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Database: PDB
Entry: 1SNZ
LinkDB: 1SNZ
Original site: 1SNZ 
HEADER    ISOMERASE                               12-MAR-04   1SNZ              
TITLE     CRYSTAL STRUCTURE OF APO HUMAN GALACTOSE MUTAROTASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDOSE 1-EPIMERASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GALACTOSE MUTAROTASE;                                       
COMPND   5 EC: 5.1.3.3;                                                         
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: GALM;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTYB12                                    
KEYWDS    MUTAROTASE, EPIMERASE, GALACTOSEMIA, ISOMERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,D.J.TIMSON,R.J.REECE,H.M.HOLDEN                            
REVDAT   4   11-OCT-17 1SNZ    1       REMARK                                   
REVDAT   3   24-FEB-09 1SNZ    1       VERSN                                    
REVDAT   2   08-JUN-04 1SNZ    1       JRNL                                     
REVDAT   1   30-MAR-04 1SNZ    0                                                
JRNL        AUTH   J.B.THODEN,D.J.TIMSON,R.J.REECE,H.M.HOLDEN                   
JRNL        TITL   MOLECULAR STRUCTURE OF HUMAN GALACTOSE MUTAROTASE            
JRNL        REF    J.BIOL.CHEM.                  V. 279 23431 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15026423                                                     
JRNL        DOI    10.1074/JBC.M402347200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 36670                          
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3667                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1740                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 36670                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5362                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 258                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.013 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.400 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER                                     
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SNZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000021862.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 275                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : SUPER LONG MIRRORS                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36670                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.26900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1L7J                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, HOMOPIPES, SODIUM CHLORIDE,    
REMARK 280  PH 5.0, BATCH, TEMPERATURE 275K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.35000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  20   CD    GLU A  20   OE2     0.068                       
REMARK 500    GLU A 102   CD    GLU A 102   OE2     0.070                       
REMARK 500    GLU A 253   CD    GLU A 253   OE2     0.080                       
REMARK 500    GLU B  61   CD    GLU B  61   OE2     0.067                       
REMARK 500    GLU B 102   CD    GLU B 102   OE2     0.069                       
REMARK 500    GLU B 143   CD    GLU B 143   OE2     0.066                       
REMARK 500    GLU B 197   CD    GLU B 197   OE2     0.068                       
REMARK 500    GLU B 253   CD    GLU B 253   OE2     0.070                       
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 A  27   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  30   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP A  32   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A  47   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A  54   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A  54   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    VAL A  55   CG1 -  CB  -  CG2 ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ASP A  91   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A 135   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 135   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 191   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 199   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 199   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 205   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A 205   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ASP A 236   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP A 243   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    SER A 251   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ASP A 313   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 313   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP B  32   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP B  54   CB  -  CG  -  OD2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ARG B  78   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP B  91   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP B 114   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP B 114   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG B 131   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ASP B 135   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP B 153   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 153   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ASP B 191   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP B 199   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B 199   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP B 205   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP B 205   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP B 236   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 236   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP B 313   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 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    GLU A  63      -39.89    -38.57                                   
REMARK 500    LYS A  68       99.72    -69.80                                   
REMARK 500    ASN A  81     -158.95     71.97                                   
REMARK 500    LYS A  85       15.01     55.13                                   
REMARK 500    LYS A 101       62.21   -154.55                                   
REMARK 500    GLU A 102      132.38    -25.42                                   
REMARK 500    HIS A 107       51.07     36.68                                   
REMARK 500    ASN A 172       92.42   -164.17                                   
REMARK 500    LEU A 208       40.37     73.39                                   
REMARK 500    ASP A 243       47.28   -164.19                                   
REMARK 500    SER A 251     -163.62   -110.48                                   
REMARK 500    CYS A 257      -55.09   -130.43                                   
REMARK 500    LYS A 300      144.43    -38.88                                   
REMARK 500    GLN A 309     -174.58   -172.05                                   
REMARK 500    ASP B  47     -159.07    -80.51                                   
REMARK 500    GLN B  67     -172.62    -67.29                                   
REMARK 500    ASN B  81     -163.73     67.18                                   
REMARK 500    LYS B 101       74.44   -150.51                                   
REMARK 500    GLU B 102      128.87    -39.38                                   
REMARK 500    ARG B 111       71.97   -119.75                                   
REMARK 500    HIS B 176       35.12    -95.24                                   
REMARK 500    ASP B 243       60.82   -164.00                                   
REMARK 500    SER B 251     -137.61    -90.09                                   
REMARK 500    CYS B 257      -52.23   -126.93                                   
REMARK 500    THR B 282       32.48    -96.36                                   
REMARK 500    GLN B 309     -175.54   -172.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SO0   RELATED DB: PDB                                   
DBREF  1SNZ A    1   342  UNP    Q96C23   GALM_HUMAN       1    342             
DBREF  1SNZ B    1   342  UNP    Q96C23   GALM_HUMAN       1    342             
SEQADV 1SNZ GLY A   -1  UNP  Q96C23              CLONING ARTIFACT               
SEQADV 1SNZ HIS A    0  UNP  Q96C23              CLONING ARTIFACT               
SEQADV 1SNZ GLY B   -1  UNP  Q96C23              CLONING ARTIFACT               
SEQADV 1SNZ HIS B    0  UNP  Q96C23              CLONING ARTIFACT               
SEQRES   1 A  344  GLY HIS MET ALA SER VAL THR ARG ALA VAL PHE GLY GLU          
SEQRES   2 A  344  LEU PRO SER GLY GLY GLY THR VAL GLU LYS PHE GLN LEU          
SEQRES   3 A  344  GLN SER ASP LEU LEU ARG VAL ASP ILE ILE SER TRP GLY          
SEQRES   4 A  344  CYS THR ILE THR ALA LEU GLU VAL LYS ASP ARG GLN GLY          
SEQRES   5 A  344  ARG ALA SER ASP VAL VAL LEU GLY PHE ALA GLU LEU GLU          
SEQRES   6 A  344  GLY TYR LEU GLN LYS GLN PRO TYR PHE GLY ALA VAL ILE          
SEQRES   7 A  344  GLY ARG VAL ALA ASN ARG ILE ALA LYS GLY THR PHE LYS          
SEQRES   8 A  344  VAL ASP GLY LYS GLU TYR HIS LEU ALA ILE ASN LYS GLU          
SEQRES   9 A  344  PRO ASN SER LEU HIS GLY GLY VAL ARG GLY PHE ASP LYS          
SEQRES  10 A  344  VAL LEU TRP THR PRO ARG VAL LEU SER ASN GLY VAL GLN          
SEQRES  11 A  344  PHE SER ARG ILE SER PRO ASP GLY GLU GLU GLY TYR PRO          
SEQRES  12 A  344  GLY GLU LEU LYS VAL TRP VAL THR TYR THR LEU ASP GLY          
SEQRES  13 A  344  GLY GLU LEU ILE VAL ASN TYR ARG ALA GLN ALA SER GLN          
SEQRES  14 A  344  ALA THR PRO VAL ASN LEU THR ASN HIS SER TYR PHE ASN          
SEQRES  15 A  344  LEU ALA GLY GLN ALA SER PRO ASN ILE ASN ASP HIS GLU          
SEQRES  16 A  344  VAL THR ILE GLU ALA ASP THR TYR LEU PRO VAL ASP GLU          
SEQRES  17 A  344  THR LEU ILE PRO THR GLY GLU VAL ALA PRO VAL GLN GLY          
SEQRES  18 A  344  THR ALA PHE ASP LEU ARG LYS PRO VAL GLU LEU GLY LYS          
SEQRES  19 A  344  HIS LEU GLN ASP PHE HIS LEU ASN GLY PHE ASP HIS ASN          
SEQRES  20 A  344  PHE CYS LEU LYS GLY SER LYS GLU LYS HIS PHE CYS ALA          
SEQRES  21 A  344  ARG VAL HIS HIS ALA ALA SER GLY ARG VAL LEU GLU VAL          
SEQRES  22 A  344  TYR THR THR GLN PRO GLY VAL GLN PHE TYR THR GLY ASN          
SEQRES  23 A  344  PHE LEU ASP GLY THR LEU LYS GLY LYS ASN GLY ALA VAL          
SEQRES  24 A  344  TYR PRO LYS HIS SER GLY PHE CYS LEU GLU THR GLN ASN          
SEQRES  25 A  344  TRP PRO ASP ALA VAL ASN GLN PRO ARG PHE PRO PRO VAL          
SEQRES  26 A  344  LEU LEU ARG PRO GLY GLU GLU TYR ASP HIS THR THR TRP          
SEQRES  27 A  344  PHE LYS PHE SER VAL ALA                                      
SEQRES   1 B  344  GLY HIS MET ALA SER VAL THR ARG ALA VAL PHE GLY GLU          
SEQRES   2 B  344  LEU PRO SER GLY GLY GLY THR VAL GLU LYS PHE GLN LEU          
SEQRES   3 B  344  GLN SER ASP LEU LEU ARG VAL ASP ILE ILE SER TRP GLY          
SEQRES   4 B  344  CYS THR ILE THR ALA LEU GLU VAL LYS ASP ARG GLN GLY          
SEQRES   5 B  344  ARG ALA SER ASP VAL VAL LEU GLY PHE ALA GLU LEU GLU          
SEQRES   6 B  344  GLY TYR LEU GLN LYS GLN PRO TYR PHE GLY ALA VAL ILE          
SEQRES   7 B  344  GLY ARG VAL ALA ASN ARG ILE ALA LYS GLY THR PHE LYS          
SEQRES   8 B  344  VAL ASP GLY LYS GLU TYR HIS LEU ALA ILE ASN LYS GLU          
SEQRES   9 B  344  PRO ASN SER LEU HIS GLY GLY VAL ARG GLY PHE ASP LYS          
SEQRES  10 B  344  VAL LEU TRP THR PRO ARG VAL LEU SER ASN GLY VAL GLN          
SEQRES  11 B  344  PHE SER ARG ILE SER PRO ASP GLY GLU GLU GLY TYR PRO          
SEQRES  12 B  344  GLY GLU LEU LYS VAL TRP VAL THR TYR THR LEU ASP GLY          
SEQRES  13 B  344  GLY GLU LEU ILE VAL ASN TYR ARG ALA GLN ALA SER GLN          
SEQRES  14 B  344  ALA THR PRO VAL ASN LEU THR ASN HIS SER TYR PHE ASN          
SEQRES  15 B  344  LEU ALA GLY GLN ALA SER PRO ASN ILE ASN ASP HIS GLU          
SEQRES  16 B  344  VAL THR ILE GLU ALA ASP THR TYR LEU PRO VAL ASP GLU          
SEQRES  17 B  344  THR LEU ILE PRO THR GLY GLU VAL ALA PRO VAL GLN GLY          
SEQRES  18 B  344  THR ALA PHE ASP LEU ARG LYS PRO VAL GLU LEU GLY LYS          
SEQRES  19 B  344  HIS LEU GLN ASP PHE HIS LEU ASN GLY PHE ASP HIS ASN          
SEQRES  20 B  344  PHE CYS LEU LYS GLY SER LYS GLU LYS HIS PHE CYS ALA          
SEQRES  21 B  344  ARG VAL HIS HIS ALA ALA SER GLY ARG VAL LEU GLU VAL          
SEQRES  22 B  344  TYR THR THR GLN PRO GLY VAL GLN PHE TYR THR GLY ASN          
SEQRES  23 B  344  PHE LEU ASP GLY THR LEU LYS GLY LYS ASN GLY ALA VAL          
SEQRES  24 B  344  TYR PRO LYS HIS SER GLY PHE CYS LEU GLU THR GLN ASN          
SEQRES  25 B  344  TRP PRO ASP ALA VAL ASN GLN PRO ARG PHE PRO PRO VAL          
SEQRES  26 B  344  LEU LEU ARG PRO GLY GLU GLU TYR ASP HIS THR THR TRP          
SEQRES  27 B  344  PHE LYS PHE SER VAL ALA                                      
FORMUL   3  HOH   *258(H2 O)                                                    
HELIX    1   1 GLU A   61  GLN A   67  1                                   7    
HELIX    2   2 GLY A  112  VAL A  116  5                                   5    
HELIX    3   3 GLY A  136  TYR A  140  5                                   5    
HELIX    4   4 LEU A  230  PHE A  237  1                                   8    
HELIX    5   5 LYS A  293  GLY A  295  5                                   3    
HELIX    6   6 ASP A  313  GLN A  317  5                                   5    
HELIX    7   7 GLU B   61  GLN B   67  1                                   7    
HELIX    8   8 GLY B  112  VAL B  116  5                                   5    
HELIX    9   9 GLY B  136  TYR B  140  5                                   5    
HELIX   10  10 LEU B  230  PHE B  237  1                                   8    
HELIX   11  11 LYS B  293  GLY B  295  5                                   3    
HELIX   12  12 ASP B  313  GLN B  317  5                                   5    
SHEET    1   A 5 SER A   3  LEU A  12  0                                        
SHEET    2   A 5 GLY A  17  GLN A  25 -1  O  LYS A  21   N  ALA A   7           
SHEET    3   A 5 ARG A  30  ILE A  34 -1  O  VAL A  31   N  LEU A  24           
SHEET    4   A 5 THR A  39  LYS A  46 -1  O  ALA A  42   N  ASP A  32           
SHEET    5   A 5 ALA A  52  ASP A  54 -1  O  SER A  53   N  VAL A  45           
SHEET    1   B 2 VAL A  75  ILE A  76  0                                        
SHEET    2   B 2 THR A 174  ASN A 175 -1  O  THR A 174   N  ILE A  76           
SHEET    1   C 2 ARG A  82  ILE A  83  0                                        
SHEET    2   C 2 SER A 105  LEU A 106 -1  O  SER A 105   N  ILE A  83           
SHEET    1   D 2 THR A  87  VAL A  90  0                                        
SHEET    2   D 2 LYS A  93  HIS A  96 -1  O  TYR A  95   N  PHE A  88           
SHEET    1   E 9 THR A 119  LEU A 123  0                                        
SHEET    2   E 9 GLY A 126  SER A 133 -1  O  GLY A 126   N  LEU A 123           
SHEET    3   E 9 LEU A 144  ASP A 153 -1  O  VAL A 148   N  PHE A 129           
SHEET    4   E 9 GLU A 156  ALA A 165 -1  O  GLN A 164   N  LYS A 145           
SHEET    5   E 9 TYR A 331  VAL A 341 -1  O  PHE A 337   N  LEU A 157           
SHEET    6   E 9 ARG A 267  THR A 273 -1  N  VAL A 268   O  SER A 340           
SHEET    7   E 9 HIS A 255  HIS A 261 -1  N  ALA A 258   O  VAL A 271           
SHEET    8   E 9 GLU A 193  ILE A 196 -1  N  GLU A 193   O  HIS A 261           
SHEET    9   E 9 VAL A 228  GLU A 229 -1  O  VAL A 228   N  VAL A 194           
SHEET    1   F 2 THR A 169  PRO A 170  0                                        
SHEET    2   F 2 LEU A 324  LEU A 325 -1  O  LEU A 325   N  THR A 169           
SHEET    1   G 5 ALA A 215  PRO A 216  0                                        
SHEET    2   G 5 ALA A 198  TYR A 201 -1  N  TYR A 201   O  ALA A 215           
SHEET    3   G 5 ASP A 243  LEU A 248 -1  O  CYS A 247   N  THR A 200           
SHEET    4   G 5 GLY A 277  TYR A 281 -1  O  VAL A 278   N  PHE A 246           
SHEET    5   G 5 CYS A 305  GLN A 309 -1  O  GLU A 307   N  GLN A 279           
SHEET    1   H 2 ASP A 287  LYS A 291  0                                        
SHEET    2   H 2 VAL A 297  PRO A 299 -1  O  TYR A 298   N  GLY A 288           
SHEET    1   I 5 SER B   3  LEU B  12  0                                        
SHEET    2   I 5 GLY B  17  GLN B  25 -1  O  LYS B  21   N  ALA B   7           
SHEET    3   I 5 ARG B  30  ILE B  34 -1  O  VAL B  31   N  LEU B  24           
SHEET    4   I 5 THR B  39  LYS B  46 -1  O  THR B  39   N  ILE B  34           
SHEET    5   I 5 ALA B  52  ASP B  54 -1  O  SER B  53   N  VAL B  45           
SHEET    1   J 2 VAL B  75  ILE B  76  0                                        
SHEET    2   J 2 THR B 174  ASN B 175 -1  O  THR B 174   N  ILE B  76           
SHEET    1   K 2 ARG B  82  ILE B  83  0                                        
SHEET    2   K 2 SER B 105  LEU B 106 -1  O  SER B 105   N  ILE B  83           
SHEET    1   L 2 THR B  87  VAL B  90  0                                        
SHEET    2   L 2 LYS B  93  HIS B  96 -1  O  TYR B  95   N  PHE B  88           
SHEET    1   M 9 THR B 119  LEU B 123  0                                        
SHEET    2   M 9 GLY B 126  SER B 133 -1  O  GLY B 126   N  LEU B 123           
SHEET    3   M 9 LEU B 144  LEU B 152 -1  O  VAL B 148   N  PHE B 129           
SHEET    4   M 9 GLU B 156  ALA B 165 -1  O  ILE B 158   N  THR B 151           
SHEET    5   M 9 TYR B 331  VAL B 341 -1  O  PHE B 337   N  LEU B 157           
SHEET    6   M 9 ARG B 267  THR B 273 -1  N  TYR B 272   O  TRP B 336           
SHEET    7   M 9 HIS B 255  HIS B 262 -1  N  CYS B 257   O  VAL B 271           
SHEET    8   M 9 GLU B 193  ILE B 196 -1  N  GLU B 193   O  HIS B 261           
SHEET    9   M 9 VAL B 228  GLU B 229 -1  O  VAL B 228   N  VAL B 194           
SHEET    1   N 2 THR B 169  PRO B 170  0                                        
SHEET    2   N 2 LEU B 324  LEU B 325 -1  O  LEU B 325   N  THR B 169           
SHEET    1   O 6 TYR B 178  PHE B 179  0                                        
SHEET    2   O 6 PHE B 304  GLN B 309 -1  O  PHE B 304   N  PHE B 179           
SHEET    3   O 6 GLY B 277  TYR B 281 -1  N  TYR B 281   O  CYS B 305           
SHEET    4   O 6 ASP B 243  LEU B 248 -1  N  HIS B 244   O  PHE B 280           
SHEET    5   O 6 ALA B 198  TYR B 201 -1  N  THR B 200   O  CYS B 247           
SHEET    6   O 6 ALA B 215  PRO B 216 -1  O  ALA B 215   N  TYR B 201           
SHEET    1   P 2 ASP B 287  LYS B 291  0                                        
SHEET    2   P 2 VAL B 297  PRO B 299 -1  O  TYR B 298   N  GLY B 288           
CISPEP   1 GLY A   77    ARG A   78          0         1.90                     
CISPEP   2 GLU A  102    PRO A  103          0        -3.28                     
CISPEP   3 GLY B   77    ARG B   78          0         3.42                     
CISPEP   4 GLU B  102    PRO B  103          0        -0.07                     
CRYST1   60.700   90.700   70.000  90.00 102.50  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016474  0.000000  0.003652        0.00000                         
SCALE2      0.000000  0.011025  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014633        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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