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Database: PDB
Entry: 4YPE
LinkDB: 4YPE
Original site: 4YPE 
HEADER    TRANSFERASE                             12-MAR-15   4YPE              
TITLE     ASH1L SET DOMAIN H2193F 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 4YPE    1       REMARK                                   
REVDAT   4   27-SEP-17 4YPE    1       JRNL   REMARK                            
REVDAT   3   16-SEP-15 4YPE    1       JRNL                                     
REVDAT   2   09-SEP-15 4YPE    1       JRNL                                     
REVDAT   1   02-SEP-15 4YPE    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20191                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1094                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1301                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.3360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 107                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : -0.10000                                             
REMARK   3    B33 (A**2) : 0.15000                                              
REMARK   3    B12 (A**2) : -0.05000                                             
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): 0.396         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.260         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.933         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3539 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4768 ; 1.940 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   422 ; 7.643 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   189 ;39.172 ;24.021       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   621 ;16.300 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;22.533 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   482 ; 0.132 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2743 ; 0.008 ; 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):  2093 ; 1.254 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3364 ; 2.305 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1446 ; 3.101 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1401 ; 4.738 ; 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 4YPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207779.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-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-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21349                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 86.1                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38500                            
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   (%): 46.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
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      154.76800            
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       77.38400            
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       77.38400            
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      154.76800            
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     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     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     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  2104    ZN     ZN B  2303              1.25            
REMARK 500   NH2  ARG B  2073     O    HOH B  2401              2.06            
REMARK 500   OD2  ASP A  2199     NZ   LYS A  2228              2.16            
REMARK 500   OD1  ASP A  2098     OG1  THR A  2100              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL B2139   CB    VAL B2139   CG1    -0.131                       
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    CYS A2117   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A2236   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    VAL A2262   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    VAL A2262   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    CYS B2117   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG B2182   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B2236   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG B2236   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 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      -80.85    -95.69                                   
REMARK 500    THR A2090       73.13     73.91                                   
REMARK 500    PRO A2123       -8.52    -57.01                                   
REMARK 500    ASN A2130       47.16   -109.15                                   
REMARK 500    GLN A2131       29.46   -147.79                                   
REMARK 500    GLU A2148     -123.07     38.36                                   
REMARK 500    ASN A2189       22.93     48.00                                   
REMARK 500    CYS A2195      140.10   -173.88                                   
REMARK 500    CYS A2195      136.15   -170.71                                   
REMARK 500    ASP A2199      130.45   -171.60                                   
REMARK 500    SER A2200       62.23     39.84                                   
REMARK 500    VAL B2078      -80.31    -96.69                                   
REMARK 500    VAL B2105      -83.91    -99.05                                   
REMARK 500    GLU B2149       15.24     59.54                                   
REMARK 500    ILE B2167      144.17   -171.69                                   
REMARK 500    ASP B2199      163.02     76.99                                   
REMARK 500    PHE B2257      -63.42    -91.63                                   
REMARK 500    ASN B2261       -4.04     67.32                                   
REMARK 500    LYS B2274       43.87   -109.37                                   
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 ALA B 2147     GLU B 2148                  144.55                    
REMARK 500 PHE B 2260     ASN B 2261                  148.13                    
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  107.8                                              
REMARK 620 3 CYS A2104   SG  102.1 102.0                                        
REMARK 620 4 CYS A2108   SG  129.2 105.5 107.1                                  
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  102.1                                              
REMARK 620 3 CYS A2122   SG   99.5 112.4                                        
REMARK 620 4 CYS A2128   SG  118.4 115.0 108.4                                  
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  111.0                                              
REMARK 620 3 CYS A2270   SG  109.3 111.7                                        
REMARK 620 4 CYS A2275   SG  109.7 103.2 111.9                                  
REMARK 620 N                    1     2     3                                   
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 B2117   SG                                                     
REMARK 620 2 CYS B2122   SG  114.1                                              
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  115.3                                              
REMARK 620 3 CYS B2270   SG  109.3 106.9                                        
REMARK 620 4 CYS B2275   SG  111.8 103.0 110.2                                  
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                                   
DBREF  4YPE A 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
DBREF  4YPE B 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
SEQADV 4YPE GLY A 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE ALA A 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE MET A 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE ALA A 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE GLY A 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE SER A 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE PHE A 2193  UNP  Q9NR48    HIS  2198 ENGINEERED MUTATION            
SEQADV 4YPE GLY B 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE ALA B 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE MET B 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE ALA B 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE GLY B 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE SER B 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPE PHE B 2193  UNP  Q9NR48    HIS  2198 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  PHE 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 LYS 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  PHE 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 LYS 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   *107(H2 O)                                                    
HELIX    1 AA1 ASN A 2110  PHE A 2114  5                                   5    
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 ASN B 2110  PHE B 2114  5                                   5    
HELIX    7 AA7 GLU B 2176  GLN B 2186  1                                  11    
HELIX    8 AA8 ASN B 2211  ILE B 2216  5                                   6    
HELIX    9 AA9 ASP B 2254  SER B 2259  1                                   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  ASP A2199 -1  N  LEU A2196   O  ILE A2204           
SHEET    1 AA3 2 LEU A2142  ARG A2146  0                                        
SHEET    2 AA3 2 TRP A2152  THR A2156 -1  O  GLY A2153   N  PHE A2145           
SHEET    1 AA4 3 PHE A2165  GLU A2168  0                                        
SHEET    2 AA4 3 VAL A2234  ALA A2241 -1  O  LEU A2239   N  ILE A2166           
SHEET    3 AA4 3 CYS A2224  VAL A2231 -1  N  GLN A2227   O  GLY A2238           
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  ASP B2199 -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  GLY B2153   N  PHE B2145           
SHEET    1 AB1 3 PHE B2165  GLU B2168  0                                        
SHEET    2 AB1 3 VAL B2234  ALA B2241 -1  O  LEU B2239   N  ILE B2167           
SHEET    3 AB1 3 CYS B2224  VAL B2231 -1  N  VAL B2231   O  VAL B2234           
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  2.57  
SSBOND   2 CYS B 2122    CYS B 2128                          1555   1555  3.00  
LINK         SG  CYS A2091                ZN    ZN A2303     1555   1555  2.12  
LINK         SG  CYS A2093                ZN    ZN A2303     1555   1555  2.20  
LINK         SG  CYS A2104                ZN    ZN A2303     1555   1555  2.12  
LINK         SG  CYS A2104                ZN    ZN A2302     1555   1555  2.45  
LINK         SG  CYS A2108                ZN    ZN A2303     1555   1555  2.38  
LINK         SG  CYS A2117                ZN    ZN A2302     1555   1555  2.18  
LINK         SG  CYS A2122                ZN    ZN A2302     1555   1555  2.43  
LINK         SG  CYS A2128                ZN    ZN A2302     1555   1555  1.94  
LINK         SG  CYS A2220                ZN    ZN A2301     1555   1555  2.29  
LINK         SG  CYS A2268                ZN    ZN A2301     1555   1555  2.08  
LINK         SG  CYS A2270                ZN    ZN A2301     1555   1555  2.14  
LINK         SG  CYS A2275                ZN    ZN A2301     1555   1555  2.48  
LINK         SG  CYS B2108                ZN    ZN B2303     1555   1555  2.24  
LINK         SG  CYS B2117                ZN    ZN B2302     1555   1555  2.12  
LINK         SG  CYS B2122                ZN    ZN B2302     1555   1555  2.26  
LINK         SG  CYS B2220                ZN    ZN B2301     1555   1555  2.26  
LINK         SG  CYS B2268                ZN    ZN B2301     1555   1555  2.27  
LINK         SG  CYS B2270                ZN    ZN B2301     1555   1555  1.95  
LINK         SG  CYS B2275                ZN    ZN B2301     1555   1555  2.34  
SITE     1 AC1  4 CYS A2220  CYS A2268  CYS A2270  CYS A2275                    
SITE     1 AC2  4 CYS A2104  CYS A2117  CYS A2122  CYS A2128                    
SITE     1 AC3  4 CYS A2091  CYS A2093  CYS A2104  CYS A2108                    
SITE     1 AC4 16 LYS A2150  TRP A2152  ASP A2192  PHE A2193                    
SITE     2 AC4 16 TYR A2194  ARG A2214  PHE A2215  ASN A2217                    
SITE     3 AC4 16 HIS A2218  TYR A2255  GLN A2266  LEU A2267                    
SITE     4 AC4 16 CYS A2268  LYS A2269  ILE A2279  HOH A2411                    
SITE     1 AC5  4 CYS B2220  CYS B2268  CYS B2270  CYS B2275                    
SITE     1 AC6  5 CYS B2104  CYS B2117  CYS B2122  CYS B2128                    
SITE     2 AC6  5  ZN B2303                                                     
SITE     1 AC7  5 CYS B2091  CYS B2104  CYS B2108  CYS B2117                    
SITE     2 AC7  5  ZN B2302                                                     
SITE     1 AC8 14 LYS B2150  TRP B2152  ASP B2192  PHE B2193                    
SITE     2 AC8 14 TYR B2194  ARG B2214  PHE B2215  ILE B2216                    
SITE     3 AC8 14 ASN B2217  HIS B2218  TYR B2255  LEU B2267                    
SITE     4 AC8 14 LYS B2269  ILE B2279                                          
CRYST1   58.838   58.838  232.152  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      0.016996  0.009813  0.000000        0.00000                         
SCALE2      0.000000  0.019625  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004308        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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