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Database: PDB
Entry: 4R7L
LinkDB: 4R7L
Original site: 4R7L 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           27-AUG-14   4R7L              
TITLE     STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH INHIBITOR 
TITLE    2 H1                                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LTA-4 HYDROLASE, LEUKOTRIENE A(4) HYDROLASE;                
COMPND   5 EC: 3.3.2.6;                                                         
COMPND   6 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: LTA4H, LTA4;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    LEUKOTRIENE A4, METALLOPROTEIN, PROTEASE, ZINC BINDING,               
KEYWDS   2 AMINOPEPTIDASE ACTIVITY, HYDROLASE-HYDROLASE INHIBITOR COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.OUYANG,K.CUI,W.LU,J.HUANG                                           
REVDAT   1   25-NOV-15 4R7L    0                                                
JRNL        AUTH   P.OUYANG,K.CUI,W.LU,J.HUANG                                  
JRNL        TITL   HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH SAHA          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 1.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 76051                          
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) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4036                            
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) : 1.66                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5487                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 278                          
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4852                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 426                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.080         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.083         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.047         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.338         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5016 ; 0.021 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4765 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6803 ; 2.086 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10998 ; 0.964 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   604 ; 6.269 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   221 ;33.970 ;24.389       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   856 ;11.764 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;16.606 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   756 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5583 ; 0.013 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1137 ; 0.001 ; 0.020       
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):  2427 ; 1.445 ; 1.555       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2424 ; 1.438 ; 1.554       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3028 ; 1.934 ; 2.331       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3029 ; 1.935 ; 2.332       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2589 ; 2.984 ; 1.861       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2589 ; 2.984 ; 1.861       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3776 ; 4.341 ; 2.671       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6069 ; 5.092 ;13.643       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6069 ; 5.092 ;13.643       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4R7L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086999.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76480                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.190                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 30.19                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 8000, 0.1MM NA-ACETATE, 0.1MM    
REMARK 280  IMIDAZOLE, 5MM YBCL3, PH 6.8, VAPOR DIFFUSION, TEMPERATURE 277K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       38.95800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.64250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.56700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.64250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.95800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.56700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASP A   610                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  174   CA   CB   CG   CD   NE   CZ   NH1                   
REMARK 480     ARG A  174   NH2                                                 
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   OE2  GLU A   245     O    HOH A  1212              1.78            
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   OD2  ASP A   481    YB     YB A   702     1545     2.16            
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    GLU A 165   CD    GLU A 165   OE1     0.071                       
REMARK 500    GLU A 228   CD    GLU A 228   OE2    -0.075                       
REMARK 500    GLU A 401   CD    GLU A 401   OE1     0.073                       
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    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A  50   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 186   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    ARG A 186   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 312   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A 338   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 338   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ASP A 368   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    MET A 520   CG  -  SD  -  CE  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A 563   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 563   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 578   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 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    GLN A  79       73.41   -109.55                                   
REMARK 500    SER A  80     -132.80     43.46                                   
REMARK 500    ASP A 183       95.44   -163.54                                   
REMARK 500    PRO A 184       -8.43    -57.94                                   
REMARK 500    GLU A 271       40.89    -80.97                                   
REMARK 500    CYS A 274      -15.17     73.98                                   
REMARK 500    LEU A 275       78.30   -154.35                                   
REMARK 500    PRO A 458      170.25    -57.00                                   
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 A 701  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SHH A 709   O2                                                     
REMARK 620 2 HIS A 299   NE2 151.9                                              
REMARK 620 3 GLU A 318   OE1  90.3  99.1                                        
REMARK 620 4 SHH A 709   O1   78.4  87.8 166.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 702  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACT A 707   OXT                                                    
REMARK 620 2 ASP A  47   OD1 127.9                                              
REMARK 620 3 HOH A1063   O    88.6 143.1                                        
REMARK 620 4 HOH A1064   O   129.0  75.4  77.0                                  
REMARK 620 5 ASP A  47   OD2  80.2  54.4 145.0  84.6                            
REMARK 620 6 ACT A 707   O    53.2 119.7  75.7  75.8  71.1                      
REMARK 620 7 HOH A 852   O   146.1  71.8  79.5  79.2 126.1 148.0                
REMARK 620 N                    1     2     3     4     5     6                 
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 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SHH A 709                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3B7S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3B7T   RELATED DB: PDB                                   
DBREF  4R7L A    0   610  UNP    P09960   LKHA4_HUMAN      1    611             
SEQADV 4R7L MET A  -20  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L GLY A  -19  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L SER A  -18  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L SER A  -17  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A  -16  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A  -15  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A  -14  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A  -13  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A  -12  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A  -11  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L SER A  -10  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L SER A   -9  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L GLY A   -8  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L LEU A   -7  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L VAL A   -6  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L PRO A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L ARG A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L GLY A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L SER A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 4R7L HIS A   -1  UNP  P09960              EXPRESSION TAG                 
SEQRES   1 A  631  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  631  LEU VAL PRO ARG GLY SER HIS MET PRO GLU ILE VAL ASP          
SEQRES   3 A  631  THR CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR          
SEQRES   4 A  631  LYS HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG          
SEQRES   5 A  631  ARG THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER          
SEQRES   6 A  631  GLN GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS          
SEQRES   7 A  631  ASP LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU          
SEQRES   8 A  631  VAL LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY          
SEQRES   9 A  631  SER PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS          
SEQRES  10 A  631  ASN GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER          
SEQRES  11 A  631  PRO LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN          
SEQRES  12 A  631  THR SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS          
SEQRES  13 A  631  GLN ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP          
SEQRES  14 A  631  THR PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER          
SEQRES  15 A  631  VAL PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG          
SEQRES  16 A  631  ASP GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS          
SEQRES  17 A  631  ILE TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR          
SEQRES  18 A  631  LEU ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN          
SEQRES  19 A  631  ILE GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN          
SEQRES  20 A  631  VAL GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER          
SEQRES  21 A  631  MET LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL          
SEQRES  22 A  631  TRP GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE          
SEQRES  23 A  631  PRO TYR GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL          
SEQRES  24 A  631  THR PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN          
SEQRES  25 A  631  VAL ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN          
SEQRES  26 A  631  LEU VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN          
SEQRES  27 A  631  GLU GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY          
SEQRES  28 A  631  ARG LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU          
SEQRES  29 A  631  GLY GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE          
SEQRES  30 A  631  GLY GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU          
SEQRES  31 A  631  THR ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO          
SEQRES  32 A  631  TYR GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN          
SEQRES  33 A  631  LEU LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS          
SEQRES  34 A  631  ALA TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR          
SEQRES  35 A  631  ASP ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP          
SEQRES  36 A  631  LYS VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP          
SEQRES  37 A  631  LEU TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR          
SEQRES  38 A  631  ASP MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN          
SEQRES  39 A  631  ARG TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE          
SEQRES  40 A  631  ASN ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU          
SEQRES  41 A  631  ASN GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU          
SEQRES  42 A  631  PRO LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN          
SEQRES  43 A  631  PHE ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP          
SEQRES  44 A  631  LEU ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE          
SEQRES  45 A  631  PRO LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET          
SEQRES  46 A  631  LYS PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE          
SEQRES  47 A  631  ASP LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU          
SEQRES  48 A  631  HIS LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL          
SEQRES  49 A  631  GLY LYS ASP LEU LYS VAL ASP                                  
HET     ZN  A 701       1                                                       
HET     YB  A 702       1                                                       
HET    GOL  A 703       6                                                       
HET    GOL  A 704       6                                                       
HET    GOL  A 705       6                                                       
HET    ACT  A 706       4                                                       
HET    ACT  A 707       4                                                       
HET    IMD  A 708       5                                                       
HET    SHH  A 709      19                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     SHH OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     SHH SAHA                                                             
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    YB 3+                                                        
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   7  ACT    2(C2 H3 O2 1-)                                               
FORMUL   9  IMD    C3 H5 N2 1+                                                  
FORMUL  10  SHH    C14 H20 N2 O3                                                
FORMUL  11  HOH   *426(H2 O)                                                    
HELIX    1   1 GLN A   79  GLY A   83  5                                   5    
HELIX    2   2 THR A  119  THR A  123  5                                   5    
HELIX    3   3 HIS A  139  ILE A  143  5                                   5    
HELIX    4   4 TYR A  200  ILE A  202  5                                   3    
HELIX    5   5 GLU A  223  GLU A  225  5                                   3    
HELIX    6   6 GLN A  226  PHE A  234  1                                   9    
HELIX    7   7 GLU A  236  GLY A  249  1                                  14    
HELIX    8   8 PRO A  280  LEU A  283  5                                   4    
HELIX    9   9 SER A  290  HIS A  299  1                                  10    
HELIX   10  10 THR A  310  ASP A  312  5                                   3    
HELIX   11  11 HIS A  313  GLY A  334  1                                  22    
HELIX   12  12 GLY A  334  GLY A  357  1                                  24    
HELIX   13  13 HIS A  360  LYS A  364  5                                   5    
HELIX   14  14 ASP A  373  TYR A  378  1                                   6    
HELIX   15  15 SER A  380  LEU A  397  1                                  18    
HELIX   16  16 GLY A  399  SER A  415  1                                  17    
HELIX   17  17 THR A  420  PHE A  432  1                                  13    
HELIX   18  18 LYS A  435  ASN A  440  1                                   6    
HELIX   19  19 ASP A  443  SER A  450  1                                   8    
HELIX   20  20 THR A  465  ALA A  478  1                                  14    
HELIX   21  21 LYS A  479  PHE A  486  5                                   8    
HELIX   22  22 ASN A  487  LYS A  492  5                                   6    
HELIX   23  23 SER A  495  GLN A  508  1                                  14    
HELIX   24  24 PRO A  513  ASN A  525  1                                  13    
HELIX   25  25 PHE A  526  ILE A  529  5                                   4    
HELIX   26  26 ASN A  531  SER A  545  1                                  15    
HELIX   27  27 TRP A  547  ASP A  549  5                                   3    
HELIX   28  28 ALA A  550  GLN A  561  1                                  12    
HELIX   29  29 ARG A  563  PHE A  577  1                                  15    
HELIX   30  30 PHE A  577  LYS A  592  1                                  16    
HELIX   31  31 ALA A  593  MET A  595  5                                   3    
HELIX   32  32 HIS A  596  LEU A  607  1                                  12    
SHEET    1   A 8 GLN A  69  GLU A  70  0                                        
SHEET    2   A 8 LEU A  59  ILE A  66 -1  N  ILE A  66   O  GLN A  69           
SHEET    3   A 8 GLU A  99  THR A 108 -1  O  SER A 105   N  GLU A  62           
SHEET    4   A 8 THR A  33  SER A  44 -1  N  LEU A  40   O  ILE A 102           
SHEET    5   A 8 CYS A  16  ASP A  28 -1  N  LYS A  19   O  THR A  41           
SHEET    6   A 8 LYS A 153  PRO A 163  1  O  SER A 161   N  CYS A  25           
SHEET    7   A 8 ARG A 186  PRO A 198 -1  O  GLN A 193   N  TYR A 156           
SHEET    8   A 8 ILE A 173  PRO A 179 -1  N  THR A 178   O  ILE A 188           
SHEET    1   B 3 LEU A  49  THR A  56  0                                        
SHEET    2   B 3 SER A  84  LEU A  94 -1  O  ILE A  88   N  LEU A  52           
SHEET    3   B 3 TYR A  73  LEU A  75 -1  N  ALA A  74   O  GLU A  87           
SHEET    1   C 4 LEU A 115  LEU A 118  0                                        
SHEET    2   C 4 TYR A 130  SER A 133 -1  O  TYR A 130   N  LEU A 118           
SHEET    3   C 4 LEU A 204  GLY A 207 -1  O  VAL A 206   N  LEU A 131           
SHEET    4   C 4 VAL A 167  MET A 170 -1  N  VAL A 167   O  GLY A 207           
SHEET    1   D 5 GLU A 210  GLY A 215  0                                        
SHEET    2   D 5 THR A 218  SER A 222 -1  O  VAL A 220   N  ARG A 212           
SHEET    3   D 5 ASP A 257  VAL A 260  1  O  VAL A 260   N  TRP A 221           
SHEET    4   D 5 LEU A 275  VAL A 278  1  O  VAL A 278   N  LEU A 259           
SHEET    5   D 5 GLY A 269  MET A 270 -1  N  MET A 270   O  PHE A 277           
SHEET    1   E 2 VAL A 306  ASN A 308  0                                        
SHEET    2   E 2 LYS A 417  ILE A 419  1  O  ILE A 419   N  THR A 307           
LINK        ZN    ZN A 701                 O2  SHH A 709     1555   1555  2.01  
LINK         NE2 HIS A 299                ZN    ZN A 701     1555   1555  2.07  
LINK         OE1 GLU A 318                ZN    ZN A 701     1555   1555  2.07  
LINK        ZN    ZN A 701                 O1  SHH A 709     1555   1555  2.16  
LINK        YB    YB A 702                 OXT ACT A 707     1555   1555  2.37  
LINK         OD1 ASP A  47                YB    YB A 702     1555   1555  2.38  
LINK        YB    YB A 702                 O   HOH A1063     1555   1555  2.39  
LINK        YB    YB A 702                 O   HOH A1064     1555   1555  2.42  
LINK         OD2 ASP A  47                YB    YB A 702     1555   1555  2.49  
LINK        YB    YB A 702                 O   ACT A 707     1555   1555  2.59  
LINK        YB    YB A 702                 O   HOH A 852     1555   1555  2.61  
CISPEP   1 GLN A  136    ALA A  137          0        -1.19                     
CISPEP   2 ALA A  510    PRO A  511          0        10.39                     
SITE     1 AC1  4 HIS A 295  HIS A 299  GLU A 318  SHH A 709                    
SITE     1 AC2  6 ASP A  47  ASP A 481  ACT A 707  HOH A 852                    
SITE     2 AC2  6 HOH A1063  HOH A1064                                          
SITE     1 AC3  4 PHE A  29  ARG A  32  TRP A 117  LEU A 118                    
SITE     1 AC4  9 GLY A 269  HIS A 295  GLU A 296  GOL A 705                    
SITE     2 AC4  9 ACT A 706  SHH A 709  HOH A 806  HOH A1222                    
SITE     3 AC4  9 HOH A1223                                                     
SITE     1 AC5  5 TYR A 378  SER A 380  TYR A 383  LYS A 565                    
SITE     2 AC5  5 GOL A 704                                                     
SITE     1 AC6  5 GLY A 268  TYR A 378  ARG A 563  GOL A 704                    
SITE     2 AC6  5 HOH A 816                                                     
SITE     1 AC7  9 ASP A  47  ASN A  48  ARG A 174  LYS A 479                    
SITE     2 AC7  9 ASP A 481   YB A 702  HOH A 854  HOH A1063                    
SITE     3 AC7  9 HOH A1064                                                     
SITE     1 AC8  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC8  6 ALA A 504  GLN A 508                                          
SITE     1 AC9 15 GLN A 136  ALA A 137  TYR A 267  GLY A 269                    
SITE     2 AC9 15 GLU A 271  HIS A 295  GLU A 296  HIS A 299                    
SITE     3 AC9 15 PHE A 314  GLU A 318  PRO A 374  TYR A 378                    
SITE     4 AC9 15 TYR A 383   ZN A 701  GOL A 704                               
CRYST1   77.916   87.134   99.285  90.00  90.00  90.00 P 21 21 21    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      0.012834  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010072        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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