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Database: PDB
Entry: 6E83
LinkDB: 6E83
Original site: 6E83 
HEADER    GENE REGULATION                         27-JUL-18   6E83              
TITLE     SOLUTION STRUCTURE OF ZZZ3 ZZ DOMAIN IN COMPLEX WITH HISTONE H3 TAIL  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZZ-TYPE ZINC FINGER-CONTAINING PROTEIN 3;                  
COMPND   3 CHAIN: B;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HISTONE H3;                                                
COMPND   7 CHAIN: A;                                                            
COMPND   8 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: ZZZ3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606                                                 
KEYWDS    ZZZ3, ZZ DOMAIN, HISTONE, CHROMATIN, GENE REGULATION                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    Y.ZHANG,T.G.KUTATELADZE                                               
REVDAT   2   03-OCT-18 6E83    1       JRNL                                     
REVDAT   1   19-SEP-18 6E83    0                                                
JRNL        AUTH   W.MI,Y.ZHANG,J.LYU,X.WANG,Q.TONG,D.PENG,Y.XUE,A.H.TENCER,    
JRNL        AUTH 2 H.WEN,W.LI,T.G.KUTATELADZE,X.SHI                             
JRNL        TITL   THE ZZ-TYPE ZINC FINGER OF ZZZ3 MODULATES THE ATAC           
JRNL        TITL 2 COMPLEX-MEDIATED HISTONE ACETYLATION AND GENE ACTIVATION.    
JRNL        REF    NAT COMMUN                    V.   9  3759 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30217978                                                     
JRNL        DOI    10.1038/S41467-018-06247-5                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER                                                
REMARK   3   AUTHORS     : D.A. CASE, I.Y. BEN-SHALOM, S.R. BROZELL, D.S.       
REMARK   3                 CERUTTI, T.E. CHEATHAM, III, V.W.D. CRUZEIRO, T.A.   
REMARK   3                 DARDEN, R.E. DUKE, D. GHOREISHI, M.K. GILSON, H.     
REMARK   3                 GOHLKE, A.W. GOETZ, D. GREENE, R HARRIS, N.          
REMARK   3                 HOMEYER, S. IZADI, A. KOVALENKO, T. KURTZMAN, T.S.   
REMARK   3                 LEE, S. LEGRAND, P. LI, C. LIN, J. LIU, T. LUCHKO,   
REMARK   3                 R. LUO, D.J. MERMELSTEIN, K.M. MERZ, Y. MIAO, G.     
REMARK   3                 MONARD, C. NGUYEN, H. NGUYEN, I. OMELYAN, A.         
REMARK   3                 ONUFRIEV, F. PAN, R. QI, D.R. ROE, A. ROITBERG, C.   
REMARK   3                 SAGUI, S. SCHOTT-VERDUGO, J. SHEN, C.L. SIMMERLING,  
REMARK   3                 J. SMITH, R. SALOMON-FERRER, J. SWAILS, R.C.         
REMARK   3                 WALKER, J. WANG, H. WEI, R.M. WOLF, X. WU, L. XIAO,  
REMARK   3                 D.M. YORK AND P.A. KOLLMAN                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6E83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000228930.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 7                                  
REMARK 210  IONIC STRENGTH                 : 0.1                                
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : 2 MM [U-13C; U-15N] ZZ DOMAIN OF   
REMARK 210                                   ZZZ3, 10 MM HISTONE H3, 100 MM     
REMARK 210                                   SODIUM CHLORIDE, 20 MM TRIS, 7 %   
REMARK 210                                   [U-99% 2H] D2O, 90% H2O/10% D2O;   
REMARK 210                                   4 MM [U-13C; U-15N] ZZ DOMAIN OF   
REMARK 210                                   ZZZ3, 100 MM SODIUM CHLORIDE, 20   
REMARK 210                                   MM TRIS, 7 % [U-99% 2H] D2O, 90%   
REMARK 210                                   H2O/10% D2O                        
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D HNCA; 3D CBCA(CO)NH; 3D         
REMARK 210                                   HBHA(CO)NH; 3D HCCH-TOCSY; 3D      
REMARK 210                                   HNCACB; 2D 1H-1H TOCSY; 3D 1H-     
REMARK 210                                   13C NOESY ALIPHATIC; 3D 1H-15N     
REMARK 210                                   NOESY; 3D FILTERED 1H-13C NOESY    
REMARK 210                                   ALIPHATIC; 3D FILTERED 1H-15N      
REMARK 210                                   NOESY                              
REMARK 210  SPECTROMETER FIELD STRENGTH    : 900 MHZ; 600 MHZ                   
REMARK 210  SPECTROMETER MODEL             : INOVA                              
REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : VNMR, NMRDRAW, ANALYSIS, X-PLOR    
REMARK 210                                   NIH                                
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500  1 ARG A   8   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500  4 ARG A   2   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  5 ARG B 835   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  5 CYS B 841   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES          
REMARK 500  6 ARG B 835   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500  7 ARG B 835   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500  8 CYS B 841   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500 10 ARG A   2   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 11 ARG B 835   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500 12 ARG B 835   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500 12 CYS B 841   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500 14 CYS B 841   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500 14 ARG A   2   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 15 ARG B 835   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500  1 VAL B 819       98.65    -53.01                                   
REMARK 500  1 LEU B 857       57.16   -141.13                                   
REMARK 500  1 THR B 860     -156.78   -115.99                                   
REMARK 500  1 ILE B 862      -44.26   -136.46                                   
REMARK 500  2 LEU B 813     -128.23     55.40                                   
REMARK 500  2 GLN B 817       98.96   -160.78                                   
REMARK 500  2 VAL B 819       87.64    -52.88                                   
REMARK 500  2 THR B 860     -167.03   -129.58                                   
REMARK 500  2 ARG A   2       78.71    -69.65                                   
REMARK 500  3 VAL B 819      106.09    -50.29                                   
REMARK 500  3 MET B 845       50.51   -140.70                                   
REMARK 500  3 LEU B 857      152.34     60.62                                   
REMARK 500  3 THR B 860     -156.62   -128.43                                   
REMARK 500  3 ILE B 862      -44.78   -132.77                                   
REMARK 500  4 VAL B 819       72.71    -57.27                                   
REMARK 500  4 LEU B 857       58.19   -141.29                                   
REMARK 500  4 ASP B 861      -54.47     57.73                                   
REMARK 500  4 ILE B 862      -36.99   -139.64                                   
REMARK 500  5 VAL B 819      103.84    -49.48                                   
REMARK 500  5 GLN B 839        0.92    -64.22                                   
REMARK 500  5 LEU B 857       57.24   -150.61                                   
REMARK 500  5 THR B 860     -156.58   -120.81                                   
REMARK 500  5 ILE B 862      -42.64   -135.36                                   
REMARK 500  5 THR A   6      -33.25     58.97                                   
REMARK 500  6 VAL B 819      101.18    -49.86                                   
REMARK 500  6 THR B 860     -156.10   -122.06                                   
REMARK 500  6 ILE B 862      -43.26   -136.75                                   
REMARK 500  7 VAL B 819      108.11    -47.86                                   
REMARK 500  7 LEU B 857       56.12   -144.49                                   
REMARK 500  7 THR B 860     -159.25   -125.93                                   
REMARK 500  7 ILE B 862      -44.82   -135.61                                   
REMARK 500  8 LEU B 813     -115.91     46.75                                   
REMARK 500  8 VAL B 819       82.42    -56.53                                   
REMARK 500  8 GLN B 839        1.86    -65.18                                   
REMARK 500  8 SER B 846       79.26    -67.74                                   
REMARK 500  8 LEU B 857       69.46   -153.09                                   
REMARK 500  8 ILE B 862      -44.82   -134.12                                   
REMARK 500  8 THR A   6      150.72     65.71                                   
REMARK 500  9 VAL B 819      107.97    -48.14                                   
REMARK 500  9 ASP B 861      -51.10     56.62                                   
REMARK 500  9 ILE B 862      -42.37   -141.13                                   
REMARK 500 10 VAL B 819      107.53    -49.87                                   
REMARK 500 10 THR B 860     -157.45   -115.56                                   
REMARK 500 10 ILE B 862      -44.63   -136.27                                   
REMARK 500 10 THR A   6       -1.38     63.01                                   
REMARK 500 10 LYS A   9      -26.97     64.08                                   
REMARK 500 11 VAL B 819      102.08    -48.55                                   
REMARK 500 11 GLN B 839        4.28    -63.09                                   
REMARK 500 11 SER B 846       79.26    -67.73                                   
REMARK 500 11 LEU B 857       57.41   -149.99                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      98 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  9 HIS B 867         0.13    SIDE CHAIN                              
REMARK 500 17 HIS B 867         0.14    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 823   SG                                                     
REMARK 620 2 CYS B 826   SG  110.2                                              
REMARK 620 3 CYS B 850   SG  112.2 106.6                                        
REMARK 620 4 CYS B 853   SG  112.2 105.4 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 838   SG                                                     
REMARK 620 2 CYS B 841   SG  123.9                                              
REMARK 620 3 HIS B 863   ND1 109.7 105.7                                        
REMARK 620 4 HIS B 867   NE2 100.6 113.0 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 102                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 30501   RELATED DB: BMRB                                 
REMARK 900 SOLUTION STRUCTURE OF ZZZ3 ZZ DOMAIN IN COMPLEX WITH HISTONE H3 TAIL 
DBREF  6E83 B  816   874  UNP    Q8IYH5   ZZZ3_HUMAN     816    874             
DBREF  6E83 A    1    12  PDB    6E83     6E83             1     12             
SEQADV 6E83 GLY B  811  UNP  Q8IYH5              EXPRESSION TAG                 
SEQADV 6E83 PRO B  812  UNP  Q8IYH5              EXPRESSION TAG                 
SEQADV 6E83 LEU B  813  UNP  Q8IYH5              EXPRESSION TAG                 
SEQADV 6E83 GLY B  814  UNP  Q8IYH5              EXPRESSION TAG                 
SEQADV 6E83 SER B  815  UNP  Q8IYH5              EXPRESSION TAG                 
SEQRES   1 B   64  GLY PRO LEU GLY SER VAL GLN HIS VAL GLY PHE LYS CYS          
SEQRES   2 B   64  ASP ASN CYS GLY ILE GLU PRO ILE GLN GLY VAL ARG TRP          
SEQRES   3 B   64  HIS CYS GLN ASP CYS PRO PRO GLU MET SER LEU ASP PHE          
SEQRES   4 B   64  CYS ASP SER CYS SER ASP CYS LEU HIS GLU THR ASP ILE          
SEQRES   5 B   64  HIS LYS GLU ASP HIS GLN LEU GLU PRO ILE TYR ARG              
SEQRES   1 A   12  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY              
HET     ZN  B 101       1                                                       
HET     ZN  B 102       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    2(ZN 2+)                                                     
HELIX    1 AA1 PRO B  842  SER B  846  5                                   5    
SHEET    1 AA1 2 VAL B 816  GLN B 817  0                                        
SHEET    2 AA1 2 GLN B 832  GLY B 833 -1  O  GLY B 833   N  VAL B 816           
SHEET    1 AA2 3 ASP B 848  PHE B 849  0                                        
SHEET    2 AA2 3 ARG B 835  CYS B 838 -1  N  TRP B 836   O  PHE B 849           
SHEET    3 AA2 3 LEU B 869  ILE B 872 -1  O  GLU B 870   N  HIS B 837           
LINK         SG  CYS B 823                ZN    ZN B 101     1555   1555  2.13  
LINK         SG  CYS B 826                ZN    ZN B 101     1555   1555  2.13  
LINK         SG  CYS B 838                ZN    ZN B 102     1555   1555  2.11  
LINK         SG  CYS B 841                ZN    ZN B 102     1555   1555  2.13  
LINK         SG  CYS B 850                ZN    ZN B 101     1555   1555  2.13  
LINK         SG  CYS B 853                ZN    ZN B 101     1555   1555  2.13  
LINK         ND1 HIS B 863                ZN    ZN B 102     1555   1555  2.05  
LINK         NE2 HIS B 867                ZN    ZN B 102     1555   1555  2.03  
SITE     1 AC1  4 CYS B 823  CYS B 826  CYS B 850  CYS B 853                    
SITE     1 AC2  4 CYS B 838  CYS B 841  HIS B 863  HIS B 867                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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