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Database: PDB
Entry: 6G6L
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Original site: 6G6L 
HEADER    APOPTOSIS                               01-APR-18   6G6L              
TITLE     THE CRYSTAL STRUCTURES OF HUMAN MYC:MAX BHLHZIP COMPLEX               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYC PROTO-ONCOGENE PROTEIN;                                
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 39,BHLHE39,PROTO-    
COMPND   5 ONCOGENE C-MYC,TRANSCRIPTION FACTOR P64;                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEIN MAX;                                               
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 SYNONYM: CLASS D BASIC HELIX-LOOP-HELIX PROTEIN 4,BHLHD4,MYC-        
COMPND  11 ASSOCIATED FACTOR X;                                                 
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 GENE: MYC, BHLHE39;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: MAX, BHLHD4;                                                   
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MYC/MAX, APOPTOSIS                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.ALLEN,G.ZINZALLA                                                  
REVDAT   3   31-JUL-19 6G6L    1       JRNL                                     
REVDAT   2   24-JUL-19 6G6L    1       JRNL                                     
REVDAT   1   10-APR-19 6G6L    0                                                
JRNL        AUTH   S.SAMMAK,N.HAMDANI,F.GORREC,M.D.ALLEN,S.M.V.FREUND,          
JRNL        AUTH 2 M.BYCROFT,G.ZINZALLA                                         
JRNL        TITL   CRYSTAL STRUCTURES AND NUCLEAR MAGNETIC RESONANCE STUDIES OF 
JRNL        TITL 2 THE APO FORM OF THE C-MYC:MAX BHLHZIP COMPLEX REVEAL A       
JRNL        TITL 3 HELICAL BASIC REGION IN THE ABSENCE OF DNA.                  
JRNL        REF    BIOCHEMISTRY                  V.  58  3144 2019              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   31260268                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.9B00296                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41512                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1979                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.1651 -  5.2998    0.75     2637   148  0.2169 0.2672        
REMARK   3     2  5.2998 -  4.2075    0.81     2861   113  0.1735 0.2364        
REMARK   3     3  4.2075 -  3.6759    0.82     2904   143  0.1693 0.2262        
REMARK   3     4  3.6759 -  3.3400    0.73     2582   142  0.2012 0.2696        
REMARK   3     5  3.3400 -  3.1006    0.80     2751   157  0.2162 0.2354        
REMARK   3     6  3.1006 -  2.9178    0.82     2920   158  0.2288 0.2626        
REMARK   3     7  2.9178 -  2.7717    0.84     2983    92  0.2385 0.2891        
REMARK   3     8  2.7717 -  2.6511    0.84     2989   141  0.2586 0.3151        
REMARK   3     9  2.6511 -  2.5490    0.86     2967   157  0.2400 0.3145        
REMARK   3    10  2.5490 -  2.4611    0.76     2686   149  0.2412 0.2956        
REMARK   3    11  2.4611 -  2.3841    0.77     2715   141  0.2512 0.3144        
REMARK   3    12  2.3841 -  2.3160    0.80     2799   120  0.2562 0.3127        
REMARK   3    13  2.3160 -  2.2550    0.82     2880   154  0.2638 0.3029        
REMARK   3    14  2.2550 -  2.2000    0.82     2859   164  0.2726 0.2980        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5066                                  
REMARK   3   ANGLE     :  0.510           6768                                  
REMARK   3   CHIRALITY :  0.034            729                                  
REMARK   3   PLANARITY :  0.003            884                                  
REMARK   3   DIHEDRAL  :  1.978           3234                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6G6L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009484.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979507                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% W/V PEG 8000, 20% V/V ETHYLENE       
REMARK 280  GLYCOL, 15% PEG 8000 15, 0.2M AMMONIUM SULFATE, PH 7, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 290K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   891                                                      
REMARK 465     HIS A   892                                                      
REMARK 465     HIS A   893                                                      
REMARK 465     HIS A   894                                                      
REMARK 465     HIS A   895                                                      
REMARK 465     HIS A   896                                                      
REMARK 465     HIS A   897                                                      
REMARK 465     GLU A   898                                                      
REMARK 465     GLU A   899                                                      
REMARK 465     ASN A   900                                                      
REMARK 465     VAL A   901                                                      
REMARK 465     LYS A   902                                                      
REMARK 465     ARG A   903                                                      
REMARK 465     ARG A   904                                                      
REMARK 465     THR A   905                                                      
REMARK 465     HIS A   906                                                      
REMARK 465     MET B   200                                                      
REMARK 465     ALA B   201                                                      
REMARK 465     ASP B   202                                                      
REMARK 465     LYS B   203                                                      
REMARK 465     ARG B   204                                                      
REMARK 465     ALA B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     ASN B   208                                                      
REMARK 465     ALA B   209                                                      
REMARK 465     LEU B   210                                                      
REMARK 465     GLU B   211                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     GLU B   282                                                      
REMARK 465     MET C   891                                                      
REMARK 465     HIS C   892                                                      
REMARK 465     HIS C   893                                                      
REMARK 465     HIS C   894                                                      
REMARK 465     HIS C   895                                                      
REMARK 465     HIS C   896                                                      
REMARK 465     HIS C   897                                                      
REMARK 465     GLU C   898                                                      
REMARK 465     GLU C   899                                                      
REMARK 465     ASN C   900                                                      
REMARK 465     VAL C   901                                                      
REMARK 465     LYS C   902                                                      
REMARK 465     ARG C   903                                                      
REMARK 465     ARG C   904                                                      
REMARK 465     THR C   905                                                      
REMARK 465     MET D   200                                                      
REMARK 465     ALA D   201                                                      
REMARK 465     ASP D   202                                                      
REMARK 465     LYS D   203                                                      
REMARK 465     ARG D   204                                                      
REMARK 465     ALA D   205                                                      
REMARK 465     HIS D   206                                                      
REMARK 465     HIS D   207                                                      
REMARK 465     ASN D   208                                                      
REMARK 465     ALA D   209                                                      
REMARK 465     LEU D   210                                                      
REMARK 465     GLU D   282                                                      
REMARK 465     MET E   891                                                      
REMARK 465     HIS E   892                                                      
REMARK 465     HIS E   893                                                      
REMARK 465     HIS E   894                                                      
REMARK 465     HIS E   895                                                      
REMARK 465     HIS E   896                                                      
REMARK 465     HIS E   897                                                      
REMARK 465     GLU E   898                                                      
REMARK 465     GLU E   899                                                      
REMARK 465     ASN E   900                                                      
REMARK 465     VAL E   901                                                      
REMARK 465     LYS E   902                                                      
REMARK 465     ARG E   903                                                      
REMARK 465     ARG E   904                                                      
REMARK 465     THR E   905                                                      
REMARK 465     HIS E   906                                                      
REMARK 465     MET F   200                                                      
REMARK 465     ALA F   201                                                      
REMARK 465     ASP F   202                                                      
REMARK 465     LYS F   203                                                      
REMARK 465     ARG F   204                                                      
REMARK 465     ALA F   205                                                      
REMARK 465     HIS F   206                                                      
REMARK 465     HIS F   207                                                      
REMARK 465     ASN F   208                                                      
REMARK 465     ALA F   209                                                      
REMARK 465     LEU F   210                                                      
REMARK 465     GLU F   282                                                      
REMARK 465     MET G   891                                                      
REMARK 465     HIS G   892                                                      
REMARK 465     HIS G   893                                                      
REMARK 465     HIS G   894                                                      
REMARK 465     HIS G   895                                                      
REMARK 465     HIS G   896                                                      
REMARK 465     HIS G   897                                                      
REMARK 465     GLU G   898                                                      
REMARK 465     GLU G   899                                                      
REMARK 465     ASN G   900                                                      
REMARK 465     VAL G   901                                                      
REMARK 465     LYS G   902                                                      
REMARK 465     ARG G   903                                                      
REMARK 465     ARG G   904                                                      
REMARK 465     THR G   905                                                      
REMARK 465     HIS G   906                                                      
REMARK 465     ASN G   907                                                      
REMARK 465     MET H   200                                                      
REMARK 465     ALA H   201                                                      
REMARK 465     ASP H   202                                                      
REMARK 465     LYS H   203                                                      
REMARK 465     ARG H   204                                                      
REMARK 465     ALA H   205                                                      
REMARK 465     HIS H   206                                                      
REMARK 465     HIS H   207                                                      
REMARK 465     ASN H   208                                                      
REMARK 465     ALA H   209                                                      
REMARK 465     LEU H   210                                                      
REMARK 465     GLU H   211                                                      
REMARK 465     ARG H   212                                                      
REMARK 465     LYS H   213                                                      
REMARK 465     ARG H   214                                                      
REMARK 465     GLU H   282                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH F   431     O    HOH F   442              1.88            
REMARK 500   O    HOH G  1148     O    HOH G  1158              1.89            
REMARK 500   O3   SO4 B   302     O    HOH B   401              1.90            
REMARK 500   OD2  ASP F   227     O    HOH F   401              1.92            
REMARK 500   O1   SO4 F   302     O    HOH F   402              1.92            
REMARK 500   O    HOH G  1113     O    HOH G  1165              1.93            
REMARK 500   O    GLU C   930     O    HOH C  1101              1.93            
REMARK 500   O    HOH H   434     O    HOH H   444              1.95            
REMARK 500   O    HOH A  1150     O    HOH G  1161              1.95            
REMARK 500   O    HOH A  1156     O    HOH A  1157              1.96            
REMARK 500   OG   SER D   224     O    HOH D   401              2.01            
REMARK 500   O    HOH A  1137     O    HOH C  1121              2.01            
REMARK 500   O3   SO4 A  1002     O    HOH A  1101              2.01            
REMARK 500   O    HOH A  1149     O    HOH B   437              2.02            
REMARK 500   OD1  ASN A   934     O    HOH A  1102              2.02            
REMARK 500   OE1  GLN E   912     O    HOH E  1101              2.03            
REMARK 500   O    HOH A  1101     O    HOH A  1138              2.04            
REMARK 500   O    HOH H   451     O    HOH H   452              2.06            
REMARK 500   O    HOH G  1177     O    HOH G  1179              2.06            
REMARK 500   O    HOH C  1144     O    HOH D   427              2.06            
REMARK 500   O    HOH C  1160     O    HOH D   439              2.06            
REMARK 500   N    HIS C   906     O    HOH C  1102              2.06            
REMARK 500   O    HOH C  1120     O    HOH C  1125              2.08            
REMARK 500   O    HOH D   430     O    HOH D   446              2.08            
REMARK 500   O    HOH C  1112     O    HOH C  1147              2.10            
REMARK 500   O    HOH B   428     O    HOH B   431              2.10            
REMARK 500   O    HOH G  1165     O    HOH H   439              2.10            
REMARK 500   NH1  ARG G   982     O    HOH G  1101              2.10            
REMARK 500   O4   SO4 B   301     O    HOH B   402              2.11            
REMARK 500   O    HOH C  1154     O    HOH D   445              2.11            
REMARK 500   O    HOH H   450     O    HOH H   451              2.11            
REMARK 500   NE2  GLN E   912     O    HOH E  1102              2.12            
REMARK 500   O    HOH B   415     O    HOH B   434              2.12            
REMARK 500   O    HOH A  1129     O    HOH A  1145              2.12            
REMARK 500   O    HOH A  1149     O    HOH B   442              2.12            
REMARK 500   O2   SO4 H   302     O    HOH H   401              2.13            
REMARK 500   O    HOH G  1127     O    HOH G  1160              2.13            
REMARK 500   O    HOH E  1141     O    HOH E  1156              2.13            
REMARK 500   O    HOH A  1118     O    HOH B   435              2.14            
REMARK 500   O    ASP B   265     O    HOH B   403              2.14            
REMARK 500   O    GLN A   954     O    HOH A  1103              2.14            
REMARK 500   OD2  ASP A   926     O    HOH A  1104              2.15            
REMARK 500   O    HOH E  1158     O    HOH G  1147              2.15            
REMARK 500   O    HOH G  1145     O    HOH G  1160              2.15            
REMARK 500   O    ASN E   907     O    HOH E  1103              2.16            
REMARK 500   O4   SO4 C  1001     O    HOH C  1103              2.17            
REMARK 500   O    HOH C  1150     O    HOH C  1165              2.18            
REMARK 500   O    HOH B   438     O    HOH B   439              2.19            
REMARK 500   NZ   LYS G   936     O    HOH G  1102              2.19            
REMARK 500   O    HOH G  1106     O    HOH G  1154              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1155     O    HOH C  1169     1455     2.09            
REMARK 500   O    HOH C  1146     O    HOH E  1150     1556     2.11            
REMARK 500   O    HOH F   436     O    HOH G  1151     1655     2.12            
REMARK 500   NH2  ARG C   925     O    HOH A  1104     1655     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU E 932       70.54    -62.15                                   
REMARK 500    ASN E 933      -55.74    165.10                                   
REMARK 500    ASN E 934      100.19    -45.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1156        DISTANCE =  8.08 ANGSTROMS                       
REMARK 525    HOH A1157        DISTANCE =  9.89 ANGSTROMS                       
REMARK 525    HOH A1158        DISTANCE = 11.56 ANGSTROMS                       
REMARK 525    HOH B 455        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH B 456        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH C1170        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH C1171        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH G1173        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH G1174        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH G1175        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH G1176        DISTANCE =  8.17 ANGSTROMS                       
REMARK 525    HOH G1177        DISTANCE =  8.36 ANGSTROMS                       
REMARK 525    HOH G1178        DISTANCE =  8.47 ANGSTROMS                       
REMARK 525    HOH G1179        DISTANCE =  9.67 ANGSTROMS                       
REMARK 525    HOH G1180        DISTANCE = 10.94 ANGSTROMS                       
REMARK 525    HOH G1181        DISTANCE = 12.98 ANGSTROMS                       
REMARK 525    HOH H 449        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH H 450        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH H 451        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH H 452        DISTANCE =  8.60 ANGSTROMS                       
REMARK 525    HOH H 453        DISTANCE =  8.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide SO4 B 302 and ARG C    
REMARK 800  919                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide SO4 F 301 and ARG G    
REMARK 800  919                                                                 
DBREF  6G6L A  898   984  UNP    P01106   MYC_HUMAN      351    437             
DBREF  6G6L B  201   282  UNP    P61244   MAX_HUMAN       22    103             
DBREF  6G6L C  898   984  UNP    P01106   MYC_HUMAN      351    437             
DBREF  6G6L D  201   282  UNP    P61244   MAX_HUMAN       22    103             
DBREF  6G6L E  898   984  UNP    P01106   MYC_HUMAN      351    437             
DBREF  6G6L F  201   282  UNP    P61244   MAX_HUMAN       22    103             
DBREF  6G6L G  898   984  UNP    P01106   MYC_HUMAN      351    437             
DBREF  6G6L H  201   282  UNP    P61244   MAX_HUMAN       22    103             
SEQADV 6G6L MET A  891  UNP  P01106              INITIATING METHIONINE          
SEQADV 6G6L HIS A  892  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS A  893  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS A  894  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS A  895  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS A  896  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS A  897  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L MET B  200  UNP  P61244              INITIATING METHIONINE          
SEQADV 6G6L MET C  891  UNP  P01106              INITIATING METHIONINE          
SEQADV 6G6L HIS C  892  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS C  893  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS C  894  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS C  895  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS C  896  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS C  897  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L MET D  200  UNP  P61244              INITIATING METHIONINE          
SEQADV 6G6L MET E  891  UNP  P01106              INITIATING METHIONINE          
SEQADV 6G6L HIS E  892  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS E  893  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS E  894  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS E  895  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS E  896  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS E  897  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L MET F  200  UNP  P61244              INITIATING METHIONINE          
SEQADV 6G6L MET G  891  UNP  P01106              INITIATING METHIONINE          
SEQADV 6G6L HIS G  892  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS G  893  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS G  894  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS G  895  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS G  896  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L HIS G  897  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6L MET H  200  UNP  P61244              INITIATING METHIONINE          
SEQRES   1 A   94  MET HIS HIS HIS HIS HIS HIS GLU GLU ASN VAL LYS ARG          
SEQRES   2 A   94  ARG THR HIS ASN VAL LEU GLU ARG GLN ARG ARG ASN GLU          
SEQRES   3 A   94  LEU LYS ARG SER PHE PHE ALA LEU ARG ASP GLN ILE PRO          
SEQRES   4 A   94  GLU LEU GLU ASN ASN GLU LYS ALA PRO LYS VAL VAL ILE          
SEQRES   5 A   94  LEU LYS LYS ALA THR ALA TYR ILE LEU SER VAL GLN ALA          
SEQRES   6 A   94  GLU GLU GLN LYS LEU ILE SER GLU GLU ASP LEU LEU ARG          
SEQRES   7 A   94  LYS ARG ARG GLU GLN LEU LYS HIS LYS LEU GLU GLN LEU          
SEQRES   8 A   94  ARG ASN SER                                                  
SEQRES   1 B   83  MET ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG          
SEQRES   2 B   83  LYS ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU          
SEQRES   3 B   83  ARG ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER          
SEQRES   4 B   83  ARG ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN          
SEQRES   5 B   83  TYR MET ARG ARG LYS ASN HIS THR HIS GLN GLN ASP ILE          
SEQRES   6 B   83  ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN          
SEQRES   7 B   83  VAL ARG ALA LEU GLU                                          
SEQRES   1 C   94  MET HIS HIS HIS HIS HIS HIS GLU GLU ASN VAL LYS ARG          
SEQRES   2 C   94  ARG THR HIS ASN VAL LEU GLU ARG GLN ARG ARG ASN GLU          
SEQRES   3 C   94  LEU LYS ARG SER PHE PHE ALA LEU ARG ASP GLN ILE PRO          
SEQRES   4 C   94  GLU LEU GLU ASN ASN GLU LYS ALA PRO LYS VAL VAL ILE          
SEQRES   5 C   94  LEU LYS LYS ALA THR ALA TYR ILE LEU SER VAL GLN ALA          
SEQRES   6 C   94  GLU GLU GLN LYS LEU ILE SER GLU GLU ASP LEU LEU ARG          
SEQRES   7 C   94  LYS ARG ARG GLU GLN LEU LYS HIS LYS LEU GLU GLN LEU          
SEQRES   8 C   94  ARG ASN SER                                                  
SEQRES   1 D   83  MET ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG          
SEQRES   2 D   83  LYS ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU          
SEQRES   3 D   83  ARG ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER          
SEQRES   4 D   83  ARG ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN          
SEQRES   5 D   83  TYR MET ARG ARG LYS ASN HIS THR HIS GLN GLN ASP ILE          
SEQRES   6 D   83  ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN          
SEQRES   7 D   83  VAL ARG ALA LEU GLU                                          
SEQRES   1 E   94  MET HIS HIS HIS HIS HIS HIS GLU GLU ASN VAL LYS ARG          
SEQRES   2 E   94  ARG THR HIS ASN VAL LEU GLU ARG GLN ARG ARG ASN GLU          
SEQRES   3 E   94  LEU LYS ARG SER PHE PHE ALA LEU ARG ASP GLN ILE PRO          
SEQRES   4 E   94  GLU LEU GLU ASN ASN GLU LYS ALA PRO LYS VAL VAL ILE          
SEQRES   5 E   94  LEU LYS LYS ALA THR ALA TYR ILE LEU SER VAL GLN ALA          
SEQRES   6 E   94  GLU GLU GLN LYS LEU ILE SER GLU GLU ASP LEU LEU ARG          
SEQRES   7 E   94  LYS ARG ARG GLU GLN LEU LYS HIS LYS LEU GLU GLN LEU          
SEQRES   8 E   94  ARG ASN SER                                                  
SEQRES   1 F   83  MET ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG          
SEQRES   2 F   83  LYS ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU          
SEQRES   3 F   83  ARG ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER          
SEQRES   4 F   83  ARG ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN          
SEQRES   5 F   83  TYR MET ARG ARG LYS ASN HIS THR HIS GLN GLN ASP ILE          
SEQRES   6 F   83  ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN          
SEQRES   7 F   83  VAL ARG ALA LEU GLU                                          
SEQRES   1 G   94  MET HIS HIS HIS HIS HIS HIS GLU GLU ASN VAL LYS ARG          
SEQRES   2 G   94  ARG THR HIS ASN VAL LEU GLU ARG GLN ARG ARG ASN GLU          
SEQRES   3 G   94  LEU LYS ARG SER PHE PHE ALA LEU ARG ASP GLN ILE PRO          
SEQRES   4 G   94  GLU LEU GLU ASN ASN GLU LYS ALA PRO LYS VAL VAL ILE          
SEQRES   5 G   94  LEU LYS LYS ALA THR ALA TYR ILE LEU SER VAL GLN ALA          
SEQRES   6 G   94  GLU GLU GLN LYS LEU ILE SER GLU GLU ASP LEU LEU ARG          
SEQRES   7 G   94  LYS ARG ARG GLU GLN LEU LYS HIS LYS LEU GLU GLN LEU          
SEQRES   8 G   94  ARG ASN SER                                                  
SEQRES   1 H   83  MET ALA ASP LYS ARG ALA HIS HIS ASN ALA LEU GLU ARG          
SEQRES   2 H   83  LYS ARG ARG ASP HIS ILE LYS ASP SER PHE HIS SER LEU          
SEQRES   3 H   83  ARG ASP SER VAL PRO SER LEU GLN GLY GLU LYS ALA SER          
SEQRES   4 H   83  ARG ALA GLN ILE LEU ASP LYS ALA THR GLU TYR ILE GLN          
SEQRES   5 H   83  TYR MET ARG ARG LYS ASN HIS THR HIS GLN GLN ASP ILE          
SEQRES   6 H   83  ASP ASP LEU LYS ARG GLN ASN ALA LEU LEU GLU GLN GLN          
SEQRES   7 H   83  VAL ARG ALA LEU GLU                                          
HET    SO4  A1001       5                                                       
HET    SO4  A1002       5                                                       
HET    SO4  B 301       5                                                       
HET    SO4  B 302       5                                                       
HET    SO4  C1001       5                                                       
HET    SO4  D 301       5                                                       
HET    SO4  D 302       5                                                       
HET    SO4  E1001       5                                                       
HET    SO4  F 301       5                                                       
HET    SO4  F 302       5                                                       
HET    SO4  G1001       5                                                       
HET    SO4  G1002       5                                                       
HET    SO4  H 301       5                                                       
HET    SO4  H 302       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  SO4    14(O4 S 2-)                                                  
FORMUL  23  HOH   *480(H2 O)                                                    
HELIX    1 AA1 VAL A  908  ASP A  926  1                                  19    
HELIX    2 AA2 PRO A  938  ASN A  983  1                                  46    
HELIX    3 AA3 ARG B  215  SER B  228  1                                  14    
HELIX    4 AA4 VAL B  229  GLN B  233  5                                   5    
HELIX    5 AA5 SER B  238  ARG B  279  1                                  42    
HELIX    6 AA6 ASN C  907  ASP C  926  1                                  20    
HELIX    7 AA7 PRO C  938  ASN C  983  1                                  46    
HELIX    8 AA8 ARG D  212  VAL D  229  1                                  18    
HELIX    9 AA9 PRO D  230  GLN D  233  5                                   4    
HELIX   10 AB1 SER D  238  ARG D  279  1                                  42    
HELIX   11 AB2 VAL E  908  ASP E  926  1                                  19    
HELIX   12 AB3 PRO E  938  ASN E  983  1                                  46    
HELIX   13 AB4 ARG F  212  SER F  228  1                                  17    
HELIX   14 AB5 VAL F  229  GLN F  233  5                                   5    
HELIX   15 AB6 SER F  238  ARG F  279  1                                  42    
HELIX   16 AB7 LEU G  909  ASP G  926  1                                  18    
HELIX   17 AB8 PRO G  938  ASN G  983  1                                  46    
HELIX   18 AB9 ASP H  216  VAL H  229  1                                  14    
HELIX   19 AC1 PRO H  230  GLN H  233  5                                   4    
HELIX   20 AC2 SER H  238  ARG H  279  1                                  42    
LINK         NH2 ARG C 919                 O1  SO4 B 302     1555   1655  1.30  
LINK         NH2 ARG G 919                 O4  SO4 F 301     1555   1455  1.30  
SITE     1 AC1  4 LYS A 939  HOH A1109  ARG B 214  LYS G 936                    
SITE     1 AC2  5 GLN A 912  ASN A 915  ARG A 919  HOH A1101                    
SITE     2 AC2  5 HIS D 258                                                     
SITE     1 AC3  5 ARG A 913  SER B 238  ARG B 239  HOH B 402                    
SITE     2 AC3  5 HOH B 406                                                     
SITE     1 AC4  6 ARG B 254  HIS B 258  GLN C 912  ASN C 915                    
SITE     2 AC4  6 ARG C 919  HOH C1103                                          
SITE     1 AC5  4 SER D 238  ARG D 239  HOH D 404  HOH D 420                    
SITE     1 AC6  3 PRO C 938  LYS C 939  ARG D 214                               
SITE     1 AC7  3 PRO E 938  LYS E 939  ARG F 214                               
SITE     1 AC8  6 ARG E 913  HOH E1109  SER F 238  ARG F 239                    
SITE     2 AC8  6 HOH F 402  HOH F 421                                          
SITE     1 AC9  6 ARG F 254  HIS F 258  ASN G 915  ARG G 919                    
SITE     2 AC9  6 HOH G1105  HOH G1112                                          
SITE     1 AD1  4 LYS A 936  PRO G 938  LYS G 939  HOH G1110                    
SITE     1 AD2  3 ARG G 913  SER H 238  ARG H 239                               
SITE     1 AD3  5 ASN E 915  ARG E 919  ARG H 254  HIS H 258                    
SITE     2 AD3  5 HOH H 401                                                     
SITE     1 AD4 17 ASP A 926  GLU A 932  GLN B 251  ARG B 254                    
SITE     2 AD4 17 ARG B 255  HOH B 401  HOH B 429  ASN C 915                    
SITE     3 AD4 17 GLU C 916  LEU C 917  LYS C 918  SER C 920                    
SITE     4 AD4 17 PHE C 921  PHE C 922  ALA C 923  SO4 C1001                    
SITE     5 AD4 17 HOH C1103                                                     
SITE     1 AD5 13 ASP E 926  GLU E 932  ARG F 254  ASN G 915                    
SITE     2 AD5 13 GLU G 916  LEU G 917  LYS G 918  SER G 920                    
SITE     3 AD5 13 PHE G 921  PHE G 922  ALA G 923  SO4 G1001                    
SITE     4 AD5 13 HOH G1112                                                     
CRYST1   48.680   74.330   80.060 107.12 107.67  90.05 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020542  0.000018  0.006887        0.00000                         
SCALE2      0.000000  0.013454  0.004375        0.00000                         
SCALE3      0.000000  0.000000  0.013785        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system