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Database: PDB
Entry: 5C6H
LinkDB: 5C6H
Original site: 5C6H 
HEADER    APOPTOSIS/APOPTOSIS REGULATOR           23-JUN-15   5C6H              
TITLE     MCL-1 COMPLEXED WITH MULE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, C, E, G, I, K, M, O, Q, S, U, W;                           
COMPND   5 FRAGMENT: UNP RESIDUES 171-327;                                      
COMPND   6 SYNONYM: BCL-2-LIKE PROTEIN 3,BCL2-L-3,BCL-2-RELATED PROTEIN         
COMPND   7 EAT/MCL1,MCL1/EAT;                                                   
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: MCL-1, RESIDUES 171-327;                              
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: MULE BH3 PEPTIDE FROM E3 UBIQUITIN-PROTEIN LIGASE HUWE1;   
COMPND  12 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X;                           
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: MULE BH3, RESIDUES 1969-1994                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MCL1, BCL2L3;                                                  
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_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    COMPLEX. MCL-1, MULE, BH3, APOPTOSIS-APOPTOSIS REGULATOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.SONG,Z.WANG,F.JI,G.CHAI,Y.LIU,X.LI,Z.LI,Y.FAN,Z.ZHANG               
REVDAT   2   18-OCT-17 5C6H    1       REMARK                                   
REVDAT   1   03-AUG-16 5C6H    0                                                
JRNL        AUTH   T.SONG,Z.WANG,F.JI,G.CHAI,Y.LIU,X.LI,Z.LI,Y.FAN,Z.ZHANG      
JRNL        TITL   STRUCTURE OF MCL-1 COMPLEXED WITH MULE AT 2.05 ANGSTROMS     
JRNL        TITL 2 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 114746                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.297                           
REMARK   3   R VALUE            (WORKING SET) : 0.295                           
REMARK   3   FREE R VALUE                     : 0.346                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5763                            
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 35.4567 -  6.3580    0.87     3262   181  0.2913 0.3098        
REMARK   3     2  6.3580 -  5.0512    0.95     3628   216  0.2985 0.3215        
REMARK   3     3  5.0512 -  4.4140    0.96     3643   175  0.2675 0.3206        
REMARK   3     4  4.4140 -  4.0111    0.97     3641   198  0.2656 0.3165        
REMARK   3     5  4.0111 -  3.7239    0.97     3717   202  0.2788 0.3228        
REMARK   3     6  3.7239 -  3.5045    0.96     3600   175  0.2814 0.3046        
REMARK   3     7  3.5045 -  3.3292    0.96     3705   210  0.3054 0.3536        
REMARK   3     8  3.3292 -  3.1844    0.97     3589   176  0.2968 0.3418        
REMARK   3     9  3.1844 -  3.0618    0.97     3764   202  0.2956 0.3435        
REMARK   3    10  3.0618 -  2.9562    0.97     3660   189  0.3018 0.3631        
REMARK   3    11  2.9562 -  2.8638    0.97     3675   200  0.2977 0.3220        
REMARK   3    12  2.8638 -  2.7820    0.97     3770   184  0.2796 0.3562        
REMARK   3    13  2.7820 -  2.7088    0.97     3664   191  0.2885 0.3495        
REMARK   3    14  2.7088 -  2.6427    0.96     3546   206  0.2939 0.3303        
REMARK   3    15  2.6427 -  2.5827    0.97     3772   198  0.2816 0.3239        
REMARK   3    16  2.5827 -  2.5277    0.97     3692   213  0.2850 0.3602        
REMARK   3    17  2.5277 -  2.4772    0.97     3586   204  0.3052 0.3546        
REMARK   3    18  2.4772 -  2.4304    0.97     3618   197  0.3076 0.3674        
REMARK   3    19  2.4304 -  2.3870    0.97     3778   187  0.2993 0.3410        
REMARK   3    20  2.3870 -  2.3466    0.96     3684   197  0.2826 0.3389        
REMARK   3    21  2.3466 -  2.3087    0.96     3617   184  0.2921 0.3417        
REMARK   3    22  2.3087 -  2.2732    0.96     3523   197  0.2940 0.3630        
REMARK   3    23  2.2732 -  2.2398    0.91     3534   191  0.3230 0.4012        
REMARK   3    24  2.2398 -  2.2083    0.96     3727   173  0.3028 0.3934        
REMARK   3    25  2.2083 -  2.1784    0.96     3680   176  0.3048 0.3777        
REMARK   3    26  2.1784 -  2.1501    0.96     3598   160  0.3047 0.4073        
REMARK   3    27  2.1501 -  2.1233    0.96     3525   200  0.3085 0.3528        
REMARK   3    28  2.1233 -  2.0977    0.96     3705   192  0.3126 0.3554        
REMARK   3    29  2.0977 -  2.0733    0.94     3630   192  0.3338 0.3815        
REMARK   3    30  2.0733 -  2.0500    0.91     3450   197  0.3522 0.4101        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.390           
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          17572                                  
REMARK   3   ANGLE     :  0.654          23617                                  
REMARK   3   CHIRALITY :  0.049           2609                                  
REMARK   3   PLANARITY :  0.003           3053                                  
REMARK   3   DIHEDRAL  : 13.910           6648                                  
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 5C6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211100.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987, 0.988, 1.0                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : APEX II CCD                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS IA32                           
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114746                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.451                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.2600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: COOT 0.8.1.1                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, CALCIUM CHLORIDE, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
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, 5, 6, 7, 8, 9, 10, 11, 12, 13               
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: 24-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9660 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9520 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9380 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9500 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
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: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2060 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9650 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N                                  
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: 9                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9530 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P                                  
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: 10                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9200 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q, R                                  
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: 11                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T                                  
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: 12                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8820 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V                                  
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: 13                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9260 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: W, X                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     GLY C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLU E   325                                                      
REMARK 465     GLY E   326                                                      
REMARK 465     GLY E   327                                                      
REMARK 465     GLU G   325                                                      
REMARK 465     GLY G   326                                                      
REMARK 465     GLY G   327                                                      
REMARK 465     GLY I   326                                                      
REMARK 465     GLY I   327                                                      
REMARK 465     SER J    25                                                      
REMARK 465     LEU J    26                                                      
REMARK 465     LEU K   324                                                      
REMARK 465     GLU K   325                                                      
REMARK 465     GLY K   326                                                      
REMARK 465     GLY K   327                                                      
REMARK 465     GLY M   326                                                      
REMARK 465     GLY M   327                                                      
REMARK 465     GLY O   326                                                      
REMARK 465     GLY O   327                                                      
REMARK 465     GLU Q   325                                                      
REMARK 465     GLY Q   326                                                      
REMARK 465     GLY Q   327                                                      
REMARK 465     SER R    25                                                      
REMARK 465     LEU R    26                                                      
REMARK 465     GLU S   325                                                      
REMARK 465     GLY S   326                                                      
REMARK 465     GLY S   327                                                      
REMARK 465     GLU U   322                                                      
REMARK 465     ASP U   323                                                      
REMARK 465     LEU U   324                                                      
REMARK 465     GLU U   325                                                      
REMARK 465     GLY U   326                                                      
REMARK 465     GLY U   327                                                      
REMARK 465     PRO V     1                                                      
REMARK 465     SER V    25                                                      
REMARK 465     LEU V    26                                                      
REMARK 465     LEU W   324                                                      
REMARK 465     GLU W   325                                                      
REMARK 465     GLY W   326                                                      
REMARK 465     GLY W   327                                                      
REMARK 465     LEU X    26                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL N   3    CG1  CG2                                            
REMARK 470     VAL S 265    O                                                   
REMARK 470     SER W 202    OG                                                  
REMARK 470     THR W 205    OG1  CG2                                            
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    VAL U   297     OG1  THR U   301              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG U 310   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG U 310   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    ASP A 172       75.86     50.38                                   
REMARK 500    GLN A 177      -56.10     71.05                                   
REMARK 500    ASP A 195     -139.79   -125.19                                   
REMARK 500    THR A 196      100.28    -55.61                                   
REMARK 500    PRO A 198       97.78    -61.86                                   
REMARK 500    ARG A 201      -45.82   -159.65                                   
REMARK 500    ASP A 236       72.02     54.71                                   
REMARK 500    LYS A 238      -15.78   -142.80                                   
REMARK 500    ASP A 323       76.28   -153.84                                   
REMARK 500    MET B   4      -87.52    -93.80                                   
REMARK 500    THR B   5      -70.44     55.49                                   
REMARK 500    GLU B   7      -60.18     67.02                                   
REMARK 500    ARG B  24      -88.00    -61.37                                   
REMARK 500    LYS C 194       95.43    -60.72                                   
REMARK 500    THR C 196       60.89   -109.89                                   
REMARK 500    MET C 199      -64.54   -152.51                                   
REMARK 500    ARG C 201      -74.68    -65.94                                   
REMARK 500    ALA C 204      -70.29    -61.62                                   
REMARK 500    GLU C 322     -133.13   -143.44                                   
REMARK 500    ASP C 323     -174.90     72.36                                   
REMARK 500    LEU C 324      117.75     66.23                                   
REMARK 500    MET D   4       44.74    -89.38                                   
REMARK 500    SER D  25      106.33    -57.43                                   
REMARK 500    MET E 199     -156.10    -79.37                                   
REMARK 500    SER E 202      -29.16   -150.07                                   
REMARK 500    ALA E 204      -88.29     52.98                                   
REMARK 500    VAL E 321      -11.39   -140.62                                   
REMARK 500    GLU E 322      133.64    -28.36                                   
REMARK 500    ASP E 323      -71.70    -72.93                                   
REMARK 500    TYR F  23       42.76    -60.54                                   
REMARK 500    SER F  25     -163.59   -106.09                                   
REMARK 500    ARG G 201     -104.08     63.18                                   
REMARK 500    SER G 255       55.82    -67.04                                   
REMARK 500    ASP G 256        8.40   -168.72                                   
REMARK 500    ASP G 323     -107.53    -50.65                                   
REMARK 500    MET H   4       76.57    -67.92                                   
REMARK 500    PRO I 198      155.71    -49.55                                   
REMARK 500    ARG I 201     -108.74    -79.87                                   
REMARK 500    SER I 202       89.78    -63.20                                   
REMARK 500    ASN I 239     -162.71   -164.43                                   
REMARK 500    LEU I 324       84.27     58.98                                   
REMARK 500    GLN J  21      -26.42     74.23                                   
REMARK 500    ALA K 193     -142.47   -102.30                                   
REMARK 500    LYS K 194      104.43   -169.68                                   
REMARK 500    ASP K 195       50.60   -104.73                                   
REMARK 500    THR K 196       63.13    -65.63                                   
REMARK 500    MET K 199     -150.80    -83.17                                   
REMARK 500    ASP K 236       70.67     54.42                                   
REMARK 500    GLU K 322      -66.96   -145.49                                   
REMARK 500    SER L  25      -64.59   -174.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      78 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS O  320     VAL O  321                  140.16                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5C6H A  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H B    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H C  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H D    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H E  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H F    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H G  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H H    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H I  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H J    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H K  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H L    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H M  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H N    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H O  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H P    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H Q  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H R    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H S  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H T    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H U  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H V    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
DBREF  5C6H W  171   327  UNP    Q07820   MCL1_HUMAN     171    327             
DBREF  5C6H X    1    26  UNP    Q7Z6Z7   HUWE1_HUMAN   1969   1994             
SEQRES   1 A  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 A  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 A  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 A  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 A  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 A  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 A  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 A  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 A  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 A  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 A  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 A  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 A  157  GLY                                                          
SEQRES   1 B   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 B   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 C  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 C  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 C  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 C  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 C  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 C  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 C  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 C  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 C  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 C  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 C  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 C  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 C  157  GLY                                                          
SEQRES   1 D   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 D   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 E  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 E  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 E  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 E  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 E  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 E  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 E  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 E  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 E  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 E  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 E  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 E  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 E  157  GLY                                                          
SEQRES   1 F   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 F   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 G  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 G  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 G  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 G  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 G  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 G  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 G  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 G  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 G  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 G  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 G  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 G  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 G  157  GLY                                                          
SEQRES   1 H   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 H   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 I  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 I  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 I  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 I  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 I  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 I  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 I  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 I  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 I  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 I  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 I  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 I  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 I  157  GLY                                                          
SEQRES   1 J   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 J   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 K  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 K  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 K  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 K  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 K  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 K  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 K  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 K  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 K  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 K  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 K  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 K  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 K  157  GLY                                                          
SEQRES   1 L   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 L   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 M  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 M  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 M  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 M  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 M  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 M  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 M  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 M  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 M  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 M  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 M  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 M  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 M  157  GLY                                                          
SEQRES   1 N   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 N   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 O  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 O  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 O  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 O  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 O  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 O  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 O  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 O  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 O  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 O  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 O  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 O  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 O  157  GLY                                                          
SEQRES   1 P   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 P   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 Q  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 Q  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 Q  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 Q  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 Q  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 Q  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 Q  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 Q  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 Q  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 Q  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 Q  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 Q  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 Q  157  GLY                                                          
SEQRES   1 R   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 R   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 S  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 S  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 S  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 S  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 S  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 S  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 S  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 S  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 S  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 S  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 S  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 S  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 S  157  GLY                                                          
SEQRES   1 T   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 T   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 U  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 U  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 U  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 U  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 U  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 U  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 U  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 U  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 U  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 U  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 U  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 U  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 U  157  GLY                                                          
SEQRES   1 V   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 V   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
SEQRES   1 W  157  GLU ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 W  157  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 W  157  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 W  157  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 W  157  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 W  157  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 W  157  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 W  157  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 W  157  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 W  157  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 W  157  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 W  157  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP LEU GLU GLY          
SEQRES  13 W  157  GLY                                                          
SEQRES   1 X   26  PRO GLY VAL MET THR GLN GLU VAL GLY GLN LEU LEU GLN          
SEQRES   2 X   26  ASP MET GLY ASP ASP VAL TYR GLN GLN TYR ARG SER LEU          
FORMUL  25  HOH   *172(H2 O)                                                    
HELIX    1 AA1 LEU A  174  GLY A  192  1                                  19    
HELIX    2 AA2 GLY A  203  HIS A  224  1                                  22    
HELIX    3 AA3 HIS A  224  ASP A  236  1                                  13    
HELIX    4 AA4 ASN A  239  ASP A  241  5                                   3    
HELIX    5 AA5 ASP A  242  PHE A  254  1                                  13    
HELIX    6 AA6 ASN A  260  ILE A  281  1                                  22    
HELIX    7 AA7 GLN A  283  SER A  285  5                                   3    
HELIX    8 AA8 CYS A  286  GLN A  309  1                                  24    
HELIX    9 AA9 ARG A  310  PHE A  319  1                                  10    
HELIX   10 AB1 GLU B    7  ARG B   24  1                                  18    
HELIX   11 AB2 ASP C  172  GLY C  192  1                                  21    
HELIX   12 AB3 GLY C  203  HIS C  224  1                                  22    
HELIX   13 AB4 HIS C  224  ASP C  236  1                                  13    
HELIX   14 AB5 ASN C  239  ASP C  241  5                                   3    
HELIX   15 AB6 ASP C  242  VAL C  253  1                                  12    
HELIX   16 AB7 ASN C  260  ILE C  281  1                                  22    
HELIX   17 AB8 GLN C  283  SER C  285  5                                   3    
HELIX   18 AB9 CYS C  286  GLN C  309  1                                  24    
HELIX   19 AC1 TRP C  312  PHE C  319  1                                   8    
HELIX   20 AC2 MET D    4  ARG D   24  1                                  21    
HELIX   21 AC3 ASP E  172  GLY E  192  1                                  21    
HELIX   22 AC4 ALA E  204  HIS E  224  1                                  21    
HELIX   23 AC5 HIS E  224  ASP E  236  1                                  13    
HELIX   24 AC6 ASN E  239  ASP E  241  5                                   3    
HELIX   25 AC7 ASP E  242  PHE E  254  1                                  13    
HELIX   26 AC8 ASN E  260  ILE E  281  1                                  22    
HELIX   27 AC9 GLN E  283  SER E  285  5                                   3    
HELIX   28 AD1 CYS E  286  GLN E  309  1                                  24    
HELIX   29 AD2 ARG E  310  PHE E  319  1                                  10    
HELIX   30 AD3 MET F    4  GLN F   22  1                                  19    
HELIX   31 AD4 ASP G  172  GLY G  192  1                                  21    
HELIX   32 AD5 SER G  202  ASP G  236  1                                  35    
HELIX   33 AD6 ASN G  239  LYS G  244  1                                   6    
HELIX   34 AD7 LYS G  244  VAL G  253  1                                  10    
HELIX   35 AD8 ASN G  260  ILE G  281  1                                  22    
HELIX   36 AD9 GLN G  283  SER G  285  5                                   3    
HELIX   37 AE1 CYS G  286  GLN G  309  1                                  24    
HELIX   38 AE2 ARG G  310  PHE G  319  1                                  10    
HELIX   39 AE3 MET H    4  ARG H   24  1                                  21    
HELIX   40 AE4 ASP I  172  GLY I  192  1                                  21    
HELIX   41 AE5 SER I  202  ASP I  236  1                                  35    
HELIX   42 AE6 ASN I  239  ASP I  241  5                                   3    
HELIX   43 AE7 ASP I  242  VAL I  253  1                                  12    
HELIX   44 AE8 ASN I  260  ILE I  281  1                                  22    
HELIX   45 AE9 GLN I  283  SER I  285  5                                   3    
HELIX   46 AF1 CYS I  286  GLN I  309  1                                  24    
HELIX   47 AF2 ARG I  310  PHE I  319  1                                  10    
HELIX   48 AF3 MET J    4  TYR J   20  1                                  17    
HELIX   49 AF4 ASP K  172  GLY K  192  1                                  21    
HELIX   50 AF5 SER K  202  ASP K  236  1                                  35    
HELIX   51 AF6 ASN K  239  ASP K  241  5                                   3    
HELIX   52 AF7 ASP K  242  PHE K  254  1                                  13    
HELIX   53 AF8 ASN K  260  ILE K  281  1                                  22    
HELIX   54 AF9 GLN K  283  SER K  285  5                                   3    
HELIX   55 AG1 CYS K  286  LYS K  302  1                                  17    
HELIX   56 AG2 LYS K  302  GLN K  309  1                                   8    
HELIX   57 AG3 ARG K  310  PHE K  319  1                                  10    
HELIX   58 AG4 THR L    5  TYR L   23  1                                  19    
HELIX   59 AG5 ASP M  172  GLY M  192  1                                  21    
HELIX   60 AG6 GLY M  203  HIS M  224  1                                  22    
HELIX   61 AG7 HIS M  224  ASP M  236  1                                  13    
HELIX   62 AG8 ASN M  239  ASP M  242  5                                   4    
HELIX   63 AG9 VAL M  243  PHE M  254  1                                  12    
HELIX   64 AH1 ASN M  260  ILE M  281  1                                  22    
HELIX   65 AH2 GLN M  283  SER M  285  5                                   3    
HELIX   66 AH3 CYS M  286  GLN M  309  1                                  24    
HELIX   67 AH4 ARG M  310  PHE M  319  1                                  10    
HELIX   68 AH5 THR N    5  ARG N   24  1                                  20    
HELIX   69 AH6 ASP O  172  GLY O  192  1                                  21    
HELIX   70 AH7 SER O  202  HIS O  224  1                                  23    
HELIX   71 AH8 HIS O  224  ASP O  236  1                                  13    
HELIX   72 AH9 ASN O  239  ASP O  242  5                                   4    
HELIX   73 AI1 VAL O  243  PHE O  254  1                                  12    
HELIX   74 AI2 ASN O  260  ILE O  281  1                                  22    
HELIX   75 AI3 GLN O  283  SER O  285  5                                   3    
HELIX   76 AI4 CYS O  286  GLN O  309  1                                  24    
HELIX   77 AI5 ARG O  310  PHE O  319  1                                  10    
HELIX   78 AI6 MET P    4  ARG P   24  1                                  21    
HELIX   79 AI7 ASP Q  172  GLY Q  192  1                                  21    
HELIX   80 AI8 ALA Q  204  HIS Q  224  1                                  21    
HELIX   81 AI9 HIS Q  224  ASP Q  236  1                                  13    
HELIX   82 AJ1 ASN Q  239  PHE Q  254  1                                  16    
HELIX   83 AJ2 ASN Q  260  ILE Q  281  1                                  22    
HELIX   84 AJ3 GLN Q  283  SER Q  285  5                                   3    
HELIX   85 AJ4 CYS Q  286  GLN Q  309  1                                  24    
HELIX   86 AJ5 ARG Q  310  HIS Q  320  1                                  11    
HELIX   87 AJ6 THR R    5  TYR R   23  1                                  19    
HELIX   88 AJ7 ASP S  172  GLY S  192  1                                  21    
HELIX   89 AJ8 SER S  202  HIS S  224  1                                  23    
HELIX   90 AJ9 HIS S  224  ASP S  236  1                                  13    
HELIX   91 AK1 ASN S  239  ASP S  242  5                                   4    
HELIX   92 AK2 VAL S  243  PHE S  254  1                                  12    
HELIX   93 AK3 ASN S  260  ILE S  281  1                                  22    
HELIX   94 AK4 GLN S  283  SER S  285  5                                   3    
HELIX   95 AK5 CYS S  286  GLN S  309  1                                  24    
HELIX   96 AK6 ARG S  310  PHE S  319  1                                  10    
HELIX   97 AK7 MET T    4  ARG T   24  1                                  21    
HELIX   98 AK8 ASP U  172  GLY U  192  1                                  21    
HELIX   99 AK9 SER U  202  ASP U  236  1                                  35    
HELIX  100 AL1 ASN U  239  ASP U  241  5                                   3    
HELIX  101 AL2 ASP U  242  PHE U  254  1                                  13    
HELIX  102 AL3 ASN U  260  ILE U  281  1                                  22    
HELIX  103 AL4 GLN U  283  SER U  285  5                                   3    
HELIX  104 AL5 CYS U  286  LYS U  302  1                                  17    
HELIX  105 AL6 LYS U  302  GLN U  309  1                                   8    
HELIX  106 AL7 ARG U  310  PHE U  319  1                                  10    
HELIX  107 AL8 MET V    4  GLN V   21  1                                  18    
HELIX  108 AL9 ASP W  172  GLY W  192  1                                  21    
HELIX  109 AM1 SER W  202  ASP W  236  1                                  35    
HELIX  110 AM2 ASN W  239  ASP W  241  5                                   3    
HELIX  111 AM3 ASP W  242  PHE W  254  1                                  13    
HELIX  112 AM4 ASN W  260  ILE W  281  1                                  22    
HELIX  113 AM5 GLN W  283  SER W  285  5                                   3    
HELIX  114 AM6 CYS W  286  GLN W  309  1                                  24    
HELIX  115 AM7 ARG W  310  PHE W  319  1                                  10    
HELIX  116 AM8 MET X    4  ARG X   24  1                                  21    
CISPEP   1 ARG A  201    SER A  202          0         3.17                     
CISPEP   2 ASP A  323    LEU A  324          0        -5.63                     
CISPEP   3 LEU A  324    GLU A  325          0        -3.79                     
CISPEP   4 PRO C  198    MET C  199          0        -4.63                     
CISPEP   5 ASP G  195    THR G  196          0        -7.46                     
CISPEP   6 MET G  199    GLY G  200          0         7.56                     
CISPEP   7 PRO H    1    GLY H    2          0         4.84                     
CISPEP   8 VAL K  321    GLU K  322          0        -2.31                     
CISPEP   9 PRO L    1    GLY L    2          0        -0.48                     
CISPEP  10 ARG M  201    SER M  202          0        -2.82                     
CISPEP  11 LEU M  324    GLU M  325          0        -1.41                     
CISPEP  12 SER N   25    LEU N   26          0        -1.91                     
CISPEP  13 GLY Q  203    ALA Q  204          0       -12.09                     
CISPEP  14 ASP S  195    THR S  196          0        -5.02                     
CISPEP  15 MET S  199    GLY S  200          0         6.07                     
CISPEP  16 PRO T    1    GLY T    2          0         1.80                     
CISPEP  17 VAL W  321    GLU W  322          0        -6.61                     
CISPEP  18 PRO X    1    GLY X    2          0         0.80                     
CRYST1   31.790  114.240  135.980  90.12  92.32  90.01 P 1          12          
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      0.031456  0.000004  0.001274        0.00000                         
SCALE2      0.000000  0.008754  0.000019        0.00000                         
SCALE3      0.000000  0.000000  0.007360        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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