GenomeNet

Database: PDB
Entry: 4Y2W
LinkDB: 4Y2W
Original site: 4Y2W 
HEADER    ISOMERASE                               10-FEB-15   4Y2W              
TITLE     CRYSTAL STRUCTURE OF A THERMOSTABLE ALANINE RACEMASE FROM             
TITLE    2 THERMOANAEROBACTER TENGCONGENSIS MB4                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE 1;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CALDANAEROBACTER SUBTERRANEUS SUBSP.            
SOURCE   3 TENGCONGENSIS MB4;                                                   
SOURCE   4 ORGANISM_COMMON: THERMOANAEROBACTER TENGCONGENSIS MB4;               
SOURCE   5 ORGANISM_TAXID: 273068;                                              
SOURCE   6 STRAIN: MB4;                                                         
SOURCE   7 GENE: ALR1, TTE1207;                                                 
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALANINE RACEMASE, GLN360, ISOMERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.XU,J.JU,H.DONG                                                      
REVDAT   1   23-SEP-15 4Y2W    0                                                
JRNL        AUTH   X.SUN,G.HE,X.WANG,S.XU,J.JU,X.XU                             
JRNL        TITL   CRYSTAL STRUCTURE OF A THERMOSTABLE ALANINE RACEMASE FROM    
JRNL        TITL 2 THERMOANAEROBACTER TENGCONGENSIS MB4 REVEALS THE ROLE OF     
JRNL        TITL 3 GLN360 IN SUBSTRATE SELECTION                                
JRNL        REF    PLOS ONE                      V.  10 33516 2015              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   26218070                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0133516                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 25425                          
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1353                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1620                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6212                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.73000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 2.79000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.347         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.260         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.927        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.884                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6341 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6346 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8536 ; 0.986 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14594 ; 0.660 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   774 ; 5.378 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   280 ;34.796 ;23.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1204 ;14.095 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;16.630 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   966 ; 0.051 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6991 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1407 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3108 ; 1.057 ; 4.504       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3107 ; 1.057 ; 4.504       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3878 ; 1.859 ; 6.753       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4Y2W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206751.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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 MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 HKL-2000                  
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26832                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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: 1SFT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 4000, 0.1M BIS-TRIS PH7.0,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                     
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       30.42150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      109.37300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.53850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      109.37300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.42150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.53850            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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    TYR A 107       32.56   -146.56                                   
REMARK 500    ARG A 138      -78.01    -98.72                                   
REMARK 500    ALA A 171       43.54   -140.67                                   
REMARK 500    ILE A 206      -25.43   -151.76                                   
REMARK 500    LEU A 220     -140.44     51.78                                   
REMARK 500    ARG A 237       49.97    -97.44                                   
REMARK 500    ASN A 298       57.34   -162.97                                   
REMARK 500    GLN A 341      106.24   -160.30                                   
REMARK 500    ASN A 342       77.04     54.22                                   
REMARK 500    TYR B 107       31.37   -145.25                                   
REMARK 500    ARG B 138      -67.98    -99.39                                   
REMARK 500    ALA B 171       47.97   -146.07                                   
REMARK 500    ILE B 206      -28.06   -146.75                                   
REMARK 500    LEU B 220     -134.31     53.16                                   
REMARK 500    ARG B 240      113.85     64.22                                   
REMARK 500    ASN B 298       54.93   -166.21                                   
REMARK 500    ASN B 342       75.50     48.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ALA A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ALA B 402                 
DBREF  4Y2W A    1   388  UNP    Q8RAK6   ALR1_CALS4       1    388             
DBREF  4Y2W B    1   388  UNP    Q8RAK6   ALR1_CALS4       1    388             
SEQADV 4Y2W VAL A    1  UNP  Q8RAK6    MET     1 ENGINEERED MUTATION            
SEQADV 4Y2W VAL B    1  UNP  Q8RAK6    MET     1 ENGINEERED MUTATION            
SEQRES   1 A  388  VAL LYS PHE ASP GLY VAL ARG PRO THR ARG VAL GLU VAL          
SEQRES   2 A  388  TYR LEU ASP ALA ILE THR HIS ASN PHE ARG GLU ILE LYS          
SEQRES   3 A  388  LYS ILE VAL GLY LYS ASN VAL LYS ILE MET ALA VAL ILE          
SEQRES   4 A  388  LYS GLY ASP ALA TYR GLY HIS GLY ALA SER TYR VAL ALA          
SEQRES   5 A  388  LYS PHE LEU GLU LYS GLU GLY VAL ASP TYR PHE GLY VAL          
SEQRES   6 A  388  ALA THR THR GLU GLU ALA LEU GLU LEU ARG GLU LYS GLY          
SEQRES   7 A  388  ILE LYS THR PRO ILE LEU ILE PHE GLY TYR THR PRO PRO          
SEQRES   8 A  388  THR GLN LEU ARG GLN ILE VAL LYS HIS ASP LEU THR GLN          
SEQRES   9 A  388  THR VAL TYR ASP ILE LYS TYR ALA LYS GLU LEU GLU LYS          
SEQRES  10 A  388  GLU SER LEU LYS GLN ASN LYS ARG ALA LYS VAL HIS ILE          
SEQRES  11 A  388  LYS ILE ASP THR GLY LEU GLY ARG ILE GLY TYR ILE ASP          
SEQRES  12 A  388  PHE ASP LEU ALA GLN LYS GLU ILE LEU GLU MET ALA ASN          
SEQRES  13 A  388  MET ARG GLY LEU ILE LEU GLU GLY ILE TYR SER HIS PHE          
SEQRES  14 A  388  ALA ALA ALA SER GLU ASP ASP ARG ASP TYR CYS LYS GLU          
SEQRES  15 A  388  GLN PHE ASP LYS PHE MET ASN LEU ILE SER SER LEU GLU          
SEQRES  16 A  388  LYS LYS ARG LEU LYS ILE PRO LEU LYS HIS ILE ALA ASN          
SEQRES  17 A  388  ALA ALA ALA ILE LEU ASN LEU ASN TYR SER HIS LEU ASP          
SEQRES  18 A  388  MET VAL ARG PRO GLY ILE ILE LEU PHE GLY ALA TYR PRO          
SEQRES  19 A  388  SER LYS ARG VAL GLU ARG LYS VAL GLU LEU ARG GLU THR          
SEQRES  20 A  388  LEU ARG PHE THR THR ARG VAL VAL HIS LEU LYS ASP VAL          
SEQRES  21 A  388  PRO ALA GLY PHE PHE ILE GLY TYR GLY LYS SER PHE VAL          
SEQRES  22 A  388  THR LYS ARG LYS SER VAL ILE ALA THR ILE PRO VAL GLY          
SEQRES  23 A  388  TYR ALA ASP GLY LEU ASP ARG ARG LEU SER ASN ASN TYR          
SEQRES  24 A  388  LYS LEU LEU LEU LYS GLY LYS TYR VAL PRO ILE VAL GLY          
SEQRES  25 A  388  ARG VAL CYS MET ASP GLN CYS MET ILE ASP VAL THR ASP          
SEQRES  26 A  388  VAL GLU GLY VAL GLU ILE GLY ASP GLU VAL VAL ILE ILE          
SEQRES  27 A  388  GLY THR GLN ASN ASN GLU THR VAL SER VAL GLU SER MET          
SEQRES  28 A  388  ALA ASP LYS ILE GLU THR ILE PRO GLN GLU VAL PHE SER          
SEQRES  29 A  388  ARG ILE SER ARG ARG VAL PRO ARG VAL TYR PHE TYR ASP          
SEQRES  30 A  388  GLY ILE LYS ILE GLY GLU VAL ASN TYR LEU LYS                  
SEQRES   1 B  388  VAL LYS PHE ASP GLY VAL ARG PRO THR ARG VAL GLU VAL          
SEQRES   2 B  388  TYR LEU ASP ALA ILE THR HIS ASN PHE ARG GLU ILE LYS          
SEQRES   3 B  388  LYS ILE VAL GLY LYS ASN VAL LYS ILE MET ALA VAL ILE          
SEQRES   4 B  388  LYS GLY ASP ALA TYR GLY HIS GLY ALA SER TYR VAL ALA          
SEQRES   5 B  388  LYS PHE LEU GLU LYS GLU GLY VAL ASP TYR PHE GLY VAL          
SEQRES   6 B  388  ALA THR THR GLU GLU ALA LEU GLU LEU ARG GLU LYS GLY          
SEQRES   7 B  388  ILE LYS THR PRO ILE LEU ILE PHE GLY TYR THR PRO PRO          
SEQRES   8 B  388  THR GLN LEU ARG GLN ILE VAL LYS HIS ASP LEU THR GLN          
SEQRES   9 B  388  THR VAL TYR ASP ILE LYS TYR ALA LYS GLU LEU GLU LYS          
SEQRES  10 B  388  GLU SER LEU LYS GLN ASN LYS ARG ALA LYS VAL HIS ILE          
SEQRES  11 B  388  LYS ILE ASP THR GLY LEU GLY ARG ILE GLY TYR ILE ASP          
SEQRES  12 B  388  PHE ASP LEU ALA GLN LYS GLU ILE LEU GLU MET ALA ASN          
SEQRES  13 B  388  MET ARG GLY LEU ILE LEU GLU GLY ILE TYR SER HIS PHE          
SEQRES  14 B  388  ALA ALA ALA SER GLU ASP ASP ARG ASP TYR CYS LYS GLU          
SEQRES  15 B  388  GLN PHE ASP LYS PHE MET ASN LEU ILE SER SER LEU GLU          
SEQRES  16 B  388  LYS LYS ARG LEU LYS ILE PRO LEU LYS HIS ILE ALA ASN          
SEQRES  17 B  388  ALA ALA ALA ILE LEU ASN LEU ASN TYR SER HIS LEU ASP          
SEQRES  18 B  388  MET VAL ARG PRO GLY ILE ILE LEU PHE GLY ALA TYR PRO          
SEQRES  19 B  388  SER LYS ARG VAL GLU ARG LYS VAL GLU LEU ARG GLU THR          
SEQRES  20 B  388  LEU ARG PHE THR THR ARG VAL VAL HIS LEU LYS ASP VAL          
SEQRES  21 B  388  PRO ALA GLY PHE PHE ILE GLY TYR GLY LYS SER PHE VAL          
SEQRES  22 B  388  THR LYS ARG LYS SER VAL ILE ALA THR ILE PRO VAL GLY          
SEQRES  23 B  388  TYR ALA ASP GLY LEU ASP ARG ARG LEU SER ASN ASN TYR          
SEQRES  24 B  388  LYS LEU LEU LEU LYS GLY LYS TYR VAL PRO ILE VAL GLY          
SEQRES  25 B  388  ARG VAL CYS MET ASP GLN CYS MET ILE ASP VAL THR ASP          
SEQRES  26 B  388  VAL GLU GLY VAL GLU ILE GLY ASP GLU VAL VAL ILE ILE          
SEQRES  27 B  388  GLY THR GLN ASN ASN GLU THR VAL SER VAL GLU SER MET          
SEQRES  28 B  388  ALA ASP LYS ILE GLU THR ILE PRO GLN GLU VAL PHE SER          
SEQRES  29 B  388  ARG ILE SER ARG ARG VAL PRO ARG VAL TYR PHE TYR ASP          
SEQRES  30 B  388  GLY ILE LYS ILE GLY GLU VAL ASN TYR LEU LYS                  
HET    PO4  A 401       5                                                       
HET    ALA  A 402       6                                                       
HET    PO4  B 401       5                                                       
HET    ALA  B 402       6                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ALA ALANINE                                                          
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   4  ALA    2(C3 H7 N O2)                                                
HELIX    1 AA1 LEU A   15  VAL A   29  1                                  15    
HELIX    2 AA2 ILE A   39  HIS A   46  1                                   8    
HELIX    3 AA3 GLY A   47  GLY A   59  1                                  13    
HELIX    4 AA4 THR A   67  LYS A   77  1                                  11    
HELIX    5 AA5 PRO A   90  THR A   92  5                                   3    
HELIX    6 AA6 GLN A   93  HIS A  100  1                                   8    
HELIX    7 AA7 ASP A  108  GLN A  122  1                                  15    
HELIX    8 AA8 ASP A  143  ASN A  156  1                                  14    
HELIX    9 AA9 ASP A  176  LYS A  196  1                                  21    
HELIX   10 AB1 ALA A  209  LEU A  215  1                                   7    
HELIX   11 AB2 ASN A  216  LEU A  220  5                                   5    
HELIX   12 AB3 GLY A  226  GLY A  231  5                                   6    
HELIX   13 AB4 GLY A  267  SER A  271  5                                   5    
HELIX   14 AB5 GLY A  286  GLY A  290  5                                   5    
HELIX   15 AB6 ASP A  292  SER A  296  5                                   5    
HELIX   16 AB7 SER A  347  ILE A  355  1                                   9    
HELIX   17 AB8 ILE A  358  ILE A  366  1                                   9    
HELIX   18 AB9 LEU B   15  VAL B   29  1                                  15    
HELIX   19 AC1 ILE B   39  HIS B   46  1                                   8    
HELIX   20 AC2 GLY B   47  GLY B   59  1                                  13    
HELIX   21 AC3 THR B   67  LYS B   77  1                                  11    
HELIX   22 AC4 PRO B   90  THR B   92  5                                   3    
HELIX   23 AC5 GLN B   93  HIS B  100  1                                   8    
HELIX   24 AC6 ASP B  108  GLN B  122  1                                  15    
HELIX   25 AC7 ASP B  143  ASN B  156  1                                  14    
HELIX   26 AC8 ASP B  176  LYS B  197  1                                  22    
HELIX   27 AC9 ASN B  208  LEU B  215  1                                   8    
HELIX   28 AD1 ASN B  216  HIS B  219  5                                   4    
HELIX   29 AD2 GLY B  226  GLY B  231  5                                   6    
HELIX   30 AD3 GLY B  267  SER B  271  5                                   5    
HELIX   31 AD4 GLY B  286  GLY B  290  5                                   5    
HELIX   32 AD5 ASP B  292  SER B  296  5                                   5    
HELIX   33 AD6 SER B  347  ILE B  355  1                                   9    
HELIX   34 AD7 ILE B  358  ILE B  366  1                                   9    
SHEET    1 AA1 6 THR A 345  VAL A 346  0                                        
SHEET    2 AA1 6 GLU A 334  THR A 340 -1  N  GLY A 339   O  VAL A 346           
SHEET    3 AA1 6 LEU A 248  ARG A 253 -1  N  THR A 252   O  VAL A 335           
SHEET    4 AA1 6 ARG A  10  TYR A  14 -1  N  ARG A  10   O  THR A 251           
SHEET    5 AA1 6 ARG A 372  TYR A 376  1  O  VAL A 373   N  VAL A  13           
SHEET    6 AA1 6 ILE A 379  VAL A 384 -1  O  VAL A 384   N  ARG A 372           
SHEET    1 AA2 9 LYS A  34  VAL A  38  0                                        
SHEET    2 AA2 9 TYR A  62  VAL A  65  1  O  GLY A  64   N  ALA A  37           
SHEET    3 AA2 9 ILE A  83  ILE A  85  1  O  LEU A  84   N  PHE A  63           
SHEET    4 AA2 9 THR A 103  VAL A 106  1  O  THR A 103   N  ILE A  83           
SHEET    5 AA2 9 ALA A 126  LYS A 131  1  O  HIS A 129   N  GLN A 104           
SHEET    6 AA2 9 LEU A 160  TYR A 166  1  O  TYR A 166   N  ILE A 130           
SHEET    7 AA2 9 LEU A 203  ASN A 208  1  O  LEU A 203   N  ILE A 165           
SHEET    8 AA2 9 MET A 222  ARG A 224  1  O  ARG A 224   N  ALA A 207           
SHEET    9 AA2 9 LYS A  34  VAL A  38  1  N  MET A  36   O  VAL A 223           
SHEET    1 AA3 5 HIS A 256  VAL A 260  0                                        
SHEET    2 AA3 5 SER A 278  ILE A 283 -1  O  ILE A 280   N  LYS A 258           
SHEET    3 AA3 5 CYS A 319  ASP A 322 -1  O  CYS A 319   N  ILE A 283           
SHEET    4 AA3 5 LYS A 306  VAL A 311 -1  N  VAL A 311   O  MET A 320           
SHEET    5 AA3 5 LYS A 300  LEU A 303 -1  N  LEU A 301   O  VAL A 308           
SHEET    1 AA4 2 PHE A 265  ILE A 266  0                                        
SHEET    2 AA4 2 PHE A 272  VAL A 273 -1  O  PHE A 272   N  ILE A 266           
SHEET    1 AA5 7 HIS B 256  VAL B 260  0                                        
SHEET    2 AA5 7 SER B 278  ILE B 283 -1  O  SER B 278   N  VAL B 260           
SHEET    3 AA5 7 CYS B 319  ASP B 322 -1  O  ILE B 321   N  ALA B 281           
SHEET    4 AA5 7 LYS B 306  VAL B 311 -1  N  VAL B 311   O  MET B 320           
SHEET    5 AA5 7 LYS B 300  LEU B 303 -1  N  LEU B 301   O  VAL B 308           
SHEET    6 AA5 7 GLU B 334  THR B 340 -1  O  VAL B 336   N  LEU B 302           
SHEET    7 AA5 7 THR B 345  VAL B 346 -1  O  VAL B 346   N  GLY B 339           
SHEET    1 AA610 HIS B 256  VAL B 260  0                                        
SHEET    2 AA610 SER B 278  ILE B 283 -1  O  SER B 278   N  VAL B 260           
SHEET    3 AA610 CYS B 319  ASP B 322 -1  O  ILE B 321   N  ALA B 281           
SHEET    4 AA610 LYS B 306  VAL B 311 -1  N  VAL B 311   O  MET B 320           
SHEET    5 AA610 LYS B 300  LEU B 303 -1  N  LEU B 301   O  VAL B 308           
SHEET    6 AA610 GLU B 334  THR B 340 -1  O  VAL B 336   N  LEU B 302           
SHEET    7 AA610 LEU B 248  ARG B 253 -1  N  PHE B 250   O  ILE B 337           
SHEET    8 AA610 ARG B  10  TYR B  14 -1  N  GLU B  12   O  ARG B 249           
SHEET    9 AA610 ARG B 372  TYR B 376  1  O  VAL B 373   N  VAL B  13           
SHEET   10 AA610 ILE B 379  VAL B 384 -1  O  VAL B 384   N  ARG B 372           
SHEET    1 AA7 9 LYS B  34  VAL B  38  0                                        
SHEET    2 AA7 9 TYR B  62  VAL B  65  1  O  TYR B  62   N  ALA B  37           
SHEET    3 AA7 9 ILE B  83  ILE B  85  1  O  LEU B  84   N  PHE B  63           
SHEET    4 AA7 9 THR B 103  VAL B 106  1  O  THR B 103   N  ILE B  83           
SHEET    5 AA7 9 ALA B 126  LYS B 131  1  O  HIS B 129   N  VAL B 106           
SHEET    6 AA7 9 LEU B 160  TYR B 166  1  O  TYR B 166   N  ILE B 130           
SHEET    7 AA7 9 LEU B 203  HIS B 205  1  O  LEU B 203   N  ILE B 165           
SHEET    8 AA7 9 MET B 222  VAL B 223  1  N  MET B 222   O  LYS B 204           
SHEET    9 AA7 9 LYS B  34  VAL B  38  1  N  MET B  36   O  VAL B 223           
SHEET    1 AA8 2 PHE B 265  ILE B 266  0                                        
SHEET    2 AA8 2 PHE B 272  VAL B 273 -1  O  PHE B 272   N  ILE B 266           
SITE     1 AC1  7 TYR A  44  ASN A 208  ALA A 209  ARG A 224                    
SITE     2 AC1  7 GLY A 226  ILE A 227  ALA B 402                               
SITE     1 AC2  6 TYR A 268  TYR A 287  CYS A 315  MET A 316                    
SITE     2 AC2  6 ARG B 138  PO4 B 401                                          
SITE     1 AC3  7 ALA A 402  TYR B  44  ASN B 208  ALA B 209                    
SITE     2 AC3  7 ARG B 224  GLY B 226  ILE B 227                               
SITE     1 AC4  5 GLN A 360  PO4 A 401  TYR B 268  TYR B 287                    
SITE     2 AC4  5 MET B 316                                                     
CRYST1   60.843   73.077  218.746  90.00  90.00  90.00 P 21 21 21    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      0.016436  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013684  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004572        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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