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Database: PDB
Entry: 3U9W
LinkDB: 3U9W
Original site: 3U9W 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           20-OCT-11   3U9W              
TITLE     STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH INHIBITOR 
TITLE    2 SC57461A                                                             
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: JM101;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT3                                       
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.NIEGOWSKI,M.THUNNISSEN,F.THOLANDER,A.RINALDO-MATTHIS,A.MUROYA,      
AUTHOR   2 J.Z.HAEGGSTROM                                                       
REVDAT   2   07-MAR-18 3U9W    1       REMARK                                   
REVDAT   1   24-OCT-12 3U9W    0                                                
JRNL        AUTH   U.OLSSON,D.NIEGOWSKI,A.STSIAPANAVA,M.THUNNISSEN,             
JRNL        AUTH 2 J.Z.HAEGGSTROM,A.RINALDO-MATTHIS                             
JRNL        TITL   STRUCTURE OF HUMAN LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH  
JRNL        TITL 2 INHIBITOR SC57461A                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 184616                         
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) : 0.134                           
REMARK   3   R VALUE            (WORKING SET) : 0.134                           
REMARK   3   FREE R VALUE                     : 0.161                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2753                            
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) : 1.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13185                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 196                          
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4860                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 811                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.97                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22000                                              
REMARK   3    B22 (A**2) : 0.92000                                              
REMARK   3    B33 (A**2) : -1.15000                                             
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): 0.036         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.037         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.024         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.223         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.969                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5243 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7170 ; 1.975 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   675 ; 6.224 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   230 ;34.046 ;24.609       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   921 ;12.124 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.082 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   806 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3980 ; 0.013 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3165 ; 2.029 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5186 ; 3.050 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2078 ; 4.538 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1952 ; 6.494 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5243 ; 2.339 ; 3.000       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY           
REMARK   4                                                                      
REMARK   4 3U9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068489.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0408                             
REMARK 200  MONOCHROMATOR                  : BENT SI (111) CRYSTAL,             
REMARK 200                                   HORIZONTALLY FOCUSING              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 184616                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.372                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9200                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.610                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG8000, 0.1 MM SODIUM ACETATE,      
REMARK 280  0.1 MM IMIDAZOLE, 5 MM YTTERBIUM(III) CHLORIDE, PH 6.8, LIQUID-     
REMARK 280  LIQUID DIFFUSION, CAPILLARIES, TEMPERATURE 298K                     
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       39.03900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.57250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.39950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.57250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.03900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.39950            
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 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   OD1  ASP A  1426     O    HOH A  8907              2.02            
REMARK 500   OE1  GLU A  1210     O    HOH A  8773              2.09            
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    ASP A1047   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A1212   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ASP A1257   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    PHE A1277   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A1443   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A1578   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A1578   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 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 A1079       71.56   -114.81                                   
REMARK 500    SER A1080     -127.68     46.11                                   
REMARK 500    SER A1080     -124.14     40.34                                   
REMARK 500    ASN A1097       -1.11     76.04                                   
REMARK 500    ASP A1183       96.29   -165.65                                   
REMARK 500    GLU A1271       45.28    -80.54                                   
REMARK 500    CYS A1274      -19.94     76.30                                   
REMARK 500    LEU A1275       85.76   -152.88                                   
REMARK 500    PHE A1432       39.24    -94.96                                   
REMARK 500    LYS A1546       33.27     71.83                                   
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 A2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 28P A7001   OAE                                                    
REMARK 620 2 HIS A1299   NE2 119.0                                              
REMARK 620 3 GLU A1318   OE1 101.5 112.4                                        
REMARK 620 4 HIS A1295   NE2 112.8 106.7 103.4                                  
REMARK 620 5 28P A7001   OAF  53.8  84.6 155.2  87.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A   2  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A8908   O                                                      
REMARK 620 2 ASP A1426   OD1  68.0                                              
REMARK 620 3 HOH A8929   O   127.3 162.1                                        
REMARK 620 4 HOH A8914   O   143.1  75.6  87.8                                  
REMARK 620 5 HOH A8915   O    81.9  70.1 100.9  80.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A1611  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A8914   O                                                      
REMARK 620 2 HOH A8913   O    76.0                                              
REMARK 620 3 ASP A1426   OD2  85.3  78.8                                        
REMARK 620 4 HOH A8915   O    88.9 150.6  75.0                                  
REMARK 620 5 HOH A8920   O   103.8 155.6 125.6  52.2                            
REMARK 620 6 ASP A1426   OD1  58.3  98.2  38.6  52.6 102.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A   7  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1426   OD1                                                    
REMARK 620 2 HOH A8908   O    63.8                                              
REMARK 620 3 HOH A8914   O    73.6 115.2                                        
REMARK 620 4 HOH A8929   O   116.0  88.2  68.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A2002  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A8062   O                                                      
REMARK 620 2 ASP A1481   OD1 131.9                                              
REMARK 620 3 HOH A8118   O    77.4 143.6                                        
REMARK 620 4 HOH A8066   O    79.2  84.9  80.2                                  
REMARK 620 5 ACT A   1   O    89.7  77.0 131.3 143.5                            
REMARK 620 6 ASP A1481   OD2  77.5  54.4 145.3  71.8  71.8                      
REMARK 620 7 ACT A   1   OXT  73.8 126.3  77.2 147.8  54.2 117.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A   5  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A1070   OE2                                                    
REMARK 620 2 HOH A8727   O   173.3                                              
REMARK 620 3 GLU A1070   OE1  47.4 138.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A   3  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A8928   O                                                      
REMARK 620 2 ASP A1175   OD1 140.1                                              
REMARK 620 3 HOH A8927   O    51.9 160.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A   4  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A1182   OE1                                                    
REMARK 620 2 IMD A 186   N3  153.6                                              
REMARK 620 3 HOH A8226   O    70.7  98.3                                        
REMARK 620 4 HOH A8421   O   122.6  79.5  88.0                                  
REMARK 620 5 ARG A1024   NH2  61.5  93.0  76.3 161.4                            
REMARK 620 6 HOH A8505   O   100.4  91.5 170.2  93.6 103.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              YB A   6  YB                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A1590   OE2                                                    
REMARK 620 2 GLU A1590   OE1  45.4                                              
REMARK 620 N                    1                                               
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 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 2009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 2010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 28P A 7001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 1611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 186                 
DBREF  3U9W A 1003  1610  UNP    P09960   LKHA4_HUMAN      4    611             
SEQRES   1 A  608  ILE VAL ASP THR CYS SER LEU ALA SER PRO ALA SER VAL          
SEQRES   2 A  608  CYS ARG THR LYS HIS LEU HIS LEU ARG CYS SER VAL ASP          
SEQRES   3 A  608  PHE THR ARG ARG THR LEU THR GLY THR ALA ALA LEU THR          
SEQRES   4 A  608  VAL GLN SER GLN GLU ASP ASN LEU ARG SER LEU VAL LEU          
SEQRES   5 A  608  ASP THR LYS ASP LEU THR ILE GLU LYS VAL VAL ILE ASN          
SEQRES   6 A  608  GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU ARG GLN SER          
SEQRES   7 A  608  TYR LYS GLY SER PRO MET GLU ILE SER LEU PRO ILE ALA          
SEQRES   8 A  608  LEU SER LYS ASN GLN GLU ILE VAL ILE GLU ILE SER PHE          
SEQRES   9 A  608  GLU THR SER PRO LYS SER SER ALA LEU GLN TRP LEU THR          
SEQRES  10 A  608  PRO GLU GLN THR SER GLY LYS GLU HIS PRO TYR LEU PHE          
SEQRES  11 A  608  SER GLN CYS GLN ALA ILE HIS CYS ARG ALA ILE LEU PRO          
SEQRES  12 A  608  CYS GLN ASP THR PRO SER VAL LYS LEU THR TYR THR ALA          
SEQRES  13 A  608  GLU VAL SER VAL PRO LYS GLU LEU VAL ALA LEU MET SER          
SEQRES  14 A  608  ALA ILE ARG ASP GLY GLU THR PRO ASP PRO GLU ASP PRO          
SEQRES  15 A  608  SER ARG LYS ILE TYR LYS PHE ILE GLN LYS VAL PRO ILE          
SEQRES  16 A  608  PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY ALA LEU GLU          
SEQRES  17 A  608  SER ARG GLN ILE GLY PRO ARG THR LEU VAL TRP SER GLU          
SEQRES  18 A  608  LYS GLU GLN VAL GLU LYS SER ALA TYR GLU PHE SER GLU          
SEQRES  19 A  608  THR GLU SER MET LEU LYS ILE ALA GLU ASP LEU GLY GLY          
SEQRES  20 A  608  PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU VAL LEU PRO          
SEQRES  21 A  608  PRO SER PHE PRO TYR GLY GLY MET GLU ASN PRO CYS LEU          
SEQRES  22 A  608  THR PHE VAL THR PRO THR LEU LEU ALA GLY ASP LYS SER          
SEQRES  23 A  608  LEU SER ASN VAL ILE ALA HIS GLU ILE SER HIS SER TRP          
SEQRES  24 A  608  THR GLY ASN LEU VAL THR ASN LYS THR TRP ASP HIS PHE          
SEQRES  25 A  608  TRP LEU ASN GLU GLY HIS THR VAL TYR LEU GLU ARG HIS          
SEQRES  26 A  608  ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE ARG HIS PHE          
SEQRES  27 A  608  ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN ASN SER VAL          
SEQRES  28 A  608  LYS THR PHE GLY GLU THR HIS PRO PHE THR LYS LEU VAL          
SEQRES  29 A  608  VAL ASP LEU THR ASP ILE ASP PRO ASP VAL ALA TYR SER          
SEQRES  30 A  608  SER VAL PRO TYR GLU LYS GLY PHE ALA LEU LEU PHE TYR          
SEQRES  31 A  608  LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE PHE LEU GLY          
SEQRES  32 A  608  PHE LEU LYS ALA TYR VAL GLU LYS PHE SER TYR LYS SER          
SEQRES  33 A  608  ILE THR THR ASP ASP TRP LYS ASP PHE LEU TYR SER TYR          
SEQRES  34 A  608  PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN VAL ASP TRP          
SEQRES  35 A  608  ASN ALA TRP LEU TYR SER PRO GLY LEU PRO PRO ILE LYS          
SEQRES  36 A  608  PRO ASN TYR ASP MET THR LEU THR ASN ALA CYS ILE ALA          
SEQRES  37 A  608  LEU SER GLN ARG TRP ILE THR ALA LYS GLU ASP ASP LEU          
SEQRES  38 A  608  ASN SER PHE ASN ALA THR ASP LEU LYS ASP LEU SER SER          
SEQRES  39 A  608  HIS GLN LEU ASN GLU PHE LEU ALA GLN THR LEU GLN ARG          
SEQRES  40 A  608  ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG MET GLN GLU          
SEQRES  41 A  608  VAL TYR ASN PHE ASN ALA ILE ASN ASN SER GLU ILE ARG          
SEQRES  42 A  608  PHE ARG TRP LEU ARG LEU CYS ILE GLN SER LYS TRP GLU          
SEQRES  43 A  608  ASP ALA ILE PRO LEU ALA LEU LYS MET ALA THR GLU GLN          
SEQRES  44 A  608  GLY ARG MET LYS PHE THR ARG PRO LEU PHE LYS ASP LEU          
SEQRES  45 A  608  ALA ALA PHE ASP LYS SER HIS ASP GLN ALA VAL ARG THR          
SEQRES  46 A  608  TYR GLN GLU HIS LYS ALA SER MET HIS PRO VAL THR ALA          
SEQRES  47 A  608  MET LEU VAL GLY LYS ASP LEU LYS VAL ASP                      
HET     ZN  A2001       1                                                       
HET     YB  A2002       1                                                       
HET     CL  A2007       1                                                       
HET     CL  A2008       1                                                       
HET    IMD  A2009       5                                                       
HET    IMD  A2010       5                                                       
HET    GOL  A2011       6                                                       
HET    28P  A7001      24                                                       
HET    ACT  A   1       4                                                       
HET     YB  A1611       1                                                       
HET     YB  A   2       1                                                       
HET     YB  A   3       1                                                       
HET     YB  A   4       1                                                       
HET     YB  A   5       1                                                       
HET     YB  A   6       1                                                       
HET     YB  A   7       1                                                       
HET    IMD  A 186       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      YB YTTERBIUM (III) ION                                              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     GOL GLYCEROL                                                         
HETNAM     28P N-[3-(4-BENZYLPHENOXY)PROPYL]-N-METHYL-BETA-ALANINE              
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3   YB    8(YB 3+)                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   6  IMD    3(C3 H5 N2 1+)                                               
FORMUL   8  GOL    C3 H8 O3                                                     
FORMUL   9  28P    C20 H25 N O3                                                 
FORMUL  10  ACT    C2 H3 O2 1-                                                  
FORMUL  19  HOH   *811(H2 O)                                                    
HELIX    1   1 GLN A 1079  GLY A 1083  5                                   5    
HELIX    2   2 THR A 1119  THR A 1123  5                                   5    
HELIX    3   3 HIS A 1139  ILE A 1143  5                                   5    
HELIX    4   4 PRO A 1198  ILE A 1202  5                                   5    
HELIX    5   5 GLU A 1223  GLU A 1225  5                                   3    
HELIX    6   6 GLN A 1226  PHE A 1234  1                                   9    
HELIX    7   7 GLU A 1236  GLY A 1249  1                                  14    
HELIX    8   8 PRO A 1280  LEU A 1283  5                                   4    
HELIX    9   9 SER A 1290  HIS A 1299  1                                  10    
HELIX   10  10 THR A 1310  ASP A 1312  5                                   3    
HELIX   11  11 HIS A 1313  GLY A 1334  1                                  22    
HELIX   12  12 GLY A 1334  GLY A 1357  1                                  24    
HELIX   13  13 HIS A 1360  LYS A 1364  5                                   5    
HELIX   14  14 ASP A 1373  TYR A 1378  1                                   6    
HELIX   15  15 SER A 1380  GLY A 1398  1                                  19    
HELIX   16  16 GLY A 1399  SER A 1415  1                                  17    
HELIX   17  17 THR A 1420  PHE A 1432  1                                  13    
HELIX   18  18 LYS A 1435  GLN A 1441  1                                   7    
HELIX   19  19 ASP A 1443  SER A 1450  1                                   8    
HELIX   20  20 THR A 1465  ALA A 1478  1                                  14    
HELIX   21  21 LYS A 1479  PHE A 1486  5                                   8    
HELIX   22  22 ASN A 1487  LYS A 1492  5                                   6    
HELIX   23  23 SER A 1495  GLN A 1508  1                                  14    
HELIX   24  24 PRO A 1513  ASN A 1525  1                                  13    
HELIX   25  25 PHE A 1526  ILE A 1529  5                                   4    
HELIX   26  26 ASN A 1531  SER A 1545  1                                  15    
HELIX   27  27 ASP A 1549  GLN A 1561  1                                  13    
HELIX   28  28 ARG A 1563  PHE A 1577  1                                  15    
HELIX   29  29 PHE A 1577  LYS A 1592  1                                  16    
HELIX   30  30 ALA A 1593  MET A 1595  5                                   3    
HELIX   31  31 HIS A 1596  LYS A 1608  1                                  13    
SHEET    1   A 8 GLN A1069  GLU A1070  0                                        
SHEET    2   A 8 THR A1060  ILE A1066 -1  N  ILE A1066   O  GLN A1069           
SHEET    3   A 8 GLU A1099  GLU A1107 -1  O  GLU A1107   N  THR A1060           
SHEET    4   A 8 THR A1033  SER A1044 -1  N  LEU A1040   O  ILE A1102           
SHEET    5   A 8 CYS A1016  ASP A1028 -1  N  LYS A1019   O  THR A1041           
SHEET    6   A 8 LEU A1154  PRO A1163  1  O  SER A1161   N  CYS A1025           
SHEET    7   A 8 ARG A1186  ILE A1197 -1  O  GLN A1193   N  TYR A1156           
SHEET    8   A 8 ILE A1173  PRO A1179 -1  N  THR A1178   O  ILE A1188           
SHEET    1   B 3 LEU A1049  THR A1056  0                                        
SHEET    2   B 3 SER A1084  LEU A1094 -1  O  ILE A1088   N  LEU A1052           
SHEET    3   B 3 TYR A1073  LEU A1075 -1  N  ALA A1074   O  GLU A1087           
SHEET    1   C 4 LEU A1115  LEU A1118  0                                        
SHEET    2   C 4 TYR A1130  SER A1133 -1  O  TYR A1130   N  LEU A1118           
SHEET    3   C 4 LEU A1204  GLY A1207 -1  O  VAL A1206   N  LEU A1131           
SHEET    4   C 4 VAL A1167  MET A1170 -1  N  VAL A1167   O  GLY A1207           
SHEET    1   D 5 GLU A1210  GLY A1215  0                                        
SHEET    2   D 5 THR A1218  SER A1222 -1  O  SER A1222   N  GLU A1210           
SHEET    3   D 5 ASP A1257  VAL A1260  1  O  VAL A1260   N  TRP A1221           
SHEET    4   D 5 LEU A1275  VAL A1278  1  O  VAL A1278   N  LEU A1259           
SHEET    5   D 5 GLY A1269  MET A1270 -1  N  MET A1270   O  PHE A1277           
SHEET    1   E 2 VAL A1306  ASN A1308  0                                        
SHEET    2   E 2 LYS A1417  ILE A1419  1  O  ILE A1419   N  THR A1307           
LINK        ZN    ZN A2001                 OAE 28P A7001     1555   1555  1.93  
LINK         NE2 HIS A1299                ZN    ZN A2001     1555   1555  1.97  
LINK         OE1 GLU A1318                ZN    ZN A2001     1555   1555  1.98  
LINK         NE2 HIS A1295                ZN    ZN A2001     1555   1555  2.01  
LINK        YB    YB A   2                 O   HOH A8908     1555   1555  2.06  
LINK        YB    YB A1611                 O   HOH A8914     1555   1555  2.07  
LINK         OD1BASP A1426                YB    YB A   7     1555   1555  2.14  
LINK        YB    YB A2002                 O   HOH A8062     1555   1555  2.17  
LINK        YB    YB A1611                 O   HOH A8913     1555   1555  2.20  
LINK         OE2 GLU A1070                YB    YB A   5     1555   1555  2.26  
LINK         OD1BASP A1426                YB    YB A   2     1555   1555  2.27  
LINK        YB    YB A   3                 O   HOH A8928     1555   1555  2.28  
LINK         OD1 ASP A1481                YB    YB A2002     1555   1555  2.33  
LINK         OD2BASP A1426                YB    YB A1611     1555   1555  2.34  
LINK        YB    YB A2002                 O   HOH A8118     1555   1555  2.34  
LINK        YB    YB A2002                 O   HOH A8066     1555   1555  2.35  
LINK        YB    YB A   5                 O   HOH A8727     1555   1555  2.38  
LINK        YB    YB A2002                 O   ACT A   1     1555   1555  2.40  
LINK         OD1 ASP A1175                YB    YB A   3     1555   1555  2.41  
LINK         OE1AGLU A1182                YB    YB A   4     1555   1555  2.42  
LINK        YB    YB A   7                 O   HOH A8908     1555   1555  2.43  
LINK        YB    YB A   2                 O   HOH A8929     1555   1555  2.45  
LINK         OD2 ASP A1481                YB    YB A2002     1555   1555  2.47  
LINK        YB    YB A2002                 OXT ACT A   1     1555   1555  2.48  
LINK        YB    YB A   2                 O   HOH A8914     1555   1555  2.51  
LINK        YB    YB A   2                 O   HOH A8915     1555   1555  2.53  
LINK        YB    YB A1611                 O   HOH A8915     1555   1555  2.54  
LINK        YB    YB A   4                 N3  IMD A 186     1555   1555  2.56  
LINK        YB    YB A   4                 O   HOH A8226     1555   1555  2.60  
LINK        ZN    ZN A2001                 OAF 28P A7001     1555   1555  2.61  
LINK        YB    YB A   4                 O   HOH A8421     1555   1555  2.70  
LINK        YB    YB A   7                 O   HOH A8914     1555   1555  2.70  
LINK        YB    YB A1611                 O   HOH A8920     1555   1555  2.72  
LINK        YB    YB A   3                 O   HOH A8927     1555   1555  2.72  
LINK         OE2AGLU A1590                YB    YB A   6     1555   1555  2.80  
LINK         OE1AGLU A1590                YB    YB A   6     1555   1555  2.86  
LINK         NH2 ARG A1024                YB    YB A   4     1555   1555  2.86  
LINK         OE1 GLU A1070                YB    YB A   5     1555   1555  2.96  
LINK        YB    YB A   7                 O   HOH A8929     1555   1555  3.31  
LINK        YB    YB A   4                 O   HOH A8505     1555   1555  3.38  
LINK         OD1BASP A1426                YB    YB A1611     1555   1555  3.43  
CISPEP   1 GLN A 1136    ALA A 1137          0         0.41                     
CISPEP   2 ALA A 1510    PRO A 1511          0         1.26                     
SITE     1 AC1  4 HIS A1295  HIS A1299  GLU A1318  28P A7001                    
SITE     1 AC2  6 ACT A   1  ASP A1047  ASP A1481  HOH A8062                    
SITE     2 AC2  6 HOH A8066  HOH A8118                                          
SITE     1 AC3  3 ASP A1058  ARG A1078  SER A1084                               
SITE     1 AC4  3 PRO A1216  PRO A1513  GLY A1515                               
SITE     1 AC5  6 GLY A1344  GLY A1347  GLU A1348  GLU A1501                    
SITE     2 AC5  6 ALA A1504  GLN A1508                                          
SITE     1 AC6  7 SER A1288  LEU A1289  SER A1496  HIS A1497                    
SITE     2 AC6  7 ASN A1500  ASN A1531  HOH A8436                               
SITE     1 AC7  8 PHE A1029  ARG A1032  TRP A1117  LEU A1118                    
SITE     2 AC7  8 PRO A1120  HOH A8236  HOH A8548  HOH A8552                    
SITE     1 AC8 18 GLN A1136  TYR A1267  GLY A1269  MET A1270                    
SITE     2 AC8 18 GLU A1271  HIS A1295  GLU A1296  HIS A1299                    
SITE     3 AC8 18 TRP A1311  PHE A1314  GLU A1318  VAL A1367                    
SITE     4 AC8 18 PRO A1374  ALA A1377  TYR A1378  PRO A1382                    
SITE     5 AC8 18 TYR A1383   ZN A2001                                          
SITE     1 AC9 10 ASP A1047  ASN A1048  ARG A1174  LYS A1479                    
SITE     2 AC9 10 ASP A1481   YB A2002  HOH A8010  HOH A8062                    
SITE     3 AC9 10 HOH A8118  HOH A8615                                          
SITE     1 BC1  6  YB A   2  ASP A1426  HOH A8913  HOH A8914                    
SITE     2 BC1  6 HOH A8915  HOH A8920                                          
SITE     1 BC2  8  YB A   7  ASP A1426  ASP A1610   YB A1611                    
SITE     2 BC2  8 HOH A8908  HOH A8914  HOH A8915  HOH A8929                    
SITE     1 BC3  4 ASP A1175  HOH A8925  HOH A8927  HOH A8928                    
SITE     1 BC4  5 IMD A 186  ARG A1024  GLU A1182  HOH A8226                    
SITE     2 BC4  5 HOH A8421                                                     
SITE     1 BC5  2 GLU A1070  HOH A8727                                          
SITE     1 BC6  2 GLU A1182  GLU A1590                                          
SITE     1 BC7  5  YB A   2  ASP A1426  ASP A1610  HOH A8908                    
SITE     2 BC7  5 HOH A8914                                                     
SITE     1 BC8  7  YB A   4  ARG A1024  CYS A1025  GLU A1159                    
SITE     2 BC8  7 ILE A1188  HOH A8226  HOH A8380                               
CRYST1   78.078   86.799   99.145  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      0.012808  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011521  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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