GenomeNet

Database: PDB
Entry: 4YPA
LinkDB: 4YPA
Original site: 4YPA 
HEADER    TRANSFERASE                             12-MAR-15   4YPA              
TITLE     ASH1L SET DOMAIN Q2265A MUTANT IN COMPLEX WITH S-ADENOSYL METHIONINE  
TITLE    2 (SAM)                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: SET DOMAIN (UNP RESIDUES 2074-2293);                       
COMPND   5 SYNONYM: ASH1-LIKE PROTEIN,HUASH1,ABSENT SMALL AND HOMEOTIC DISKS    
COMPND   6 PROTEIN 1 HOMOLOG,LYSINE N-METHYLTRANSFERASE 2H;                     
COMPND   7 EC: 2.1.1.43;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ASH1L, KIAA1420, KMT2H;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HISTONE METHYLATION, SET DOMAIN, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.S.ROGAWSKI,J.NDOJ,H.J.CHO,I.MAILLARD,J.GREMBECKA,T.CIERPICKI        
REVDAT   5   04-OCT-17 4YPA    1       REMARK                                   
REVDAT   4   27-SEP-17 4YPA    1       JRNL   REMARK                            
REVDAT   3   16-SEP-15 4YPA    1       JRNL                                     
REVDAT   2   09-SEP-15 4YPA    1       JRNL                                     
REVDAT   1   02-SEP-15 4YPA    0                                                
JRNL        AUTH   D.S.ROGAWSKI,J.NDOJ,H.J.CHO,I.MAILLARD,J.GREMBECKA,          
JRNL        AUTH 2 T.CIERPICKI                                                  
JRNL        TITL   TWO LOOPS UNDERGOING CONCERTED DYNAMICS REGULATE THE         
JRNL        TITL 2 ACTIVITY OF THE ASH1L HISTONE METHYLTRANSFERASE.             
JRNL        REF    BIOCHEMISTRY                  V.  54  5401 2015              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   26292256                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.5B00697                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 73.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 38087                          
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) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2003                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2758                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.17                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 136                          
REMARK   3   BIN FREE R VALUE                    : 0.3760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 120                                     
REMARK   3   SOLVENT ATOMS            : 214                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -0.26000                                             
REMARK   3    B12 (A**2) : -0.15000                                             
REMARK   3    B13 (A**2) : -0.15000                                             
REMARK   3    B23 (A**2) : -0.09000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.528         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.313         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.634         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.868                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7188 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9682 ; 1.644 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   854 ; 6.788 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   380 ;38.506 ;24.105       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1264 ;18.956 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    56 ;18.546 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   980 ; 0.108 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5556 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4272 ; 0.987 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6862 ; 1.836 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2916 ; 2.538 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2820 ; 4.041 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A   2069       A    2280      4                      
REMARK   3           1     C   2069       C    2280      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1712 ; 0.380 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1712 ; 1.060 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   2069       B    2280      4                      
REMARK   3           1     D   2069       D    2280      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1712 ; 0.330 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1712 ; 0.860 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4YPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207830.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.3-8.7                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40091                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4YNM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MAGNESIUM CHLORIDE, TRIS,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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  2281                                                      
REMARK 465     LYS A  2282                                                      
REMARK 465     SER A  2283                                                      
REMARK 465     GLN A  2284                                                      
REMARK 465     ARG A  2285                                                      
REMARK 465     VAL A  2286                                                      
REMARK 465     ASN A  2287                                                      
REMARK 465     GLY A  2288                                                      
REMARK 465     GLY B  2063                                                      
REMARK 465     ALA B  2064                                                      
REMARK 465     MET B  2065                                                      
REMARK 465     ALA B  2066                                                      
REMARK 465     GLY B  2067                                                      
REMARK 465     SER B  2068                                                      
REMARK 465     GLY B  2281                                                      
REMARK 465     LYS B  2282                                                      
REMARK 465     SER B  2283                                                      
REMARK 465     GLN B  2284                                                      
REMARK 465     ARG B  2285                                                      
REMARK 465     VAL B  2286                                                      
REMARK 465     ASN B  2287                                                      
REMARK 465     GLY B  2288                                                      
REMARK 465     GLY C  2280                                                      
REMARK 465     GLY C  2281                                                      
REMARK 465     LYS C  2282                                                      
REMARK 465     SER C  2283                                                      
REMARK 465     GLN C  2284                                                      
REMARK 465     ARG C  2285                                                      
REMARK 465     VAL C  2286                                                      
REMARK 465     ASN C  2287                                                      
REMARK 465     GLY C  2288                                                      
REMARK 465     GLY D  2063                                                      
REMARK 465     ALA D  2064                                                      
REMARK 465     MET D  2065                                                      
REMARK 465     ALA D  2066                                                      
REMARK 465     GLY D  2067                                                      
REMARK 465     SER D  2068                                                      
REMARK 465     GLY D  2280                                                      
REMARK 465     GLY D  2281                                                      
REMARK 465     LYS D  2282                                                      
REMARK 465     SER D  2283                                                      
REMARK 465     GLN D  2284                                                      
REMARK 465     ARG D  2285                                                      
REMARK 465     VAL D  2286                                                      
REMARK 465     ASN D  2287                                                      
REMARK 465     GLY D  2288                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B  2091    ZN     ZN B  2301              0.68            
REMARK 500   SG   CYS D  2091    ZN     ZN D  2301              1.39            
REMARK 500   SG   CYS A  2093    ZN     ZN A  3001              1.60            
REMARK 500   SG   CYS D  2093    ZN     ZN D  2301              1.65            
REMARK 500   OE2  GLU B  2087     ND2  ASN C  2120              1.95            
REMARK 500   ND2  ASN B  2261     O    HOH B  2401              2.13            
REMARK 500   OD1  ASP C  2097     O    HOH C  2401              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A  2157     SD   MET B  2112     1565     1.71            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ALA A2088   C     THR A2089   N       0.147                       
REMARK 500    THR A2100   CB    THR A2100   OG1     0.137                       
REMARK 500    CYS B2091   CB    CYS B2091   SG      0.234                       
REMARK 500    CYS B2091   C     ASN B2092   N       0.179                       
REMARK 500    ASN B2092   C     CYS B2093   N       0.203                       
REMARK 500    ASP B2107   C     CYS B2108   N       0.165                       
REMARK 500    ASP C2098   CG    ASP C2098   OD2    -0.155                       
REMARK 500    GLU D2176   CD    GLU D2176   OE1     0.067                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A2093   CA  -  CB  -  SG  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    CYS A2104   O   -  C   -  N   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    THR B2090   CA  -  C   -  N   ANGL. DEV. = -14.9 DEGREES          
REMARK 500    THR B2090   O   -  C   -  N   ANGL. DEV. =   9.7 DEGREES          
REMARK 500    CYS B2091   C   -  N   -  CA  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    CYS B2091   CA  -  CB  -  SG  ANGL. DEV. =  25.3 DEGREES          
REMARK 500    CYS B2093   CA  -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    LYS B2094   C   -  N   -  CA  ANGL. DEV. = -19.4 DEGREES          
REMARK 500    THR C2090   CA  -  CB  -  CG2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A2079      -64.30    -94.76                                   
REMARK 500    GLU A2087       61.41   -111.16                                   
REMARK 500    ALA A2088      140.62    -37.09                                   
REMARK 500    THR A2089       36.81    115.78                                   
REMARK 500    ASP A2099      -15.18    -44.20                                   
REMARK 500    VAL A2105     -157.25    -68.09                                   
REMARK 500    GLU A2149       -2.10     77.42                                   
REMARK 500    GLN A2186      -30.14   -135.00                                   
REMARK 500    ASN A2189       36.89    -95.36                                   
REMARK 500    SER A2200       67.29     18.30                                   
REMARK 500    ASN A2232       53.09     37.60                                   
REMARK 500    THR B2090      110.35    106.75                                   
REMARK 500    CYS B2091      179.87    -54.61                                   
REMARK 500    LYS B2095      117.78    -29.24                                   
REMARK 500    VAL B2105      -68.60   -109.98                                   
REMARK 500    ASN B2130       40.70   -108.90                                   
REMARK 500    GLN B2131       34.73   -143.98                                   
REMARK 500    GLU B2137       49.30    -75.37                                   
REMARK 500    GLU B2176        2.98    -65.84                                   
REMARK 500    HIS B2188     -106.45      9.98                                   
REMARK 500    TYR B2194       57.86   -109.89                                   
REMARK 500    THR C2089     -148.93   -116.77                                   
REMARK 500    PRO C2096     -177.53    -69.63                                   
REMARK 500    VAL C2105     -160.62    -69.55                                   
REMARK 500    GLU C2126        1.32    -68.15                                   
REMARK 500    ASN C2130       44.20    -98.56                                   
REMARK 500    GLN C2131       38.30   -140.39                                   
REMARK 500    GLU C2137       49.99    -81.78                                   
REMARK 500    GLN C2140       46.88   -101.82                                   
REMARK 500    CYS C2141       35.04   -143.26                                   
REMARK 500    GLU C2149        0.79     80.43                                   
REMARK 500    ILE C2166      -51.98   -120.74                                   
REMARK 500    GLN C2186      -36.02   -139.65                                   
REMARK 500    ASN C2189       44.01   -101.80                                   
REMARK 500    ASP C2199     -137.47   -143.62                                   
REMARK 500    THR D2090      141.36    111.58                                   
REMARK 500    GLN D2131       36.74   -143.38                                   
REMARK 500    GLU D2137       45.02    -77.79                                   
REMARK 500    GLU D2149       -2.49     68.57                                   
REMARK 500    GLU D2176       28.33    -76.96                                   
REMARK 500    GLN D2186      -42.40   -130.77                                   
REMARK 500    HIS D2188      -79.52    -14.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A 2088     THR A 2089                  134.59                    
REMARK 500 SER B 2259     PHE B 2260                  148.39                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2091   SG                                                     
REMARK 620 2 CYS A2108   SG  109.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2104   SG                                                     
REMARK 620 2 CYS A2117   SG  105.2                                              
REMARK 620 3 CYS A2122   SG  102.1 118.1                                        
REMARK 620 4 CYS A2128   SG  118.2 109.9 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A2220   SG                                                     
REMARK 620 2 CYS A2268   SG  112.5                                              
REMARK 620 3 CYS A2270   SG  112.8 106.5                                        
REMARK 620 4 CYS A2275   SG  109.2 106.3 109.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2093   SG                                                     
REMARK 620 2 CYS B2104   SG  107.3                                              
REMARK 620 3 CYS B2108   SG  108.9 125.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2104   SG                                                     
REMARK 620 2 CYS B2117   SG  120.1                                              
REMARK 620 3 CYS B2122   SG   95.7 122.2                                        
REMARK 620 4 CYS B2128   SG  104.7 103.6 109.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B2220   SG                                                     
REMARK 620 2 CYS B2268   SG  113.3                                              
REMARK 620 3 CYS B2270   SG  112.8 113.0                                        
REMARK 620 4 CYS B2275   SG  108.5 103.2 105.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C2091   SG                                                     
REMARK 620 2 CYS C2093   SG  110.8                                              
REMARK 620 3 CYS C2104   SG  115.6 108.5                                        
REMARK 620 4 CYS C2108   SG  110.8 107.5 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C2104   SG                                                     
REMARK 620 2 CYS C2117   SG  105.5                                              
REMARK 620 3 CYS C2122   SG  110.9 119.2                                        
REMARK 620 4 CYS C2128   SG  108.8 104.0 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C2303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C2220   SG                                                     
REMARK 620 2 CYS C2268   SG  111.7                                              
REMARK 620 3 CYS C2270   SG  115.5 108.3                                        
REMARK 620 4 CYS C2275   SG  109.9 103.6 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D2301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2104   SG                                                     
REMARK 620 2 CYS D2108   SG  107.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D2302  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2104   SG                                                     
REMARK 620 2 CYS D2117   SG  116.6                                              
REMARK 620 3 CYS D2122   SG  103.9 120.1                                        
REMARK 620 4 CYS D2128   SG  107.9 106.5 100.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D2303  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2220   SG                                                     
REMARK 620 2 CYS D2268   SG  116.9                                              
REMARK 620 3 CYS D2270   SG  115.9 107.1                                        
REMARK 620 4 CYS D2275   SG  108.7 104.9 101.9                                  
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 3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 2303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM B 2304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 2303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM C 2304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 2301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 2302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 2303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM D 2304                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YNM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YNP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YPE   RELATED DB: PDB                                   
DBREF  4YPA A 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
DBREF  4YPA B 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
DBREF  4YPA C 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
DBREF  4YPA D 2069  2288  UNP    Q9NR48   ASH1L_HUMAN   2074   2293             
SEQADV 4YPA GLY A 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA A 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA MET A 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA A 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA GLY A 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA SER A 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA A 2265  UNP  Q9NR48    GLN  2270 ENGINEERED MUTATION            
SEQADV 4YPA GLY B 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA B 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA MET B 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA B 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA GLY B 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA SER B 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA B 2265  UNP  Q9NR48    GLN  2270 ENGINEERED MUTATION            
SEQADV 4YPA GLY C 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA C 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA MET C 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA C 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA GLY C 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA SER C 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA C 2265  UNP  Q9NR48    GLN  2270 ENGINEERED MUTATION            
SEQADV 4YPA GLY D 2063  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA D 2064  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA MET D 2065  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA D 2066  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA GLY D 2067  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA SER D 2068  UNP  Q9NR48              EXPRESSION TAG                 
SEQADV 4YPA ALA D 2265  UNP  Q9NR48    GLN  2270 ENGINEERED MUTATION            
SEQRES   1 A  226  GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN          
SEQRES   2 A  226  VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA          
SEQRES   3 A  226  THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG          
SEQRES   4 A  226  LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE          
SEQRES   5 A  226  ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN          
SEQRES   6 A  226  CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN          
SEQRES   7 A  226  CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY          
SEQRES   8 A  226  ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE          
SEQRES   9 A  226  ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE          
SEQRES  10 A  226  ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP          
SEQRES  11 A  226  HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP          
SEQRES  12 A  226  SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS          
SEQRES  13 A  226  SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL          
SEQRES  14 A  226  ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP          
SEQRES  15 A  226  MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE          
SEQRES  16 A  226  HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS          
SEQRES  17 A  226  GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER          
SEQRES  18 A  226  GLN ARG VAL ASN GLY                                          
SEQRES   1 B  226  GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN          
SEQRES   2 B  226  VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA          
SEQRES   3 B  226  THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG          
SEQRES   4 B  226  LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE          
SEQRES   5 B  226  ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN          
SEQRES   6 B  226  CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN          
SEQRES   7 B  226  CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY          
SEQRES   8 B  226  ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE          
SEQRES   9 B  226  ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE          
SEQRES  10 B  226  ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP          
SEQRES  11 B  226  HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP          
SEQRES  12 B  226  SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS          
SEQRES  13 B  226  SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL          
SEQRES  14 B  226  ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP          
SEQRES  15 B  226  MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE          
SEQRES  16 B  226  HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS          
SEQRES  17 B  226  GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER          
SEQRES  18 B  226  GLN ARG VAL ASN GLY                                          
SEQRES   1 C  226  GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN          
SEQRES   2 C  226  VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA          
SEQRES   3 C  226  THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG          
SEQRES   4 C  226  LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE          
SEQRES   5 C  226  ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN          
SEQRES   6 C  226  CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN          
SEQRES   7 C  226  CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY          
SEQRES   8 C  226  ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE          
SEQRES   9 C  226  ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE          
SEQRES  10 C  226  ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP          
SEQRES  11 C  226  HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP          
SEQRES  12 C  226  SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS          
SEQRES  13 C  226  SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL          
SEQRES  14 C  226  ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP          
SEQRES  15 C  226  MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE          
SEQRES  16 C  226  HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS          
SEQRES  17 C  226  GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER          
SEQRES  18 C  226  GLN ARG VAL ASN GLY                                          
SEQRES   1 D  226  GLY ALA MET ALA GLY SER TYR LYS LYS ILE ARG SER ASN          
SEQRES   2 D  226  VAL TYR VAL ASP VAL LYS PRO LEU SER GLY TYR GLU ALA          
SEQRES   3 D  226  THR THR CYS ASN CYS LYS LYS PRO ASP ASP ASP THR ARG          
SEQRES   4 D  226  LYS GLY CYS VAL ASP ASP CYS LEU ASN ARG MET ILE PHE          
SEQRES   5 D  226  ALA GLU CYS SER PRO ASN THR CYS PRO CYS GLY GLU GLN          
SEQRES   6 D  226  CYS CYS ASN GLN ARG ILE GLN ARG HIS GLU TRP VAL GLN          
SEQRES   7 D  226  CYS LEU GLU ARG PHE ARG ALA GLU GLU LYS GLY TRP GLY          
SEQRES   8 D  226  ILE ARG THR LYS GLU PRO LEU LYS ALA GLY GLN PHE ILE          
SEQRES   9 D  226  ILE GLU TYR LEU GLY GLU VAL VAL SER GLU GLN GLU PHE          
SEQRES  10 D  226  ARG ASN ARG MET ILE GLU GLN TYR HIS ASN HIS SER ASP          
SEQRES  11 D  226  HIS TYR CYS LEU ASN LEU ASP SER GLY MET VAL ILE ASP          
SEQRES  12 D  226  SER TYR ARG MET GLY ASN GLU ALA ARG PHE ILE ASN HIS          
SEQRES  13 D  226  SER CYS ASP PRO ASN CYS GLU MET GLN LYS TRP SER VAL          
SEQRES  14 D  226  ASN GLY VAL TYR ARG ILE GLY LEU TYR ALA LEU LYS ASP          
SEQRES  15 D  226  MET PRO ALA GLY THR GLU LEU THR TYR ASP TYR ASN PHE          
SEQRES  16 D  226  HIS SER PHE ASN VAL GLU LYS ALA GLN LEU CYS LYS CYS          
SEQRES  17 D  226  GLY PHE GLU LYS CYS ARG GLY ILE ILE GLY GLY LYS SER          
SEQRES  18 D  226  GLN ARG VAL ASN GLY                                          
HET     ZN  A3001       1                                                       
HET     ZN  A3002       1                                                       
HET     ZN  A3003       1                                                       
HET    SAM  A3004      27                                                       
HET     ZN  B2301       1                                                       
HET     ZN  B2302       1                                                       
HET     ZN  B2303       1                                                       
HET    SAM  B2304      27                                                       
HET     ZN  C2301       1                                                       
HET     ZN  C2302       1                                                       
HET     ZN  C2303       1                                                       
HET    SAM  C2304      27                                                       
HET     ZN  D2301       1                                                       
HET     ZN  D2302       1                                                       
HET     ZN  D2303       1                                                       
HET    SAM  D2304      27                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAM S-ADENOSYLMETHIONINE                                             
FORMUL   5   ZN    12(ZN 2+)                                                    
FORMUL   8  SAM    4(C15 H22 N6 O5 S)                                           
FORMUL  21  HOH   *214(H2 O)                                                    
HELIX    1 AA1 CYS A 2108  ILE A 2113  1                                   6    
HELIX    2 AA2 CYS A 2124  CYS A 2128  5                                   5    
HELIX    3 AA3 GLU A 2176  GLN A 2186  1                                  11    
HELIX    4 AA4 ASN A 2211  ILE A 2216  5                                   6    
HELIX    5 AA5 ASP A 2254  SER A 2259  1                                   6    
HELIX    6 AA6 ASN B 2110  PHE B 2114  5                                   5    
HELIX    7 AA7 CYS B 2124  CYS B 2128  5                                   5    
HELIX    8 AA8 GLN B 2177  GLN B 2186  1                                  10    
HELIX    9 AA9 ASN B 2211  ILE B 2216  5                                   6    
HELIX   10 AB1 ASP B 2254  HIS B 2258  5                                   5    
HELIX   11 AB2 ASN C 2110  PHE C 2114  5                                   5    
HELIX   12 AB3 CYS C 2124  CYS C 2128  5                                   5    
HELIX   13 AB4 GLU C 2176  GLN C 2186  1                                  11    
HELIX   14 AB5 ASN C 2211  ILE C 2216  5                                   6    
HELIX   15 AB6 ASP C 2254  SER C 2259  1                                   6    
HELIX   16 AB7 ASN D 2110  PHE D 2114  5                                   5    
HELIX   17 AB8 CYS D 2124  CYS D 2128  5                                   5    
HELIX   18 AB9 GLN D 2177  GLN D 2186  1                                  10    
HELIX   19 AC1 ASN D 2211  ILE D 2216  5                                   6    
HELIX   20 AC2 ASP D 2254  SER D 2259  5                                   6    
SHEET    1 AA1 2 LYS A2070  LYS A2071  0                                        
SHEET    2 AA1 2 MET A2209  GLY A2210  1  O  GLY A2210   N  LYS A2070           
SHEET    1 AA2 4 VAL A2076  TYR A2077  0                                        
SHEET    2 AA2 4 GLU A2172  SER A2175  1  O  VAL A2173   N  VAL A2076           
SHEET    3 AA2 4 MET A2202  ASP A2205 -1  O  VAL A2203   N  VAL A2174           
SHEET    4 AA2 4 CYS A2195  ASP A2199 -1  N  ASP A2199   O  MET A2202           
SHEET    1 AA3 2 LEU A2142  ARG A2146  0                                        
SHEET    2 AA3 2 TRP A2152  THR A2156 -1  O  GLY A2153   N  PHE A2145           
SHEET    1 AA4 3 PHE A2165  GLU A2168  0                                        
SHEET    2 AA4 3 VAL A2234  ALA A2241 -1  O  LEU A2239   N  ILE A2167           
SHEET    3 AA4 3 CYS A2224  VAL A2231 -1  N  VAL A2231   O  VAL A2234           
SHEET    1 AA5 2 ASN A2217  HIS A2218  0                                        
SHEET    2 AA5 2 THR A2252  TYR A2253  1  O  TYR A2253   N  ASN A2217           
SHEET    1 AA6 2 GLN A2266  LEU A2267  0                                        
SHEET    2 AA6 2 ILE A2278  ILE A2279 -1  O  ILE A2279   N  GLN A2266           
SHEET    1 AA7 2 LYS B2070  LYS B2071  0                                        
SHEET    2 AA7 2 MET B2209  GLY B2210  1  O  GLY B2210   N  LYS B2070           
SHEET    1 AA8 4 VAL B2076  TYR B2077  0                                        
SHEET    2 AA8 4 GLU B2172  SER B2175  1  O  VAL B2173   N  VAL B2076           
SHEET    3 AA8 4 MET B2202  ASP B2205 -1  O  VAL B2203   N  VAL B2174           
SHEET    4 AA8 4 CYS B2195  ASN B2197 -1  N  LEU B2196   O  ILE B2204           
SHEET    1 AA9 2 LEU B2142  ARG B2146  0                                        
SHEET    2 AA9 2 TRP B2152  THR B2156 -1  O  ARG B2155   N  GLU B2143           
SHEET    1 AB1 3 PHE B2165  GLU B2168  0                                        
SHEET    2 AB1 3 VAL B2234  ALA B2241 -1  O  LEU B2239   N  ILE B2166           
SHEET    3 AB1 3 CYS B2224  VAL B2231 -1  N  GLU B2225   O  TYR B2240           
SHEET    1 AB2 2 ASN B2217  HIS B2218  0                                        
SHEET    2 AB2 2 THR B2252  TYR B2253  1  O  TYR B2253   N  ASN B2217           
SHEET    1 AB3 2 GLN B2266  LEU B2267  0                                        
SHEET    2 AB3 2 ILE B2278  ILE B2279 -1  O  ILE B2279   N  GLN B2266           
SHEET    1 AB4 2 LYS C2070  LYS C2071  0                                        
SHEET    2 AB4 2 MET C2209  GLY C2210  1  O  GLY C2210   N  LYS C2070           
SHEET    1 AB5 4 VAL C2076  TYR C2077  0                                        
SHEET    2 AB5 4 GLU C2172  SER C2175  1  O  VAL C2173   N  VAL C2076           
SHEET    3 AB5 4 MET C2202  ASP C2205 -1  O  VAL C2203   N  VAL C2174           
SHEET    4 AB5 4 CYS C2195  ASP C2199 -1  N  LEU C2196   O  ILE C2204           
SHEET    1 AB6 2 LEU C2142  ARG C2146  0                                        
SHEET    2 AB6 2 TRP C2152  THR C2156 -1  O  GLY C2153   N  PHE C2145           
SHEET    1 AB7 3 PHE C2165  GLU C2168  0                                        
SHEET    2 AB7 3 VAL C2234  ALA C2241 -1  O  LEU C2239   N  ILE C2166           
SHEET    3 AB7 3 CYS C2224  VAL C2231 -1  N  VAL C2231   O  VAL C2234           
SHEET    1 AB8 2 ASN C2217  HIS C2218  0                                        
SHEET    2 AB8 2 THR C2252  TYR C2253  1  O  TYR C2253   N  ASN C2217           
SHEET    1 AB9 2 GLN C2266  LEU C2267  0                                        
SHEET    2 AB9 2 ILE C2278  ILE C2279 -1  O  ILE C2279   N  GLN C2266           
SHEET    1 AC1 2 LYS D2070  LYS D2071  0                                        
SHEET    2 AC1 2 MET D2209  GLY D2210  1  O  GLY D2210   N  LYS D2070           
SHEET    1 AC2 4 VAL D2076  TYR D2077  0                                        
SHEET    2 AC2 4 GLU D2172  SER D2175  1  O  VAL D2173   N  VAL D2076           
SHEET    3 AC2 4 MET D2202  ASP D2205 -1  O  ASP D2205   N  GLU D2172           
SHEET    4 AC2 4 CYS D2195  ASN D2197 -1  N  LEU D2196   O  ILE D2204           
SHEET    1 AC3 2 LEU D2142  ARG D2146  0                                        
SHEET    2 AC3 2 TRP D2152  THR D2156 -1  O  GLY D2153   N  PHE D2145           
SHEET    1 AC4 3 PHE D2165  GLU D2168  0                                        
SHEET    2 AC4 3 VAL D2234  ALA D2241 -1  O  LEU D2239   N  ILE D2167           
SHEET    3 AC4 3 CYS D2224  VAL D2231 -1  N  GLU D2225   O  TYR D2240           
SHEET    1 AC5 2 ASN D2217  HIS D2218  0                                        
SHEET    2 AC5 2 THR D2252  TYR D2253  1  O  TYR D2253   N  ASN D2217           
SHEET    1 AC6 2 GLN D2266  LEU D2267  0                                        
SHEET    2 AC6 2 ILE D2278  ILE D2279 -1  O  ILE D2279   N  GLN D2266           
SSBOND   1 CYS A 2093    CYS A 2104                          1555   1555  2.33  
SSBOND   2 CYS B 2091    CYS B 2093                          1555   1555  2.30  
SSBOND   3 CYS B 2091    CYS B 2104                          1555   1555  2.82  
SSBOND   4 CYS B 2091    CYS B 2108                          1555   1555  2.40  
SSBOND   5 CYS D 2091    CYS D 2093                          1555   1555  2.26  
LINK         SG  CYS A2091                ZN    ZN A3001     1555   1555  2.40  
LINK         SG  CYS A2104                ZN    ZN A3002     1555   1555  2.63  
LINK         SG  CYS A2108                ZN    ZN A3001     1555   1555  2.42  
LINK         SG  CYS A2117                ZN    ZN A3002     1555   1555  2.29  
LINK         SG  CYS A2122                ZN    ZN A3002     1555   1555  2.52  
LINK         SG  CYS A2128                ZN    ZN A3002     1555   1555  2.38  
LINK         SG  CYS A2220                ZN    ZN A3003     1555   1555  2.25  
LINK         SG  CYS A2268                ZN    ZN A3003     1555   1555  2.32  
LINK         SG  CYS A2270                ZN    ZN A3003     1555   1555  2.27  
LINK         SG  CYS A2275                ZN    ZN A3003     1555   1555  2.35  
LINK         SG  CYS B2093                ZN    ZN B2301     1555   1555  2.29  
LINK         SG  CYS B2104                ZN    ZN B2301     1555   1555  2.34  
LINK         SG  CYS B2104                ZN    ZN B2302     1555   1555  2.30  
LINK         SG  CYS B2108                ZN    ZN B2301     1555   1555  2.23  
LINK         SG  CYS B2117                ZN    ZN B2302     1555   1555  2.49  
LINK         SG  CYS B2122                ZN    ZN B2302     1555   1555  2.26  
LINK         SG  CYS B2128                ZN    ZN B2302     1555   1555  2.39  
LINK         SG  CYS B2220                ZN    ZN B2303     1555   1555  2.30  
LINK         SG  CYS B2268                ZN    ZN B2303     1555   1555  2.29  
LINK         SG  CYS B2270                ZN    ZN B2303     1555   1555  2.27  
LINK         SG  CYS B2275                ZN    ZN B2303     1555   1555  2.41  
LINK         SG  CYS C2091                ZN    ZN C2301     1555   1555  2.21  
LINK         SG  CYS C2093                ZN    ZN C2301     1555   1555  2.18  
LINK         SG  CYS C2104                ZN    ZN C2302     1555   1555  2.15  
LINK         SG  CYS C2104                ZN    ZN C2301     1555   1555  2.37  
LINK         SG  CYS C2108                ZN    ZN C2301     1555   1555  2.27  
LINK         SG  CYS C2117                ZN    ZN C2302     1555   1555  2.35  
LINK         SG  CYS C2122                ZN    ZN C2302     1555   1555  2.16  
LINK         SG  CYS C2128                ZN    ZN C2302     1555   1555  2.35  
LINK         SG  CYS C2220                ZN    ZN C2303     1555   1555  2.35  
LINK         SG  CYS C2268                ZN    ZN C2303     1555   1555  2.25  
LINK         SG  CYS C2270                ZN    ZN C2303     1555   1555  2.23  
LINK         SG  CYS C2275                ZN    ZN C2303     1555   1555  2.40  
LINK         SG  CYS D2104                ZN    ZN D2301     1555   1555  2.40  
LINK         SG  CYS D2104                ZN    ZN D2302     1555   1555  2.21  
LINK         SG  CYS D2108                ZN    ZN D2301     1555   1555  2.41  
LINK         SG  CYS D2117                ZN    ZN D2302     1555   1555  2.48  
LINK         SG  CYS D2122                ZN    ZN D2302     1555   1555  2.31  
LINK         SG  CYS D2128                ZN    ZN D2302     1555   1555  2.21  
LINK         SG  CYS D2220                ZN    ZN D2303     1555   1555  2.32  
LINK         SG  CYS D2268                ZN    ZN D2303     1555   1555  2.14  
LINK         SG  CYS D2270                ZN    ZN D2303     1555   1555  2.21  
LINK         SG  CYS D2275                ZN    ZN D2303     1555   1555  2.44  
SITE     1 AC1  4 CYS A2091  CYS A2093  CYS A2104  CYS A2108                    
SITE     1 AC2  4 CYS A2104  CYS A2117  CYS A2122  CYS A2128                    
SITE     1 AC3  4 CYS A2220  CYS A2268  CYS A2270  CYS A2275                    
SITE     1 AC4 18 LYS A2150  TRP A2152  SER A2191  ASP A2192                    
SITE     2 AC4 18 HIS A2193  TYR A2194  ARG A2214  PHE A2215                    
SITE     3 AC4 18 ILE A2216  ASN A2217  HIS A2218  TYR A2255                    
SITE     4 AC4 18 GLN A2266  LEU A2267  CYS A2268  LYS A2269                    
SITE     5 AC4 18 ILE A2279  HOH A3131                                          
SITE     1 AC5  4 CYS B2091  CYS B2093  CYS B2104  CYS B2108                    
SITE     1 AC6  4 CYS B2104  CYS B2117  CYS B2122  CYS B2128                    
SITE     1 AC7  4 CYS B2220  CYS B2268  CYS B2270  CYS B2275                    
SITE     1 AC8 13 LYS B2150  TRP B2152  ASP B2192  HIS B2193                    
SITE     2 AC8 13 TYR B2194  ARG B2214  ASN B2217  HIS B2218                    
SITE     3 AC8 13 TYR B2255  GLN B2266  LEU B2267  LYS B2269                    
SITE     4 AC8 13 ILE B2279                                                     
SITE     1 AC9  4 CYS C2091  CYS C2093  CYS C2104  CYS C2108                    
SITE     1 AD1  4 CYS C2104  CYS C2117  CYS C2122  CYS C2128                    
SITE     1 AD2  4 CYS C2220  CYS C2268  CYS C2270  CYS C2275                    
SITE     1 AD3 16 LYS C2150  TRP C2152  SER C2191  ASP C2192                    
SITE     2 AD3 16 HIS C2193  TYR C2194  ARG C2214  PHE C2215                    
SITE     3 AD3 16 ASN C2217  HIS C2218  TYR C2255  GLN C2266                    
SITE     4 AD3 16 LEU C2267  CYS C2268  LYS C2269  ILE C2279                    
SITE     1 AD4  5 CYS D2091  CYS D2093  CYS D2104  CYS D2108                    
SITE     2 AD4  5  ZN D2302                                                     
SITE     1 AD5  5 CYS D2104  CYS D2117  CYS D2122  CYS D2128                    
SITE     2 AD5  5  ZN D2301                                                     
SITE     1 AD6  4 CYS D2220  CYS D2268  CYS D2270  CYS D2275                    
SITE     1 AD7 16 LYS D2150  GLY D2151  TRP D2152  ASP D2192                    
SITE     2 AD7 16 HIS D2193  TYR D2194  ARG D2214  ASN D2217                    
SITE     3 AD7 16 HIS D2218  TYR D2255  GLN D2266  LEU D2267                    
SITE     4 AD7 16 CYS D2268  LYS D2269  ILE D2279  HOH D2419                    
CRYST1   53.682   61.773   73.233  91.57  93.83  90.46 P 1           4          
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      0.018628  0.000150  0.001253        0.00000                         
SCALE2      0.000000  0.016189  0.000455        0.00000                         
SCALE3      0.000000  0.000000  0.013691        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system