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Database: PDB
Entry: 1C7U
LinkDB: 1C7U
Original site: 1C7U 
HEADER    TRANSCRIPTION/DNA                       17-MAR-00   1C7U              
TITLE     COMPLEX OF THE DNA BINDING CORE DOMAIN OF THE TRANSCRIPTION           
TITLE    2 FACTOR MEF2A WITH A 20MER OLIGONUCLEOTIDE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOCYTE-SPECIFIC ENHANCER FACTOR 2A, C4 FORM;              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 2-86;                                             
COMPND   5 SYNONYM: TRANSCRIPTION FACTOR MEF2A;                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-                                                        
COMPND   9 D(*CP*TP*CP*GP*GP*CP*TP*AP*TP*TP*AP*AP*TP*AP*GP*CP*CP*GP*AP          
COMPND  10 *G)-3';                                                              
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BE23;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET11A;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    DNA BINDING PROTEIN, TRANSCRIPTION FACTOR, MADS-BOX, SAM              
KEYWDS   2 DOMAIN, TRANSCRIPTION/DNA COMPLEX                                    
EXPDTA    SOLUTION NMR                                                          
AUTHOR    G.M.CLORE,K.HUANG                                                     
REVDAT   4   24-FEB-09 1C7U    1       VERSN                                    
REVDAT   3   05-APR-05 1C7U    1       JRNL   COMPND REMARK                     
REVDAT   2   14-JUN-00 1C7U    1       JRNL                                     
REVDAT   1   27-MAR-00 1C7U    0                                                
JRNL        AUTH   K.HUANG,J.M.LOUIS,L.DONALDSON,F.L.LIM,                       
JRNL        AUTH 2 A.D.SHARROCKS,G.M.CLORE                                      
JRNL        TITL   SOLUTION STRUCTURE OF THE MEF2A-DNA COMPLEX:                 
JRNL        TITL 2 STRUCTURAL BASIS FOR THE MODULATION OF DNA BENDING           
JRNL        TITL 3 AND SPECIFICITY BY MADS-BOX TRANSCRIPTION FACTORS            
JRNL        REF    EMBO J.                       V.  19  2615 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   10835359                                                     
JRNL        DOI    10.1093/EMBOJ/19.11.2615                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR/CNS                                           
REMARK   3   AUTHORS     : BRUNGER,ADAMS, CLORE, DELANO, GROS, GROSSE-          
REMARK   3                 KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,          
REMARK   3                 READ, RICE WARREN                                    
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING        
REMARK   3  PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING      
REMARK   3  THE PROGRAM XPLOR/CNS MODIFIED TO INCORPORATE COUPLING CONSTANT     
REMARK   3  RESTRAINTS (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104,     
REMARK   3  99-103), CARBON CHEMICAL SHIFT RESTRAINTS, (KUSZEWSKI ET AL.        
REMARK   3  (1995) J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, RESIDUAL    
REMARK   3  DIPOLAR COUPLING RESTRAINTS (CLORE ET AL. J. MAGN. RESON 131,       
REMARK   3  159-162 (1998); J. MAGN 133, 216-221 (1998)), AND A                 
REMARK   3  CONFORMATIONAL DATABASE POTENTIAL FOR PROTEINS AND NUCLEIC ACIDS    
REMARK   3  (KUSZEWSKI ET AL. PROTEIN SCI. 5, 1067-1080 (1996); J. MAGN.        
REMARK   3  RESON 125, 171-177 (1997)).                                         
REMARK   3                                                                      
REMARK   3  IN THIS ENTRY THE LAST NUMERICAL COLUMN IS THE RMS OF THE           
REMARK   3  35 INDIVIDUAL SIMULATED ANNEALING STRUCTURES ABOUT THE              
REMARK   3  MEAN COORDINATE POSITIONS.  THE LATTER ARE OBTAINED                 
REMARK   3  BY TAKING THE AVERAGE OF THE 35 SIMULATED ANNEALING                 
REMARK   3  STRUCTURES BEST-FITTED TO RESIDUES 1-73 AND 101-173                 
REMARK   3  OF THE PROTEIN AND RESIDUES 201-240 OF THE DNA.                     
REMARK   3  RESIDUES 74-85 AND 174-185 ARE DISORDERED IN SOLUTION               
REMARK   3  AND ARE THEREFORE NOT INCLUDED IN THE COORDINATES.                  
REMARK   3  THE RESTRAINED MINIMIZED MEAN STRUCTURE IS OBTAINED                 
REMARK   3  BY RESTRAINED REGULARIZATION OF THE AVERAGE COORDINATES             
REMARK   3  AGAINST THE SAME TARGET FUNCTION USED TO CALCULATE THE              
REMARK   3  SIMULATED ANNEALING STRUCTURES.                                     
REMARK   4                                                                      
REMARK   4 1C7U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB001443.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 308                                
REMARK 210  PH                             : 6.6                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : (1) TRIPLE RESONANCE FOR           
REMARK 210                                   ASSIGNMENT OF PROTEIN. (2)         
REMARK 210                                   QUANTITATIVE J CORRELATION FOR     
REMARK 210                                   COUPLING CONSTANTS. (3) 3D AND     
REMARK 210                                   4D HETERONUCLEAR SEPARATED AND     
REMARK 210                                   FILTERED NOE EXPTS. (4) 2D 12C     
REMARK 210                                   -FILTERED EXPERIMENTS FOR DNA      
REMARK 210                                   ASSIGNMENTS. (5) IPAP EXPTS        
REMARK 210                                   FOR DIPOLAR COUPLINGS DIPOLAR      
REMARK 210                                   COUPLINGS WERE MEASURED IN A       
REMARK 210                                   BICELLE LIQUID CRYSTALLINE         
REMARK 210                                   MEDIUM.                            
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ, 600 MHZ, 750 MHZ          
REMARK 210  SPECTROMETER MODEL             : DMX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CNS/X-PLOR                         
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 35                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : REGULARIZED MEAN STRUCTURE         
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: SOLVED BY MULTI HETERONUCLEAR NMR AND IS BASED ON 4560       
REMARK 210  EXPERIMENTAL NMR RESTRAINTS (I.E. 2280 UNIQUE ONES SINCE            
REMARK 210  PROTEIN IS A HOMODIMER AND DNA IS PALINDROMIC). NOE                 
REMARK 210  RESTRAINTS: (A) PROTEIN: 664 SEQUENTIAL, 504 MEDIUM RANGE, 212      
REMARK 210  LONG RANGE, 616 INTRARESIDUE, 174 INTERSUBUNIT. (B) DNA: 428        
REMARK 210  INTRARESIDUE, 196 SEQUENTIAL INTRASTRAND, 24 INTERSTRAND. (C)       
REMARK 210  PROTEIN- DNA 168. H-BOND RESTRAINTS: PROTEIN 138, DNA 120.          
REMARK 210  TORSION ANGLE RESTRAINTS: PROTEIN 480 (142 PHI, 142 PSI, 112        
REMARK 210  CHI1, 68 CHI2, 16 CHI3), DNA 228. THREE-BOND HN-HALPHA              
REMARK 210  COUPLING CONSTANTS: 72. SECONDARY 13C SHIFTS: 140 13CALPHA,         
REMARK 210  140 13CBETA. DIPOLAR COUPLINGS: 1DNH PROTEIN: 70, 1DCH DNA 70.      
REMARK 210  REPULSIVE RESTRAINTS: 106                                           
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;                   
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                            
REMARK 465     RES C SSSEQI                                                     
REMARK 465     HIS A    75                                                      
REMARK 465     GLU A    76                                                      
REMARK 465     SER A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     ASN A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ASP A    82                                                      
REMARK 465     ILE A    83                                                      
REMARK 465     VAL A    84                                                      
REMARK 465     GLU A    85                                                      
REMARK 465     HIS B   175                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     ARG B   178                                                      
REMARK 465     THR B   179                                                      
REMARK 465     ASN B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     ASP B   182                                                      
REMARK 465     ILE B   183                                                      
REMARK 465     VAL B   184                                                      
REMARK 465     GLU B   185                                                      
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     DT C 209   C5     DT C 209   C7      0.038                       
REMARK 500     DT C 210   C5     DT C 210   C7      0.037                       
REMARK 500     DT D 229   C5     DT D 229   C7      0.038                       
REMARK 500     DT D 230   C5     DT D 230   C7      0.037                       
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     DC C 201   C4' -  C3' -  C2' ANGL. DEV. =   7.6 DEGREES          
REMARK 500     DC C 201   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DT C 202   C4' -  C3' -  C2' ANGL. DEV. =   6.4 DEGREES          
REMARK 500     DC C 203   C4' -  C3' -  C2' ANGL. DEV. =   7.0 DEGREES          
REMARK 500     DG C 204   C4' -  C3' -  C2' ANGL. DEV. =   7.7 DEGREES          
REMARK 500     DG C 204   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DG C 205   C4' -  C3' -  C2' ANGL. DEV. =   6.2 DEGREES          
REMARK 500     DG C 205   O4' -  C1' -  C2' ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DC C 206   C4' -  C3' -  C2' ANGL. DEV. =   7.2 DEGREES          
REMARK 500     DC C 206   O4' -  C1' -  C2' ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DT C 207   C4' -  C3' -  C2' ANGL. DEV. =   7.0 DEGREES          
REMARK 500     DA C 208   C4' -  C3' -  C2' ANGL. DEV. =   5.9 DEGREES          
REMARK 500     DA C 208   O4' -  C1' -  C2' ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DT C 209   C4' -  C3' -  C2' ANGL. DEV. =   7.1 DEGREES          
REMARK 500     DT C 209   O4' -  C1' -  C2' ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DT C 210   C4' -  C3' -  C2' ANGL. DEV. =   8.0 DEGREES          
REMARK 500     DT C 210   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DA C 211   C4' -  C3' -  C2' ANGL. DEV. =   8.4 DEGREES          
REMARK 500     DA C 211   O4' -  C1' -  C2' ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DA C 212   C4' -  C3' -  C2' ANGL. DEV. =   7.8 DEGREES          
REMARK 500     DT C 213   C4' -  C3' -  C2' ANGL. DEV. =   7.3 DEGREES          
REMARK 500     DT C 213   O4' -  C1' -  C2' ANGL. DEV. =   3.8 DEGREES          
REMARK 500     DA C 214   C4' -  C3' -  C2' ANGL. DEV. =   6.8 DEGREES          
REMARK 500     DG C 215   C4' -  C3' -  C2' ANGL. DEV. =   7.1 DEGREES          
REMARK 500     DC C 216   C4' -  C3' -  C2' ANGL. DEV. =   6.5 DEGREES          
REMARK 500     DC C 217   C4' -  C3' -  C2' ANGL. DEV. =   6.8 DEGREES          
REMARK 500     DG C 218   C4' -  C3' -  C2' ANGL. DEV. =   6.5 DEGREES          
REMARK 500     DA C 219   C4' -  C3' -  C2' ANGL. DEV. =   6.2 DEGREES          
REMARK 500     DG C 220   C4' -  C3' -  C2' ANGL. DEV. =   5.5 DEGREES          
REMARK 500     DC D 221   C4' -  C3' -  C2' ANGL. DEV. =   7.5 DEGREES          
REMARK 500     DC D 221   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DT D 222   C4' -  C3' -  C2' ANGL. DEV. =   6.4 DEGREES          
REMARK 500     DC D 223   C4' -  C3' -  C2' ANGL. DEV. =   7.0 DEGREES          
REMARK 500     DG D 224   C4' -  C3' -  C2' ANGL. DEV. =   7.8 DEGREES          
REMARK 500     DG D 224   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DG D 225   C4' -  C3' -  C2' ANGL. DEV. =   6.3 DEGREES          
REMARK 500     DG D 225   O4' -  C1' -  C2' ANGL. DEV. =   3.4 DEGREES          
REMARK 500     DC D 226   C4' -  C3' -  C2' ANGL. DEV. =   7.2 DEGREES          
REMARK 500     DC D 226   O4' -  C1' -  C2' ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DT D 227   C4' -  C3' -  C2' ANGL. DEV. =   6.9 DEGREES          
REMARK 500     DA D 228   C4' -  C3' -  C2' ANGL. DEV. =   5.9 DEGREES          
REMARK 500     DA D 228   O4' -  C1' -  C2' ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DT D 229   C4' -  C3' -  C2' ANGL. DEV. =   7.2 DEGREES          
REMARK 500     DT D 229   O4' -  C1' -  C2' ANGL. DEV. =   3.5 DEGREES          
REMARK 500     DT D 230   C4' -  C3' -  C2' ANGL. DEV. =   8.0 DEGREES          
REMARK 500     DT D 230   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DA D 231   C4' -  C3' -  C2' ANGL. DEV. =   8.5 DEGREES          
REMARK 500     DA D 232   C4' -  C3' -  C2' ANGL. DEV. =   7.8 DEGREES          
REMARK 500     DT D 233   C4' -  C3' -  C2' ANGL. DEV. =   7.4 DEGREES          
REMARK 500     DT D 233   O4' -  C1' -  C2' ANGL. DEV. =   3.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 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    ARG A   2       -9.41    -57.91                                   
REMARK 500    ASN A  51       74.26     67.48                                   
REMARK 500    ASP A  60      107.37     49.99                                   
REMARK 500    ARG B 102       -9.31    -57.92                                   
REMARK 500    ASN B 151       74.19     66.50                                   
REMARK 500    ASP B 160      107.40     50.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1C7U A    1    85  UNP    Q02078   MEF2A_HUMAN      2     86             
DBREF  1C7U B  101   185  UNP    Q02078   MEF2A_HUMAN      2     86             
DBREF  1C7U C  201   220  PDB    1C7U     1C7U           201    220             
DBREF  1C7U D  221   240  PDB    1C7U     1C7U           221    240             
SEQADV 1C7U ALA A   38  UNP  Q02078    CYS    39 CONFLICT                       
SEQADV 1C7U ALA A   40  UNP  Q02078    CYS    41 CONFLICT                       
SEQADV 1C7U ALA B  138  UNP  Q02078    CYS    39 CONFLICT                       
SEQADV 1C7U ALA B  140  UNP  Q02078    CYS    41 CONFLICT                       
SEQRES   1 A   85  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 A   85  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 A   85  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU ALA ASP          
SEQRES   4 A   85  ALA GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 A   85  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 A   85  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 A   85  THR ASN SER ASP ILE VAL GLU                                  
SEQRES   1 B   85  GLY ARG LYS LYS ILE GLN ILE THR ARG ILE MET ASP GLU          
SEQRES   2 B   85  ARG ASN ARG GLN VAL THR PHE THR LYS ARG LYS PHE GLY          
SEQRES   3 B   85  LEU MET LYS LYS ALA TYR GLU LEU SER VAL LEU ALA ASP          
SEQRES   4 B   85  ALA GLU ILE ALA LEU ILE ILE PHE ASN SER SER ASN LYS          
SEQRES   5 B   85  LEU PHE GLN TYR ALA SER THR ASP MET ASP LYS VAL LEU          
SEQRES   6 B   85  LEU LYS TYR THR GLU TYR ASN GLU PRO HIS GLU SER ARG          
SEQRES   7 B   85  THR ASN SER ASP ILE VAL GLU                                  
SEQRES   1 C   20   DC  DT  DC  DG  DG  DC  DT  DA  DT  DT  DA  DA  DT          
SEQRES   2 C   20   DA  DG  DC  DC  DG  DA  DG                                  
SEQRES   1 D   20   DC  DT  DC  DG  DG  DC  DT  DA  DT  DT  DA  DA  DT          
SEQRES   2 D   20   DA  DG  DC  DC  DG  DA  DG                                  
HELIX    1   1 ASP A   12  ASP A   39  1                                  28    
HELIX    2   2 ASP A   60  ASN A   72  1                                  13    
HELIX    3   3 ASP B  112  ASP B  139  1                                  28    
HELIX    4   4 ASP B  160  ASN B  172  1                                  13    
SHEET    1   A 4 LYS A  52  TYR A  56  0                                        
SHEET    2   A 4 ILE A  42  ASN A  48 -1  N  LEU A  44   O  TYR A  56           
SHEET    3   A 4 GLU B 141  ASN B 148 -1  O  GLU B 141   N  PHE A  47           
SHEET    4   A 4 LYS B 152  TYR B 156 -1  O  LYS B 152   N  ASN B 148           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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