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Database: PDB
Entry: 4RVB
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Original site: 4RVB 
HEADER    HYDROLASE                               25-NOV-14   4RVB              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF THE HUMAN LEUKOTRIENE A4 HYDROLASE      
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: PET28A                                    
KEYWDS    AMINOPEPTIDASES, EPOXIDE HYDROLASES, HYDROLYSIS, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.OUYANG,W.LU,K.CUI,J.HUANG                                           
REVDAT   1   02-DEC-15 4RVB    0                                                
JRNL        AUTH   P.OUYANG,W.LU,K.CUI,J.HUANG                                  
JRNL        TITL   CRYSTAL STRUCTURE ANALYSIS OF THE HUMAN LEUKOTRIENE A4       
JRNL        TITL 2 HYDROLASE                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 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) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 48698                          
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) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2534                            
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) : 1.93                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3525                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.25                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 195                          
REMARK   3   BIN FREE R VALUE                    : 0.1940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4853                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 564                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.00000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
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): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.338         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5014 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4750 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6803 ; 1.820 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10966 ; 0.893 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   606 ; 6.678 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   222 ;35.833 ;24.414       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   856 ;12.772 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;19.339 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   756 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5595 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1138 ; 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):  2431 ; 1.199 ; 1.175       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2426 ; 1.182 ; 1.172       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3032 ; 1.698 ; 1.750       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3033 ; 1.700 ; 1.752       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2583 ; 2.430 ; 1.476       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2584 ; 2.430 ; 1.476       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3772 ; 3.771 ; 2.093       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  6267 ; 6.021 ;10.830       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  6268 ; 6.021 ;10.833       
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 4RVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB087840.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
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) : 0.97852                            
REMARK 200  MONOCHROMATOR                  : MONOCHROMATOR SAGITALLY FOCUSED    
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48698                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.270                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
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) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3FTX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 8000, 100MM IMIDAZOLE PH 6.2,    
REMARK 280  100MM NAACETATE, 5MM YBCL3, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
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       38.96950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.61400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.57650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.61400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.96950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.57650            
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     ILE A     3                                                      
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   OE1  GLU A   401     O    HOH A  1136              1.35            
REMARK 500   O    HOH A  1024     O    HOH A  1314              1.83            
REMARK 500   O    HOH A   912     O    HOH A  1274              1.88            
REMARK 500   OE1  GLU A   182     O    HOH A   819              1.89            
REMARK 500   OE2  GLU A   182     O    HOH A   819              1.99            
REMARK 500   CD   GLU A   182     O    HOH A   819              2.16            
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   O    HOH A  1139     O    HOH A  1280     2554     2.11            
REMARK 500   OD1  ASP A   175     O    HOH A  1034     4545     2.17            
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 174   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG A 338   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    LEU A 407   CB  -  CG  -  CD2 ANGL. DEV. = -10.3 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       66.38   -111.99                                   
REMARK 500    SER A  80     -131.63     48.52                                   
REMARK 500    ASN A  97       -1.31     73.93                                   
REMARK 500    ASP A 183       91.81   -167.56                                   
REMARK 500    GLU A 271       44.10    -78.69                                   
REMARK 500    CYS A 274      -12.19     71.83                                   
REMARK 500    LEU A 275       81.37   -153.64                                   
REMARK 500    PHE A 432       37.42    -96.68                                   
REMARK 500    LYS A 546       37.18     75.60                                   
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 VAL A  609     ASP A  610                  131.22                    
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 702  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 318   OE1                                                    
REMARK 620 2 HIS A 299   NE2 107.5                                              
REMARK 620 3 ACT A 704   O   100.3 132.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A 701  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 481   OD2                                                    
REMARK 620 2 HOH A 803   O   132.9                                              
REMARK 620 3 ASP A 481   OD1  54.4  78.6                                        
REMARK 620 4 ACT A 703   OXT  78.9  90.2  74.4                                  
REMARK 620 5 ACT A 703   O   128.4  72.8 119.5  54.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 702                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 711                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4R7L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4RSY   RELATED DB: PDB                                   
DBREF  4RVB A    0   610  UNP    P09960   LKHA4_HUMAN      1    611             
SEQADV 4RVB MET A  -20  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB GLY A  -19  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB SER A  -18  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB SER A  -17  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB HIS A  -16  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB HIS A  -15  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB HIS A  -14  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB HIS A  -13  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB HIS A  -12  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB HIS A  -11  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB SER A  -10  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB SER A   -9  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB GLY A   -8  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB LEU A   -7  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB VAL A   -6  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB PRO A   -5  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB ARG A   -4  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB GLY A   -3  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB SER A   -2  UNP  P09960              EXPRESSION TAG                 
SEQADV 4RVB 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     YB  A 701       1                                                       
HET     ZN  A 702       1                                                       
HET    ACT  A 703       4                                                       
HET    ACT  A 704       4                                                       
HET    IMD  A 705       5                                                       
HET    IMD  A 706       5                                                       
HET    IMD  A 707       5                                                       
HET    GOL  A 708       6                                                       
HET    GOL  A 709       6                                                       
HET    ACY  A 710       4                                                       
HET    ACY  A 711       4                                                       
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM      ZN ZINC ION                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACY ACETIC ACID                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   YB    YB 3+                                                        
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  ACT    2(C2 H3 O2 1-)                                               
FORMUL   6  IMD    3(C3 H5 N2 1+)                                               
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  11  ACY    2(C2 H4 O2)                                                  
FORMUL  13  HOH   *564(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  HIS A  313  5                                   4    
HELIX   11  11 PHE A  314  GLY A  334  1                                  21    
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  GLY A  398  1                                  19    
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  LYS A  608  1                                  13    
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  GLU A 107   N  THR A  60           
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  ASP A  28   O  THR A  33           
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         OE1 GLU A 318                ZN    ZN A 702     1555   1555  1.93  
LINK         NE2 HIS A 299                ZN    ZN A 702     1555   1555  2.03  
LINK        ZN    ZN A 702                 O   ACT A 704     1555   1555  2.04  
LINK         OD2 ASP A 481                YB    YB A 701     1555   1555  2.35  
LINK        YB    YB A 701                 O   HOH A 803     1555   1555  2.39  
LINK         OD1 ASP A 481                YB    YB A 701     1555   1555  2.40  
LINK        YB    YB A 701                 OXT ACT A 703     1555   1555  2.41  
LINK        YB    YB A 701                 O   ACT A 703     1555   1555  2.56  
CISPEP   1 GLN A  136    ALA A  137          0        -5.51                     
CISPEP   2 ALA A  510    PRO A  511          0         9.33                     
SITE     1 AC1  6 ASP A  47  ASP A 481  ACT A 703  HOH A 803                    
SITE     2 AC1  6 HOH A1027  HOH A1357                                          
SITE     1 AC2  4 HIS A 295  HIS A 299  GLU A 318  ACT A 704                    
SITE     1 AC3 10 ASP A  47  ASN A  48  ARG A 174  LYS A 479                    
SITE     2 AC3 10 ASP A 481   YB A 701  HOH A 803  HOH A 830                    
SITE     3 AC3 10 HOH A1162  HOH A1357                                          
SITE     1 AC4 10 GLY A 269  GLU A 271  HIS A 295  GLU A 296                    
SITE     2 AC4 10 HIS A 299  GLU A 318  TYR A 383   ZN A 702                    
SITE     3 AC4 10 HOH A 953  HOH A1359                                          
SITE     1 AC5  6 GLY A 344  GLY A 347  GLU A 348  GLU A 501                    
SITE     2 AC5  6 ALA A 504  GLN A 508                                          
SITE     1 AC6  5 TRP A 311  PHE A 314  VAL A 367  ALA A 377                    
SITE     2 AC6  5 HOH A1310                                                     
SITE     1 AC7  5 PHE A  29  ARG A  32  LEU A 118  PRO A 129                    
SITE     2 AC7  5 HOH A1219                                                     
SITE     1 AC8  8 SER A 288  LEU A 289  SER A 496  HIS A 497                    
SITE     2 AC8  8 ASN A 500  ASN A 531  GLU A 533  HOH A1133                    
SITE     1 AC9  2 LYS A 417  SER A 418                                          
CRYST1   77.939   87.153   99.228  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      0.012831  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010078        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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