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LongText Report for: 3UMJ-pdb

Name Class
3UMJ-pdb
HEADER    HYDROLASE                               13-NOV-11   3UMJ              
TITLE     CRYSTAL STRUCTURE OF D311E LIPASE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THERMOSTABLE LIPASE;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 30-416;                                       
COMPND   5 EC: 3.1.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS ZALIHAE;                            
SOURCE   3 ORGANISM_TAXID: 213419;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX/T1S                                  
KEYWDS    THERMOSTABLE D311E LIPASE, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.RUSLAN,R.N.Z.R.A.RAHMAN,T.C.LEOW,M.S.M.ALI,M.BASRI,A.B.SALLEH       
REVDAT   1   22-FEB-12 3UMJ    0                                                
JRNL        AUTH   R.RUSLAN,R.N.Z.R.A.RAHMAN,T.C.LEOW,M.S.M.ALI,M.BASRI,        
JRNL        AUTH 2 A.B.SALLEH                                                   
JRNL        TITL   IMPROVEMENT OF THERMAL STABILITY VIA OUTER-LOOP ION PAIR     
JRNL        TITL 2 INTERACTION OF MUTATED T1 LIPASE FROM GEOBACILLUS ZALIHAE    
JRNL        TITL 3 STRAIN T1                                                    
JRNL        REF    INT J MOL SCI                 V.  13   943 2012              
JRNL        REFN                   ESSN 1422-0067                               
JRNL        PMID   22312296                                                     
JRNL        DOI    10.3390/IJMS13010943                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 50139                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2677                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3443                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 185                          
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6102                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 622                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.01000                                             
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): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.109         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.106         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6285 ; 0.022 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8543 ; 1.786 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   771 ; 6.430 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   314 ;33.822 ;23.121       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   951 ;14.681 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;19.483 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   893 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4956 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3825 ; 1.064 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6124 ; 1.817 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2460 ; 3.108 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2419 ; 4.822 ; 4.500       
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   : 1.40                                          
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 3UMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-NOV-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068940.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.540                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER PLATINUM 135                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SADABS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88705                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.570                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.900                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 2.930                              
REMARK 200  R MERGE                    (I) : 0.08330                            
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.15                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19460                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.010                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: XPREP                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 2DSN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.1M SODIUM PHOSPHATE, 0.1M    
REMARK 280  POTASSIUM PHOSPHATE, 1.5M NACL, PH 5.5, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 293.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
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        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       58.66150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.58100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.66150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.58100            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 B 389  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 620  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     SER A     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   415     O    HOH A   559              1.69            
REMARK 500   O    GLY A    32     O1   GOL A  1001              1.86            
REMARK 500   O    HOH A   414     O    HOH A   502              1.93            
REMARK 500   OE1  GLN A   387     O    HOH A   683              1.95            
REMARK 500   NH1  ARG B    47     O    HOH B   658              1.96            
REMARK 500   O    GLY A    32     C1   GOL A  1001              1.96            
REMARK 500   O    HOH A   406     O    HOH A   407              1.99            
REMARK 500   O    HOH A   612     O    HOH B   666              2.00            
REMARK 500   O    HOH A   612     O    HOH A   705              2.07            
REMARK 500   O    HOH B   432     O    HOH B   627              2.08            
REMARK 500   N    HIS A   153     O    HOH A   609              2.08            
REMARK 500   O    GLY A    35     O1   GOL A  1001              2.08            
REMARK 500   O    THR A   272     O    HOH A   542              2.09            
REMARK 500   OD1  ASP B   182     O    HOH B   526              2.12            
REMARK 500   O    HOH A   404     O    HOH A   584              2.13            
REMARK 500   O    HOH A   402     O    HOH A   598              2.14            
REMARK 500   O    HOH A   479     O    HOH A   537              2.15            
REMARK 500   O    HOH A   542     O    HOH A   591              2.15            
REMARK 500   O    HIS A   153     O    HOH A   708              2.17            
REMARK 500   O    HOH A   708     O    HOH A   710              2.18            
REMARK 500   O    HOH B   431     O    HOH B   503              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   391     O    HOH A   706     4446     1.17            
REMARK 500   O    HOH A   392     O    HOH A   609     4446     1.28            
REMARK 500   O3   GOL A  1001     O    HOH A   686     4446     1.39            
REMARK 500   O    HOH A   389     O    HOH A   559     4456     1.43            
REMARK 500   O    HOH A   390     O    HOH A   707     4446     1.66            
REMARK 500   C3   GOL A  1001     O    HOH A   686     4446     1.97            
REMARK 500   O1   GOL A  1001     C1   GOL A  1002     4446     2.02            
REMARK 500   O    HOH A   665     O    HOH B   664     4456     2.06            
REMARK 500   O    HOH A   396     O    HOH A   605     4446     2.12            
REMARK 500   O    HOH A   393     O    HOH A   710     4446     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU A 307   CA  -  CB  -  CG  ANGL. DEV. =  19.1 DEGREES          
REMARK 500    LEU B 285   CB  -  CG  -  CD2 ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ASP B 317   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 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    SER A 113     -135.96     61.18                                   
REMARK 500    VAL A 203      -56.59     67.67                                   
REMARK 500    ARG A 271       41.07   -149.21                                   
REMARK 500    LEU A 277      -75.98    -89.25                                   
REMARK 500    ASN A 304       83.43   -155.51                                   
REMARK 500    ASP A 310     -152.48   -114.09                                   
REMARK 500    ILE A 319      -37.36   -138.65                                   
REMARK 500    LYS A 329      -48.46   -133.07                                   
REMARK 500    ASN A 367       91.97   -164.36                                   
REMARK 500    SER B 113     -136.17     66.28                                   
REMARK 500    VAL B 203      -60.36     70.17                                   
REMARK 500    LEU B 208       39.05    -98.85                                   
REMARK 500    ARG B 271       38.61   -142.00                                   
REMARK 500    LEU B 277      -62.85    -98.48                                   
REMARK 500    ASP B 310     -155.93   -130.85                                   
REMARK 500    ILE B 319      -47.24   -142.53                                   
REMARK 500    LYS B 329      -52.48   -126.62                                   
REMARK 500    ASN B 367       91.82   -163.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 154        24.5      L          L   OUTSIDE RANGE           
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 470        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A 529        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH A 533        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A 600        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A 655        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A 675        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B 678        DISTANCE =  6.96 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 238   OD2                                                    
REMARK 620 2 ASP B  61   OD1 126.9                                              
REMARK 620 3 HIS B  81   NE2 113.3  99.0                                        
REMARK 620 4 HIS B  87   NE2  99.7 115.3 100.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 238   OD2                                                    
REMARK 620 2 HIS A  81   NE2 106.1                                              
REMARK 620 3 ASP A  61   OD1 129.7  95.1                                        
REMARK 620 4 HIS A  87   NE2  98.8 108.0 117.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 902  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 286   O                                                      
REMARK 620 2 GLU A 360   OE2  84.6                                              
REMARK 620 3 PRO A 366   O   173.6  95.2                                        
REMARK 620 4 ASP A 365   OD2  99.0 106.8  87.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 902  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 286   O                                                      
REMARK 620 2 GLU B 360   OE2  85.9                                              
REMARK 620 3 ASP B 365   OD2 105.2 106.2                                        
REMARK 620 4 PRO B 366   O   167.8  94.3  86.5                                  
REMARK 620 5 HOH B 516   O    87.6  86.3 162.5  80.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 904  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B 113   OG                                                     
REMARK 620 2 HOH B 550   O   112.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 904                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 903                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 904                  
DBREF  3UMJ A    2   388  UNP    Q842J9   Q842J9_9BACI    30    416             
DBREF  3UMJ B    2   388  UNP    Q842J9   Q842J9_9BACI    30    416             
SEQADV 3UMJ GLU A  311  UNP  Q842J9    ASP   339 ENGINEERED MUTATION            
SEQADV 3UMJ GLU B  311  UNP  Q842J9    ASP   339 ENGINEERED MUTATION            
SEQRES   1 A  387  SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS          
SEQRES   2 A  387  GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE          
SEQRES   3 A  387  LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP          
SEQRES   4 A  387  LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL          
SEQRES   5 A  387  GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA          
SEQRES   6 A  387  TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA          
SEQRES   7 A  387  ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG          
SEQRES   8 A  387  THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY          
SEQRES   9 A  387  ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR          
SEQRES  10 A  387  ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN          
SEQRES  11 A  387  GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU          
SEQRES  12 A  387  SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER          
SEQRES  13 A  387  VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU          
SEQRES  14 A  387  VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU          
SEQRES  15 A  387  GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN          
SEQRES  16 A  387  VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP          
SEQRES  17 A  387  GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP          
SEQRES  18 A  387  HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR          
SEQRES  19 A  387  SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY          
SEQRES  20 A  387  ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN          
SEQRES  21 A  387  THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG          
SEQRES  22 A  387  GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET          
SEQRES  23 A  387  ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY          
SEQRES  24 A  387  SER TYR ARG ASN PRO THR LEU GLY ILE ASP GLU ARG TRP          
SEQRES  25 A  387  LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN          
SEQRES  26 A  387  GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR          
SEQRES  27 A  387  ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY          
SEQRES  28 A  387  THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP          
SEQRES  29 A  387  PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG          
SEQRES  30 A  387  LEU ALA GLU GLN LEU ALA SER LEU GLN PRO                      
SEQRES   1 B  387  SER LEU ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS          
SEQRES   2 B  387  GLY PHE THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE          
SEQRES   3 B  387  LYS TYR TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP          
SEQRES   4 B  387  LEU ASN ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL          
SEQRES   5 B  387  GLY PRO LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA          
SEQRES   6 B  387  TYR ALA GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA          
SEQRES   7 B  387  ALA HIS ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG          
SEQRES   8 B  387  THR TYR PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY          
SEQRES   9 B  387  ARG ILE HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR          
SEQRES  10 B  387  ALA ARG MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN          
SEQRES  11 B  387  GLU GLU ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU          
SEQRES  12 B  387  SER PRO LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER          
SEQRES  13 B  387  VAL THR THR ILE ALA THR PRO HIS ASP GLY THR THR LEU          
SEQRES  14 B  387  VAL ASN MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU          
SEQRES  15 B  387  GLN LYS ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN          
SEQRES  16 B  387  VAL PRO TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP          
SEQRES  17 B  387  GLN TRP GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP          
SEQRES  18 B  387  HIS TYR PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR          
SEQRES  19 B  387  SER THR ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY          
SEQRES  20 B  387  ALA GLU LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN          
SEQRES  21 B  387  THR TYR TYR LEU SER PHE SER THR GLU ARG THR TYR ARG          
SEQRES  22 B  387  GLY ALA LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET          
SEQRES  23 B  387  ASN ALA PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY          
SEQRES  24 B  387  SER TYR ARG ASN PRO THR LEU GLY ILE ASP GLU ARG TRP          
SEQRES  25 B  387  LEU GLU ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN          
SEQRES  26 B  387  GLY PRO LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR          
SEQRES  27 B  387  ASP GLY THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY          
SEQRES  28 B  387  THR TYR ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP          
SEQRES  29 B  387  PRO ASN PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG          
SEQRES  30 B  387  LEU ALA GLU GLN LEU ALA SER LEU GLN PRO                      
HET     ZN  A 901       1                                                       
HET    GOL  A1001       6                                                       
HET    GOL  A1002       6                                                       
HET     CL  A 903       1                                                       
HET     NA  A 904       1                                                       
HET     CA  A 902       1                                                       
HET     CA  B 902       1                                                       
HET     ZN  B 901       1                                                       
HET    GOL  B1001       6                                                       
HET     CL  B 903       1                                                       
HET     NA  B 904       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM      CA CALCIUM ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   7   NA    2(NA 1+)                                                     
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL  14  HOH   *622(H2 O)                                                    
HELIX    1   1 GLU A   23  PHE A   27  5                                   5    
HELIX    2   2 GLY A   31  GLY A   35  5                                   5    
HELIX    3   3 ASP A   36  ASN A   44  1                                   9    
HELIX    4   4 SER A   58  GLY A   72  1                                  15    
HELIX    5   5 GLY A   78  GLY A   86  1                                   9    
HELIX    6   6 LEU A   98  ARG A  103  5                                   6    
HELIX    7   7 GLN A  114  GLY A  129  1                                  16    
HELIX    8   8 SER A  130  ASN A  141  1                                  12    
HELIX    9   9 SER A  145  GLU A  149  5                                   5    
HELIX   10  10 THR A  168  MET A  173  5                                   6    
HELIX   11  11 ASP A  175  ALA A  191  1                                  17    
HELIX   12  12 SER A  220  ARG A  230  1                                  11    
HELIX   13  13 SER A  231  SER A  236  1                                   6    
HELIX   14  14 THR A  239  SER A  245  1                                   7    
HELIX   15  15 SER A  245  VAL A  256  1                                  12    
HELIX   16  16 ASN A  288  CYS A  295  1                                   8    
HELIX   17  17 CYS A  295  GLY A  300  1                                   6    
HELIX   18  18 ASN A  304  GLY A  308  5                                   5    
HELIX   19  19 ASP A  310  LEU A  314  5                                   5    
HELIX   20  20 ASN A  321  ASN A  326  5                                   6    
HELIX   21  21 LEU A  359  GLY A  363  5                                   5    
HELIX   22  22 ASP A  371  SER A  385  1                                  15    
HELIX   23  23 GLU B   23  PHE B   27  5                                   5    
HELIX   24  24 GLY B   31  GLY B   35  5                                   5    
HELIX   25  25 ASP B   36  ASN B   44  1                                   9    
HELIX   26  26 SER B   58  GLY B   72  1                                  15    
HELIX   27  27 GLY B   78  GLY B   86  1                                   9    
HELIX   28  28 LEU B   98  ARG B  103  5                                   6    
HELIX   29  29 GLN B  114  GLY B  129  1                                  16    
HELIX   30  30 SER B  130  ASN B  141  1                                  12    
HELIX   31  31 SER B  145  GLU B  149  5                                   5    
HELIX   32  32 THR B  168  MET B  173  5                                   6    
HELIX   33  33 ASP B  175  ALA B  191  1                                  17    
HELIX   34  34 LEU B  208  GLY B  212  5                                   5    
HELIX   35  35 SER B  220  ARG B  230  1                                  11    
HELIX   36  36 SER B  231  SER B  236  1                                   6    
HELIX   37  37 THR B  239  SER B  245  1                                   7    
HELIX   38  38 SER B  245  VAL B  256  1                                  12    
HELIX   39  39 ASN B  288  CYS B  295  1                                   8    
HELIX   40  40 CYS B  295  GLY B  300  1                                   6    
HELIX   41  41 ASN B  304  GLY B  308  5                                   5    
HELIX   42  42 ASP B  310  LEU B  314  5                                   5    
HELIX   43  43 ASN B  321  MET B  325  5                                   5    
HELIX   44  44 ASP B  371  SER B  385  1                                  15    
SHEET    1   A 7 THR A  48  THR A  50  0                                        
SHEET    2   A 7 ILE A  10  LEU A  13  1  N  LEU A  12   O  TYR A  49           
SHEET    3   A 7 ILE A 107  HIS A 112  1  O  HIS A 108   N  VAL A  11           
SHEET    4   A 7 VAL A 155  ILE A 161  1  O  SER A 157   N  ILE A 109           
SHEET    5   A 7 TYR A 263  THR A 269  1  O  LEU A 265   N  THR A 160           
SHEET    6   A 7 TRP A 348  TYR A 354  1  O  MET A 351   N  SER A 266           
SHEET    7   A 7 ILE A 336  PRO A 338  1  N  VAL A 337   O  TRP A 348           
SHEET    1   B 2 GLY A  73  ASP A  76  0                                        
SHEET    2   B 2 PHE A  90  TYR A  94 -1  O  TYR A  94   N  GLY A  73           
SHEET    1   C 2 THR A 272  ARG A 274  0                                        
SHEET    2   C 2 HIS A 281  PRO A 283 -1  O  TYR A 282   N  TYR A 273           
SHEET    1   D 7 THR B  48  THR B  50  0                                        
SHEET    2   D 7 ILE B  10  LEU B  13  1  N  LEU B  12   O  TYR B  49           
SHEET    3   D 7 ILE B 107  HIS B 112  1  O  HIS B 108   N  VAL B  11           
SHEET    4   D 7 VAL B 155  ILE B 161  1  O  THR B 159   N  ILE B 109           
SHEET    5   D 7 TYR B 263  THR B 269  1  O  LEU B 265   N  THR B 160           
SHEET    6   D 7 TRP B 348  TYR B 354  1  O  TYR B 354   N  SER B 268           
SHEET    7   D 7 ILE B 336  PRO B 338  1  N  VAL B 337   O  TRP B 348           
SHEET    1   E 2 GLY B  73  ASP B  76  0                                        
SHEET    2   E 2 PHE B  90  TYR B  94 -1  O  ARG B  92   N  VAL B  75           
SHEET    1   F 2 THR B 272  ARG B 274  0                                        
SHEET    2   F 2 HIS B 281  PRO B 283 -1  O  TYR B 282   N  TYR B 273           
LINK         OD2 ASP B 238                ZN    ZN B 901     1555   1555  2.04  
LINK         OD1 ASP B  61                ZN    ZN B 901     1555   1555  2.05  
LINK         NE2 HIS B  81                ZN    ZN B 901     1555   1555  2.07  
LINK         OD2 ASP A 238                ZN    ZN A 901     1555   1555  2.08  
LINK         NE2 HIS A  81                ZN    ZN A 901     1555   1555  2.12  
LINK         OD1 ASP A  61                ZN    ZN A 901     1555   1555  2.13  
LINK         NE2 HIS B  87                ZN    ZN B 901     1555   1555  2.24  
LINK         O   GLY A 286                CA    CA A 902     1555   1555  2.25  
LINK         OE2 GLU A 360                CA    CA A 902     1555   1555  2.27  
LINK         NE2 HIS A  87                ZN    ZN A 901     1555   1555  2.28  
LINK         O   GLY B 286                CA    CA B 902     1555   1555  2.29  
LINK         OE2 GLU B 360                CA    CA B 902     1555   1555  2.34  
LINK         OD2 ASP B 365                CA    CA B 902     1555   1555  2.37  
LINK         O   PRO B 366                CA    CA B 902     1555   1555  2.37  
LINK         OG  SER B 113                NA    NA B 904     1555   1555  2.40  
LINK         O   PRO A 366                CA    CA A 902     1555   1555  2.42  
LINK         OD2 ASP A 365                CA    CA A 902     1555   1555  2.58  
LINK         OH  TYR A  29                NA    NA A 904     1555   1555  2.85  
LINK        NA    NA B 904                 O   HOH B 550     1555   1555  2.19  
LINK        CA    CA B 902                 O   HOH B 516     1555   1555  2.98  
SITE     1 AC1  4 ASP A  61  HIS A  81  HIS A  87  ASP A 238                    
SITE     1 AC2  9 GLY A  31  GLY A  32  VAL A  33  ARG A  34                    
SITE     2 AC2  9 GLY A  35  GLU A 149  HIS A 152  HOH A 686                    
SITE     3 AC2  9 GOL A1002                                                     
SITE     1 AC3  9 GLY A  26  PHE A  27  LYS A  28  GLY A  32                    
SITE     2 AC3  9 GLY A  35  ASP A  36  GLY A 150  HIS A 152                    
SITE     3 AC3  9 GOL A1001                                                     
SITE     1 AC4  3 ARG A 214  GLN A 216  ARG A 227                               
SITE     1 AC5  4 GLY A  15  PHE A  16  THR A  17  TYR A  29                    
SITE     1 AC6  4 GLY A 286  GLU A 360  ASP A 365  PRO A 366                    
SITE     1 AC7  5 GLY B 286  GLU B 360  ASP B 365  PRO B 366                    
SITE     2 AC7  5 HOH B 516                                                     
SITE     1 AC8  4 ASP B  61  HIS B  81  HIS B  87  ASP B 238                    
SITE     1 AC9  7 TRP B  60  HIS B  81  HIS B  85  HOH B 430                    
SITE     2 AC9  7 HOH B 505  HOH B 532  HOH B 687                               
SITE     1 BC1  4 LEU B 213  ARG B 214  GLN B 216  ARG B 227                    
SITE     1 BC2  4 PHE B  16  SER B 113  HIS B 358  HOH B 550                    
CRYST1  117.323   81.162  100.140  90.00  96.49  90.00 C 1 2 1       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      0.008523  0.000000  0.000969        0.00000                         
SCALE2      0.000000  0.012321  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010050        0.00000                         
TER    3049      PRO A 388                                                      
TER    6104      PRO B 388                                                      
MASTER      502    0   11   44   22    0   17    6 6750    2   45   60          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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