GenomeNet

Database: PDB
Entry: 5V9I
LinkDB: 5V9I
Original site: 5V9I 
HEADER    TRANSFERASE                             23-MAR-17   5V9I              
TITLE     CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF G9A WITH MS0105              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 913-1193;                                         
COMPND   5 SYNONYM: EUCHROMATIC HISTONE-LYSINE N-METHYLTRANSFERASE 2,HLA-B-     
COMPND   6 ASSOCIATED TRANSCRIPT 8,HISTONE H3-K9 METHYLTRANSFERASE 3,H3-K9-     
COMPND   7 HMTASE 3,LYSINE N-METHYLTRANSFERASE 1C,PROTEIN G9A;                  
COMPND   8 EC: 2.1.1.-,2.1.1.43;                                                
COMPND   9 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: EHMT2, BAT8, C6ORF30, G9A, KMT1C, NG36;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P28A-LIC                                  
KEYWDS    EHMT2, BAT8, METHYLTRANSFERASE, STRUCTURAL GENOMICS, STRUCTURAL       
KEYWDS   2 GENOMICS CONSORTIUM, SGC, TRANSFERASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.DONG,H.ZENG,J.LIU,Y.XIONG,N.BABAULT,J.JIN,J.R.WALKER,C.BOUNTRA,     
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,H.WU,P.J.BROWN,STRUCTURAL GENOMICS        
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   1   21-MAR-18 5V9I    0                                                
JRNL        AUTH   H.ZENG,A.DONG,J.LIU,Y.XIONG,N.BABAULT,J.JIN,J.R.WALKER,      
JRNL        AUTH 2 C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,H.WU,P.J.BROWN          
JRNL        TITL   CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF G9A WITH MS0105     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 119034                         
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)  : 0.234                          
REMARK   3   R VALUE            (WORKING SET)  : 0.234                          
REMARK   3   FREE R VALUE                      : 0.275                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 1.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1188                           
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) : 1.74                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.78                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.99                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 8809                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2340                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 8710                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2340                   
REMARK   3   BIN FREE R VALUE                        : 0.2690                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 1.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 99                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8321                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 290                                     
REMARK   3   SOLVENT ATOMS            : 700                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.75                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.79960                                              
REMARK   3    B22 (A**2) : -3.66100                                             
REMARK   3    B33 (A**2) : -1.13860                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 4.91560                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.270               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.142               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.136               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.139               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.135               
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      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 9048   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 12322  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3200   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 228    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1480   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 9048   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1183   ; 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   : 11205  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.96                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.37                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 14.52                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|916 - A|1506 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.5360    1.0129   76.2360           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1766 T22:    0.3161                                    
REMARK   3     T33:    0.1058 T12:    0.1075                                    
REMARK   3     T13:   -0.0341 T23:   -0.0427                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5986 L22:    0.6948                                    
REMARK   3     L33:    1.2462 L12:   -0.0455                                    
REMARK   3     L13:    0.8662 L23:    0.1601                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0980 S12:   -0.4796 S13:    0.0043                     
REMARK   3     S21:    0.2142 S22:    0.1972 S23:   -0.1281                     
REMARK   3     S31:   -0.0200 S32:   -0.3202 S33:   -0.0992                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|918 - B|1506 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.2630    1.6738   43.8565           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1063 T22:    0.0950                                    
REMARK   3     T33:    0.1026 T12:   -0.0131                                    
REMARK   3     T13:   -0.0010 T23:    0.0219                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5518 L22:    0.4805                                    
REMARK   3     L33:    0.5932 L12:   -0.2038                                    
REMARK   3     L13:    0.6897 L23:   -0.1069                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0088 S12:    0.1331 S13:    0.0808                     
REMARK   3     S21:   -0.0616 S22:    0.0520 S23:    0.0212                     
REMARK   3     S31:    0.0432 S32:    0.0310 S33:   -0.0432                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|916 - C|1506 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    0.0173   -1.6003    8.8736           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1062 T22:    0.1023                                    
REMARK   3     T33:    0.1347 T12:    0.0458                                    
REMARK   3     T13:   -0.0072 T23:   -0.0072                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1423 L22:    0.6532                                    
REMARK   3     L33:    0.9833 L12:    0.1351                                    
REMARK   3     L13:    0.4454 L23:    0.1951                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0201 S12:   -0.1295 S13:   -0.0501                     
REMARK   3     S21:    0.1724 S22:    0.0650 S23:   -0.0904                     
REMARK   3     S31:    0.0248 S32:   -0.1159 S33:   -0.0851                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|918 - D|1506 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.3106   -0.5400  -23.0070           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0781 T22:    0.0992                                    
REMARK   3     T33:    0.1017 T12:   -0.0234                                    
REMARK   3     T13:    0.0062 T23:    0.0202                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.0659 L22:    0.6764                                    
REMARK   3     L33:    0.7092 L12:   -0.0384                                    
REMARK   3     L13:    0.5597 L23:   -0.1401                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0278 S12:    0.2114 S13:    0.0604                     
REMARK   3     S21:   -0.1051 S22:    0.0562 S23:    0.0466                     
REMARK   3     S31:    0.0476 S32:    0.0370 S33:   -0.0284                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5V9I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227020.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-14                          
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                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97915                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000, HKL                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 119624                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59600                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 2O8J                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M NACL, 0.1 M BIS      
REMARK 280  -TRIS PH6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K        
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       38.75450            
REMARK 290   SMTRY3   2  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: 3660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 2980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   911                                                      
REMARK 465     SER A   912                                                      
REMARK 465     ASN A   913                                                      
REMARK 465     ARG A   914                                                      
REMARK 465     ALA A   915                                                      
REMARK 465     ASN A  1091                                                      
REMARK 465     LYS A  1092                                                      
REMARK 465     ASP A  1093                                                      
REMARK 465     GLY A  1094                                                      
REMARK 465     GLN A  1186                                                      
REMARK 465     SER A  1187                                                      
REMARK 465     ARG A  1188                                                      
REMARK 465     LEU A  1189                                                      
REMARK 465     ALA A  1190                                                      
REMARK 465     ARG A  1191                                                      
REMARK 465     LEU A  1192                                                      
REMARK 465     ASP A  1193                                                      
REMARK 465     GLY B   911                                                      
REMARK 465     SER B   912                                                      
REMARK 465     ASN B   913                                                      
REMARK 465     ARG B   914                                                      
REMARK 465     ALA B   915                                                      
REMARK 465     ILE B   916                                                      
REMARK 465     ARG B   917                                                      
REMARK 465     ASN B  1091                                                      
REMARK 465     LYS B  1092                                                      
REMARK 465     ASP B  1093                                                      
REMARK 465     GLY B  1094                                                      
REMARK 465     ALA B  1190                                                      
REMARK 465     ARG B  1191                                                      
REMARK 465     LEU B  1192                                                      
REMARK 465     ASP B  1193                                                      
REMARK 465     GLY C   911                                                      
REMARK 465     SER C   912                                                      
REMARK 465     ASN C   913                                                      
REMARK 465     ARG C   914                                                      
REMARK 465     ALA C   915                                                      
REMARK 465     ASN C  1091                                                      
REMARK 465     LYS C  1092                                                      
REMARK 465     ASP C  1093                                                      
REMARK 465     GLY C  1094                                                      
REMARK 465     GLU C  1185                                                      
REMARK 465     GLN C  1186                                                      
REMARK 465     SER C  1187                                                      
REMARK 465     ARG C  1188                                                      
REMARK 465     LEU C  1189                                                      
REMARK 465     ALA C  1190                                                      
REMARK 465     ARG C  1191                                                      
REMARK 465     LEU C  1192                                                      
REMARK 465     ASP C  1193                                                      
REMARK 465     GLY D   911                                                      
REMARK 465     SER D   912                                                      
REMARK 465     ASN D   913                                                      
REMARK 465     ARG D   914                                                      
REMARK 465     ALA D   915                                                      
REMARK 465     ILE D   916                                                      
REMARK 465     ARG D   917                                                      
REMARK 465     ASN D  1091                                                      
REMARK 465     LYS D  1092                                                      
REMARK 465     ASP D  1093                                                      
REMARK 465     GLY D  1094                                                      
REMARK 465     SER D  1187                                                      
REMARK 465     ARG D  1188                                                      
REMARK 465     LEU D  1189                                                      
REMARK 465     ALA D  1190                                                      
REMARK 465     ARG D  1191                                                      
REMARK 465     LEU D  1192                                                      
REMARK 465     ASP D  1193                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ILE A 916    CG1  CG2  CD1                                       
REMARK 470     ARG A 917    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 920    CG   CD   CE   NZ                                   
REMARK 470     ARG A 924    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 972    OE1  NE2                                            
REMARK 470     VAL A 977    CG1  CG2                                            
REMARK 470     SER A 983    OG                                                  
REMARK 470     ILE A 992    CD1                                                 
REMARK 470     ARG A 993    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 998    NZ                                                  
REMARK 470     GLN A1004    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1008    CE   NZ                                             
REMARK 470     LYS A1028    NZ                                                  
REMARK 470     GLU A1081    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1090    CG   OD1  OD2                                       
REMARK 470     GLU A1095    N    CB   CG   CD   OE1  OE2                        
REMARK 470     ARG A1145    CD   NE   CZ   NH1  NH2                             
REMARK 470     ILE A1161    CD1                                                 
REMARK 470     LYS A1164    NZ                                                  
REMARK 470     GLU A1173    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1174    CG   CD   CE   NZ                                   
REMARK 470     LYS A1176    CG   CD   CE   NZ                                   
REMARK 470     GLU A1180    CG   CD   OE1  OE2                                  
REMARK 470     ILE A1182    CG1  CG2  CD1                                       
REMARK 470     GLU A1185    CG   CD   OE1  OE2                                  
REMARK 470     THR B 918    OG1  CG2                                            
REMARK 470     LYS B 920    CG   CD   CE   NZ                                   
REMARK 470     ASN B 963    CG   OD1  ND2                                       
REMARK 470     GLN B1004    CD   OE1  NE2                                       
REMARK 470     GLU B1005    CG   CD   OE1  OE2                                  
REMARK 470     ILE B1009    CD1                                                 
REMARK 470     GLU B1010    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1047    CE   NZ                                             
REMARK 470     GLU B1081    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1090    CG   OD1  OD2                                       
REMARK 470     GLU B1095    N    CB   CG   CD   OE1  OE2                        
REMARK 470     ARG B1145    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B1173    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1174    CE   NZ                                             
REMARK 470     LYS B1176    CE   NZ                                             
REMARK 470     ARG C 917    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 920    CG   CD   CE   NZ                                   
REMARK 470     ARG C 924    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 977    CG1  CG2                                            
REMARK 470     SER C 983    OG                                                  
REMARK 470     ILE C 992    CD1                                                 
REMARK 470     ARG C 993    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C 998    CE   NZ                                             
REMARK 470     GLN C1004    CG   CD   OE1  NE2                                  
REMARK 470     ILE C1009    CD1                                                 
REMARK 470     GLU C1010    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1047    NZ                                                  
REMARK 470     GLU C1081    CG   CD   OE1  OE2                                  
REMARK 470     ASP C1090    CG   OD1  OD2                                       
REMARK 470     GLU C1095    N    CA   CB   CG   CD   OE1  OE2                   
REMARK 470     ARG C1145    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS C1164    CE   NZ                                             
REMARK 470     GLU C1173    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1174    NZ                                                  
REMARK 470     LYS C1176    CG   CD   CE   NZ                                   
REMARK 470     ILE C1182    CG1  CG2  CD1                                       
REMARK 470     LEU C1184    CG   CD1  CD2                                       
REMARK 470     THR D 918    OG1  CG2                                            
REMARK 470     LYS D 920    CG   CD   CE   NZ                                   
REMARK 470     ILE D 992    CG1  CG2  CD1                                       
REMARK 470     GLN D1004    CG   CD   OE1  NE2                                  
REMARK 470     GLU D1005    CD   OE1  OE2                                       
REMARK 470     ILE D1009    CG1  CG2  CD1                                       
REMARK 470     GLU D1010    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1047    CG   CD   CE   NZ                                   
REMARK 470     GLU D1081    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1095    N    CB   CG   CD   OE1  OE2                        
REMARK 470     ARG D1145    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D1164    NZ                                                  
REMARK 470     GLU D1173    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1174    CD   CE   NZ                                        
REMARK 470     LEU D1184    CG   CD1  CD2                                       
REMARK 470     GLU D1185    CG   CD   OE1  OE2                                  
REMARK 470     GLN D1186    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 978     -158.58    -84.10                                   
REMARK 500    ILE A 992      -55.46     73.31                                   
REMARK 500    ASN A1029       50.48   -113.89                                   
REMARK 500    ILE A1064      -67.10   -103.10                                   
REMARK 500    LEU A1089       70.79   -109.69                                   
REMARK 500    LEU A1089       69.05   -109.95                                   
REMARK 500    ASN A1106     -160.92   -110.17                                   
REMARK 500    MET A1126      -93.22   -128.14                                   
REMARK 500    ASP B 925      105.68   -160.22                                   
REMARK 500    ASP B 978     -151.40   -102.37                                   
REMARK 500    ILE B 992      -57.72     78.96                                   
REMARK 500    ASN B1029       51.19   -109.13                                   
REMARK 500    ARG B1030       33.31   -149.08                                   
REMARK 500    ILE B1064      -65.04   -103.84                                   
REMARK 500    ASN B1106     -161.03   -106.07                                   
REMARK 500    ASP B1116       78.59   -115.71                                   
REMARK 500    MET B1126      -89.96   -131.12                                   
REMARK 500    ASP C 925      108.07   -163.33                                   
REMARK 500    ASP C 978     -156.03    -83.75                                   
REMARK 500    ILE C 992      -51.79     72.48                                   
REMARK 500    ASN C1029       54.58   -111.72                                   
REMARK 500    ARG C1030       19.13   -142.89                                   
REMARK 500    ILE C1064      -64.58   -101.52                                   
REMARK 500    LEU C1089       73.09   -107.64                                   
REMARK 500    ASN C1106     -162.28   -107.06                                   
REMARK 500    ASP C1116       77.81   -115.74                                   
REMARK 500    MET C1126      -92.78   -128.77                                   
REMARK 500    ASP D 978     -150.33   -105.35                                   
REMARK 500    ILE D 992      -53.07     83.02                                   
REMARK 500    ASN D1029       55.35   -113.31                                   
REMARK 500    ARG D1030       30.34   -151.96                                   
REMARK 500    ILE D1064      -65.76   -103.17                                   
REMARK 500    ASN D1106     -161.83   -108.28                                   
REMARK 500    ASP D1116       78.50   -117.51                                   
REMARK 500    MET D1126      -89.92   -129.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     90P A 1506                                                       
REMARK 610     90P B 1506                                                       
REMARK 610     90P C 1506                                                       
REMARK 610     90P D 1506                                                       
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 A1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 987   SG  118.4                                              
REMARK 620 3 CYS A1017   SG   98.6 114.4                                        
REMARK 620 4 CYS A1021   SG  108.0 105.0 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 974   SG                                                     
REMARK 620 2 CYS A 976   SG   97.9                                              
REMARK 620 3 CYS A 980   SG  107.4 107.5                                        
REMARK 620 4 CYS A 985   SG  113.8 106.9 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 980   SG                                                     
REMARK 620 2 CYS A1017   SG  108.1                                              
REMARK 620 3 CYS A1023   SG  103.6 104.3                                        
REMARK 620 4 CYS A1027   SG  115.4 110.0 114.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A1115   SG                                                     
REMARK 620 2 CYS A1168   SG  112.7                                              
REMARK 620 3 CYS A1170   SG  109.0 107.0                                        
REMARK 620 4 CYS A1175   SG  106.3 115.5 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 987   SG  113.2                                              
REMARK 620 3 CYS B1017   SG  107.3 111.1                                        
REMARK 620 4 CYS B1021   SG  108.6  99.3 117.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 974   SG                                                     
REMARK 620 2 CYS B 976   SG  105.0                                              
REMARK 620 3 CYS B 980   SG  107.4 103.6                                        
REMARK 620 4 CYS B 985   SG  113.3 108.0 118.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 980   SG                                                     
REMARK 620 2 CYS B1017   SG  111.4                                              
REMARK 620 3 CYS B1023   SG  104.1 106.1                                        
REMARK 620 4 CYS B1027   SG  114.9 105.6 114.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1115   SG                                                     
REMARK 620 2 CYS B1168   SG  111.5                                              
REMARK 620 3 CYS B1170   SG  110.9 108.8                                        
REMARK 620 4 CYS B1175   SG  105.4 110.6 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 974   SG                                                     
REMARK 620 2 CYS C 976   SG  101.5                                              
REMARK 620 3 CYS C 980   SG  105.6 106.8                                        
REMARK 620 4 CYS C 985   SG  115.5 107.0 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 974   SG                                                     
REMARK 620 2 CYS C 987   SG  116.4                                              
REMARK 620 3 CYS C1017   SG  104.4 113.5                                        
REMARK 620 4 CYS C1021   SG  103.6 100.6 118.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 980   SG                                                     
REMARK 620 2 CYS C1017   SG  107.3                                              
REMARK 620 3 CYS C1023   SG  106.5 102.8                                        
REMARK 620 4 CYS C1027   SG  118.0 105.9 115.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C1115   SG                                                     
REMARK 620 2 CYS C1168   SG  110.9                                              
REMARK 620 3 CYS C1170   SG  110.3 107.1                                        
REMARK 620 4 CYS C1175   SG  104.9 113.1 110.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 974   SG                                                     
REMARK 620 2 CYS D 976   SG  104.3                                              
REMARK 620 3 CYS D 980   SG  105.6 108.9                                        
REMARK 620 4 CYS D 985   SG  114.7 107.2 115.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 974   SG                                                     
REMARK 620 2 CYS D 987   SG  114.3                                              
REMARK 620 3 CYS D1017   SG  106.5 112.6                                        
REMARK 620 4 CYS D1021   SG  106.0 100.8 116.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 980   SG                                                     
REMARK 620 2 CYS D1017   SG  112.1                                              
REMARK 620 3 CYS D1023   SG  108.9 106.3                                        
REMARK 620 4 CYS D1027   SG  111.1 104.2 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1504  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D1115   SG                                                     
REMARK 620 2 CYS D1168   SG  109.6                                              
REMARK 620 3 CYS D1170   SG  111.2 106.3                                        
REMARK 620 4 CYS D1175   SG  106.0 112.8 111.1                                  
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 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P A 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P B 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM C 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P C 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM D 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 90P D 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 1508                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5V9J   RELATED DB: PDB                                   
DBREF  5V9I A  913  1193  UNP    Q96KQ7   EHMT2_HUMAN    913   1193             
DBREF  5V9I B  913  1193  UNP    Q96KQ7   EHMT2_HUMAN    913   1193             
DBREF  5V9I C  913  1193  UNP    Q96KQ7   EHMT2_HUMAN    913   1193             
DBREF  5V9I D  913  1193  UNP    Q96KQ7   EHMT2_HUMAN    913   1193             
SEQADV 5V9I GLY A  911  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I SER A  912  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I GLY B  911  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I SER B  912  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I GLY C  911  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I SER C  912  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I GLY D  911  UNP  Q96KQ7              EXPRESSION TAG                 
SEQADV 5V9I SER D  912  UNP  Q96KQ7              EXPRESSION TAG                 
SEQRES   1 A  283  GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS          
SEQRES   2 A  283  ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO          
SEQRES   3 A  283  CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP          
SEQRES   4 A  283  TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET          
SEQRES   5 A  283  ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR          
SEQRES   6 A  283  CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY          
SEQRES   7 A  283  GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG          
SEQRES   8 A  283  LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE          
SEQRES   9 A  283  PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS          
SEQRES  10 A  283  LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU          
SEQRES  11 A  283  GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG          
SEQRES  12 A  283  ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU          
SEQRES  13 A  283  TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL          
SEQRES  14 A  283  ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS          
SEQRES  15 A  283  ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY          
SEQRES  16 A  283  ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN          
SEQRES  17 A  283  ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU          
SEQRES  18 A  283  ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE          
SEQRES  19 A  283  ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG          
SEQRES  20 A  283  PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS          
SEQRES  21 A  283  GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA          
SEQRES  22 A  283  LEU GLU GLN SER ARG LEU ALA ARG LEU ASP                      
SEQRES   1 B  283  GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS          
SEQRES   2 B  283  ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO          
SEQRES   3 B  283  CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP          
SEQRES   4 B  283  TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET          
SEQRES   5 B  283  ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR          
SEQRES   6 B  283  CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY          
SEQRES   7 B  283  GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG          
SEQRES   8 B  283  LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE          
SEQRES   9 B  283  PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS          
SEQRES  10 B  283  LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU          
SEQRES  11 B  283  GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG          
SEQRES  12 B  283  ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU          
SEQRES  13 B  283  TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL          
SEQRES  14 B  283  ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS          
SEQRES  15 B  283  ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY          
SEQRES  16 B  283  ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN          
SEQRES  17 B  283  ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU          
SEQRES  18 B  283  ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE          
SEQRES  19 B  283  ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG          
SEQRES  20 B  283  PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS          
SEQRES  21 B  283  GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA          
SEQRES  22 B  283  LEU GLU GLN SER ARG LEU ALA ARG LEU ASP                      
SEQRES   1 C  283  GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS          
SEQRES   2 C  283  ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO          
SEQRES   3 C  283  CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP          
SEQRES   4 C  283  TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET          
SEQRES   5 C  283  ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR          
SEQRES   6 C  283  CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY          
SEQRES   7 C  283  GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG          
SEQRES   8 C  283  LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE          
SEQRES   9 C  283  PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS          
SEQRES  10 C  283  LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU          
SEQRES  11 C  283  GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG          
SEQRES  12 C  283  ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU          
SEQRES  13 C  283  TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL          
SEQRES  14 C  283  ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS          
SEQRES  15 C  283  ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY          
SEQRES  16 C  283  ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN          
SEQRES  17 C  283  ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU          
SEQRES  18 C  283  ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE          
SEQRES  19 C  283  ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG          
SEQRES  20 C  283  PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS          
SEQRES  21 C  283  GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA          
SEQRES  22 C  283  LEU GLU GLN SER ARG LEU ALA ARG LEU ASP                      
SEQRES   1 D  283  GLY SER ASN ARG ALA ILE ARG THR GLU LYS ILE ILE CYS          
SEQRES   2 D  283  ARG ASP VAL ALA ARG GLY TYR GLU ASN VAL PRO ILE PRO          
SEQRES   3 D  283  CYS VAL ASN GLY VAL ASP GLY GLU PRO CYS PRO GLU ASP          
SEQRES   4 D  283  TYR LYS TYR ILE SER GLU ASN CYS GLU THR SER THR MET          
SEQRES   5 D  283  ASN ILE ASP ARG ASN ILE THR HIS LEU GLN HIS CYS THR          
SEQRES   6 D  283  CYS VAL ASP ASP CYS SER SER SER ASN CYS LEU CYS GLY          
SEQRES   7 D  283  GLN LEU SER ILE ARG CYS TRP TYR ASP LYS ASP GLY ARG          
SEQRES   8 D  283  LEU LEU GLN GLU PHE ASN LYS ILE GLU PRO PRO LEU ILE          
SEQRES   9 D  283  PHE GLU CYS ASN GLN ALA CYS SER CYS TRP ARG ASN CYS          
SEQRES  10 D  283  LYS ASN ARG VAL VAL GLN SER GLY ILE LYS VAL ARG LEU          
SEQRES  11 D  283  GLN LEU TYR ARG THR ALA LYS MET GLY TRP GLY VAL ARG          
SEQRES  12 D  283  ALA LEU GLN THR ILE PRO GLN GLY THR PHE ILE CYS GLU          
SEQRES  13 D  283  TYR VAL GLY GLU LEU ILE SER ASP ALA GLU ALA ASP VAL          
SEQRES  14 D  283  ARG GLU ASP ASP SER TYR LEU PHE ASP LEU ASP ASN LYS          
SEQRES  15 D  283  ASP GLY GLU VAL TYR CYS ILE ASP ALA ARG TYR TYR GLY          
SEQRES  16 D  283  ASN ILE SER ARG PHE ILE ASN HIS LEU CYS ASP PRO ASN          
SEQRES  17 D  283  ILE ILE PRO VAL ARG VAL PHE MET LEU HIS GLN ASP LEU          
SEQRES  18 D  283  ARG PHE PRO ARG ILE ALA PHE PHE SER SER ARG ASP ILE          
SEQRES  19 D  283  ARG THR GLY GLU GLU LEU GLY PHE ASP TYR GLY ASP ARG          
SEQRES  20 D  283  PHE TRP ASP ILE LYS SER LYS TYR PHE THR CYS GLN CYS          
SEQRES  21 D  283  GLY SER GLU LYS CYS LYS HIS SER ALA GLU ALA ILE ALA          
SEQRES  22 D  283  LEU GLU GLN SER ARG LEU ALA ARG LEU ASP                      
HET     ZN  A1501       1                                                       
HET     ZN  A1502       1                                                       
HET     ZN  A1503       1                                                       
HET     ZN  A1504       1                                                       
HET    SAM  A1505      27                                                       
HET    90P  A1506      27                                                       
HET    GOL  A1507       6                                                       
HET    GOL  A1508       6                                                       
HET    GOL  A1509       6                                                       
HET    UNX  A1510       1                                                       
HET     ZN  B1501       1                                                       
HET     ZN  B1502       1                                                       
HET     ZN  B1503       1                                                       
HET     ZN  B1504       1                                                       
HET    SAM  B1505      27                                                       
HET    90P  B1506      27                                                       
HET    GOL  B1507       6                                                       
HET    GOL  B1508       6                                                       
HET    GOL  B1509       6                                                       
HET    UNX  B1510       1                                                       
HET    UNX  B1511       1                                                       
HET     ZN  C1501       1                                                       
HET     ZN  C1502       1                                                       
HET     ZN  C1503       1                                                       
HET     ZN  C1504       1                                                       
HET    SAM  C1505      27                                                       
HET    90P  C1506      32                                                       
HET    GOL  C1507       6                                                       
HET    UNX  C1508       1                                                       
HET     ZN  D1501       1                                                       
HET     ZN  D1502       1                                                       
HET     ZN  D1503       1                                                       
HET     ZN  D1504       1                                                       
HET    SAM  D1505      27                                                       
HET    90P  D1506      32                                                       
HET    GOL  D1507       6                                                       
HET    GOL  D1508       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
HETNAM     90P N~2~-CYCLOHEXYL-N~4~-(1-ETHYLPIPERIDIN-4-YL)-6,7-                
HETNAM   2 90P  DIMETHOXY-N~2~-METHYLQUINAZOLINE-2,4-DIAMINE                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   ZN    16(ZN 2+)                                                    
FORMUL   9  SAM    4(C15 H22 N6 O5 S)                                           
FORMUL  10  90P    4(C24 H37 N5 O2)                                             
FORMUL  11  GOL    9(C3 H8 O3)                                                  
FORMUL  14  UNX    4(X)                                                         
FORMUL  42  HOH   *700(H2 O)                                                    
HELIX    1 AA1 ASN A  967  LEU A  971  5                                   5    
HELIX    2 AA2 CYS A  985  LEU A  990  1                                   6    
HELIX    3 AA3 VAL A 1031  GLY A 1035  5                                   5    
HELIX    4 AA4 ASP A 1074  ASP A 1078  1                                   5    
HELIX    5 AA5 ILE A 1107  ILE A 1111  5                                   5    
HELIX    6 AA6 GLY A 1155  SER A 1163  1                                   9    
HELIX    7 AA7 SER A 1178  GLU A 1185  1                                   8    
HELIX    8 AA8 ASN B  967  LEU B  971  5                                   5    
HELIX    9 AA9 CYS B  985  SER B  991  1                                   7    
HELIX   10 AB1 VAL B 1031  GLY B 1035  5                                   5    
HELIX   11 AB2 ASP B 1074  ASP B 1078  1                                   5    
HELIX   12 AB3 ILE B 1107  ILE B 1111  5                                   5    
HELIX   13 AB4 GLY B 1155  SER B 1163  1                                   9    
HELIX   14 AB5 SER B 1178  LEU B 1189  1                                  12    
HELIX   15 AB6 ASN C  967  LEU C  971  5                                   5    
HELIX   16 AB7 CYS C  985  LEU C  990  1                                   6    
HELIX   17 AB8 VAL C 1031  GLY C 1035  5                                   5    
HELIX   18 AB9 ASP C 1074  ASP C 1078  1                                   5    
HELIX   19 AC1 ILE C 1107  ILE C 1111  5                                   5    
HELIX   20 AC2 GLY C 1155  SER C 1163  1                                   9    
HELIX   21 AC3 SER C 1178  LEU C 1184  1                                   7    
HELIX   22 AC4 ASN D  967  LEU D  971  5                                   5    
HELIX   23 AC5 CYS D  985  SER D  991  1                                   7    
HELIX   24 AC6 VAL D 1031  GLY D 1035  5                                   5    
HELIX   25 AC7 ASP D 1074  ASP D 1078  1                                   5    
HELIX   26 AC8 ILE D 1107  ILE D 1111  5                                   5    
HELIX   27 AC9 GLY D 1155  SER D 1163  1                                   9    
HELIX   28 AD1 SER D 1178  GLN D 1186  1                                   9    
SHEET    1 AA1 4 LYS A 920  CYS A 923  0                                        
SHEET    2 AA1 4 CYS A 937  ASN A 939 -1  O  CYS A 937   N  CYS A 923           
SHEET    3 AA1 4 LEU A1040  ARG A1044  1  O  LEU A1042   N  VAL A 938           
SHEET    4 AA1 4 TRP A1050  ALA A1054 -1  O  GLY A1051   N  TYR A1043           
SHEET    1 AA2 4 LYS A 951  TYR A 952  0                                        
SHEET    2 AA2 4 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA2 4 GLY A1069  SER A1073 -1  N  GLU A1070   O  ASP A1100           
SHEET    4 AA2 4 CYS A 957  GLU A 958  1  N  CYS A 957   O  LEU A1071           
SHEET    1 AA3 3 LYS A 951  TYR A 952  0                                        
SHEET    2 AA3 3 TYR A1097  GLY A1105  1  O  TYR A1103   N  LYS A 951           
SHEET    3 AA3 3 LEU A1086  LEU A1089 -1  N  PHE A1087   O  ILE A1099           
SHEET    1 AA4 4 ILE A1014  PHE A1015  0                                        
SHEET    2 AA4 4 ILE A1119  PHE A1125  1  O  ARG A1123   N  ILE A1014           
SHEET    3 AA4 4 ARG A1135  SER A1140 -1  O  ALA A1137   N  VAL A1122           
SHEET    4 AA4 4 PHE A1063  TYR A1067 -1  N  TYR A1067   O  ILE A1136           
SHEET    1 AA5 2 ASN A1112  HIS A1113  0                                        
SHEET    2 AA5 2 GLY A1151  PHE A1152  1  O  PHE A1152   N  ASN A1112           
SHEET    1 AA6 4 LYS B 920  CYS B 923  0                                        
SHEET    2 AA6 4 CYS B 937  ASN B 939 -1  O  CYS B 937   N  CYS B 923           
SHEET    3 AA6 4 LEU B1040  ARG B1044  1  O  LEU B1042   N  VAL B 938           
SHEET    4 AA6 4 TRP B1050  ALA B1054 -1  O  GLY B1051   N  TYR B1043           
SHEET    1 AA7 4 LYS B 951  TYR B 952  0                                        
SHEET    2 AA7 4 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA7 4 GLY B1069  SER B1073 -1  N  ILE B1072   O  CYS B1098           
SHEET    4 AA7 4 CYS B 957  GLU B 958  1  N  CYS B 957   O  LEU B1071           
SHEET    1 AA8 3 LYS B 951  TYR B 952  0                                        
SHEET    2 AA8 3 TYR B1097  GLY B1105  1  O  TYR B1103   N  LYS B 951           
SHEET    3 AA8 3 LEU B1086  LEU B1089 -1  N  PHE B1087   O  ILE B1099           
SHEET    1 AA9 4 ILE B1014  PHE B1015  0                                        
SHEET    2 AA9 4 ILE B1119  PHE B1125  1  O  PHE B1125   N  ILE B1014           
SHEET    3 AA9 4 ARG B1135  SER B1140 -1  O  ALA B1137   N  VAL B1122           
SHEET    4 AA9 4 PHE B1063  TYR B1067 -1  N  CYS B1065   O  PHE B1138           
SHEET    1 AB1 2 ASN B1112  HIS B1113  0                                        
SHEET    2 AB1 2 GLY B1151  PHE B1152  1  O  PHE B1152   N  ASN B1112           
SHEET    1 AB2 4 LYS C 920  CYS C 923  0                                        
SHEET    2 AB2 4 CYS C 937  ASN C 939 -1  O  CYS C 937   N  CYS C 923           
SHEET    3 AB2 4 LEU C1040  ARG C1044  1  O  LEU C1042   N  VAL C 938           
SHEET    4 AB2 4 TRP C1050  ALA C1054 -1  O  GLY C1051   N  TYR C1043           
SHEET    1 AB3 4 LYS C 951  TYR C 952  0                                        
SHEET    2 AB3 4 TYR C1097  GLY C1105  1  O  TYR C1103   N  LYS C 951           
SHEET    3 AB3 4 GLY C1069  SER C1073 -1  N  GLU C1070   O  ASP C1100           
SHEET    4 AB3 4 CYS C 957  GLU C 958  1  N  CYS C 957   O  LEU C1071           
SHEET    1 AB4 3 LYS C 951  TYR C 952  0                                        
SHEET    2 AB4 3 TYR C1097  GLY C1105  1  O  TYR C1103   N  LYS C 951           
SHEET    3 AB4 3 LEU C1086  LEU C1089 -1  N  PHE C1087   O  ILE C1099           
SHEET    1 AB5 4 ILE C1014  PHE C1015  0                                        
SHEET    2 AB5 4 ILE C1119  PHE C1125  1  O  ARG C1123   N  ILE C1014           
SHEET    3 AB5 4 ARG C1135  SER C1140 -1  O  ALA C1137   N  VAL C1122           
SHEET    4 AB5 4 PHE C1063  TYR C1067 -1  N  ILE C1064   O  PHE C1138           
SHEET    1 AB6 2 ASN C1112  HIS C1113  0                                        
SHEET    2 AB6 2 GLY C1151  PHE C1152  1  O  PHE C1152   N  ASN C1112           
SHEET    1 AB7 4 LYS D 920  CYS D 923  0                                        
SHEET    2 AB7 4 CYS D 937  ASN D 939 -1  O  CYS D 937   N  CYS D 923           
SHEET    3 AB7 4 LEU D1040  ARG D1044  1  O  LEU D1042   N  VAL D 938           
SHEET    4 AB7 4 TRP D1050  ALA D1054 -1  O  GLY D1051   N  TYR D1043           
SHEET    1 AB8 4 LYS D 951  TYR D 952  0                                        
SHEET    2 AB8 4 TYR D1097  GLY D1105  1  O  TYR D1103   N  LYS D 951           
SHEET    3 AB8 4 GLY D1069  SER D1073 -1  N  GLU D1070   O  ASP D1100           
SHEET    4 AB8 4 CYS D 957  GLU D 958  1  N  CYS D 957   O  LEU D1071           
SHEET    1 AB9 3 LYS D 951  TYR D 952  0                                        
SHEET    2 AB9 3 TYR D1097  GLY D1105  1  O  TYR D1103   N  LYS D 951           
SHEET    3 AB9 3 LEU D1086  LEU D1089 -1  N  PHE D1087   O  ILE D1099           
SHEET    1 AC1 4 ILE D1014  PHE D1015  0                                        
SHEET    2 AC1 4 ILE D1119  PHE D1125  1  O  PHE D1125   N  ILE D1014           
SHEET    3 AC1 4 ARG D1135  SER D1140 -1  O  PHE D1139   N  ILE D1120           
SHEET    4 AC1 4 PHE D1063  TYR D1067 -1  N  CYS D1065   O  PHE D1138           
SHEET    1 AC2 2 ASN D1112  HIS D1113  0                                        
SHEET    2 AC2 2 GLY D1151  PHE D1152  1  O  PHE D1152   N  ASN D1112           
LINK         SG  CYS A 974                ZN    ZN A1501     1555   1555  2.55  
LINK         SG  CYS A 974                ZN    ZN A1503     1555   1555  2.43  
LINK         SG  CYS A 976                ZN    ZN A1503     1555   1555  2.54  
LINK         SG  CYS A 980                ZN    ZN A1502     1555   1555  2.48  
LINK         SG  CYS A 980                ZN    ZN A1503     1555   1555  2.19  
LINK         SG  CYS A 985                ZN    ZN A1503     1555   1555  2.22  
LINK         SG  CYS A 987                ZN    ZN A1501     1555   1555  2.21  
LINK         SG  CYS A1017                ZN    ZN A1501     1555   1555  2.48  
LINK         SG  CYS A1017                ZN    ZN A1502     1555   1555  2.34  
LINK         SG  CYS A1021                ZN    ZN A1501     1555   1555  2.30  
LINK         SG  CYS A1023                ZN    ZN A1502     1555   1555  2.24  
LINK         SG  CYS A1027                ZN    ZN A1502     1555   1555  2.23  
LINK         SG  CYS A1115                ZN    ZN A1504     1555   1555  2.34  
LINK         SG  CYS A1168                ZN    ZN A1504     1555   1555  2.15  
LINK         SG  CYS A1170                ZN    ZN A1504     1555   1555  2.41  
LINK         SG  CYS A1175                ZN    ZN A1504     1555   1555  2.24  
LINK         SG  CYS B 974                ZN    ZN B1501     1555   1555  2.46  
LINK         SG  CYS B 974                ZN    ZN B1503     1555   1555  2.36  
LINK         SG  CYS B 976                ZN    ZN B1503     1555   1555  2.44  
LINK         SG  CYS B 980                ZN    ZN B1503     1555   1555  2.33  
LINK         SG  CYS B 980                ZN    ZN B1502     1555   1555  2.40  
LINK         SG  CYS B 985                ZN    ZN B1503     1555   1555  2.34  
LINK         SG  CYS B 987                ZN    ZN B1501     1555   1555  2.37  
LINK         SG  CYS B1017                ZN    ZN B1501     1555   1555  2.42  
LINK         SG  CYS B1017                ZN    ZN B1502     1555   1555  2.39  
LINK         SG  CYS B1021                ZN    ZN B1501     1555   1555  2.20  
LINK         SG  CYS B1023                ZN    ZN B1502     1555   1555  2.28  
LINK         SG  CYS B1027                ZN    ZN B1502     1555   1555  2.34  
LINK         SG  CYS B1115                ZN    ZN B1504     1555   1555  2.39  
LINK         SG  CYS B1168                ZN    ZN B1504     1555   1555  2.26  
LINK         SG  CYS B1170                ZN    ZN B1504     1555   1555  2.37  
LINK         SG  CYS B1175                ZN    ZN B1504     1555   1555  2.28  
LINK         SG  CYS C 974                ZN    ZN C1503     1555   1555  2.41  
LINK         SG  CYS C 974                ZN    ZN C1501     1555   1555  2.57  
LINK         SG  CYS C 976                ZN    ZN C1503     1555   1555  2.41  
LINK         SG  CYS C 980                ZN    ZN C1503     1555   1555  2.27  
LINK         SG  CYS C 980                ZN    ZN C1502     1555   1555  2.31  
LINK         SG  CYS C 985                ZN    ZN C1503     1555   1555  2.25  
LINK         SG  CYS C 987                ZN    ZN C1501     1555   1555  2.27  
LINK         SG  CYS C1017                ZN    ZN C1501     1555   1555  2.41  
LINK         SG  CYS C1017                ZN    ZN C1502     1555   1555  2.43  
LINK         SG  CYS C1021                ZN    ZN C1501     1555   1555  2.25  
LINK         SG  CYS C1023                ZN    ZN C1502     1555   1555  2.24  
LINK         SG  CYS C1027                ZN    ZN C1502     1555   1555  2.23  
LINK         SG  CYS C1115                ZN    ZN C1504     1555   1555  2.47  
LINK         SG  CYS C1168                ZN    ZN C1504     1555   1555  2.29  
LINK         SG  CYS C1170                ZN    ZN C1504     1555   1555  2.33  
LINK         SG  CYS C1175                ZN    ZN C1504     1555   1555  2.34  
LINK         SG  CYS D 974                ZN    ZN D1503     1555   1555  2.35  
LINK         SG  CYS D 974                ZN    ZN D1501     1555   1555  2.50  
LINK         SG  CYS D 976                ZN    ZN D1503     1555   1555  2.40  
LINK         SG  CYS D 980                ZN    ZN D1503     1555   1555  2.54  
LINK         SG  CYS D 980                ZN    ZN D1502     1555   1555  2.19  
LINK         SG  CYS D 985                ZN    ZN D1503     1555   1555  2.28  
LINK         SG  CYS D 987                ZN    ZN D1501     1555   1555  2.30  
LINK         SG  CYS D1017                ZN    ZN D1501     1555   1555  2.41  
LINK         SG  CYS D1017                ZN    ZN D1502     1555   1555  2.43  
LINK         SG  CYS D1021                ZN    ZN D1501     1555   1555  2.28  
LINK         SG  CYS D1023                ZN    ZN D1502     1555   1555  2.16  
LINK         SG  CYS D1027                ZN    ZN D1502     1555   1555  2.34  
LINK         SG  CYS D1115                ZN    ZN D1504     1555   1555  2.38  
LINK         SG  CYS D1168                ZN    ZN D1504     1555   1555  2.21  
LINK         SG  CYS D1170                ZN    ZN D1504     1555   1555  2.46  
LINK         SG  CYS D1175                ZN    ZN D1504     1555   1555  2.26  
SITE     1 AC1  4 CYS A 974  CYS A 987  CYS A1017  CYS A1021                    
SITE     1 AC2  4 CYS A 980  CYS A1017  CYS A1023  CYS A1027                    
SITE     1 AC3  4 CYS A 974  CYS A 976  CYS A 980  CYS A 985                    
SITE     1 AC4  4 CYS A1115  CYS A1168  CYS A1170  CYS A1175                    
SITE     1 AC5 18 MET A1048  TRP A1050  SER A1084  TYR A1085                    
SITE     2 AC5 18 ARG A1109  PHE A1110  ASN A1112  HIS A1113                    
SITE     3 AC5 18 TYR A1154  PHE A1158  PHE A1166  THR A1167                    
SITE     4 AC5 18 CYS A1168  GLN A1169  HOH A1610  HOH A1663                    
SITE     5 AC5 18 HOH A1696  HOH A1706                                          
SITE     1 AC6 12 ASP A1074  ALA A1077  ASP A1078  ARG A1080                    
SITE     2 AC6 12 ASP A1083  LEU A1086  ASP A1088  CYS A1098                    
SITE     3 AC6 12 ARG A1157  PHE A1158  LYS A1162  GOL A1509                    
SITE     1 AC7 12 GLU A 931  VAL A1032  GLY A1035  ILE A1036                    
SITE     2 AC7 12 PHE A1063  CYS A1065  GLU A1066  ASN A1106                    
SITE     3 AC7 12 HOH A1601  HOH A1613  HOH A1623  HOH A1674                    
SITE     1 AC8  4 ILE A 921  PRO A 936  VAL A 938  GLN A1041                    
SITE     1 AC9 10 LEU A1086  PHE A1087  ASP A1088  PHE A1152                    
SITE     2 AC9 10 ASP A1153  TYR A1154  90P A1506  HOH A1603                    
SITE     3 AC9 10 HOH A1632  HOH A1723                                          
SITE     1 AD1  4 CYS B 974  CYS B 987  CYS B1017  CYS B1021                    
SITE     1 AD2  4 CYS B 980  CYS B1017  CYS B1023  CYS B1027                    
SITE     1 AD3  4 CYS B 974  CYS B 976  CYS B 980  CYS B 985                    
SITE     1 AD4  4 CYS B1115  CYS B1168  CYS B1170  CYS B1175                    
SITE     1 AD5 19 MET B1048  TRP B1050  SER B1084  TYR B1085                    
SITE     2 AD5 19 ARG B1109  PHE B1110  ILE B1111  ASN B1112                    
SITE     3 AD5 19 HIS B1113  TYR B1154  PHE B1158  PHE B1166                    
SITE     4 AD5 19 THR B1167  CYS B1168  GLN B1169  HOH B1608                    
SITE     5 AD5 19 HOH B1649  HOH B1735  HOH B1756                               
SITE     1 AD6 11 ASP B1074  ALA B1077  ASP B1078  ARG B1080                    
SITE     2 AD6 11 ASP B1083  LEU B1086  ASP B1088  CYS B1098                    
SITE     3 AD6 11 ARG B1157  PHE B1158  HOH B1715                               
SITE     1 AD7  9 VAL B1032  GLY B1035  ILE B1036  PHE B1063                    
SITE     2 AD7  9 GLU B1066  ASN B1106  HOH B1604  HOH B1638                    
SITE     3 AD7  9 HOH B1648                                                     
SITE     1 AD8  8 ASP B 942  ARG B1044  THR B1045  ALA B1046                    
SITE     2 AD8  8 LYS B1047  MET B1048  GLY B1049  HOH B1657                    
SITE     1 AD9  7 ASN B 956  LEU B1071  HIS B1128  PHE B1133                    
SITE     2 AD9  7 PRO B1134  ARG B1135  HOH B1623                               
SITE     1 AE1  4 CYS C 974  CYS C 987  CYS C1017  CYS C1021                    
SITE     1 AE2  4 CYS C 980  CYS C1017  CYS C1023  CYS C1027                    
SITE     1 AE3  4 CYS C 974  CYS C 976  CYS C 980  CYS C 985                    
SITE     1 AE4  4 CYS C1115  CYS C1168  CYS C1170  CYS C1175                    
SITE     1 AE5 19 MET C1048  TRP C1050  SER C1084  TYR C1085                    
SITE     2 AE5 19 ARG C1109  PHE C1110  ILE C1111  ASN C1112                    
SITE     3 AE5 19 HIS C1113  TYR C1154  PHE C1158  PHE C1166                    
SITE     4 AE5 19 CYS C1168  GLN C1169  HOH C1613  HOH C1618                    
SITE     5 AE5 19 HOH C1627  HOH C1670  HOH C1740                               
SITE     1 AE6 10 ASP C1074  ALA C1077  ASP C1078  ARG C1080                    
SITE     2 AE6 10 ASP C1083  LEU C1086  ASP C1088  CYS C1098                    
SITE     3 AE6 10 ARG C1157  PHE C1158                                          
SITE     1 AE7 11 VAL C1032  GLY C1035  ILE C1036  PHE C1063                    
SITE     2 AE7 11 CYS C1065  GLU C1066  ASN C1106  ARG C1135                    
SITE     3 AE7 11 HOH C1642  HOH C1649  HOH C1658                               
SITE     1 AE8  4 CYS D 974  CYS D 987  CYS D1017  CYS D1021                    
SITE     1 AE9  4 CYS D 980  CYS D1017  CYS D1023  CYS D1027                    
SITE     1 AF1  4 CYS D 974  CYS D 976  CYS D 980  CYS D 985                    
SITE     1 AF2  4 CYS D1115  CYS D1168  CYS D1170  CYS D1175                    
SITE     1 AF3 19 MET D1048  TRP D1050  SER D1084  TYR D1085                    
SITE     2 AF3 19 ARG D1109  PHE D1110  ASN D1112  HIS D1113                    
SITE     3 AF3 19 TYR D1154  PHE D1158  PHE D1166  CYS D1168                    
SITE     4 AF3 19 GLN D1169  HOH D1617  HOH D1618  HOH D1692                    
SITE     5 AF3 19 HOH D1696  HOH D1704  HOH D1734                               
SITE     1 AF4 11 ASP D1074  ALA D1077  ASP D1078  ARG D1080                    
SITE     2 AF4 11 ASP D1083  LEU D1086  ASP D1088  CYS D1098                    
SITE     3 AF4 11 ARG D1157  PHE D1158  LYS D1162                               
SITE     1 AF5  7 TRP C1024  ASP D 925  GLY D 929  GLU D 931                    
SITE     2 AF5  7 ASN D 932  VAL D 933  PRO D 934                               
SITE     1 AF6  6 ASP D 942  THR D1045  ALA D1046  MET D1048                    
SITE     2 AF6  6 GLY D1049  HOH D1711                                          
CRYST1   56.607   77.509  134.794  90.00  91.41  90.00 P 1 21 1      8          
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      0.017666  0.000000  0.000435        0.00000                         
SCALE2      0.000000  0.012902  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007421        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system