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Database: PDB
Entry: 4YPU
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Original site: 4YPU 
HEADER    TRANSFERASE                             13-MAR-15   4YPU              
TITLE     ASH1L SET DOMAIN K2264L MUTANT IN COMPLEX WITH S-ADENOSYL METHIONINE  
TITLE    2 (SAM)                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SET DOMAIN (UNP RESIDUES 2074-2293);                       
COMPND   5 SYNONYM: ASH1-LIKE PROTEIN,HUASH1,ABSENT SMALL AND HOMEOTIC DISKS    
COMPND   6 PROTEIN 1 HOMOLOG,LYSINE N-METHYLTRANSFERASE 2H;                     
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ASH1L, KIAA1420, KMT2H;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HISTONE METHYLATION, SET DOMAIN, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.S.ROGAWSKI,J.NDOJ,H.J.CHO,I.MAILLARD,J.GREMBECKA,T.CIERPICKI        
REVDAT   5   04-OCT-17 4YPU    1       REMARK                                   
REVDAT   4   27-SEP-17 4YPU    1       JRNL   REMARK                            
REVDAT   3   16-SEP-15 4YPU    1       JRNL                                     
REVDAT   2   09-SEP-15 4YPU    1       JRNL                                     
REVDAT   1   02-SEP-15 4YPU    0                                                
JRNL        AUTH   D.S.ROGAWSKI,J.NDOJ,H.J.CHO,I.MAILLARD,J.GREMBECKA,          
JRNL        AUTH 2 T.CIERPICKI                                                  
JRNL        TITL   TWO LOOPS UNDERGOING CONCERTED DYNAMICS REGULATE THE         
JRNL        TITL 2 ACTIVITY OF THE ASH1L HISTONE METHYLTRANSFERASE.             
JRNL        REF    BIOCHEMISTRY                  V.  54  5401 2015              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   26292256                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.5B00697                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 14072                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 749                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 984                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.3990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3277                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.14                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.17000                                             
REMARK   3    B22 (A**2) : -0.17000                                             
REMARK   3    B33 (A**2) : 0.26000                                              
REMARK   3    B12 (A**2) : -0.09000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.521         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.396         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.312         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.035        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.875                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3406 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4586 ; 1.479 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   400 ; 6.243 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   183 ;40.181 ;24.044       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   596 ;17.295 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;23.035 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   463 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2634 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2009 ; 0.896 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3226 ; 1.693 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1397 ; 2.043 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1360 ; 3.367 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4YPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207904.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3-7.8                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14871                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4YNM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 20 MM TRIS, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      150.69533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       75.34767            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       75.34767            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      150.69533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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  2063                                                      
REMARK 465     ALA A  2064                                                      
REMARK 465     MET A  2065                                                      
REMARK 465     ALA A  2066                                                      
REMARK 465     GLY A  2281                                                      
REMARK 465     LYS A  2282                                                      
REMARK 465     SER A  2283                                                      
REMARK 465     GLN A  2284                                                      
REMARK 465     ARG A  2285                                                      
REMARK 465     VAL A  2286                                                      
REMARK 465     ASN A  2287                                                      
REMARK 465     GLY A  2288                                                      
REMARK 465     GLY B  2063                                                      
REMARK 465     ALA B  2064                                                      
REMARK 465     MET B  2065                                                      
REMARK 465     ALA B  2066                                                      
REMARK 465     GLU B  2087                                                      
REMARK 465     ALA B  2088                                                      
REMARK 465     THR B  2089                                                      
REMARK 465     THR B  2090                                                      
REMARK 465     CYS B  2091                                                      
REMARK 465     ASN B  2092                                                      
REMARK 465     CYS B  2093                                                      
REMARK 465     LYS B  2094                                                      
REMARK 465     LYS B  2095                                                      
REMARK 465     PRO B  2096                                                      
REMARK 465     ASP B  2097                                                      
REMARK 465     ASP B  2098                                                      
REMARK 465     ASP B  2099                                                      
REMARK 465     THR B  2100                                                      
REMARK 465     ARG B  2101                                                      
REMARK 465     LYS B  2102                                                      
REMARK 465     GLY B  2103                                                      
REMARK 465     SER B  2259                                                      
REMARK 465     PHE B  2260                                                      
REMARK 465     ASN B  2261                                                      
REMARK 465     VAL B  2262                                                      
REMARK 465     GLU B  2263                                                      
REMARK 465     LEU B  2264                                                      
REMARK 465     GLY B  2280                                                      
REMARK 465     GLY B  2281                                                      
REMARK 465     LYS B  2282                                                      
REMARK 465     SER B  2283                                                      
REMARK 465     GLN B  2284                                                      
REMARK 465     ARG B  2285                                                      
REMARK 465     VAL B  2286                                                      
REMARK 465     ASN B  2287                                                      
REMARK 465     GLY B  2288                                                      
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   SG   CYS B  2128    ZN     ZN B  2302              1.65            
REMARK 500   OE1  GLN B  2131     NH1  ARG B  2135              2.10            
REMARK 500   O    TYR B  2086     O    HOH B  2401              2.18            
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 A2236   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    VAL A2078      -72.82    -67.77                                   
REMARK 500    THR A2090      121.51    -11.96                                   
REMARK 500    THR A2100       21.62    -78.36                                   
REMARK 500    ASP A2106     -109.73    -75.91                                   
REMARK 500    ASP A2107       55.48    -94.87                                   
REMARK 500    ASN A2120        0.09    -69.01                                   
REMARK 500    THR A2121       -2.77   -150.21                                   
REMARK 500    GLN A2131       27.58   -143.30                                   
REMARK 500    ALA A2162      127.63    -39.05                                   
REMARK 500    GLN A2186      -45.50   -160.37                                   
REMARK 500    LEU A2198      -78.07   -112.75                                   
REMARK 500    GLU A2263       64.28     61.68                                   
REMARK 500    LEU A2264       64.77   -110.37                                   
REMARK 500    VAL B2078      -86.59    -80.02                                   
REMARK 500    PRO B2082       95.04    -67.81                                   
REMARK 500    ASP B2106       -6.04   -140.20                                   
REMARK 500    PHE B2114       52.81     73.05                                   
REMARK 500    PRO B2119       34.78    -61.31                                   
REMARK 500    ASN B2120      -60.47   -137.74                                   
REMARK 500    CYS B2124       31.91    -83.93                                   
REMARK 500    GLU B2126      -73.34    -65.85                                   
REMARK 500    CYS B2128      108.58    -46.29                                   
REMARK 500    GLN B2131       42.99   -149.26                                   
REMARK 500    GLU B2148      118.61    -33.88                                   
REMARK 500    ALA B2162      122.91    -32.62                                   
REMARK 500    ILE B2167      148.23   -173.73                                   
REMARK 500    ASP B2199      -66.05    116.77                                   
REMARK 500    SER B2200       48.88    -86.21                                   
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 A2303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2091   SG                                                     
REMARK 620 2 CYS A2093   SG  105.2                                              
REMARK 620 3 CYS A2104   SG  117.0  99.1                                        
REMARK 620 4 CYS A2108   SG  115.2 104.2 113.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2104   SG                                                     
REMARK 620 2 CYS A2117   SG  113.9                                              
REMARK 620 3 CYS A2122   SG  103.7 106.3                                        
REMARK 620 4 CYS A2128   SG  109.3 112.0 111.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2220   SG                                                     
REMARK 620 2 CYS A2268   SG  114.4                                              
REMARK 620 3 CYS A2275   SG  106.4 100.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2104   SG                                                     
REMARK 620 2 CYS B2117   SG   92.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2104   SG                                                     
REMARK 620 2 CYS B2108   SG   87.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2220   SG                                                     
REMARK 620 2 CYS B2268   SG  111.0                                              
REMARK 620 3 CYS B2270   SG  119.2 117.5                                        
REMARK 620 4 CYS B2275   SG  101.8  90.6 111.6                                  
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 A 2301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 2303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 2304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 2304                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YNM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YNP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YPA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YPE   RELATED DB: PDB                                   
DBREF  4YPU A 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
DBREF  4YPU B 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
SEQADV 4YPU GLY A 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU ALA A 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU MET A 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU ALA A 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU GLY A 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU SER A 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU LEU A 2264  UNP  Q9NR48    LYS  2269 ENGINEERED MUTATION            
SEQADV 4YPU GLY B 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU ALA B 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU MET B 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU ALA B 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU GLY B 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU SER B 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPU LEU B 2264  UNP  Q9NR48    LYS  2269 ENGINEERED MUTATION            
SEQRES   1 A  226  GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN          
SEQRES   2 A  226  VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA          
SEQRES   3 A  226  THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG          
SEQRES   4 A  226  LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE          
SEQRES   5 A  226  ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN          
SEQRES   6 A  226  CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN          
SEQRES   7 A  226  CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY          
SEQRES   8 A  226  ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE          
SEQRES   9 A  226  ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE          
SEQRES  10 A  226  ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP          
SEQRES  11 A  226  HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP          
SEQRES  12 A  226  SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS          
SEQRES  13 A  226  SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL          
SEQRES  14 A  226  ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP          
SEQRES  15 A  226  MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE          
SEQRES  16 A  226  HIS SER PHE ASN VAL GLU LEU GLN GLN LEU CYS LYS CYS          
SEQRES  17 A  226  GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER          
SEQRES  18 A  226  GLN ARG VAL ASN GLY                                          
SEQRES   1 B  226  GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN          
SEQRES   2 B  226  VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA          
SEQRES   3 B  226  THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG          
SEQRES   4 B  226  LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE          
SEQRES   5 B  226  ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN          
SEQRES   6 B  226  CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN          
SEQRES   7 B  226  CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY          
SEQRES   8 B  226  ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE          
SEQRES   9 B  226  ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE          
SEQRES  10 B  226  ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP          
SEQRES  11 B  226  HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP          
SEQRES  12 B  226  SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS          
SEQRES  13 B  226  SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL          
SEQRES  14 B  226  ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP          
SEQRES  15 B  226  MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE          
SEQRES  16 B  226  HIS SER PHE ASN VAL GLU LEU GLN GLN LEU CYS LYS CYS          
SEQRES  17 B  226  GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER          
SEQRES  18 B  226  GLN ARG VAL ASN GLY                                          
HET     ZN  A2301       1                                                       
HET     ZN  A2302       1                                                       
HET     ZN  A2303       1                                                       
HET    SAM  A2304      27                                                       
HET     ZN  B2301       1                                                       
HET     ZN  B2302       1                                                       
HET     ZN  B2303       1                                                       
HET    SAM  B2304      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   3   ZN    6(ZN 2+)                                                     
FORMUL   6  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL  11  HOH   *36(H2 O)                                                     
HELIX    1 AA1 CYS A 2108  ILE A 2113  1                                   6    
HELIX    2 AA2 CYS A 2124  CYS A 2128  5                                   5    
HELIX    3 AA3 GLU A 2176  GLN A 2186  1                                  11    
HELIX    4 AA4 ASN A 2211  ILE A 2216  5                                   6    
HELIX    5 AA5 ASP A 2254  SER A 2259  1                                   6    
HELIX    6 AA6 GLU B 2176  GLN B 2186  1                                  11    
HELIX    7 AA7 ASN B 2211  ILE B 2216  5                                   6    
SHEET    1 AA1 2 LYS A2070  LYS A2071  0                                        
SHEET    2 AA1 2 MET A2209  GLY A2210  1  O  GLY A2210   N  LYS A2070           
SHEET    1 AA2 4 VAL A2076  TYR A2077  0                                        
SHEET    2 AA2 4 GLU A2172  SER A2175  1  O  VAL A2173   N  VAL A2076           
SHEET    3 AA2 4 MET A2202  ASP A2205 -1  O  ASP A2205   N  GLU A2172           
SHEET    4 AA2 4 CYS A2195  ASN A2197 -1  N  LEU A2196   O  ILE A2204           
SHEET    1 AA3 2 LEU A2142  ALA A2147  0                                        
SHEET    2 AA3 2 GLY A2151  THR A2156 -1  O  GLY A2151   N  ALA A2147           
SHEET    1 AA4 3 PHE A2165  TYR A2169  0                                        
SHEET    2 AA4 3 VAL A2234  ALA A2241 -1  O  LEU A2239   N  ILE A2167           
SHEET    3 AA4 3 CYS A2224  VAL A2231 -1  N  TRP A2229   O  ARG A2236           
SHEET    1 AA5 2 ASN A2217  HIS A2218  0                                        
SHEET    2 AA5 2 THR A2252  TYR A2253  1  O  TYR A2253   N  ASN A2217           
SHEET    1 AA6 2 GLN A2266  LEU A2267  0                                        
SHEET    2 AA6 2 ILE A2278  ILE A2279 -1  O  ILE A2279   N  GLN A2266           
SHEET    1 AA7 2 LYS B2070  LYS B2071  0                                        
SHEET    2 AA7 2 MET B2209  GLY B2210  1  O  GLY B2210   N  LYS B2070           
SHEET    1 AA8 4 VAL B2076  TYR B2077  0                                        
SHEET    2 AA8 4 GLU B2172  SER B2175  1  O  VAL B2173   N  VAL B2076           
SHEET    3 AA8 4 MET B2202  ASP B2205 -1  O  ASP B2205   N  GLU B2172           
SHEET    4 AA8 4 CYS B2195  ASN B2197 -1  N  LEU B2196   O  ILE B2204           
SHEET    1 AA9 2 LEU B2142  ARG B2146  0                                        
SHEET    2 AA9 2 TRP B2152  THR B2156 -1  O  ARG B2155   N  GLU B2143           
SHEET    1 AB1 3 PHE B2165  GLU B2168  0                                        
SHEET    2 AB1 3 VAL B2234  ALA B2241 -1  O  LEU B2239   N  ILE B2166           
SHEET    3 AB1 3 CYS B2224  VAL B2231 -1  N  GLN B2227   O  GLY B2238           
SHEET    1 AB2 2 ASN B2217  HIS B2218  0                                        
SHEET    2 AB2 2 THR B2252  TYR B2253  1  O  TYR B2253   N  ASN B2217           
SSBOND   1 CYS B 2104    CYS B 2108                          1555   1555  2.91  
SSBOND   2 CYS B 2122    CYS B 2128                          1555   1555  2.05  
LINK         SG  CYS A2091                ZN    ZN A2303     1555   1555  2.01  
LINK         SG  CYS A2093                ZN    ZN A2303     1555   1555  2.43  
LINK         SG  CYS A2104                ZN    ZN A2303     1555   1555  2.30  
LINK         SG  CYS A2104                ZN    ZN A2302     1555   1555  2.41  
LINK         SG  CYS A2108                ZN    ZN A2303     1555   1555  2.26  
LINK         SG  CYS A2117                ZN    ZN A2302     1555   1555  2.13  
LINK         SG  CYS A2122                ZN    ZN A2302     1555   1555  2.13  
LINK         SG  CYS A2128                ZN    ZN A2302     1555   1555  2.17  
LINK         SG  CYS A2220                ZN    ZN A2301     1555   1555  2.33  
LINK         SG  CYS A2268                ZN    ZN A2301     1555   1555  2.12  
LINK         SG  CYS A2275                ZN    ZN A2301     1555   1555  2.38  
LINK         SG  CYS B2104                ZN    ZN B2302     1555   1555  2.65  
LINK         SG  CYS B2104                ZN    ZN B2303     1555   1555  2.23  
LINK         SG  CYS B2108                ZN    ZN B2303     1555   1555  1.98  
LINK         SG  CYS B2117                ZN    ZN B2302     1555   1555  2.29  
LINK         SG  CYS B2220                ZN    ZN B2301     1555   1555  2.23  
LINK         SG  CYS B2268                ZN    ZN B2301     1555   1555  2.06  
LINK         SG  CYS B2270                ZN    ZN B2301     1555   1555  1.95  
LINK         SG  CYS B2275                ZN    ZN B2301     1555   1555  2.68  
SITE     1 AC1  4 CYS A2220  CYS A2268  CYS A2270  CYS A2275                    
SITE     1 AC2  5 CYS A2104  CYS A2117  CYS A2122  CYS A2128                    
SITE     2 AC2  5  ZN A2303                                                     
SITE     1 AC3  5 CYS A2091  CYS A2093  CYS A2104  CYS A2108                    
SITE     2 AC3  5  ZN A2302                                                     
SITE     1 AC4 14 LYS A2150  TRP A2152  SER A2191  ASP A2192                    
SITE     2 AC4 14 HIS A2193  TYR A2194  ARG A2214  PHE A2215                    
SITE     3 AC4 14 ASN A2217  HIS A2218  TYR A2255  GLN A2266                    
SITE     4 AC4 14 LEU A2267  LYS A2269                                          
SITE     1 AC5  4 CYS B2220  CYS B2268  CYS B2270  CYS B2275                    
SITE     1 AC6  4 CYS B2104  CYS B2117  CYS B2122  CYS B2128                    
SITE     1 AC7  3 CYS B2104  CYS B2108  LEU B2109                               
SITE     1 AC8 15 LYS B2150  GLY B2151  TRP B2152  SER B2191                    
SITE     2 AC8 15 ASP B2192  HIS B2193  TYR B2194  ARG B2214                    
SITE     3 AC8 15 PHE B2215  ASN B2217  HIS B2218  TYR B2255                    
SITE     4 AC8 15 GLN B2266  LEU B2267  LYS B2269                               
CRYST1   59.108   59.108  226.043  90.00  90.00 120.00 P 32 2 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      0.016918  0.009768  0.000000        0.00000                         
SCALE2      0.000000  0.019535  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004424        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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