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Database: PDB
Entry: 4Z4P
LinkDB: 4Z4P
Original site: 4Z4P 
HEADER    TRANSFERASE                             02-APR-15   4Z4P              
TITLE     STRUCTURE OF THE MLL4 SET DOMAIN                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE 2D;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 5385-5539;                                    
COMPND   5 SYNONYM: LYSINE N-METHYLTRANSFERASE 2D,ALL1-RELATED PROTEIN,         
COMPND   6 MYELOID/LYMPHOID OR MIXED-LINEAGE LEUKEMIA PROTEIN 2;                
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KMT2D, ALR, MLL2, MLL4;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI #1/H766;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 1354003                                     
KEYWDS    TRANSFERASE, SET DOMAIN METHYLTRANSFERASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.ZHANG,A.MITTAL,J.REID,S.REICH,S.J.GAMBLIN,J.R.WILSON                
REVDAT   2   14-OCT-15 4Z4P    1       JRNL                                     
REVDAT   1   09-SEP-15 4Z4P    0                                                
JRNL        AUTH   Y.ZHANG,A.MITTAL,J.REID,S.REICH,S.J.GAMBLIN,J.R.WILSON       
JRNL        TITL   EVOLVING CATALYTIC PROPERTIES OF THE MLL FAMILY SET DOMAIN.  
JRNL        REF    STRUCTURE                     V.  23  1921 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26320581                                                     
JRNL        DOI    10.1016/J.STR.2015.07.018                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0124                                      
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) : 47.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 7143                           
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 366                             
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) : 502                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 34                           
REMARK   3   BIN FREE R VALUE                    : 0.1670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1335                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 27                                      
REMARK   3   SOLVENT ATOMS            : 60                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.63000                                             
REMARK   3    B22 (A**2) : -0.43000                                             
REMARK   3    B33 (A**2) : 1.55000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.16000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.194         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.000         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.017         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   : 1.20                                          
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                                                           
REMARK   4                                                                      
REMARK   4 4Z4P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208630.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7566                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
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) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1O9S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL 20 % ETHANOL, PH 8.5,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       20.34600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 9770 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A  5379                                                      
REMARK 465     HIS A  5541                                                      
REMARK 465     HIS A  5542                                                      
REMARK 465     HIS A  5543                                                      
REMARK 465     HIS A  5544                                                      
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    ILE A5406      -62.16   -108.79                                   
REMARK 500    ASN A5456     -165.51   -161.82                                   
REMARK 500    ASP A5489       65.31     35.65                                   
REMARK 500    GLN A5513       51.52     73.23                                   
REMARK 500    GLU A5517       71.59    -53.41                                   
REMARK 500    ASP A5518     -123.67     40.75                                   
REMARK 500    ASP A5519      -71.91     76.15                                   
REMARK 500    GLU A5522      141.33   -176.80                                   
REMARK 500    LYS A5534       -5.71     62.17                                   
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 A5601  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A5477   SG                                                     
REMARK 620 2 CYS A5525   SG  112.2                                              
REMARK 620 3 CYS A5527   SG  106.9 113.1                                        
REMARK 620 4 CYS A5532   SG  110.2 103.5 111.0                                  
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 5601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 5602                
DBREF  4Z4P A 5382  5536  UNP    O14686   KMT2D_HUMAN   5385   5539             
SEQADV 4Z4P MET A 5379  UNP  O14686              INITIATING METHIONINE          
SEQADV 4Z4P THR A 5380  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P LEU A 5381  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P GLU A 5522  UNP  O14686    LYS  5525 ENGINEERED MUTATION            
SEQADV 4Z4P LYS A 5537  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P GLY A 5538  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P HIS A 5539  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P HIS A 5540  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P HIS A 5541  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P HIS A 5542  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P HIS A 5543  UNP  O14686              EXPRESSION TAG                 
SEQADV 4Z4P HIS A 5544  UNP  O14686              EXPRESSION TAG                 
SEQRES   1 A  166  MET THR LEU HIS SER LYS SER SER GLN TYR ARG ARG LEU          
SEQRES   2 A  166  ARG THR GLU TRP LYS ASN ASN VAL TYR LEU ALA ARG SER          
SEQRES   3 A  166  ARG ILE GLN GLY LEU GLY LEU TYR ALA ALA LYS ASP LEU          
SEQRES   4 A  166  GLU LYS HIS THR MET VAL ILE GLU TYR ILE GLY THR ILE          
SEQRES   5 A  166  ILE ARG ASN GLU VAL ALA ASN ARG ARG GLU LYS ILE TYR          
SEQRES   6 A  166  GLU GLU GLN ASN ARG GLY ILE TYR MET PHE ARG ILE ASN          
SEQRES   7 A  166  ASN GLU HIS VAL ILE ASP ALA THR LEU THR GLY GLY PRO          
SEQRES   8 A  166  ALA ARG TYR ILE ASN HIS SER CYS ALA PRO ASN CYS VAL          
SEQRES   9 A  166  ALA GLU VAL VAL THR PHE ASP LYS GLU ASP LYS ILE ILE          
SEQRES  10 A  166  ILE ILE SER SER ARG ARG ILE PRO LYS GLY GLU GLU LEU          
SEQRES  11 A  166  THR TYR ASP TYR GLN PHE ASP PHE GLU ASP ASP GLN HIS          
SEQRES  12 A  166  GLU ILE PRO CYS HIS CYS GLY ALA TRP ASN CYS ARG LYS          
SEQRES  13 A  166  TRP MET LYS GLY HIS HIS HIS HIS HIS HIS                      
HET     ZN  A5601       1                                                       
HET    SAH  A5602      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  SAH    C14 H20 N6 O5 S                                              
FORMUL   4  HOH   *60(H2 O)                                                     
HELIX    1 AA1 SER A 5383  ASN A 5398  1                                  16    
HELIX    2 AA2 ASN A 5433  GLU A 5445  1                                  13    
HELIX    3 AA3 GLY A 5468  ILE A 5473  5                                   6    
SHEET    1 AA1 2 VAL A5399  ARG A5403  0                                        
SHEET    2 AA1 2 LEU A5409  ALA A5413 -1  O  GLY A5410   N  ALA A5402           
SHEET    1 AA2 3 MET A5422  GLU A5425  0                                        
SHEET    2 AA2 3 GLU A5491  SER A5498 -1  O  ILE A5496   N  VAL A5423           
SHEET    3 AA2 3 CYS A5481  PHE A5488 -1  N  VAL A5482   O  ILE A5497           
SHEET    1 AA3 3 THR A5429  ARG A5432  0                                        
SHEET    2 AA3 3 HIS A5459  ASP A5462 -1  O  VAL A5460   N  ILE A5431           
SHEET    3 AA3 3 MET A5452  ARG A5454 -1  N  PHE A5453   O  ILE A5461           
SHEET    1 AA4 2 ASN A5474  HIS A5475  0                                        
SHEET    2 AA4 2 THR A5509  TYR A5510  1  O  TYR A5510   N  ASN A5474           
SHEET    1 AA5 2 ILE A5523  PRO A5524  0                                        
SHEET    2 AA5 2 TRP A5535  MET A5536 -1  O  MET A5536   N  ILE A5523           
LINK         SG  CYS A5477                ZN    ZN A5601     1555   1555  2.53  
LINK         SG  CYS A5525                ZN    ZN A5601     1555   1555  2.24  
LINK         SG  CYS A5527                ZN    ZN A5601     1555   1555  2.24  
LINK         SG  CYS A5532                ZN    ZN A5601     1555   1555  2.42  
SITE     1 AC1  4 CYS A5477  CYS A5525  CYS A5527  CYS A5532                    
SITE     1 AC2 17 ILE A5406  GLN A5407  GLY A5408  LEU A5409                    
SITE     2 AC2 17 TYR A5451  ARG A5471  TYR A5472  ASN A5474                    
SITE     3 AC2 17 HIS A5475  TYR A5512  ILE A5523  PRO A5524                    
SITE     4 AC2 17 CYS A5525  HIS A5526  CYS A5527  MET A5536                    
SITE     5 AC2 17 HIS A5539                                                     
CRYST1   38.299   40.692   50.965  90.00 109.78  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026110  0.000000  0.009390        0.00000                         
SCALE2      0.000000  0.024575  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020852        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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