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Database: PDB
Entry: 6G6K
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HEADER    APOPTOSIS                               01-APR-18   6G6K              
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;                                                         
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;                                                         
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 6G6K    1       JRNL                                     
REVDAT   2   24-JUL-19 6G6K    1       JRNL                                     
REVDAT   1   10-APR-19 6G6K    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.    1.35 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) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.910                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 80678                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7247                            
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 38.2811 -  4.1930    0.98     5749   261  0.2207 0.2400        
REMARK   3     2  4.1930 -  3.3287    0.86     4959   311  0.1720 0.1814        
REMARK   3     3  3.3287 -  2.9081    0.70     4093   175  0.1786 0.2015        
REMARK   3     4  2.9081 -  2.6423    0.82     4826   249  0.1764 0.2089        
REMARK   3     5  2.6423 -  2.4529    0.84     4924   249  0.1620 0.1994        
REMARK   3     6  2.4529 -  2.3083    0.85     4924   259  0.1577 0.2221        
REMARK   3     7  2.3083 -  2.1928    0.88     5026   306  0.1489 0.1889        
REMARK   3     8  2.1928 -  2.0973    0.86     5016   276  0.1371 0.1455        
REMARK   3     9  2.0973 -  2.0166    0.89     5105   276  0.1347 0.1640        
REMARK   3    10  2.0166 -  1.9470    0.87     5151   232  0.1426 0.2250        
REMARK   3    11  1.9470 -  1.8861    0.86     4885   269  0.1515 0.2037        
REMARK   3    12  1.8861 -  1.8322    0.67     3942   224  0.1514 0.1974        
REMARK   3    13  1.8322 -  1.7840    0.66     3724   228  0.1588 0.2223        
REMARK   3    14  1.7840 -  1.7404    0.73     4258   228  0.1571 0.2058        
REMARK   3    15  1.7404 -  1.7009    0.79     4619   219  0.1323 0.1686        
REMARK   3    16  1.7009 -  1.6647    0.80     4714   252  0.1355 0.1813        
REMARK   3    17  1.6647 -  1.6314    0.81     4726   238  0.1346 0.1732        
REMARK   3    18  1.6314 -  1.6006    0.85     4854   290  0.1387 0.1939        
REMARK   3    19  1.6006 -  1.5720    0.81     4776   211  0.1478 0.1879        
REMARK   3    20  1.5720 -  1.5454    0.82     4747   250  0.1501 0.2073        
REMARK   3    21  1.5454 -  1.5204    0.85     4904   259  0.1656 0.2050        
REMARK   3    22  1.5204 -  1.4970    0.82     4783   225  0.1577 0.1687        
REMARK   3    23  1.4970 -  1.4750    0.83     4928   198  0.1725 0.2005        
REMARK   3    24  1.4750 -  1.4542    0.85     4834   228  0.1927 0.2156        
REMARK   3    25  1.4542 -  1.4346    0.84     4997   248  0.2164 0.2576        
REMARK   3    26  1.4346 -  1.4160    0.84     4887   243  0.2292 0.2839        
REMARK   3    27  1.4160 -  1.3983    0.83     4882   240  0.2564 0.2605        
REMARK   3    28  1.3983 -  1.3814    0.75     4194   197  0.2665 0.3118        
REMARK   3    29  1.3814 -  1.3653    0.63     3812   220  0.2984 0.3336        
REMARK   3    30  1.3653 -  1.3500    0.66     3792   186  0.3266 0.3343        
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.990           
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      :  0.005           2896                                  
REMARK   3   ANGLE     :  0.756           3884                                  
REMARK   3   CHIRALITY :  0.057            415                                  
REMARK   3   PLANARITY :  0.004            521                                  
REMARK   3   DIHEDRAL  :  2.008           1953                                  
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 6G6K 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_1200009483.                                   
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                             : 7.5                                
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) : 0.97950                            
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   : 80704                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.270                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.9                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1KNP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% W/V PEG 8000, 20% V/V ETHYLENE       
REMARK 280  GLYCOL, 0.075 %(W/V) OF EACH ADDITIVE, 5 %(V/V) ETOH, 0.1 M MOPS/   
REMARK 280  HEPES-NA, PH 7.5, ADDITIVE: 0.75 %(W/V) MENTHOL, 0.75 %(W/V)        
REMARK 280  CAFFEIC ACID, 0.75 %(W/V) D-QUINIC ACID, 0.75 %(W/V) SHIKIMIC       
REMARK 280  ACID, 0.75 %(W/V) GALLIC ACID MONOHYDRATE, 0.75 %(W/V) N-           
REMARK 280  VANILLYLNONANAMIDE., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  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                                                    
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: 3330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 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     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     LEU B   281                                                      
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     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     LEU D   281                                                      
REMARK 465     GLU D   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 D   306     O    HOH D   342              1.82            
REMARK 500   OE1  GLU A   935     O    HOH A  1102              1.87            
REMARK 500   O    HOH A  1191     O    HOH A  1199              1.92            
REMARK 500   O    HOH A  1108     O    HOH A  1180              1.94            
REMARK 500   O    HOH A  1189     O    HOH A  1191              1.97            
REMARK 500   O    HOH C  1187     O    HOH C  1196              2.01            
REMARK 500   O    HOH A  1189     O    HOH A  1199              2.02            
REMARK 500   O    HOH C  1159     O    HOH C  1175              2.06            
REMARK 500   OE1  GLU C   956     O    HOH C  1101              2.15            
REMARK 500   O    HOH D   359     O    HOH D   363              2.15            
REMARK 500   OE1  GLU A   898     O    HOH A  1103              2.15            
REMARK 500   O    HOH C  1172     O    HOH C  1190              2.17            
REMARK 500   O    GLN D   233     O    HOH D   302              2.19            
REMARK 500   O    ASN D   208     O    HOH D   303              2.19            
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    GLN B 233      105.35    -55.97                                   
REMARK 500    GLN D 233      105.25    -53.90                                   
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 A1204        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A1205        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A1206        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH C1197        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH C1198        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH D 379        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH D 380        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH D 381        DISTANCE =  6.30 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 1001                 
DBREF  6G6K A  898   984  UNP    P01106   MYC_HUMAN      351    437             
DBREF  6G6K B  201   282  UNP    P61244   MAX_HUMAN       22    103             
DBREF  6G6K C  898   984  UNP    P01106   MYC_HUMAN      351    437             
DBREF  6G6K D  201   282  UNP    P61244   MAX_HUMAN       22    103             
SEQADV 6G6K MET A  891  UNP  P01106              INITIATING METHIONINE          
SEQADV 6G6K HIS A  892  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS A  893  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS A  894  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS A  895  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS A  896  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS A  897  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K MET B  200  UNP  P61244              INITIATING METHIONINE          
SEQADV 6G6K MET C  891  UNP  P01106              INITIATING METHIONINE          
SEQADV 6G6K HIS C  892  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS C  893  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS C  894  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS C  895  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS C  896  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K HIS C  897  UNP  P01106              EXPRESSION TAG                 
SEQADV 6G6K MET D  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                                          
HET     CL  A1001       1                                                       
HET     CL  C1001       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  HOH   *359(H2 O)                                                    
HELIX    1 AA1 HIS A  896  ASP A  926  1                                  31    
HELIX    2 AA2 GLN A  927  GLU A  932  5                                   6    
HELIX    3 AA3 PRO A  938  ASN A  983  1                                  46    
HELIX    4 AA4 HIS B  206  VAL B  229  1                                  24    
HELIX    5 AA5 SER B  238  ALA B  280  1                                  43    
HELIX    6 AA6 GLU C  898  ASP C  926  1                                  29    
HELIX    7 AA7 GLN C  927  GLU C  932  5                                   6    
HELIX    8 AA8 PRO C  938  ASN C  983  1                                  46    
HELIX    9 AA9 HIS D  206  VAL D  229  1                                  24    
HELIX   10 AB1 SER D  238  ALA D  280  1                                  43    
SITE     1 AC1  2 LYS A 939  ARG B 239                                          
SITE     1 AC2  3 LYS C 939  ARG D 239  HOH D 357                               
CRYST1   30.399   52.310   73.089  93.89 101.92 106.79 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.032895  0.009925  0.008373        0.00000                         
SCALE2      0.000000  0.019968  0.002744        0.00000                         
SCALE3      0.000000  0.000000  0.014115        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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