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LongText Report for: 5w8o-pdb

Name Class
5w8o-pdb
HEADER    TRANSFERASE                             22-JUN-17   5W8O              
TITLE     HOMOSERINE TRANSACETYLASE META FROM MYCOBACTERIUM HASSIACUM           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 13-372;                                       
COMPND   5 SYNONYM: HOMOSERINE O-TRANS-ACETYLASE,HOMOSERINE TRANSACETYLASE;     
COMPND   6 EC: 2.3.1.31;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM HASSIACUM (STRAIN DSM 44199 / CIP 
SOURCE   3 105218 / JCM 12690 / 3849);                                          
SOURCE   4 ORGANISM_TAXID: 1122247;                                             
SOURCE   5 STRAIN: DSM 44199 / CIP 105218 / JCM 12690 / 3849;                   
SOURCE   6 GENE: METX, C731_1248;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);                             
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PCDF-NT                                   
KEYWDS    HOMOSERINE O-ACETYLTRANSFERASE, HOMOSERINE O-TRANS-ACETYLASE, HTA,    
KEYWDS   2 METX, METHIONINE BIOSYNTHESIS, RV3341, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.W.REED,E.S.RODRIGUEZ,J.LI,K.V.KOROTKOV                              
REVDAT   2   27-SEP-17 5W8O    1       REMARK                                   
REVDAT   1   12-JUL-17 5W8O    0                                                
JRNL        AUTH   E.S.RODRIGUEZ,R.W.REED,J.LI,K.V.KOROTKOV                     
JRNL        TITL   STRUCTURES OF HOMOSERINE TRANSACETYLASE META FROM            
JRNL        TITL 2 MYCOBACTERIA                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2722                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.110                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 118621                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5840                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.6086 -  4.5664    0.96     7325   363  0.1699 0.1750        
REMARK   3     2  4.5664 -  3.6249    0.97     7302   349  0.1320 0.1359        
REMARK   3     3  3.6249 -  3.1668    0.92     7012   326  0.1444 0.1577        
REMARK   3     4  3.1668 -  2.8773    0.97     7384   360  0.1341 0.1695        
REMARK   3     5  2.8773 -  2.6711    0.97     7366   339  0.1320 0.1831        
REMARK   3     6  2.6711 -  2.5136    0.97     7364   376  0.1304 0.1623        
REMARK   3     7  2.5136 -  2.3877    0.93     6976   417  0.1231 0.1623        
REMARK   3     8  2.3877 -  2.2838    0.96     7201   405  0.1247 0.1677        
REMARK   3     9  2.2838 -  2.1959    0.97     7362   391  0.1225 0.1722        
REMARK   3    10  2.1959 -  2.1201    0.97     7346   378  0.1287 0.1651        
REMARK   3    11  2.1201 -  2.0538    0.97     7283   425  0.1332 0.1802        
REMARK   3    12  2.0538 -  1.9951    0.97     7315   409  0.1345 0.1920        
REMARK   3    13  1.9951 -  1.9426    0.98     7354   433  0.1296 0.1711        
REMARK   3    14  1.9426 -  1.8952    0.92     6965   418  0.1476 0.2046        
REMARK   3    15  1.8952 -  1.8521    0.94     7051   360  0.1530 0.2034        
REMARK   3    16  1.8521 -  1.8127    0.96     7298   414  0.1619 0.2207        
REMARK   3    17  1.8127 -  1.7764    0.97     7266   395  0.1767 0.2145        
REMARK   3    18  1.7764 -  1.7429    0.97     7393   350  0.1840 0.2094        
REMARK   3    19  1.7429 -  1.7118    0.97     7358   337  0.1921 0.2447        
REMARK   3    20  1.7118 -  1.6827    0.97     7481   357  0.1991 0.2236        
REMARK   3    21  1.6827 -  1.6556    0.97     7209   394  0.2048 0.2466        
REMARK   3    22  1.6556 -  1.6301    0.97     7371   371  0.2111 0.2235        
REMARK   3    23  1.6301 -  1.6062    0.93     7025   345  0.2238 0.2661        
REMARK   3    24  1.6062 -  1.5835    0.91     6899   358  0.2430 0.2685        
REMARK   3    25  1.5835 -  1.5621    0.94     7246   326  0.2570 0.2692        
REMARK   3    26  1.5621 -  1.5418    0.96     7122   365  0.2665 0.3076        
REMARK   3    27  1.5418 -  1.5226    0.96     7364   400  0.2882 0.3455        
REMARK   3    28  1.5226 -  1.5042    0.96     7212   386  0.2978 0.3259        
REMARK   3    29  1.5042 -  1.4867    0.97     7265   386  0.3265 0.3360        
REMARK   3    30  1.4867 -  1.4700    0.97     7396   377  0.3382 0.3699        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.050           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           5264                                  
REMARK   3   ANGLE     :  0.765           7173                                  
REMARK   3   CHIRALITY :  0.067            814                                  
REMARK   3   PLANARITY :  0.005            946                                  
REMARK   3   DIHEDRAL  : 14.925           1876                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5W8O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228583.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111) AND SI(220) DOUBLE         
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : RH COATED FLAT BENT M0, TOROIDAL   
REMARK 200                                   FOCUSING POST-MONOCHROMATOR M1     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION NOV 1, 2016            
REMARK 200                                   BUILT=20161205                     
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION NOV 1, 2016         
REMARK 200                                   BUILT=20161205                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118675                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.584                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.776                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.0100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.78                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.01300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.460                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.7.17                                         
REMARK 200 STARTING MODEL: 3I1I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RECTANGULAR PRISM                                            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M CALCIUM ACETATE, 21% PEG3350, 3%   
REMARK 280  1,6-DIAMINOHEXANE, 0.05M CHES PH 9.5, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 294K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.61500            
REMARK 290   SMTRY3   2  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: 4330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLY A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     ASN A    73                                                      
REMARK 465     TYR A    74                                                      
REMARK 465     PRO A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     ASP A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     PRO A   254                                                      
REMARK 465     LEU A   255                                                      
REMARK 465     LEU A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     CYS A   338                                                      
REMARK 465     ARG A   339                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     GLY B    71                                                      
REMARK 465     PRO B    72                                                      
REMARK 465     ASN B    73                                                      
REMARK 465     TYR B    74                                                      
REMARK 465     PRO B    75                                                      
REMARK 465     THR B    76                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     CYS B   338                                                      
REMARK 465     ARG B   339                                                      
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   HG   SER A   291     O    HOH A   502              1.55            
REMARK 500   O    HOH B   508     O    HOH B   750              1.99            
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   616     O    HOH B   515     1554     1.96            
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    ARG A 107       52.14   -119.89                                   
REMARK 500    SER A 157     -130.30     62.69                                   
REMARK 500    ASP A 293       98.35   -170.05                                   
REMARK 500    TYR A 323       76.08   -118.44                                   
REMARK 500    PRO A 336       -8.62    -56.39                                   
REMARK 500    ARG B 107       52.01   -117.65                                   
REMARK 500    SER B 157     -131.10     64.26                                   
REMARK 500    ASP B 293       98.10   -169.23                                   
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 772        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A 773        DISTANCE =  6.44 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                              NA A 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A  22   O                                                      
REMARK 620 2 HOH A 551   O    96.8                                              
REMARK 620 3 HOH B 759   O   135.0 126.6                                        
REMARK 620 4 HOH B 766   O    90.9 133.2  69.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  81   O                                                      
REMARK 620 2 ASP A  81   OD1  77.6                                              
REMARK 620 3 VAL A  84   O    79.6 102.1                                        
REMARK 620 4 HOH A 635   O   141.8  84.4  71.6                                  
REMARK 620 5 HOH A 726   O   142.9  93.4 137.3  70.7                            
REMARK 620 6 HOH A 715   O    96.1 170.3  83.8 104.9  87.2                      
REMARK 620 7 HOH B 518   O    75.3  86.7 150.9 137.4  68.3  84.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B  22   O                                                      
REMARK 620 2 HOH B 759   O    85.4                                              
REMARK 620 3 HOH B 766   O    89.3  74.2                                        
REMARK 620 4 HOH B 525   O    80.7 142.3 139.9                                  
REMARK 620 5 HOH B 771   O    88.2  80.3 154.5  64.4                            
REMARK 620 6 HOH A 721   O   168.8  83.4  87.1 108.7  90.5                      
REMARK 620 7 HOH A 723   O   106.1 144.5  72.5  73.2 132.4  82.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  81   O                                                      
REMARK 620 2 ASP B  81   OD1  81.4                                              
REMARK 620 3 VAL B  84   O    82.6 108.4                                        
REMARK 620 4 HOH B 585   O    63.8 138.7  89.4                                  
REMARK 620 5 HOH B 687   O   142.5  75.1  77.7 146.2                            
REMARK 620 6 HOH B 801   O   148.0 122.3 106.2  85.3  69.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 701   O                                                      
REMARK 620 2 HOH B 522   O    86.8                                              
REMARK 620 3 HOH B 597   O   150.0 112.4                                        
REMARK 620 4 HOH B 750   O    53.5  89.5 101.9                                  
REMARK 620 5 HOH B 508   O    89.6  72.1  75.7  40.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 404  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GOL B 403   O1                                                     
REMARK 620 2 HOH B 576   O    77.0                                              
REMARK 620 3 HOH B 748   O   124.8  66.7                                        
REMARK 620 4 GOL B 403   O2   79.8 112.7  77.9                                  
REMARK 620 5 HOH A 572   O    88.5 148.5 141.5  91.4                            
REMARK 620 6 HOH A 711   O   128.8  83.2  87.3 150.8  84.6                      
REMARK 620 7 HOH B 502   O    57.4  74.6 137.9 134.4  74.0  72.1                
REMARK 620 8 HOH B 743   O   150.9 127.8  65.5  76.2  76.0  74.8 136.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
DBREF  5W8O A   13   372  UNP    K5B926   K5B926_MYCHD    13    372             
DBREF  5W8O B   13   372  UNP    K5B926   K5B926_MYCHD    13    372             
SEQADV 5W8O GLY A   10  UNP  K5B926              EXPRESSION TAG                 
SEQADV 5W8O ALA A   11  UNP  K5B926              EXPRESSION TAG                 
SEQADV 5W8O MET A   12  UNP  K5B926              EXPRESSION TAG                 
SEQADV 5W8O GLY B   10  UNP  K5B926              EXPRESSION TAG                 
SEQADV 5W8O ALA B   11  UNP  K5B926              EXPRESSION TAG                 
SEQADV 5W8O MET B   12  UNP  K5B926              EXPRESSION TAG                 
SEQRES   1 A  363  GLY ALA MET ALA GLU GLY GLU LEU GLY ILE VAL ASP ILE          
SEQRES   2 A  363  GLY ALA LEU THR LEU GLU SER GLY ALA VAL ILE ASP ASN          
SEQRES   3 A  363  VAL GLN ILE ALA VAL GLU ARG TRP GLY GLU LEU SER PRO          
SEQRES   4 A  363  SER ARG ASP ASN VAL VAL VAL VAL LEU HIS ALA LEU THR          
SEQRES   5 A  363  GLY ASP SER HIS VAL ALA GLY PRO ALA GLY PRO ASN TYR          
SEQRES   6 A  363  PRO THR PRO GLY TRP TRP ASP GLY VAL VAL GLY PRO GLY          
SEQRES   7 A  363  ALA ALA ILE ASP THR ARG ARG TRP CYS ALA ILE ALA THR          
SEQRES   8 A  363  ASN VAL LEU GLY GLY CYS ARG GLY SER THR GLY PRO GLY          
SEQRES   9 A  363  SER LEU HIS PRO ASP GLY LYS ALA TRP GLY SER ARG PHE          
SEQRES  10 A  363  PRO ALA VAL THR VAL ARG ASP GLN VAL ARG ALA ASP LEU          
SEQRES  11 A  363  ALA ALA LEU ASN ALA MET GLY ILE HIS GLN VAL ALA ALA          
SEQRES  12 A  363  VAL VAL GLY GLY SER MET GLY GLY ALA ARG ALA LEU GLU          
SEQRES  13 A  363  TRP VAL ILE GLY HIS PRO GLU THR VAL ARG ALA GLY LEU          
SEQRES  14 A  363  ILE LEU ALA VAL GLY ALA ARG ALA THR ALA ASP GLN ILE          
SEQRES  15 A  363  GLY THR GLN SER THR GLN VAL ALA ALA ILE LYS ALA ASP          
SEQRES  16 A  363  PRO ASN TRP GLN ASN GLY ASP TYR TYR GLY THR GLY LEU          
SEQRES  17 A  363  LYS PRO ASP VAL GLY LEU GLN ILE ALA ARG ARG PHE ALA          
SEQRES  18 A  363  HIS LEU THR TYR ARG GLY GLU VAL GLU LEU ASP THR ARG          
SEQRES  19 A  363  PHE GLY ASN ALA PRO GLN ASP ASP GLU ASN PRO LEU LEU          
SEQRES  20 A  363  GLY GLY ARG TYR ALA VAL GLU SER TYR LEU GLU TYR GLN          
SEQRES  21 A  363  GLY ARG LYS LEU VAL ASP ARG PHE ASP ALA GLY THR TYR          
SEQRES  22 A  363  VAL THR LEU THR ASP SER LEU SER SER HIS ASP VAL GLY          
SEQRES  23 A  363  ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU ARG SER CYS          
SEQRES  24 A  363  GLU VAL PRO VAL VAL VAL GLY GLY PHE THR SER ASP ARG          
SEQRES  25 A  363  LEU TYR PRO LEU ARG LEU GLN GLU GLU LEU ALA GLU LEU          
SEQRES  26 A  363  MET PRO GLY CYS ARG GLY LEU ASN VAL VAL GLU SER ILE          
SEQRES  27 A  363  TYR GLY HIS ASP GLY PHE LEU ILE GLU THR GLU ALA VAL          
SEQRES  28 A  363  GLY LYS LEU ILE ARG GLN THR LEU GLU LEU ALA SER              
SEQRES   1 B  363  GLY ALA MET ALA GLU GLY GLU LEU GLY ILE VAL ASP ILE          
SEQRES   2 B  363  GLY ALA LEU THR LEU GLU SER GLY ALA VAL ILE ASP ASN          
SEQRES   3 B  363  VAL GLN ILE ALA VAL GLU ARG TRP GLY GLU LEU SER PRO          
SEQRES   4 B  363  SER ARG ASP ASN VAL VAL VAL VAL LEU HIS ALA LEU THR          
SEQRES   5 B  363  GLY ASP SER HIS VAL ALA GLY PRO ALA GLY PRO ASN TYR          
SEQRES   6 B  363  PRO THR PRO GLY TRP TRP ASP GLY VAL VAL GLY PRO GLY          
SEQRES   7 B  363  ALA ALA ILE ASP THR ARG ARG TRP CYS ALA ILE ALA THR          
SEQRES   8 B  363  ASN VAL LEU GLY GLY CYS ARG GLY SER THR GLY PRO GLY          
SEQRES   9 B  363  SER LEU HIS PRO ASP GLY LYS ALA TRP GLY SER ARG PHE          
SEQRES  10 B  363  PRO ALA VAL THR VAL ARG ASP GLN VAL ARG ALA ASP LEU          
SEQRES  11 B  363  ALA ALA LEU ASN ALA MET GLY ILE HIS GLN VAL ALA ALA          
SEQRES  12 B  363  VAL VAL GLY GLY SER MET GLY GLY ALA ARG ALA LEU GLU          
SEQRES  13 B  363  TRP VAL ILE GLY HIS PRO GLU THR VAL ARG ALA GLY LEU          
SEQRES  14 B  363  ILE LEU ALA VAL GLY ALA ARG ALA THR ALA ASP GLN ILE          
SEQRES  15 B  363  GLY THR GLN SER THR GLN VAL ALA ALA ILE LYS ALA ASP          
SEQRES  16 B  363  PRO ASN TRP GLN ASN GLY ASP TYR TYR GLY THR GLY LEU          
SEQRES  17 B  363  LYS PRO ASP VAL GLY LEU GLN ILE ALA ARG ARG PHE ALA          
SEQRES  18 B  363  HIS LEU THR TYR ARG GLY GLU VAL GLU LEU ASP THR ARG          
SEQRES  19 B  363  PHE GLY ASN ALA PRO GLN ASP ASP GLU ASN PRO LEU LEU          
SEQRES  20 B  363  GLY GLY ARG TYR ALA VAL GLU SER TYR LEU GLU TYR GLN          
SEQRES  21 B  363  GLY ARG LYS LEU VAL ASP ARG PHE ASP ALA GLY THR TYR          
SEQRES  22 B  363  VAL THR LEU THR ASP SER LEU SER SER HIS ASP VAL GLY          
SEQRES  23 B  363  ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU ARG SER CYS          
SEQRES  24 B  363  GLU VAL PRO VAL VAL VAL GLY GLY PHE THR SER ASP ARG          
SEQRES  25 B  363  LEU TYR PRO LEU ARG LEU GLN GLU GLU LEU ALA GLU LEU          
SEQRES  26 B  363  MET PRO GLY CYS ARG GLY LEU ASN VAL VAL GLU SER ILE          
SEQRES  27 B  363  TYR GLY HIS ASP GLY PHE LEU ILE GLU THR GLU ALA VAL          
SEQRES  28 B  363  GLY LYS LEU ILE ARG GLN THR LEU GLU LEU ALA SER              
HET     NA  A 401       1                                                       
HET     CA  A 402       1                                                       
HET     CA  A 403       1                                                       
HET     CA  A 404       1                                                       
HET     NA  B 401       1                                                       
HET     CA  B 402       1                                                       
HET    GOL  B 403      12                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   4   CA    4(CA 2+)                                                     
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *593(H2 O)                                                    
HELIX    1 AA1 TRP A   80  GLY A   82  5                                   3    
HELIX    2 AA2 TRP A  122  PHE A  126  5                                   5    
HELIX    3 AA3 THR A  130  MET A  145  1                                  16    
HELIX    4 AA4 SER A  157  HIS A  170  1                                  14    
HELIX    5 AA5 THR A  187  ALA A  203  1                                  17    
HELIX    6 AA6 TRP A  207  ASP A  211  5                                   5    
HELIX    7 AA7 PRO A  219  ARG A  235  1                                  17    
HELIX    8 AA8 GLY A  236  GLY A  245  1                                  10    
HELIX    9 AA9 TYR A  260  ASP A  275  1                                  16    
HELIX   10 AB1 ASP A  278  SER A  291  1                                  14    
HELIX   11 AB2 GLY A  300  SER A  307  1                                   8    
HELIX   12 AB3 PRO A  324  MET A  335  1                                  12    
HELIX   13 AB4 TYR A  348  HIS A  350  5                                   3    
HELIX   14 AB5 ASP A  351  GLU A  356  1                                   6    
HELIX   15 AB6 GLU A  356  SER A  372  1                                  17    
HELIX   16 AB7 TRP B   80  GLY B   82  5                                   3    
HELIX   17 AB8 TRP B  122  PHE B  126  5                                   5    
HELIX   18 AB9 THR B  130  MET B  145  1                                  16    
HELIX   19 AC1 SER B  157  HIS B  170  1                                  14    
HELIX   20 AC2 THR B  187  ALA B  203  1                                  17    
HELIX   21 AC3 TRP B  207  ASP B  211  5                                   5    
HELIX   22 AC4 PRO B  219  ARG B  235  1                                  17    
HELIX   23 AC5 GLY B  236  GLY B  245  1                                  10    
HELIX   24 AC6 ASN B  253  GLY B  257  5                                   5    
HELIX   25 AC7 TYR B  260  ASP B  275  1                                  16    
HELIX   26 AC8 ASP B  278  SER B  291  1                                  14    
HELIX   27 AC9 GLY B  300  SER B  307  1                                   8    
HELIX   28 AD1 PRO B  324  MET B  335  1                                  12    
HELIX   29 AD2 TYR B  348  HIS B  350  5                                   3    
HELIX   30 AD3 ASP B  351  GLU B  356  1                                   6    
HELIX   31 AD4 GLU B  356  SER B  372  1                                  17    
SHEET    1 AA1 8 GLY A  18  THR A  26  0                                        
SHEET    2 AA1 8 VAL A  32  TRP A  43 -1  O  VAL A  40   N  GLY A  18           
SHEET    3 AA1 8 CYS A  96  THR A 100 -1  O  ALA A  97   N  TRP A  43           
SHEET    4 AA1 8 VAL A  53  LEU A  57  1  N  VAL A  56   O  ILE A  98           
SHEET    5 AA1 8 VAL A 150  GLY A 156  1  O  ALA A 152   N  VAL A  55           
SHEET    6 AA1 8 VAL A 174  LEU A 180  1  O  LEU A 178   N  VAL A 153           
SHEET    7 AA1 8 VAL A 312  PHE A 317  1  O  VAL A 313   N  ILE A 179           
SHEET    8 AA1 8 ASN A 342  VAL A 344  1  O  VAL A 344   N  GLY A 316           
SHEET    1 AA2 2 VAL A  84  GLY A  85  0                                        
SHEET    2 AA2 2 ILE A  90  ASP A  91  1  O  ILE A  90   N  GLY A  85           
SHEET    1 AA3 8 GLY B  18  THR B  26  0                                        
SHEET    2 AA3 8 VAL B  32  TRP B  43 -1  O  VAL B  40   N  GLY B  18           
SHEET    3 AA3 8 CYS B  96  THR B 100 -1  O  ALA B  97   N  TRP B  43           
SHEET    4 AA3 8 VAL B  53  LEU B  57  1  N  VAL B  56   O  ILE B  98           
SHEET    5 AA3 8 VAL B 150  GLY B 156  1  O  ALA B 152   N  VAL B  55           
SHEET    6 AA3 8 VAL B 174  LEU B 180  1  O  LEU B 178   N  VAL B 153           
SHEET    7 AA3 8 VAL B 312  PHE B 317  1  O  VAL B 313   N  ILE B 179           
SHEET    8 AA3 8 ASN B 342  VAL B 344  1  O  VAL B 344   N  GLY B 316           
SHEET    1 AA4 2 VAL B  84  GLY B  85  0                                        
SHEET    2 AA4 2 ILE B  90  ASP B  91  1  O  ILE B  90   N  GLY B  85           
LINK         O   ILE A  22                NA    NA A 401     1555   1555  2.33  
LINK         O   ASP A  81                CA    CA A 402     1555   1555  2.35  
LINK         OD1 ASP A  81                CA    CA A 402     1555   1555  2.29  
LINK         O   VAL A  84                CA    CA A 402     1555   1555  2.42  
LINK         O   ILE B  22                NA    NA B 401     1555   1555  2.28  
LINK         O   ASP B  81                CA    CA B 402     1555   1555  2.48  
LINK         OD1 ASP B  81                CA    CA B 402     1555   1555  2.60  
LINK         O   VAL B  84                CA    CA B 402     1555   1555  2.37  
LINK        NA    NA A 401                 O   HOH A 551     1555   1555  2.74  
LINK        CA    CA A 402                 O   HOH A 635     1555   1555  2.44  
LINK        CA    CA A 402                 O   HOH A 726     1555   1555  2.39  
LINK        CA    CA A 402                 O   HOH A 715     1555   1555  2.39  
LINK        CA    CA A 403                 O   HOH A 701     1555   1555  2.48  
LINK        CA    CA A 403                 O   HOH B 522     1555   1555  2.60  
LINK        CA    CA A 403                 O   HOH B 597     1555   1555  2.44  
LINK        CA    CA A 403                 O   HOH B 750     1555   1555  3.06  
LINK        CA    CA A 403                 O   HOH B 508     1555   1555  2.52  
LINK        CA    CA A 404                 O1  GOL B 403     1555   1555  2.28  
LINK        CA    CA A 404                 O   HOH B 576     1555   1555  2.42  
LINK        CA    CA A 404                 O   HOH B 748     1555   1555  2.34  
LINK        CA    CA A 404                 O2  GOL B 403     1555   1555  2.55  
LINK        CA    CA A 404                 O   HOH A 572     1555   1555  2.29  
LINK        CA    CA A 404                 O   HOH A 711     1555   1555  2.33  
LINK        CA    CA A 404                 O   HOH B 502     1555   1555  2.45  
LINK        CA    CA A 404                 O   HOH B 743     1555   1555  2.39  
LINK        NA    NA B 401                 O   HOH B 759     1555   1555  2.47  
LINK        NA    NA B 401                 O   HOH B 766     1555   1555  2.48  
LINK        NA    NA B 401                 O   HOH B 525     1555   1555  2.42  
LINK        NA    NA B 401                 O   HOH B 771     1555   1555  2.56  
LINK        CA    CA B 402                 O   HOH B 585     1555   1555  2.64  
LINK        CA    CA B 402                 O   HOH B 687     1555   1555  2.21  
LINK        CA    CA B 402                 O   HOH B 801     1555   1555  2.77  
LINK        NA    NA A 401                 O   HOH B 759     1555   1554  2.63  
LINK        NA    NA A 401                 O   HOH B 766     1555   1554  2.63  
LINK        CA    CA A 402                 O   HOH B 518     1555   2554  2.39  
LINK        NA    NA B 401                 O   HOH A 721     1555   1556  2.26  
LINK        NA    NA B 401                 O   HOH A 723     1555   1556  2.42  
SITE     1 AC1  4 ILE A  22  HOH A 551  HOH B 759  HOH B 766                    
SITE     1 AC2  5 ASP A  81  VAL A  84  HOH A 635  HOH A 715                    
SITE     2 AC2  5 HOH A 726                                                     
SITE     1 AC3  5 HOH A 701  HOH B 508  HOH B 522  HOH B 597                    
SITE     2 AC3  5 HOH B 750                                                     
SITE     1 AC4  7 HOH A 572  HOH A 711  GOL B 403  HOH B 502                    
SITE     2 AC4  7 HOH B 576  HOH B 743  HOH B 748                               
SITE     1 AC5  7 HOH A 721  HOH A 723  ILE B  22  HOH B 525                    
SITE     2 AC5  7 HOH B 759  HOH B 766  HOH B 771                               
SITE     1 AC6  5 ASP B  81  VAL B  84  HOH B 585  HOH B 687                    
SITE     2 AC6  5 HOH B 801                                                     
SITE     1 AC7 11 GLU A 263   CA A 404  GLN B 194  SER B 195                    
SITE     2 AC7 11 ASP B 287  SER B 290  HOH B 502  HOH B 510                    
SITE     3 AC7 11 HOH B 576  HOH B 743  HOH B 748                               
CRYST1   47.750   93.230   81.590  90.00  94.78  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020942  0.000000  0.001752        0.00000                         
SCALE2      0.000000  0.010726  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012299        0.00000                         
TER    5084      SER A 372                                                      
TER   10255      SER B 372                                                      
MASTER      433    0    7   31   20    0   14    6 5731    2   53   56          
END                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
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