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Database: PDB
Entry: 1ZSY
LinkDB: 1ZSY
Original site: 1ZSY 
HEADER    OXIDOREDUCTASE                          25-MAY-05   1ZSY              
TITLE     THE STRUCTURE OF HUMAN MITOCHONDRIAL 2-ENOYL THIOESTER REDUCTASE (CGI-
TITLE    2 63)                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOCHONDRIAL 2-ENOYL THIOESTER REDUCTASE;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TRANS-2-ENOYL-COA REDUCTASE, HSNRBF-1, NRBF-1, CGI-63,      
COMPND   5 NUCLEAR RECEPTOR-BINDING FACTOR 1;                                   
COMPND   6 EC: 1.3.1.38;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: HOMOLOG OF YEAST 2-ENOYL THIOESTER REDUCTASE          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MECR, NBRF1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4                                 
KEYWDS    MEDIUM-CHAIN DEHYDROGENASE/REDUCTASE, OXIDOREDUCTASE, 2-ENOYL         
KEYWDS   2 THIOESTER REDUCTASE, FATTY ACID SYNTHESIS (TYPE 2), STRUCTURAL       
KEYWDS   3 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.LUKACIK,N.SHAFQAT,K.L.KAVANAGH,C.JOHANSSON,C.SMEE,A.EDWARDS,        
AUTHOR   2 C.ARROWSMITH,M.SUNDSTROM,F.VON DELFT,U.OPPERMANN,STRUCTURAL GENOMICS 
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   3   13-JUL-11 1ZSY    1       VERSN                                    
REVDAT   2   24-FEB-09 1ZSY    1       VERSN                                    
REVDAT   1   07-JUN-05 1ZSY    0                                                
JRNL        AUTH   P.LUKACIK,N.SHAFQAT,K.L.KAVANAGH,C.JOHANSSON,C.SMEE,         
JRNL        AUTH 2 A.EDWARDS,C.ARROWSMITH,M.SUNDSTROM,F.VON DELFT,U.OPPERMANN   
JRNL        TITL   THE STRUCTURE OF HUMAN MITOCHONDRIAL 2-ENOYL THIOESTER       
JRNL        TITL 2 REDUCTASE (CGI-63)                                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 52854                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2813                            
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) : 1.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.79                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3891                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 229                          
REMARK   3   BIN FREE R VALUE                    : 0.2210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2604                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 345                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 20.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.02000                                             
REMARK   3    B22 (A**2) : 0.69000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
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): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.053         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.174         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2766 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3775 ; 1.419 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   375 ; 5.533 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;38.869 ;24.434       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   468 ;13.138 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.592 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   438 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2077 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1302 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1934 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   288 ; 0.143 ; 0.200       
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):    50 ; 0.164 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.148 ; 0.200       
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):  1831 ; 1.888 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2896 ; 2.924 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1032 ; 5.150 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   869 ; 7.559 ;12.000       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    23        A   357                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7400  18.9740  19.1270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0346 T22:  -0.0641                                     
REMARK   3      T33:  -0.0416 T12:  -0.0024                                     
REMARK   3      T13:  -0.0048 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6535 L22:   0.3879                                     
REMARK   3      L33:   0.6189 L12:   0.1537                                     
REMARK   3      L13:   0.5231 L23:   0.0901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0303 S12:   0.0820 S13:  -0.1117                       
REMARK   3      S21:   0.0182 S22:   0.0328 S23:  -0.0562                       
REMARK   3      S31:   0.0204 S32:   0.0232 S33:  -0.0631                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 1ZSY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033081.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.984                              
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55668                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : 0.11300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1GU7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULPHATE, 0.16M SODIUM     
REMARK 280  CHLORIDE, 0.08M SODIUM CACODYLATE , PH 6.5, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.09500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.59200            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       63.68600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.09500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.59200            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       63.68600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.09500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.59200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       63.68600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.09500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       58.59200            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       63.68600            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 801  LIES ON A SPECIAL POSITION.                          
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     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CD   OE1  OE2                                       
REMARK 470     LYS A 232    CG   CD   CE   NZ                                   
REMARK 470     ASN A 233    CG   OD1                                            
REMARK 470     LYS A 236    CE   NZ                                             
REMARK 470     LYS A 251    CD   CE   NZ                                        
REMARK 470     MET A 272    SD   CE                                             
REMARK 470     LYS A 274    CG   CD   CE   NZ                                   
REMARK 470     LYS A 287    CE   NZ                                             
REMARK 470     GLU A 310    CD   OE1  OE2                                       
REMARK 470     GLU A 342    CG   CD   OE1  OE2                                  
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 321   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 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    LEU A  18       47.05    -87.61                                   
REMARK 500    ASN A  77       69.22   -115.62                                   
REMARK 500    VAL A 150      -74.12   -117.53                                   
REMARK 500    ASP A 237       -4.05     76.00                                   
REMARK 500    CYS A 247       27.11   -147.19                                   
REMARK 500    LYS A 274       -3.35     86.13                                   
REMARK 500    GLN A 275       76.55   -116.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 831        DISTANCE =  5.09 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 503                 
DBREF  1ZSY A   24   357  UNP    Q9BV79   MECR_HUMAN      40    373             
SEQADV 1ZSY MET A    1  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY HIS A    2  UNP  Q9BV79              EXPRESSION TAG                 
SEQADV 1ZSY HIS A    3  UNP  Q9BV79              EXPRESSION TAG                 
SEQADV 1ZSY HIS A    4  UNP  Q9BV79              EXPRESSION TAG                 
SEQADV 1ZSY HIS A    5  UNP  Q9BV79              EXPRESSION TAG                 
SEQADV 1ZSY HIS A    6  UNP  Q9BV79              EXPRESSION TAG                 
SEQADV 1ZSY HIS A    7  UNP  Q9BV79              EXPRESSION TAG                 
SEQADV 1ZSY SER A    8  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY SER A    9  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY GLY A   10  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY VAL A   11  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY ASP A   12  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY LEU A   13  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY GLY A   14  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY THR A   15  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY GLU A   16  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY ASN A   17  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY LEU A   18  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY TYR A   19  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY PHE A   20  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY GLN A   21  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY SER A   22  UNP  Q9BV79              CLONING ARTIFACT               
SEQADV 1ZSY MET A   23  UNP  Q9BV79              CLONING ARTIFACT               
SEQRES   1 A  357  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  357  GLY THR GLU ASN LEU TYR PHE GLN SER MET PRO ALA ARG          
SEQRES   3 A  357  VAL ARG ALA LEU VAL TYR GLY HIS HIS GLY ASP PRO ALA          
SEQRES   4 A  357  LYS VAL VAL GLU LEU LYS ASN LEU GLU LEU ALA ALA VAL          
SEQRES   5 A  357  ARG GLY SER ASP VAL ARG VAL LYS MET LEU ALA ALA PRO          
SEQRES   6 A  357  ILE ASN PRO SER ASP ILE ASN MET ILE GLN GLY ASN TYR          
SEQRES   7 A  357  GLY LEU LEU PRO GLU LEU PRO ALA VAL GLY GLY ASN GLU          
SEQRES   8 A  357  GLY VAL ALA GLN VAL VAL ALA VAL GLY SER ASN VAL THR          
SEQRES   9 A  357  GLY LEU LYS PRO GLY ASP TRP VAL ILE PRO ALA ASN ALA          
SEQRES  10 A  357  GLY LEU GLY THR TRP ARG THR GLU ALA VAL PHE SER GLU          
SEQRES  11 A  357  GLU ALA LEU ILE GLN VAL PRO SER ASP ILE PRO LEU GLN          
SEQRES  12 A  357  SER ALA ALA THR LEU GLY VAL ASN PRO CYS THR ALA TYR          
SEQRES  13 A  357  ARG MET LEU MET ASP PHE GLU GLN LEU GLN PRO GLY ASP          
SEQRES  14 A  357  SER VAL ILE GLN ASN ALA SER ASN SER GLY VAL GLY GLN          
SEQRES  15 A  357  ALA VAL ILE GLN ILE ALA ALA ALA LEU GLY LEU ARG THR          
SEQRES  16 A  357  ILE ASN VAL VAL ARG ASP ARG PRO ASP ILE GLN LYS LEU          
SEQRES  17 A  357  SER ASP ARG LEU LYS SER LEU GLY ALA GLU HIS VAL ILE          
SEQRES  18 A  357  THR GLU GLU GLU LEU ARG ARG PRO GLU MET LYS ASN PHE          
SEQRES  19 A  357  PHE LYS ASP MET PRO GLN PRO ARG LEU ALA LEU ASN CYS          
SEQRES  20 A  357  VAL GLY GLY LYS SER SER THR GLU LEU LEU ARG GLN LEU          
SEQRES  21 A  357  ALA ARG GLY GLY THR MET VAL THR TYR GLY GLY MET ALA          
SEQRES  22 A  357  LYS GLN PRO VAL VAL ALA SER VAL SER LEU LEU ILE PHE          
SEQRES  23 A  357  LYS ASP LEU LYS LEU ARG GLY PHE TRP LEU SER GLN TRP          
SEQRES  24 A  357  LYS LYS ASP HIS SER PRO ASP GLN PHE LYS GLU LEU ILE          
SEQRES  25 A  357  LEU THR LEU CYS ASP LEU ILE ARG ARG GLY GLN LEU THR          
SEQRES  26 A  357  ALA PRO ALA CYS SER GLN VAL PRO LEU GLN ASP TYR GLN          
SEQRES  27 A  357  SER ALA LEU GLU ALA SER MET LYS PRO PHE ILE SER SER          
SEQRES  28 A  357  LYS GLN ILE LEU THR MET                                      
HET    SO4  A 500       5                                                       
HET    GOL  A 501       6                                                       
HET    GOL  A 502       6                                                       
HET    GOL  A 503       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   6  HOH   *345(H2 O)                                                    
HELIX    1   1 ASP A   37  VAL A   41  1                                   5    
HELIX    2   2 ASN A   67  GLY A   76  1                                  10    
HELIX    3   3 PRO A  141  LEU A  148  1                                   8    
HELIX    4   4 VAL A  150  PHE A  162  1                                  13    
HELIX    5   5 SER A  178  GLY A  192  1                                  15    
HELIX    6   6 ASP A  204  LEU A  215  1                                  12    
HELIX    7   7 GLU A  223  ARG A  228  1                                   6    
HELIX    8   8 PRO A  229  PHE A  234  5                                   6    
HELIX    9   9 GLY A  249  ARG A  258  1                                  10    
HELIX   10  10 SER A  280  LYS A  287  1                                   8    
HELIX   11  11 TRP A  295  HIS A  303  1                                   9    
HELIX   12  12 SER A  304  ARG A  321  1                                  18    
HELIX   13  13 ASP A  336  MET A  345  1                                  10    
SHEET    1   A 3 VAL A  42  LEU A  47  0                                        
SHEET    2   A 3 VAL A  27  TYR A  32 -1  N  ALA A  29   O  LYS A  45           
SHEET    3   A 3 ALA A  86  VAL A  87 -1  O  ALA A  86   N  TYR A  32           
SHEET    1   B 5 GLU A 125  SER A 129  0                                        
SHEET    2   B 5 ASP A  56  PRO A  65 -1  N  VAL A  59   O  ALA A 126           
SHEET    3   B 5 VAL A  93  VAL A  99 -1  O  VAL A  97   N  ARG A  58           
SHEET    4   B 5 TRP A 111  PRO A 114 -1  O  VAL A 112   N  ALA A  94           
SHEET    5   B 5 LEU A 133  VAL A 136 -1  O  ILE A 134   N  ILE A 113           
SHEET    1   C 4 GLU A 125  SER A 129  0                                        
SHEET    2   C 4 ASP A  56  PRO A  65 -1  N  VAL A  59   O  ALA A 126           
SHEET    3   C 4 LYS A 352  THR A 356 -1  O  LEU A 355   N  ALA A  64           
SHEET    4   C 4 CYS A 329  PRO A 333  1  N  SER A 330   O  LYS A 352           
SHEET    1   D 6 HIS A 219  THR A 222  0                                        
SHEET    2   D 6 ARG A 194  VAL A 199  1  N  ASN A 197   O  HIS A 219           
SHEET    3   D 6 SER A 170  GLN A 173  1  N  GLN A 173   O  VAL A 198           
SHEET    4   D 6 LEU A 243  ASN A 246  1  O  LEU A 245   N  ILE A 172           
SHEET    5   D 6 THR A 265  THR A 268  1  O  VAL A 267   N  ASN A 246           
SHEET    6   D 6 LYS A 290  GLY A 293  1  O  LYS A 290   N  MET A 266           
CISPEP   1 LEU A   84    PRO A   85          0        -0.62                     
SITE     1 AC1  9 ALA A 175  SER A 176  ASN A 177  SER A 178                    
SITE     2 AC1  9 VAL A 199  ARG A 200  ARG A 202  HOH A 581                    
SITE     3 AC1  9 HOH A 724                                                     
SITE     1 AC2  9 PRO A  68  ASN A 151  SER A 178  GLY A 179                    
SITE     2 AC2  9 VAL A 180  LYS A 352  HOH A 548  HOH A 564                    
SITE     3 AC2  9 HOH A 772                                                     
SITE     1 AC3  7 ASN A  17  GLN A 166  PRO A 167  GLY A 168                    
SITE     2 AC3  7 ASP A 169  HOH A 640  HOH A 757                               
SITE     1 AC4  2 HIS A  34  HIS A  35                                          
CRYST1   74.190  117.184  127.372  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008534  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007851        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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