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Database: PDB
Entry: 5TEG
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HEADER    TRANSFERASE                             21-SEP-16   5TEG              
TITLE     CRYSTAL STRUCTURE OF HSETD8 IN COMPLEX WITH HISTONE H4K20 NORLEUCINE  
TITLE    2 MUTANT PEPTIDE AND S-ADENOSYLMETHIONINE                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: N-LYSINE METHYLTRANSFERASE KMT5A;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 234-393;                                      
COMPND   5 SYNONYM: H4-K20-HMTASE KMT5A,HISTONE-LYSINE N-METHYLTRANSFERASE      
COMPND   6 KMT5A,LYSINE N-METHYLTRANSFERASE 5A,LYSINE-SPECIFIC METHYLASE 5A,    
COMPND   7 PR/SET DOMAIN-CONTAINING PROTEIN 07,PR/SET07,SET DOMAIN-CONTAINING   
COMPND   8 PROTEIN 8;                                                           
COMPND   9 EC: 2.1.1.-,2.1.1.43;                                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 2;                                                           
COMPND  13 MOLECULE: HISTONE H4 MUTANT PEPTIDE WITH H4K20NORLEUCINE;            
COMPND  14 CHAIN: D, E;                                                         
COMPND  15 FRAGMENT: UNP RESIDUES 16-23;                                        
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 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: KMT5A, PRSET7, SET07, SET8, SETD8;                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-T1R;                             
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSFERASE, HISTONE H4, NORLEUCINE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.A.JUDGE,A.M.PETROS                                                  
REVDAT   3   25-APR-18 5TEG    1       JRNL                                     
REVDAT   2   21-DEC-16 5TEG    1       JRNL                                     
REVDAT   1   07-DEC-16 5TEG    0                                                
JRNL        AUTH   R.A.JUDGE,H.ZHU,A.K.UPADHYAY,P.M.BODELLE,C.W.HUTCHINS,       
JRNL        AUTH 2 M.TORRENT,V.L.MARIN,W.YU,M.VEDADI,F.LI,P.J.BROWN,            
JRNL        AUTH 3 W.N.PAPPANO,C.SUN,A.M.PETROS                                 
JRNL        TITL   TURNING A SUBSTRATE PEPTIDE INTO A POTENT INHIBITOR FOR THE  
JRNL        TITL 2 HISTONE METHYLTRANSFERASE SETD8.                             
JRNL        REF    ACS MED CHEM LETT             V.   7  1102 2016              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   27994746                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.6B00303                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.11.6                                    
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 83124                          
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)  : 0.191                          
REMARK   3   R VALUE            (WORKING SET)  : 0.189                          
REMARK   3   FREE R VALUE                      : 0.210                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.040                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 4188                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.33                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 76.45                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5140                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4891                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2140                   
REMARK   3   BIN FREE R VALUE                        : 0.2360                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.84                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 249                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2682                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 330                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.24                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.94600                                              
REMARK   3    B22 (A**2) : -0.75370                                             
REMARK   3    B33 (A**2) : -0.19220                                             
REMARK   3    B12 (A**2) : -0.06360                                             
REMARK   3    B13 (A**2) : 1.50060                                              
REMARK   3    B23 (A**2) : 0.98810                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.170               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.054               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.055               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.053               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.054               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2784   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3736   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1030   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 70     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 427    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2784   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 357    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3243   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.07                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.40                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 14.44                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5TEG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224094.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83159                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.811                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: 1ZKK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 33% (V/V) PENTAERYTHRITOL ETHOXYLATE,    
REMARK 280  50 MM AMMONIUM SULFATE, 50 MM BIS-TRIS PH 6.5, VAPOR DIFFUSION,     
REMARK 280  TEMPERATURE 290K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9640 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9350 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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     LYS B   193                                                      
REMARK 465     SER B   194                                                      
REMARK 465     LYS E    16                                                      
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 A 242      -66.12   -104.79                                   
REMARK 500    LEU A 278     -120.83     60.11                                   
REMARK 500    VAL B 242      -60.43   -107.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 401                 
DBREF  5TEG A  193   352  UNP    Q9NQR1   KMT5A_HUMAN    234    393             
DBREF  5TEG B  193   352  UNP    Q9NQR1   KMT5A_HUMAN    234    393             
DBREF  5TEG D   16    23  PDB    5TEG     5TEG            16     23             
DBREF  5TEG E   16    23  PDB    5TEG     5TEG            16     23             
SEQADV 5TEG SER A  302  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQADV 5TEG SER B  302  UNP  Q9NQR1    CYS   343 ENGINEERED MUTATION            
SEQRES   1 A  160  LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS ARG          
SEQRES   2 A  160  ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY MET          
SEQRES   3 A  160  LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL ILE          
SEQRES   4 A  160  ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL GLU          
SEQRES   5 A  160  TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS LYS          
SEQRES   6 A  160  ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY CYS          
SEQRES   7 A  160  TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR CYS          
SEQRES   8 A  160  VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG LEU          
SEQRES   9 A  160  ILE ASN HIS SER LYS SER GLY ASN CYS GLN THR LYS LEU          
SEQRES  10 A  160  HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE ALA          
SEQRES  11 A  160  SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR ASP          
SEQRES  12 A  160  TYR GLY ASP ARG SER LYS ALA SER ILE GLU ALA HIS PRO          
SEQRES  13 A  160  TRP LEU LYS HIS                                              
SEQRES   1 B  160  LYS SER LYS ALA GLU LEU GLN SER GLU GLU ARG LYS ARG          
SEQRES   2 B  160  ILE ASP GLU LEU ILE GLU SER GLY LYS GLU GLU GLY MET          
SEQRES   3 B  160  LYS ILE ASP LEU ILE ASP GLY LYS GLY ARG GLY VAL ILE          
SEQRES   4 B  160  ALA THR LYS GLN PHE SER ARG GLY ASP PHE VAL VAL GLU          
SEQRES   5 B  160  TYR HIS GLY ASP LEU ILE GLU ILE THR ASP ALA LYS LYS          
SEQRES   6 B  160  ARG GLU ALA LEU TYR ALA GLN ASP PRO SER THR GLY CYS          
SEQRES   7 B  160  TYR MET TYR TYR PHE GLN TYR LEU SER LYS THR TYR CYS          
SEQRES   8 B  160  VAL ASP ALA THR ARG GLU THR ASN ARG LEU GLY ARG LEU          
SEQRES   9 B  160  ILE ASN HIS SER LYS SER GLY ASN CYS GLN THR LYS LEU          
SEQRES  10 B  160  HIS ASP ILE ASP GLY VAL PRO HIS LEU ILE LEU ILE ALA          
SEQRES  11 B  160  SER ARG ASP ILE ALA ALA GLY GLU GLU LEU LEU TYR ASP          
SEQRES  12 B  160  TYR GLY ASP ARG SER LYS ALA SER ILE GLU ALA HIS PRO          
SEQRES  13 B  160  TRP LEU LYS HIS                                              
SEQRES   1 D    8  LYS ARG HIS ARG NLE VAL LEU ARG                              
SEQRES   1 E    8  LYS ARG HIS ARG NLE VAL LEU ARG                              
HET    NLE  D  20       8                                                       
HET    NLE  E  20       8                                                       
HET    SAM  A 401      27                                                       
HET    SAM  B 401      27                                                       
HETNAM     NLE NORLEUCINE                                                       
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   3  NLE    2(C6 H13 N O2)                                               
FORMUL   5  SAM    2(C15 H22 N6 O5 S)                                           
FORMUL   7  HOH   *330(H2 O)                                                    
HELIX    1 AA1 SER A  194  GLY A  213  1                                  20    
HELIX    2 AA2 ILE A  252  ALA A  263  1                                  12    
HELIX    3 AA3 LEU A  293  ILE A  297  5                                   5    
HELIX    4 AA4 SER A  340  HIS A  347  1                                   8    
HELIX    5 AA5 PRO A  348  HIS A  352  5                                   5    
HELIX    6 AA6 ALA B  196  GLY B  213  1                                  18    
HELIX    7 AA7 ILE B  252  GLN B  264  1                                  13    
HELIX    8 AA8 LEU B  293  ILE B  297  5                                   5    
HELIX    9 AA9 SER B  340  HIS B  347  1                                   8    
HELIX   10 AB1 PRO B  348  HIS B  352  5                                   5    
SHEET    1 AA1 2 MET A 218  ILE A 223  0                                        
SHEET    2 AA1 2 GLY A 227  ALA A 232 -1  O  ILE A 231   N  LYS A 219           
SHEET    1 AA2 3 PHE A 241  TYR A 245  0                                        
SHEET    2 AA2 3 VAL A 315  ALA A 322 -1  O  LEU A 320   N  VAL A 243           
SHEET    3 AA2 3 CYS A 305  ILE A 312 -1  N  LYS A 308   O  ILE A 319           
SHEET    1 AA3 4 ASP A 248  GLU A 251  0                                        
SHEET    2 AA3 4 LYS A 280  ASP A 285 -1  O  ASP A 285   N  ASP A 248           
SHEET    3 AA3 4 MET A 272  TYR A 277 -1  N  PHE A 275   O  TYR A 282           
SHEET    4 AA3 4 NLE D  20  VAL D  21  1  O  NLE D  20   N  TYR A 274           
SHEET    1 AA4 2 ASN A 298  HIS A 299  0                                        
SHEET    2 AA4 2 LEU A 333  TYR A 334  1  O  TYR A 334   N  ASN A 298           
SHEET    1 AA5 2 MET B 218  ILE B 223  0                                        
SHEET    2 AA5 2 GLY B 227  ALA B 232 -1  O  GLY B 227   N  ILE B 223           
SHEET    1 AA6 3 PHE B 241  TYR B 245  0                                        
SHEET    2 AA6 3 VAL B 315  ALA B 322 -1  O  LEU B 320   N  VAL B 243           
SHEET    3 AA6 3 CYS B 305  ILE B 312 -1  N  HIS B 310   O  HIS B 317           
SHEET    1 AA7 4 ASP B 248  GLU B 251  0                                        
SHEET    2 AA7 4 LYS B 280  ASP B 285 -1  O  ASP B 285   N  ASP B 248           
SHEET    3 AA7 4 MET B 272  TYR B 277 -1  N  PHE B 275   O  TYR B 282           
SHEET    4 AA7 4 NLE E  20  VAL E  21  1  O  NLE E  20   N  TYR B 274           
SHEET    1 AA8 2 ASN B 298  HIS B 299  0                                        
SHEET    2 AA8 2 LEU B 333  TYR B 334  1  O  TYR B 334   N  ASN B 298           
LINK         C   ARG D  19                 N   NLE D  20     1555   1555  1.33  
LINK         C   NLE D  20                 N   VAL D  21     1555   1555  1.34  
LINK         C   ARG E  19                 N   NLE E  20     1555   1555  1.33  
LINK         C   NLE E  20                 N   VAL E  21     1555   1555  1.36  
SITE     1 AC1 16 GLY A 225  LYS A 226  ARG A 228  CYS A 270                    
SITE     2 AC1 16 TYR A 271  ARG A 295  LEU A 296  ILE A 297                    
SITE     3 AC1 16 ASN A 298  HIS A 299  TYR A 336  TRP A 349                    
SITE     4 AC1 16 HOH A 501  HOH A 558  HOH A 622  HIS D  18                    
SITE     1 AC2 20 HOH A 615  GLY B 225  LYS B 226  ARG B 228                    
SITE     2 AC2 20 CYS B 270  TYR B 271  ARG B 295  LEU B 296                    
SITE     3 AC2 20 ILE B 297  ASN B 298  HIS B 299  TYR B 336                    
SITE     4 AC2 20 TRP B 349  HOH B 509  HOH B 546  HOH B 551                    
SITE     5 AC2 20 HOH B 573  HOH B 587  HOH B 619  HIS E  18                    
CRYST1   44.310   45.059   52.649 114.73  90.77  90.81 P 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      0.022568  0.000319  0.000481        0.00000                         
SCALE2      0.000000  0.022195  0.010231        0.00000                         
SCALE3      0.000000  0.000000  0.020916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system