Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 7cog-pdb

Name Class
7cog-pdb
HEADER    HYDROLASE                               04-AUG-20   7COG              
TITLE     CHOLESTEROL ESTERASE FROM BURKHOLDERIA STABILIS (MONOCLINIC CRYSTAL   
TITLE    2 FORM)                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CHOLESTEROL ESTERASE;                                       
COMPND   5 OTHER_DETAILS: WP_096474789.1                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA STABILIS;                          
SOURCE   3 ORGANISM_TAXID: 95485                                                
KEYWDS    CHOLESTEROL ESTERASE, LIPASE, BURKHOLDERIA STABILIS, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YASUTAKE,T.TAMURA                                                   
REVDAT   1   16-DEC-20 7COG    0                                                
JRNL        AUTH   Y.YASUTAKE,K.KONISHI,S.MURAMATSU,K.YOSHIDA,S.ABURATANI,      
JRNL        AUTH 2 S.I.SAKASEGAWA,T.TAMURA                                      
JRNL        TITL   BACTERIAL TRIACYLGLYCEROL LIPASE IS A POTENTIAL CHOLESTEROL  
JRNL        TITL 2 ESTERASE: IDENTIFICATION OF A KEY DETERMINANT FOR            
JRNL        TITL 3 STEROL-BINDING SPECIFICITY.                                  
JRNL        REF    INT.J.BIOL.MACROMOL.          V. 167   578 2021              
JRNL        REFN                   ISSN 0141-8130                               
JRNL        DOI    10.1016/J.IJBIOMAC.2020.11.184                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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 : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.200                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 71684                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3554                            
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 29.9501 -  5.6866    0.95     3583   168  0.2210 0.2517        
REMARK   3     2  5.6866 -  4.5186    0.94     3473   188  0.1991 0.1993        
REMARK   3     3  4.5186 -  3.9489    0.94     3382   193  0.1943 0.2035        
REMARK   3     4  3.9489 -  3.5885    0.95     3434   182  0.2127 0.2813        
REMARK   3     5  3.5885 -  3.3316    0.94     3378   209  0.2302 0.2735        
REMARK   3     6  3.3316 -  3.1354    0.95     3395   182  0.2335 0.2826        
REMARK   3     7  3.1354 -  2.9786    0.95     3422   183  0.2357 0.2572        
REMARK   3     8  2.9786 -  2.8490    0.95     3407   180  0.2349 0.2545        
REMARK   3     9  2.8490 -  2.7394    0.96     3413   156  0.2373 0.2460        
REMARK   3    10  2.7394 -  2.6449    0.95     3373   189  0.2431 0.2646        
REMARK   3    11  2.6449 -  2.5623    0.95     3394   177  0.2447 0.3018        
REMARK   3    12  2.5623 -  2.4891    0.95     3353   168  0.2457 0.2726        
REMARK   3    13  2.4891 -  2.4236    0.95     3410   192  0.2624 0.2925        
REMARK   3    14  2.4236 -  2.3645    0.96     3423   149  0.2695 0.2589        
REMARK   3    15  2.3645 -  2.3107    0.95     3395   177  0.2759 0.2751        
REMARK   3    16  2.3107 -  2.2616    0.95     3345   171  0.2768 0.3099        
REMARK   3    17  2.2616 -  2.2164    0.94     3379   188  0.2866 0.2915        
REMARK   3    18  2.2164 -  2.1745    0.95     3390   165  0.2958 0.3593        
REMARK   3    19  2.1745 -  2.1357    0.94     3329   174  0.2959 0.3327        
REMARK   3    20  2.1357 -  2.0995    0.94     3413   150  0.2939 0.2942        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.002           9576                                  
REMARK   3   ANGLE     :  0.499          13120                                  
REMARK   3   CHIRALITY :  0.040           1560                                  
REMARK   3   PLANARITY :  0.003           1708                                  
REMARK   3   DIHEDRAL  :  9.253           5536                                  
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 7COG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300017935.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.098                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.360                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.7000                             
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) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.310                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1YS1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PEG4000, 2-PROPANOL,     
REMARK 280  PH 6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K             
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       23.54600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 13000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
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 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 13070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 13430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 90 ANGSTROM**2                            
REMARK 350 SURFACE AREA OF THE COMPLEX: 12910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A   2     -163.47   -160.48                                   
REMARK 500    THR A  18       -0.98     63.59                                   
REMARK 500    SER A  87     -126.00     60.26                                   
REMARK 500    SER A 219      118.41   -173.72                                   
REMARK 500    PHE A 221       -4.62     73.17                                   
REMARK 500    LEU A 234      -39.13     69.55                                   
REMARK 500    LEU A 266      -20.68   -141.35                                   
REMARK 500    ASP B   2     -158.03    -98.03                                   
REMARK 500    ALA B   5       24.02   -140.03                                   
REMARK 500    THR B  18      -15.92     63.44                                   
REMARK 500    TYR B  23      -98.39    -31.99                                   
REMARK 500    ALA B  24     -169.47    -77.23                                   
REMARK 500    VAL B  26      -26.81    142.99                                   
REMARK 500    ASP B  56     -167.40   -113.61                                   
REMARK 500    SER B  87     -133.78     60.49                                   
REMARK 500    THR B 150       41.28   -102.29                                   
REMARK 500    ASP B 159       91.69   -161.62                                   
REMARK 500    THR B 217      -55.78   -120.89                                   
REMARK 500    LEU B 234      -45.80     74.28                                   
REMARK 500    SER B 279      145.29   -174.43                                   
REMARK 500    SER C  87     -131.62     59.80                                   
REMARK 500    THR C 217     -105.73   -114.62                                   
REMARK 500    LEU C 234      -53.13     70.20                                   
REMARK 500    VAL D  26      -67.06   -121.04                                   
REMARK 500    SER D  87     -132.73     59.83                                   
REMARK 500    THR D 217      -91.06   -123.05                                   
REMARK 500    LEU D 218     -160.50   -124.58                                   
REMARK 500    PHE D 221     -127.65     62.12                                   
REMARK 500    LEU D 234      -38.47     74.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 242   OD2                                                    
REMARK 620 2 ASP A 288   OD1 167.7                                              
REMARK 620 3 GLN A 292   O    87.5  93.7                                        
REMARK 620 4 VAL A 296   O    92.3 100.0  85.2                                  
REMARK 620 5 HOH A 518   O    73.1  94.6  90.9 165.0                            
REMARK 620 6 HOH A 520   O    93.0  85.9 179.2  94.2  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 242   OD2                                                    
REMARK 620 2 ASP B 288   OD1 172.9                                              
REMARK 620 3 GLN B 292   O    82.8  92.2                                        
REMARK 620 4 VAL B 296   O    82.9  91.2  78.1                                  
REMARK 620 5 HOH B 506   O    98.9  85.4 172.4  94.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 242   OD2                                                    
REMARK 620 2 ASP C 288   OD1 159.9                                              
REMARK 620 3 GLN C 292   O    95.4  94.3                                        
REMARK 620 4 VAL C 296   O   101.4  95.9  91.7                                  
REMARK 620 5 HOH C 508   O    74.0  88.6  89.1 175.3                            
REMARK 620 6 HOH C 511   O    85.4  81.5 167.7 100.2  79.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 242   OD2                                                    
REMARK 620 2 ASP D 288   OD1 179.2                                              
REMARK 620 3 GLN D 292   O    90.8  88.4                                        
REMARK 620 4 VAL D 296   O    87.0  93.0  80.4                                  
REMARK 620 5 HOH D 504   O    93.2  86.6  84.4 164.9                            
REMARK 620 6 HOH D 516   O   107.0  73.8 162.2  99.9  94.5                      
REMARK 620 N                    1     2     3     4     5                       
DBREF1 7COG A    1   320  UNP                  A0A1Y1BQV9_9BURK                 
DBREF2 7COG A     A0A1Y1BQV9                         45         364             
DBREF1 7COG B    1   320  UNP                  A0A1Y1BQV9_9BURK                 
DBREF2 7COG B     A0A1Y1BQV9                         45         364             
DBREF1 7COG C    1   320  UNP                  A0A1Y1BQV9_9BURK                 
DBREF2 7COG C     A0A1Y1BQV9                         45         364             
DBREF1 7COG D    1   320  UNP                  A0A1Y1BQV9_9BURK                 
DBREF2 7COG D     A0A1Y1BQV9                         45         364             
SEQRES   1 A  320  ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU          
SEQRES   2 A  320  VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL          
SEQRES   3 A  320  LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN          
SEQRES   4 A  320  HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE          
SEQRES   5 A  320  GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU          
SEQRES   6 A  320  LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA          
SEQRES   7 A  320  THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU          
SEQRES   8 A  320  THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL          
SEQRES   9 A  320  ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER          
SEQRES  10 A  320  GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP          
SEQRES  11 A  320  PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL          
SEQRES  12 A  320  ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR          
SEQRES  13 A  320  ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR          
SEQRES  14 A  320  ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA          
SEQRES  15 A  320  GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO          
SEQRES  16 A  320  THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER          
SEQRES  17 A  320  TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE          
SEQRES  18 A  320  GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU          
SEQRES  19 A  320  VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA          
SEQRES  20 A  320  LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER          
SEQRES  21 A  320  GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU          
SEQRES  22 A  320  TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS          
SEQRES  23 A  320  ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA          
SEQRES  24 A  320  PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA          
SEQRES  25 A  320  ASN ARG LEU LYS LEU ALA GLY VAL                              
SEQRES   1 B  320  ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU          
SEQRES   2 B  320  VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL          
SEQRES   3 B  320  LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN          
SEQRES   4 B  320  HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE          
SEQRES   5 B  320  GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU          
SEQRES   6 B  320  LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA          
SEQRES   7 B  320  THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU          
SEQRES   8 B  320  THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL          
SEQRES   9 B  320  ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER          
SEQRES  10 B  320  GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP          
SEQRES  11 B  320  PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL          
SEQRES  12 B  320  ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR          
SEQRES  13 B  320  ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR          
SEQRES  14 B  320  ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA          
SEQRES  15 B  320  GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO          
SEQRES  16 B  320  THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER          
SEQRES  17 B  320  TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE          
SEQRES  18 B  320  GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU          
SEQRES  19 B  320  VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA          
SEQRES  20 B  320  LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER          
SEQRES  21 B  320  GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU          
SEQRES  22 B  320  TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS          
SEQRES  23 B  320  ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA          
SEQRES  24 B  320  PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA          
SEQRES  25 B  320  ASN ARG LEU LYS LEU ALA GLY VAL                              
SEQRES   1 C  320  ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU          
SEQRES   2 C  320  VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL          
SEQRES   3 C  320  LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN          
SEQRES   4 C  320  HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE          
SEQRES   5 C  320  GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU          
SEQRES   6 C  320  LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA          
SEQRES   7 C  320  THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU          
SEQRES   8 C  320  THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL          
SEQRES   9 C  320  ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER          
SEQRES  10 C  320  GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP          
SEQRES  11 C  320  PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL          
SEQRES  12 C  320  ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR          
SEQRES  13 C  320  ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR          
SEQRES  14 C  320  ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA          
SEQRES  15 C  320  GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO          
SEQRES  16 C  320  THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER          
SEQRES  17 C  320  TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE          
SEQRES  18 C  320  GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU          
SEQRES  19 C  320  VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA          
SEQRES  20 C  320  LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER          
SEQRES  21 C  320  GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU          
SEQRES  22 C  320  TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS          
SEQRES  23 C  320  ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA          
SEQRES  24 C  320  PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA          
SEQRES  25 C  320  ASN ARG LEU LYS LEU ALA GLY VAL                              
SEQRES   1 D  320  ALA ASP ASP TYR ALA THR THR ARG TYR PRO ILE VAL LEU          
SEQRES   2 D  320  VAL HIS GLY LEU THR GLY THR ASP LYS TYR ALA GLY VAL          
SEQRES   3 D  320  LEU GLU TYR TRP TYR GLY ILE GLN GLU ASP LEU GLN GLN          
SEQRES   4 D  320  HIS GLY ALA THR VAL TYR VAL ALA ASN LEU SER GLY PHE          
SEQRES   5 D  320  GLN SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU          
SEQRES   6 D  320  LEU ALA TYR VAL LYS THR VAL LEU ALA ALA THR GLY ALA          
SEQRES   7 D  320  THR LYS VAL ASN LEU VAL GLY HIS SER GLN GLY GLY LEU          
SEQRES   8 D  320  THR SER ARG TYR VAL ALA ALA VAL ALA PRO ASP LEU VAL          
SEQRES   9 D  320  ALA SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER          
SEQRES  10 D  320  GLU PHE ALA ASP PHE VAL GLN GLY VAL LEU ALA TYR ASP          
SEQRES  11 D  320  PRO THR GLY LEU SER SER SER VAL ILE ALA ALA PHE VAL          
SEQRES  12 D  320  ASN VAL PHE GLY ILE LEU THR SER SER SER HIS ASN THR          
SEQRES  13 D  320  ASN GLN ASP ALA LEU ALA SER LEU LYS THR LEU THR THR          
SEQRES  14 D  320  ALA GLN ALA ALA THR TYR ASN GLN ASN TYR PRO SER ALA          
SEQRES  15 D  320  GLY LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA PRO          
SEQRES  16 D  320  THR GLU THR VAL GLY GLY ASN THR HIS LEU LEU TYR SER          
SEQRES  17 D  320  TRP ALA GLY THR ALA ILE GLN PRO THR LEU SER VAL PHE          
SEQRES  18 D  320  GLY VAL THR GLY ALA THR ASP THR SER THR ILE PRO LEU          
SEQRES  19 D  320  VAL ASP PRO ALA ASN ALA LEU ASP PRO SER THR LEU ALA          
SEQRES  20 D  320  LEU PHE GLY THR GLY THR VAL MET ILE ASN ARG GLY SER          
SEQRES  21 D  320  GLY GLN ASN ASP GLY LEU VAL SER LYS CYS SER ALA LEU          
SEQRES  22 D  320  TYR GLY GLN VAL LEU SER THR SER TYR LYS TRP ASN HIS          
SEQRES  23 D  320  ILE ASP GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA          
SEQRES  24 D  320  PHE ALA GLU ASP PRO VAL ALA VAL ILE ARG THR HIS ALA          
SEQRES  25 D  320  ASN ARG LEU LYS LEU ALA GLY VAL                              
HET     CA  A 401       1                                                       
HET     CA  B 401       1                                                       
HET     CA  C 401       1                                                       
HET     CA  D 401       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   9  HOH   *88(H2 O)                                                     
HELIX    1 AA1 ALA A   24  VAL A   26  5                                   3    
HELIX    2 AA2 GLY A   32  GLN A   39  1                                   8    
HELIX    3 AA3 GLY A   60  GLY A   77  1                                  18    
HELIX    4 AA4 SER A   87  ALA A  100  1                                  14    
HELIX    5 AA5 SER A  117  ALA A  128  1                                  12    
HELIX    6 AA6 GLY A  133  SER A  151  1                                  19    
HELIX    7 AA7 ASP A  159  LEU A  167  1                                   9    
HELIX    8 AA8 THR A  168  TYR A  179  1                                  12    
HELIX    9 AA9 PRO A  237  ASP A  242  1                                   6    
HELIX   10 AB1 PRO A  243  ASN A  257  1                                  15    
HELIX   11 AB2 LYS A  269  LEU A  273  5                                   5    
HELIX   12 AB3 ILE A  287  ASN A  291  5                                   5    
HELIX   13 AB4 ASP A  303  GLY A  319  1                                  17    
HELIX   14 AB5 GLY B   32  HIS B   40  1                                   9    
HELIX   15 AB6 GLY B   60  GLY B   77  1                                  18    
HELIX   16 AB7 SER B   87  ALA B  100  1                                  14    
HELIX   17 AB8 SER B  117  LEU B  127  1                                  11    
HELIX   18 AB9 ALA B  128  ASP B  130  5                                   3    
HELIX   19 AC1 GLY B  133  THR B  150  1                                  18    
HELIX   20 AC2 ASP B  159  LEU B  167  1                                   9    
HELIX   21 AC3 THR B  168  TYR B  179  1                                  12    
HELIX   22 AC4 PRO B  237  ASP B  242  1                                   6    
HELIX   23 AC5 ASP B  242  ARG B  258  1                                  17    
HELIX   24 AC6 ASP B  303  GLY B  319  1                                  17    
HELIX   25 AC7 GLY C   32  HIS C   40  1                                   9    
HELIX   26 AC8 GLY C   60  GLY C   77  1                                  18    
HELIX   27 AC9 GLN C   88  ALA C  100  1                                  13    
HELIX   28 AD1 SER C  117  TYR C  129  1                                  13    
HELIX   29 AD2 GLY C  133  THR C  150  1                                  18    
HELIX   30 AD3 ASP C  159  LEU C  167  1                                   9    
HELIX   31 AD4 THR C  168  TYR C  179  1                                  12    
HELIX   32 AD5 PRO C  237  ASP C  242  1                                   6    
HELIX   33 AD6 PRO C  243  ASN C  257  1                                  15    
HELIX   34 AD7 ILE C  287  ASN C  291  5                                   5    
HELIX   35 AD8 ASP C  303  GLY C  319  1                                  17    
HELIX   36 AD9 ALA D   24  VAL D   26  5                                   3    
HELIX   37 AE1 GLY D   32  HIS D   40  1                                   9    
HELIX   38 AE2 GLY D   60  GLY D   77  1                                  18    
HELIX   39 AE3 GLN D   88  ALA D  100  1                                  13    
HELIX   40 AE4 SER D  117  ALA D  128  1                                  12    
HELIX   41 AE5 GLY D  133  THR D  150  1                                  18    
HELIX   42 AE6 ASP D  159  LEU D  167  1                                   9    
HELIX   43 AE7 THR D  168  TYR D  179  1                                  12    
HELIX   44 AE8 PRO D  237  ASP D  242  1                                   6    
HELIX   45 AE9 PRO D  243  ASN D  257  1                                  15    
HELIX   46 AF1 SER D  268  LEU D  273  1                                   6    
HELIX   47 AF2 HIS D  286  ASN D  291  5                                   6    
HELIX   48 AF3 ASP D  303  GLY D  319  1                                  17    
SHEET    1 AA1 6 VAL A  44  VAL A  46  0                                        
SHEET    2 AA1 6 ILE A  11  VAL A  14  1  N  ILE A  11   O  TYR A  45           
SHEET    3 AA1 6 VAL A  81  HIS A  86  1  O  VAL A  84   N  VAL A  12           
SHEET    4 AA1 6 VAL A 104  ILE A 110  1  O  THR A 108   N  GLY A  85           
SHEET    5 AA1 6 ASN A 202  GLY A 211  1  O  LEU A 205   N  VAL A 107           
SHEET    6 AA1 6 THR A 196  VAL A 199 -1  N  GLU A 197   O  HIS A 204           
SHEET    1 AA2 6 VAL A  44  VAL A  46  0                                        
SHEET    2 AA2 6 ILE A  11  VAL A  14  1  N  ILE A  11   O  TYR A  45           
SHEET    3 AA2 6 VAL A  81  HIS A  86  1  O  VAL A  84   N  VAL A  12           
SHEET    4 AA2 6 VAL A 104  ILE A 110  1  O  THR A 108   N  GLY A  85           
SHEET    5 AA2 6 ASN A 202  GLY A 211  1  O  LEU A 205   N  VAL A 107           
SHEET    6 AA2 6 GLN A 276  TYR A 282  1  O  LEU A 278   N  SER A 208           
SHEET    1 AA3 2 LYS A  22  TYR A  23  0                                        
SHEET    2 AA3 2 LEU A  27  GLU A  28 -1  O  LEU A  27   N  TYR A  23           
SHEET    1 AA4 2 ILE A 214  THR A 217  0                                        
SHEET    2 AA4 2 GLY A 225  ASP A 228 -1  O  THR A 227   N  GLN A 215           
SHEET    1 AA5 6 VAL B  44  VAL B  46  0                                        
SHEET    2 AA5 6 ILE B  11  VAL B  14  1  N  ILE B  11   O  TYR B  45           
SHEET    3 AA5 6 VAL B  81  HIS B  86  1  O  VAL B  84   N  VAL B  14           
SHEET    4 AA5 6 VAL B 104  ILE B 110  1  O  ILE B 110   N  GLY B  85           
SHEET    5 AA5 6 ASN B 202  TRP B 209  1  O  TYR B 207   N  VAL B 107           
SHEET    6 AA5 6 THR B 196  VAL B 199 -1  N  GLU B 197   O  HIS B 204           
SHEET    1 AA6 6 VAL B  44  VAL B  46  0                                        
SHEET    2 AA6 6 ILE B  11  VAL B  14  1  N  ILE B  11   O  TYR B  45           
SHEET    3 AA6 6 VAL B  81  HIS B  86  1  O  VAL B  84   N  VAL B  14           
SHEET    4 AA6 6 VAL B 104  ILE B 110  1  O  ILE B 110   N  GLY B  85           
SHEET    5 AA6 6 ASN B 202  TRP B 209  1  O  TYR B 207   N  VAL B 107           
SHEET    6 AA6 6 GLN B 276  SER B 279  1  O  LEU B 278   N  SER B 208           
SHEET    1 AA7 2 ILE B 214  VAL B 220  0                                        
SHEET    2 AA7 2 VAL B 223  ASP B 228 -1  O  GLY B 225   N  LEU B 218           
SHEET    1 AA8 6 VAL C  44  VAL C  46  0                                        
SHEET    2 AA8 6 ILE C  11  VAL C  14  1  N  ILE C  11   O  TYR C  45           
SHEET    3 AA8 6 VAL C  81  HIS C  86  1  O  VAL C  84   N  VAL C  14           
SHEET    4 AA8 6 VAL C 104  ILE C 110  1  O  THR C 108   N  LEU C  83           
SHEET    5 AA8 6 ASN C 202  GLY C 211  1  O  LEU C 205   N  VAL C 107           
SHEET    6 AA8 6 THR C 196  VAL C 199 -1  N  GLU C 197   O  HIS C 204           
SHEET    1 AA9 6 VAL C  44  VAL C  46  0                                        
SHEET    2 AA9 6 ILE C  11  VAL C  14  1  N  ILE C  11   O  TYR C  45           
SHEET    3 AA9 6 VAL C  81  HIS C  86  1  O  VAL C  84   N  VAL C  14           
SHEET    4 AA9 6 VAL C 104  ILE C 110  1  O  THR C 108   N  LEU C  83           
SHEET    5 AA9 6 ASN C 202  GLY C 211  1  O  LEU C 205   N  VAL C 107           
SHEET    6 AA9 6 GLN C 276  TYR C 282  1  O  LEU C 278   N  SER C 208           
SHEET    1 AB1 2 ILE C 214  VAL C 220  0                                        
SHEET    2 AB1 2 VAL C 223  ASP C 228 -1  O  GLY C 225   N  THR C 217           
SHEET    1 AB2 6 VAL D  44  VAL D  46  0                                        
SHEET    2 AB2 6 ILE D  11  VAL D  14  1  N  ILE D  11   O  TYR D  45           
SHEET    3 AB2 6 VAL D  81  HIS D  86  1  O  VAL D  84   N  VAL D  14           
SHEET    4 AB2 6 VAL D 104  ILE D 110  1  O  THR D 108   N  GLY D  85           
SHEET    5 AB2 6 ASN D 202  GLY D 211  1  O  LEU D 205   N  VAL D 107           
SHEET    6 AB2 6 THR D 196  VAL D 199 -1  N  GLU D 197   O  HIS D 204           
SHEET    1 AB3 6 VAL D  44  VAL D  46  0                                        
SHEET    2 AB3 6 ILE D  11  VAL D  14  1  N  ILE D  11   O  TYR D  45           
SHEET    3 AB3 6 VAL D  81  HIS D  86  1  O  VAL D  84   N  VAL D  14           
SHEET    4 AB3 6 VAL D 104  ILE D 110  1  O  THR D 108   N  GLY D  85           
SHEET    5 AB3 6 ASN D 202  GLY D 211  1  O  LEU D 205   N  VAL D 107           
SHEET    6 AB3 6 GLN D 276  TYR D 282  1  O  GLN D 276   N  LEU D 206           
SHEET    1 AB4 2 LYS D  22  TYR D  23  0                                        
SHEET    2 AB4 2 LEU D  27  GLU D  28 -1  O  LEU D  27   N  TYR D  23           
SHEET    1 AB5 2 ILE D 214  VAL D 220  0                                        
SHEET    2 AB5 2 VAL D 223  ASP D 228 -1  O  THR D 227   N  GLN D 215           
SSBOND   1 CYS A  190    CYS A  270                          1555   1555  2.03  
SSBOND   2 CYS B  190    CYS B  270                          1555   1555  2.03  
SSBOND   3 CYS C  190    CYS C  270                          1555   1555  2.04  
SSBOND   4 CYS D  190    CYS D  270                          1555   1555  2.03  
LINK         OD2 ASP A 242                CA    CA A 401     1555   1555  2.39  
LINK         OD1 ASP A 288                CA    CA A 401     1555   1555  2.36  
LINK         O   GLN A 292                CA    CA A 401     1555   1555  2.53  
LINK         O   VAL A 296                CA    CA A 401     1555   1555  2.45  
LINK        CA    CA A 401                 O   HOH A 518     1555   1555  2.43  
LINK        CA    CA A 401                 O   HOH A 520     1555   1555  2.45  
LINK         OD2 ASP B 242                CA    CA B 401     1555   1555  2.44  
LINK         OD1 ASP B 288                CA    CA B 401     1555   1555  2.37  
LINK         O   GLN B 292                CA    CA B 401     1555   1555  2.66  
LINK         O   VAL B 296                CA    CA B 401     1555   1555  2.48  
LINK        CA    CA B 401                 O   HOH B 506     1555   1555  2.70  
LINK         OD2 ASP C 242                CA    CA C 401     1555   1555  2.41  
LINK         OD1 ASP C 288                CA    CA C 401     1555   1555  2.28  
LINK         O   GLN C 292                CA    CA C 401     1555   1555  2.39  
LINK         O   VAL C 296                CA    CA C 401     1555   1555  2.35  
LINK        CA    CA C 401                 O   HOH C 508     1555   1555  2.41  
LINK        CA    CA C 401                 O   HOH C 511     1555   1555  2.57  
LINK         OD2 ASP D 242                CA    CA D 401     1555   1555  2.36  
LINK         OD1 ASP D 288                CA    CA D 401     1555   1555  2.34  
LINK         O   GLN D 292                CA    CA D 401     1555   1555  2.61  
LINK         O   VAL D 296                CA    CA D 401     1555   1555  2.45  
LINK        CA    CA D 401                 O   HOH D 504     1555   1555  2.50  
LINK        CA    CA D 401                 O   HOH D 516     1555   1555  2.51  
CISPEP   1 GLN A  292    LEU A  293          0         1.28                     
CISPEP   2 GLN B  292    LEU B  293          0         1.30                     
CISPEP   3 GLN C  292    LEU C  293          0         0.38                     
CISPEP   4 GLN D  292    LEU D  293          0         2.03                     
CRYST1  186.292   47.092   70.082  90.00  90.05  90.00 P 1 21 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      0.005368  0.000000  0.000005        0.00000                         
SCALE2      0.000000  0.021235  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014269        0.00000                         
TER    2346      VAL A 320                                                      
TER    4692      VAL B 320                                                      
TER    7038      VAL C 320                                                      
TER    9384      VAL D 320                                                      
MASTER      332    0    4   48   60    0    0    6 9472    4   39  100          
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:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer