEGREES          
REMARK 500    GLN P 589   CA  -  C   -  N   ANGL. DEV. = -21.2 DEGREES          
REMARK 500    ASP X 149   CA  -  C   -  N   ANGL. DEV. =  29.6 DEGREES          
REMARK 500    ASP X 149   O   -  C   -  N   ANGL. DEV. = -30.0 DEGREES          
REMARK 500    LYS X 175   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG X 179   N   -  CA  -  CB  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ARG X 179   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    SER X 183   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG X 186   CA  -  CB  -  CG  ANGL. DEV. =  23.2 DEGREES          
REMARK 500    ARG X 186   CG  -  CD  -  NE  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ARG X 186   NH1 -  CZ  -  NH2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG X 186   NE  -  CZ  -  NH2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG X 195   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    LYS X 281   CA  -  CB  -  CG  ANGL. DEV. =  24.9 DEGREES          
REMARK 500    GLN X 293   N   -  CA  -  CB  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    PHE X 298   CB  -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    PHE X 298   CB  -  CG  -  CD2 ANGL. DEV. =  -8.0 DEGREES          
REMARK 500    PHE X 298   CB  -  CG  -  CD1 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    LEU X 317   CB  -  CG  -  CD2 ANGL. DEV. =  15.6 DEGREES          
REMARK 500    PHE X 320   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    LYS X 331   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LYS X 331   N   -  CA  -  C   ANGL. DEV. =  17.6 DEGREES          
REMARK 500    ASP X 335   O   -  C   -  N   ANGL. DEV. =  12.0 DEGREES          
REMARK 500    ASP X 354   C   -  N   -  CA  ANGL. DEV. =  18.5 DEGREES          
REMARK 500    MET X 361   CG  -  SD  -  CE  ANGL. DEV. = -11.6 DEGREES          
REMARK 500    PRO X 368   CA  -  N   -  CD  ANGL. DEV. = -12.3 DEGREES          
REMARK 500    LEU X 369   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    TRP X 372   CB  -  CA  -  C   ANGL. DEV. = -14.1 DEGREES          
REMARK 500    TRP X 372   CB  -  CG  -  CD1 ANGL. DEV. = -14.7 DEGREES          
REMARK 500    VAL X 412   CG1 -  CB  -  CG2 ANGL. DEV. =  10.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG P  22     -167.35     61.97                                   
REMARK 500    SER P  28      -55.74     79.26                                   
REMARK 500    PHE P  67      -70.31    -81.98                                   
REMARK 500    ASP P  68       36.49    140.78                                   
REMARK 500    THR P  77       45.56     73.50                                   
REMARK 500    SER P  88     -171.37    174.48                                   
REMARK 500    ARG P  96      169.51     55.56                                   
REMARK 500    LEU P 131       32.38     71.37                                   
REMARK 500    ARG P 133     -147.95   -155.45                                   
REMARK 500    ASP P 135      119.23    -31.87                                   
REMARK 500    ASP P 136     -159.17    -88.38                                   
REMARK 500    PRO P 138       88.80    -27.82                                   
REMARK 500    LYS P 186     -162.83    -77.28                                   
REMARK 500    MET P 195       92.56    -68.41                                   
REMARK 500    LYS P 197     -128.63    -72.66                                   
REMARK 500    TYR P 251      -20.37     73.31                                   
REMARK 500    SER P 299      -13.11     72.01                                   
REMARK 500    ALA P 339      -12.96     94.89                                   
REMARK 500    ALA P 350     -139.57     66.74                                   
REMARK 500    ALA P 353     -157.33   -145.20                                   
REMARK 500    LYS P 412       63.91   -105.11                                   
REMARK 500    PRO P 424      -70.42    -44.53                                   
REMARK 500    LYS P 425       56.98     32.96                                   
REMARK 500    ILE P 438      124.93   -172.70                                   
REMARK 500    VAL P 451      -62.77    -95.92                                   
REMARK 500    ARG P 456       74.66     72.02                                   
REMARK 500    GLU P 493       75.68     42.83                                   
REMARK 500    LYS P 547      -79.78   -137.84                                   
REMARK 500    ARG P 573     -147.39    -98.09                                   
REMARK 500    THR X 162      155.54    -34.04                                   
REMARK 500    ARG X 163      126.58    178.69                                   
REMARK 500    THR X 164      144.90   -172.54                                   
REMARK 500    VAL X 171      -66.48   -143.90                                   
REMARK 500    ASP X 172      178.07    127.33                                   
REMARK 500    LEU X 173      117.26    125.49                                   
REMARK 500    LYS X 175       95.40    134.48                                   
REMARK 500    HIS X 177       -8.95   -164.18                                   
REMARK 500    ARG X 179      -60.77    -16.23                                   
REMARK 500    GLN X 182        0.65    -56.64                                   
REMARK 500    ALA X 184        2.88    -53.60                                   
REMARK 500    LEU X 185      -24.05   -140.35                                   
REMARK 500    ASN X 213       50.96     92.72                                   
REMARK 500    ASP X 214      155.85     66.47                                   
REMARK 500    LYS X 215     -108.53     52.77                                   
REMARK 500    ALA X 227      -82.03    -29.49                                   
REMARK 500    LEU X 233      -61.78    -95.88                                   
REMARK 500    ARG X 242      -20.42     90.08                                   
REMARK 500    GLU X 280      -99.67    -55.99                                   
REMARK 500    LYS X 281      -79.57    -21.93                                   
REMARK 500    LYS X 282      -96.63    -39.19                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      90 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 ASP X  140     ASP X  141                 -148.54                    
REMARK 500 ASP X  141     LYS X  142                 -145.18                    
REMARK 500 SER X  392     GLU X  393                  147.63                    
REMARK 500 PHE X  401     GLY X  402                 -146.23                    
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 P 574         0.13    SIDE CHAIN                              
REMARK 500    ASP X 141         0.08    SIDE CHAIN                              
REMARK 500    ASP X 149         0.09    SIDE CHAIN                              
REMARK 500    ARG X 179         0.20    SIDE CHAIN                              
REMARK 500    ARG X 191         0.21    SIDE CHAIN                              
REMARK 500    TYR X 198         0.06    SIDE CHAIN                              
REMARK 500    ASP X 214         0.09    SIDE CHAIN                              
REMARK 500    ASN X 217         0.08    SIDE CHAIN                              
REMARK 500    ASP X 240         0.07    SIDE CHAIN                              
REMARK 500    PHE X 298         0.38    SIDE CHAIN                              
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    GLN P 589        -17.00                                           
REMARK 500    PRO X 174         10.80                                           
REMARK 500    ARG X 191        -14.21                                           
REMARK 500    GLU X 192        -13.94                                           
REMARK 500    ASN X 262        -12.63                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 P1611  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS P  16   SG                                                     
REMARK 620 2 SF4 P1611   S1  149.7                                              
REMARK 620 3 SF4 P1611   S2   74.1 108.5                                        
REMARK 620 4 SF4 P1611   S3  102.2 106.1 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 P1611  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS P  21   SG                                                     
REMARK 620 2 SF4 P1611   S1  122.2                                              
REMARK 620 3 SF4 P1611   S3  140.6  95.8                                        
REMARK 620 4 SF4 P1611   S4   76.1 101.9 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 P1610  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS P  55   SG                                                     
REMARK 620 2 SF4 P1610   S1  114.3                                              
REMARK 620 3 SF4 P1610   S3   62.6  95.8                                        
REMARK 620 4 SF4 P1610   S4  143.2 101.8 108.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 P1610  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS P  61   CB                                                     
REMARK 620 2 SF4 P1610   S1  135.7                                              
REMARK 620 3 SF4 P1610   S2   64.2  99.9                                        
REMARK 620 4 SF4 P1610   S4  123.3 100.6 107.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG P1613  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER P 117   OG                                                     
REMARK 620 2 ATP P1609   O2B  95.1                                              
REMARK 620 3 ATP P1609   O1G 148.6  78.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP P 1609                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 P 1610                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 P 1611                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP P 1612                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 1613                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CRN   RELATED DB: PDB                                   
REMARK 900 CRYO-EM OF A PRETERMINATION COMPLEX WITH ERF1 AND ERF3               
REMARK 900 RELATED ID: EMD-2598   RELATED DB: EMDB                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST 139 AMINO ACIDS ARE MISSING. THE C-TERMINAL                
REMARK 999 AMINO ACIDS 422-440 ARE MISSING                                      
DBREF  4CRM P    1   608  UNP    Q03195   RLI1_YEAST       1    608             
DBREF  4CRM X  140   421  UNP    P12385   ERF1_YEAST     140    421             
SEQRES   1 P  608  MET SER ASP LYS ASN SER ARG ILE ALA ILE VAL SER ALA          
SEQRES   2 P  608  ASP LYS CYS LYS PRO LYS LYS CYS ARG GLN GLU CYS LYS          
SEQRES   3 P  608  ARG SER CYS PRO VAL VAL LYS THR GLY LYS LEU CYS ILE          
SEQRES   4 P  608  GLU VAL THR PRO THR SER LYS ILE ALA PHE ILE SER GLU          
SEQRES   5 P  608  ILE LEU CYS ILE GLY CYS GLY ILE CYS VAL LYS LYS CYS          
SEQRES   6 P  608  PRO PHE ASP ALA ILE GLN ILE ILE ASN LEU PRO THR ASN          
SEQRES   7 P  608  LEU GLU ALA HIS VAL THR HIS ARG TYR SER ALA ASN SER          
SEQRES   8 P  608  PHE LYS LEU HIS ARG LEU PRO THR PRO ARG PRO GLY GLN          
SEQRES   9 P  608  VAL LEU GLY LEU VAL GLY THR ASN GLY ILE GLY LYS SER          
SEQRES  10 P  608  THR ALA LEU LYS ILE LEU ALA GLY LYS GLN LYS PRO ASN          
SEQRES  11 P  608  LEU GLY ARG PHE ASP ASP PRO PRO GLU TRP GLN GLU ILE          
SEQRES  12 P  608  ILE LYS TYR PHE ARG GLY SER GLU LEU GLN ASN TYR PHE          
SEQRES  13 P  608  THR LYS MET LEU GLU ASP ASP ILE LYS ALA ILE ILE LYS          
SEQRES  14 P  608  PRO GLN TYR VAL ASP ASN ILE PRO ARG ALA ILE LYS GLY          
SEQRES  15 P  608  PRO VAL GLN LYS VAL GLY GLU LEU LEU LYS LEU ARG MET          
SEQRES  16 P  608  GLU LYS SER PRO GLU ASP VAL LYS ARG TYR ILE LYS ILE          
SEQRES  17 P  608  LEU GLN LEU GLU ASN VAL LEU LYS ARG ASP ILE GLU LYS          
SEQRES  18 P  608  LEU SER GLY GLY GLU LEU GLN ARG PHE ALA ILE GLY MET          
SEQRES  19 P  608  SER CYS VAL GLN GLU ALA ASP VAL TYR MET PHE ASP GLU          
SEQRES  20 P  608  PRO SER SER TYR LEU ASP VAL LYS GLN ARG LEU ASN ALA          
SEQRES  21 P  608  ALA GLN ILE ILE ARG SER LEU LEU ALA PRO THR LYS TYR          
SEQRES  22 P  608  VAL ILE CYS VAL GLU HIS ASP LEU SER VAL LEU ASP TYR          
SEQRES  23 P  608  LEU SER ASP PHE VAL CYS ILE ILE TYR GLY VAL PRO SER          
SEQRES  24 P  608  VAL TYR GLY VAL VAL THR LEU PRO ALA SER VAL ARG GLU          
SEQRES  25 P  608  GLY ILE ASN ILE PHE LEU ASP GLY HIS ILE PRO ALA GLU          
SEQRES  26 P  608  ASN LEU ARG PHE ARG THR GLU ALA LEU GLN PHE ARG ILE          
SEQRES  27 P  608  ALA ASP ALA THR GLU ASP LEU GLN ASN ASP SER ALA SER          
SEQRES  28 P  608  ARG ALA PHE SER TYR PRO SER LEU LYS LYS THR GLN GLY          
SEQRES  29 P  608  ASP PHE VAL LEU ASN VAL GLU GLU GLY GLU PHE SER ASP          
SEQRES  30 P  608  SER GLU ILE LEU VAL MET MET GLY GLU ASN GLY THR GLY          
SEQRES  31 P  608  LYS THR THR LEU ILE LYS LEU LEU ALA GLY ALA LEU LYS          
SEQRES  32 P  608  PRO ASP GLU GLY GLN ASP ILE PRO LYS LEU ASN VAL SER          
SEQRES  33 P  608  MET LYS PRO GLN LYS ILE ALA PRO LYS PHE PRO GLY THR          
SEQRES  34 P  608  VAL ARG GLN LEU PHE PHE LYS LYS ILE ARG GLY GLN PHE          
SEQRES  35 P  608  LEU ASN PRO GLN PHE GLN THR ASP VAL VAL LYS PRO LEU          
SEQRES  36 P  608  ARG ILE ASP ASP ILE ILE ASP GLN GLU VAL GLN HIS LEU          
SEQRES  37 P  608  SER GLY GLY GLU LEU GLN ARG VAL ALA ILE VAL LEU ALA          
SEQRES  38 P  608  LEU GLY ILE PRO ALA ASP ILE TYR LEU ILE ASP GLU PRO          
SEQRES  39 P  608  SER ALA TYR LEU ASP SER GLU GLN ARG ILE ILE CYS SER          
SEQRES  40 P  608  LYS VAL ILE ARG ARG PHE ILE LEU HIS ASN LYS LYS THR          
SEQRES  41 P  608  ALA PHE ILE VAL GLU HIS ASP PHE ILE MET ALA THR TYR          
SEQRES  42 P  608  LEU ALA ASP LYS VAL ILE VAL PHE GLU GLY ILE PRO SER          
SEQRES  43 P  608  LYS ASN ALA HIS ALA ARG ALA PRO GLU SER LEU LEU THR          
SEQRES  44 P  608  GLY CYS ASN ARG PHE LEU LYS ASN LEU ASN VAL THR PHE          
SEQRES  45 P  608  ARG ARG ASP PRO ASN SER PHE ARG PRO ARG ILE ASN LYS          
SEQRES  46 P  608  LEU ASP SER GLN MET ASP LYS GLU GLN LYS SER SER GLY          
SEQRES  47 P  608  ASN TYR PHE PHE LEU ASP ASN THR GLY ILE                      
SEQRES   1 X  282  ASP ASP LYS PHE GLY PHE ILE VAL MET ASP GLY GLN GLY          
SEQRES   2 X  282  THR LEU PHE GLY SER VAL SER GLY ASN THR ARG THR VAL          
SEQRES   3 X  282  LEU HIS LYS PHE THR VAL ASP LEU PRO LYS LYS HIS GLY          
SEQRES   4 X  282  ARG GLY GLY GLN SER ALA LEU ARG PHE ALA ARG LEU ARG          
SEQRES   5 X  282  GLU GLU LYS ARG HIS ASN TYR VAL ARG LYS VAL ALA GLU          
SEQRES   6 X  282  VAL ALA VAL GLN ASN PHE ILE THR ASN ASP LYS VAL ASN          
SEQRES   7 X  282  VAL LYS GLY LEU ILE LEU ALA GLY SER ALA ASP PHE LYS          
SEQRES   8 X  282  THR ASP LEU ALA LYS SER GLU LEU PHE ASP PRO ARG LEU          
SEQRES   9 X  282  ALA CYS LYS VAL ILE SER ILE VAL ASP VAL SER TYR GLY          
SEQRES  10 X  282  GLY GLU ASN GLY PHE ASN GLN ALA ILE GLU LEU SER ALA          
SEQRES  11 X  282  GLU ALA LEU ALA ASN VAL LYS TYR VAL GLN GLU LYS LYS          
SEQRES  12 X  282  LEU LEU GLU ALA TYR PHE ASP GLU ILE SER GLN ASP THR          
SEQRES  13 X  282  GLY LYS PHE CYS TYR GLY ILE ASP ASP THR LEU LYS ALA          
SEQRES  14 X  282  LEU ASP LEU GLY ALA VAL GLU LYS LEU ILE VAL PHE GLU          
SEQRES  15 X  282  ASN LEU GLU THR ILE ARG TYR THR PHE LYS ASP ALA GLU          
SEQRES  16 X  282  ASP ASN GLU VAL ILE LYS PHE ALA GLU PRO GLU ALA LYS          
SEQRES  17 X  282  ASP LYS SER PHE ALA ILE ASP LYS ALA THR GLY GLN GLU          
SEQRES  18 X  282  MET ASP VAL VAL SER GLU GLU PRO LEU ILE GLU TRP LEU          
SEQRES  19 X  282  ALA ALA ASN TYR LYS ASN PHE GLY ALA THR LEU GLU PHE          
SEQRES  20 X  282  ILE THR ASP LYS SER SER GLU GLY ALA GLN PHE VAL THR          
SEQRES  21 X  282  GLY PHE GLY GLY ILE GLY ALA MET LEU ARG TYR LYS VAL          
SEQRES  22 X  282  ASN PHE GLU GLN LEU VAL ASP GLU SER                          
HET    ATP  P1609      31                                                       
HET    SF4  P1610       8                                                       
HET    SF4  P1611       8                                                       
HET    ADP  P1612      27                                                       
HET     MG  P1613       1                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4  SF4    2(FE4 S4)                                                    
FORMUL   6  ADP    C10 H15 N5 O10 P2                                            
FORMUL   7   MG    MG 2+                                                        
FORMUL   8  HOH   *(H2 O)                                                       
HELIX    1   1 CYS P   29  GLY P   35  1                                   7    
HELIX    2   2 GLY P   59  CYS P   65  1                                   7    
HELIX    3   3 GLY P  115  GLY P  125  1                                  11    
HELIX    4   4 GLU P  139  PHE P  147  1                                   9    
HELIX    5   5 GLU P  151  ASP P  162  1                                  12    
HELIX    6   6 ASN P  175  ILE P  180  1                                   6    
HELIX    7   7 LYS P  186  MET P  195  1                                  10    
HELIX    8   8 SER P  198  GLN P  210  1                                  13    
HELIX    9   9 GLU P  212  LYS P  216  5                                   5    
HELIX   10  10 SER P  223  GLN P  238  1                                  16    
HELIX   11  11 ASP P  253  SER P  266  1                                  14    
HELIX   12  12 LEU P  267  ALA P  269  5                                   3    
HELIX   13  13 ASP P  280  SER P  288  1                                   9    
HELIX   14  14 VAL P  310  GLY P  320  1                                  11    
HELIX   15  15 GLY P  390  GLY P  400  1                                  11    
HELIX   16  16 THR P  429  ILE P  438  1                                  10    
HELIX   17  17 ARG P  439  LEU P  443  5                                   5    
HELIX   18  18 ASN P  444  VAL P  451  1                                   8    
HELIX   19  19 VAL P  451  ARG P  456  1                                   6    
HELIX   20  20 SER P  469  LEU P  482  1                                  14    
HELIX   21  21 ASP P  499  LYS P  518  1                                  20    
HELIX   22  22 ASP P  527  ALA P  535  1                                   9    
HELIX   23  23 LEU P  557  ASN P  569  1                                  13    
HELIX   24  24 SER P  588  GLY P  598  1                                  11    
HELIX   25  25 LEU X  185  ILE X  211  1                                  27    
HELIX   26  26 ALA X  227  PHE X  229  5                                   3    
HELIX   27  27 LYS X  230  LYS X  235  1                                   6    
HELIX   28  28 LEU X  243  CYS X  245  5                                   3    
HELIX   29  29 GLY X  256  LEU X  267  1                                  12    
HELIX   30  30 SER X  268  GLU X  280  1                                  13    
HELIX   31  31 GLU X  280  ILE X  291  1                                  12    
HELIX   32  32 TYR X  300  LEU X  311  1                                  12    
HELIX   33  33 ALA X  346  PHE X  351  1                                   6    
HELIX   34  34 LEU X  369  ALA X  375  1                                   7    
HELIX   35  35 ASN X  376  GLY X  381  1                                   6    
HELIX   36  36 GLU X  393  GLY X  400  1                                   8    
SHEET    1  PA 2 SER P   6  VAL P  11  0                                        
SHEET    2  PA 2 ILE P  70  LEU P  75 -1  O  GLN P  71   N  ILE P  10           
SHEET    1  PB 2 ILE P  39  THR P  42  0                                        
SHEET    2  PB 2 ILE P  47  ILE P  50 -1  O  ILE P  47   N  THR P  42           
SHEET    1  PC 2 VAL P  83  ARG P  86  0                                        
SHEET    2  PC 2 LYS P  93  HIS P  95 -1  O  LEU P  94   N  THR P  84           
SHEET    1  PD 6 ILE P 167  LYS P 169  0                                        
SHEET    2  PD 6 VAL P 242  ASP P 246  1  O  VAL P 242   N  ILE P 167           
SHEET    3  PD 6 TYR P 273  VAL P 277  1  O  TYR P 273   N  TYR P 243           
SHEET    4  PD 6 VAL P 105  VAL P 109  1  O  LEU P 106   N  CYS P 276           
SHEET    5  PD 6 PHE P 290  TYR P 295  1  O  PHE P 290   N  GLY P 107           
SHEET    6  PD 6 VAL P 303  VAL P 304 -1  O  VAL P 303   N  TYR P 295           
SHEET    1  PE 6 ILE P 167  LYS P 169  0                                        
SHEET    2  PE 6 VAL P 242  ASP P 246  1  O  VAL P 242   N  ILE P 167           
SHEET    3  PE 6 TYR P 273  VAL P 277  1  O  TYR P 273   N  TYR P 243           
SHEET    4  PE 6 VAL P 105  VAL P 109  1  O  LEU P 106   N  CYS P 276           
SHEET    5  PE 6 PHE P 290  TYR P 295  1  O  PHE P 290   N  GLY P 107           
SHEET    6  PE 6 ALA P 308  SER P 309 -1  O  ALA P 308   N  VAL P 291           
SHEET    1  PF 2 VAL P 303  VAL P 304  0                                        
SHEET    2  PF 2 PHE P 290  TYR P 295 -1  O  TYR P 295   N  VAL P 303           
SHEET    1  PG 2 HIS P 321  ILE P 322  0                                        
SHEET    2  PG 2 LEU P 327  ARG P 328 -1  O  LEU P 327   N  ILE P 322           
SHEET    1  PH 2 SER P 355  TYR P 356  0                                        
SHEET    2  PH 2 GLY P 373  GLU P 374 -1  O  GLY P 373   N  TYR P 356           
SHEET    1  PI 4 LEU P 359  THR P 362  0                                        
SHEET    2  PI 4 VAL P 367  VAL P 370 -1  O  LEU P 368   N  LYS P 361           
SHEET    3  PI 4 ASN P 548  HIS P 550  1  O  ALA P 549   N  ASN P 369           
SHEET    4  PI 4 GLU P 542  ILE P 544 -1  O  GLU P 542   N  HIS P 550           
SHEET    1  PJ 6 VAL P 415  LYS P 418  0                                        
SHEET    2  PJ 6 ILE P 488  ASP P 492  1  O  ILE P 488   N  SER P 416           
SHEET    3  PJ 6 THR P 520  VAL P 524  1  O  THR P 520   N  TYR P 489           
SHEET    4  PJ 6 ILE P 380  MET P 384  1  O  LEU P 381   N  ILE P 523           
SHEET    5  PJ 6 LYS P 537  VAL P 540  1  O  LYS P 537   N  VAL P 382           
SHEET    6  PJ 6 GLU P 555  SER P 556 -1  O  GLU P 555   N  VAL P 538           
SHEET    1  XA 5 THR X 162  PHE X 169  0                                        
SHEET    2  XA 5 THR X 153  SER X 159 -1  O  THR X 153   N  PHE X 169           
SHEET    3  XA 5 PHE X 143  MET X 148 -1  O  PHE X 143   N  VAL X 158           
SHEET    4  XA 5 LEU X 221  ALA X 224  1  O  ILE X 222   N  ILE X 146           
SHEET    5  XA 5 VAL X 247  VAL X 251  1  N  ILE X 248   O  LEU X 221           
SHEET    1  XB 4 PHE X 298  CYS X 299  0                                        
SHEET    2  XB 4 ALA X 406  LEU X 408 -1  O  ALA X 406   N  CYS X 299           
SHEET    3  XB 4 VAL X 314  ILE X 318 -1  N  GLU X 315   O  MET X 407           
SHEET    4  XB 4 LEU X 384  GLU X 385  1  N  GLU X 385   O  LEU X 317           
SHEET    1  XC 3 ASN X 336  PHE X 341  0                                        
SHEET    2  XC 3 ILE X 326  LYS X 331 -1  O  ILE X 326   N  PHE X 341           
SHEET    3  XC 3 VAL X 363  PRO X 368 -1  N  VAL X 364   O  THR X 329           
LINK         SG  CYS P  16                FE4  SF4 P1611     1555   1555  2.42  
LINK         SG  CYS P  21                FE2  SF4 P1611     1555   1555  1.74  
LINK         SG  CYS P  55                FE2  SF4 P1610     1555   1555  2.62  
LINK         CB  CYS P  61                FE3  SF4 P1610     1555   1555  2.18  
LINK         OG  SER P 117                MG    MG P1613     1555   1555  1.19  
LINK         O2B ATP P1609                MG    MG P1613     1555   1555  2.20  
LINK         O1G ATP P1609                MG    MG P1613     1555   1555  2.67  
SITE     1 AC1 12 HOH P1903  TYR P  87  PHE P  92  ASN P 112                    
SITE     2 AC1 12 GLY P 113  ILE P 114  GLY P 115  LYS P 116                    
SITE     3 AC1 12 SER P 117  THR P 118  SER P 299   MG P1613                    
SITE     1 AC2  8 CYS P  29  CYS P  38  ILE P  50  CYS P  55                    
SITE     2 AC2  8 CYS P  58  GLY P  59  CYS P  61  ILE P  72                    
SITE     1 AC3 11 CYS P  16  LYS P  17  PRO P  18  CYS P  21                    
SITE     2 AC3 11 ARG P  22  GLU P  24  CYS P  25  CYS P  65                    
SITE     3 AC3 11 PRO P  66  PHE P  67  ALA P  69                               
SITE     1 AC4 12 ARG P 217  GLN P 363  PHE P 366  GLU P 386                    
SITE     2 AC4 12 ASN P 387  GLY P 388  THR P 389  GLY P 390                    
SITE     3 AC4 12 LYS P 391  THR P 392  THR P 393  SER P 546                    
SITE     1 AC5  3 SER P 117  GLN P 171  ATP P1609                               
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