Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6zyf-pdb

Name Class
6zyf-pdb
HEADER    SIGNALING PROTEIN                       31-JUL-20   6ZYF              
TITLE     NOTUM_GHRELIN COMPLEX                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PALMITOLEOYL-PROTEIN CARBOXYLESTERASE NOTUM;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HNOTUM;                                                     
COMPND   5 EC: 3.1.1.98;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NOTUM, OK/SW-CL.30;                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    NOTUM GHRELIN, SIGNALING PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHAO,E.Y.JONES                                                      
REVDAT   1   10-MAR-21 6ZYF    0                                                
JRNL        AUTH   Y.ZHAO,L.N.SCHUHMACHER,M.ROBERTS,S.KAKUGAWA,G.BINEVA-TODD,   
JRNL        AUTH 2 S.HOWELL,N.O'REILLY,C.PERRET,A.P.SNIJDERS,J.P.VINCENT,       
JRNL        AUTH 3 E.Y.JONES                                                    
JRNL        TITL   NOTUM DEACYLATES OCTANOYLATED GHRELIN                        
JRNL        REF    MOLECULAR METABOLISM                       2021              
JRNL        DOI    10.1016/J.MOLMET.2021.101201                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.18.2_3874                                   
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) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 92.04                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 44663                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2257                            
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 92.0400 -  5.5200    1.00     2891   159  0.1827 0.1905        
REMARK   3     2  5.5200 -  4.3800    1.00     2748   146  0.1656 0.1903        
REMARK   3     3  4.3800 -  3.8300    1.00     2710   150  0.1885 0.2460        
REMARK   3     4  3.8300 -  3.4800    1.00     2684   147  0.2151 0.2268        
REMARK   3     5  3.4800 -  3.2300    1.00     2692   146  0.2335 0.2527        
REMARK   3     6  3.2300 -  3.0400    1.00     2682   117  0.2546 0.2753        
REMARK   3     7  3.0400 -  2.8800    0.99     2671   132  0.2672 0.3016        
REMARK   3     8  2.8800 -  2.7600    0.99     2643   156  0.2679 0.2531        
REMARK   3     9  2.7600 -  2.6500    0.99     2606   145  0.2771 0.3060        
REMARK   3    10  2.6500 -  2.5600    0.99     2622   122  0.2843 0.3077        
REMARK   3    11  2.5600 -  2.4800    0.99     2626   140  0.3011 0.3456        
REMARK   3    12  2.4800 -  2.4100    0.98     2594   133  0.3088 0.3003        
REMARK   3    13  2.4100 -  2.3500    0.98     2599   146  0.3373 0.3594        
REMARK   3    14  2.3500 -  2.2900    0.98     2577   117  0.3587 0.3587        
REMARK   3    15  2.2900 -  2.2400    0.97     2564   157  0.3632 0.4001        
REMARK   3    16  2.2400 -  2.1900    0.95     2497   144  0.3828 0.3705        
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.53                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 86 THROUGH 107 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -54.5398  29.4557 -19.9132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4847 T22:   0.2339                                     
REMARK   3      T33:  -0.1849 T12:  -0.6144                                     
REMARK   3      T13:  -0.1244 T23:  -0.8531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0567 L22:   0.0826                                     
REMARK   3      L33:   0.0373 L12:  -0.0155                                     
REMARK   3      L13:   0.0183 L23:   0.0398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1751 S12:  -0.2209 S13:   0.5212                       
REMARK   3      S21:   0.1289 S22:  -0.0643 S23:  -0.3105                       
REMARK   3      S31:  -0.0846 S32:   0.0277 S33:  -0.1377                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 159 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -53.4575  21.0980 -22.9363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2005 T22:   0.3707                                     
REMARK   3      T33:   0.0909 T12:  -0.6057                                     
REMARK   3      T13:  -0.2624 T23:  -0.3100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3584 L22:   0.3544                                     
REMARK   3      L33:   0.2151 L12:  -0.1119                                     
REMARK   3      L13:   0.2686 L23:   0.3057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5241 S12:  -0.1645 S13:   0.5835                       
REMARK   3      S21:  -0.1135 S22:  -0.0759 S23:  -0.4647                       
REMARK   3      S31:  -0.2936 S32:  -0.4007 S33:   0.3539                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 160 THROUGH 451 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -60.4824  12.5313 -34.2413              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3638 T22:   0.3459                                     
REMARK   3      T33:   0.2319 T12:  -0.1924                                     
REMARK   3      T13:   0.0127 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3571 L22:   1.2422                                     
REMARK   3      L33:   0.6150 L12:   0.5204                                     
REMARK   3      L13:   0.2182 L23:  -0.2493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0370 S12:   0.0379 S13:   0.0436                       
REMARK   3      S21:  -0.1238 S22:  -0.0049 S23:   0.0205                       
REMARK   3      S31:   0.1374 S32:  -0.0960 S33:   0.0267                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 86 THROUGH 147 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -33.2070  31.2850 -12.8616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3544 T22:   0.4315                                     
REMARK   3      T33:   0.1584 T12:  -0.2291                                     
REMARK   3      T13:   0.0447 T23:  -0.1104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4812 L22:   0.5160                                     
REMARK   3      L33:   0.0320 L12:   0.4557                                     
REMARK   3      L13:   0.2222 L23:   0.2505                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4491 S12:   0.4788 S13:  -0.0806                       
REMARK   3      S21:  -0.2465 S22:   0.4860 S23:   0.1038                       
REMARK   3      S31:   0.2061 S32:  -0.4403 S33:  -0.0020                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 148 THROUGH 185 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -39.3678  28.6198  -3.6876              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3463 T22:   0.3911                                     
REMARK   3      T33:   0.2909 T12:  -0.1780                                     
REMARK   3      T13:   0.0521 T23:  -0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1974 L22:   0.1135                                     
REMARK   3      L33:   0.0857 L12:   0.0295                                     
REMARK   3      L13:   0.1440 L23:   0.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1265 S12:   0.1349 S13:  -0.0472                       
REMARK   3      S21:  -0.1214 S22:   0.1930 S23:   0.0485                       
REMARK   3      S31:   0.2979 S32:  -0.2095 S33:   0.0057                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 186 THROUGH 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9203  40.4688 -11.3976              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3656 T22:   0.3719                                     
REMARK   3      T33:   0.3568 T12:  -0.1722                                     
REMARK   3      T13:   0.0316 T23:   0.0589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4116 L22:   0.2320                                     
REMARK   3      L33:   0.1165 L12:  -0.0611                                     
REMARK   3      L13:   0.1534 L23:  -0.0640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4539 S12:   0.4570 S13:   0.4345                       
REMARK   3      S21:  -0.2121 S22:   0.3798 S23:   0.0891                       
REMARK   3      S31:  -0.0163 S32:  -0.0444 S33:  -0.0537                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 225 THROUGH 286 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9213  32.3196  -3.1246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2383 T22:   0.1962                                     
REMARK   3      T33:   0.3657 T12:  -0.0089                                     
REMARK   3      T13:   0.0264 T23:  -0.0611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4896 L22:   0.1511                                     
REMARK   3      L33:  -0.1161 L12:   0.3839                                     
REMARK   3      L13:   0.0354 L23:   0.0294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1781 S12:   0.1479 S13:   0.0778                       
REMARK   3      S21:   0.0627 S22:   0.2205 S23:  -0.3567                       
REMARK   3      S31:   0.0659 S32:   0.0955 S33:  -0.0147                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 287 THROUGH 394 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7955  25.5621  -0.5157              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2435 T22:   0.2704                                     
REMARK   3      T33:   0.5812 T12:   0.0164                                     
REMARK   3      T13:   0.0560 T23:  -0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4978 L22:   0.3284                                     
REMARK   3      L33:   0.3193 L12:   0.3432                                     
REMARK   3      L13:   0.1066 L23:  -0.1168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1832 S12:   0.0118 S13:  -0.3953                       
REMARK   3      S21:   0.0681 S22:   0.1498 S23:  -0.5834                       
REMARK   3      S31:   0.0114 S32:   0.1548 S33:   0.0040                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 451 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.6022  21.8094  13.2791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5353 T22:   0.4092                                     
REMARK   3      T33:   0.5452 T12:  -0.0557                                     
REMARK   3      T13:  -0.1022 T23:   0.2197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2226 L22:   0.0304                                     
REMARK   3      L33:   0.1517 L12:   0.1158                                     
REMARK   3      L13:   0.1245 L23:  -0.0068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0418 S12:  -1.2924 S13:  -0.5673                       
REMARK   3      S21:   0.6392 S22:  -0.1159 S23:   0.0703                       
REMARK   3      S31:   0.2987 S32:  -0.0046 S33:  -0.0240                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 86 THROUGH 194 OR       
REMARK   3                          RESID 199 THROUGH 418 OR RESID 432          
REMARK   3                          THROUGH 451 OR RESID 501))                  
REMARK   3     SELECTION          : (CHAIN B AND (RESID 86 THROUGH 143 OR       
REMARK   3                          (RESID 144 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD )) OR RESID 145 THROUGH 451 OR RESID     
REMARK   3                          501))                                       
REMARK   3     ATOM PAIRS NUMBER  : 3269                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ZYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292110524.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92819                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45353                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 92.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4UZQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0 0.1 M KCL 15% PEG     
REMARK 280  MME 5000, EVAPORATION, TEMPERATURE 296K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       37.70900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       92.03600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.70900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       92.03600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     GLY A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     GLN A    83                                                      
REMARK 465     GLN A    84                                                      
REMARK 465     LEU A    85                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     ASN A   198                                                      
REMARK 465     ASP A   420                                                      
REMARK 465     SER A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     LYS A   423                                                      
REMARK 465     ALA A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     LYS A   426                                                      
REMARK 465     THR A   427                                                      
REMARK 465     PRO A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     LYS A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     GLY A   452                                                      
REMARK 465     THR A   453                                                      
REMARK 465     LYS A   454                                                      
REMARK 465     HIS A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     HIS A   457                                                      
REMARK 465     HIS A   458                                                      
REMARK 465     HIS A   459                                                      
REMARK 465     HIS A   460                                                      
REMARK 465     GLU B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     GLY B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     ALA B    82                                                      
REMARK 465     GLN B    83                                                      
REMARK 465     GLN B    84                                                      
REMARK 465     LEU B    85                                                      
REMARK 465     SER B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     LYS B   197                                                      
REMARK 465     ASN B   198                                                      
REMARK 465     HIS B   419                                                      
REMARK 465     ASP B   420                                                      
REMARK 465     SER B   421                                                      
REMARK 465     HIS B   422                                                      
REMARK 465     LYS B   423                                                      
REMARK 465     ALA B   424                                                      
REMARK 465     SER B   425                                                      
REMARK 465     LYS B   426                                                      
REMARK 465     THR B   427                                                      
REMARK 465     PRO B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     LYS B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     GLY B   452                                                      
REMARK 465     THR B   453                                                      
REMARK 465     LYS B   454                                                      
REMARK 465     HIS B   455                                                      
REMARK 465     HIS B   456                                                      
REMARK 465     HIS B   457                                                      
REMARK 465     HIS B   458                                                      
REMARK 465     HIS B   459                                                      
REMARK 465     HIS B   460                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 144    NE   CZ   NH1  NH2                                  
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   NZ   LYS A   194     O    GLU A   196              2.13            
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    TRP A 128     -140.15     59.10                                   
REMARK 500    SER A 192      168.33     65.07                                   
REMARK 500    SER A 195      -97.25    -84.61                                   
REMARK 500    ALA A 232     -121.74     60.29                                   
REMARK 500    PHE A 339       76.09   -119.84                                   
REMARK 500    GLU A 390      154.08     71.37                                   
REMARK 500    ILE A 391      -31.86   -164.71                                   
REMARK 500    TRP B 128     -140.53     60.00                                   
REMARK 500    SER B 193       78.81   -105.75                                   
REMARK 500    ALA B 232     -122.15     60.52                                   
REMARK 500    ILE B 283      -13.10     50.70                                   
REMARK 500    THR B 352       37.64    -97.82                                   
REMARK 500    GLU B 390      154.80     71.30                                   
REMARK 500    ILE B 391     -138.00   -165.05                                   
REMARK 500    ILE B 392      -22.76     38.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     K4Q B  502                                                       
DBREF  6ZYF A   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
DBREF  6ZYF B   81   451  UNP    Q6P988   NOTUM_HUMAN     81    451             
SEQADV 6ZYF GLU A   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF THR A   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF GLY A   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF ALA A  232  UNP  Q6P988    SER   232 CONFLICT                       
SEQADV 6ZYF SER A  330  UNP  Q6P988    CYS   330 CONFLICT                       
SEQADV 6ZYF GLY A  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF THR A  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF LYS A  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS A  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS A  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS A  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS A  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS A  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS A  460  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF GLU B   78  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF THR B   79  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF GLY B   80  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF ALA B  232  UNP  Q6P988    SER   232 CONFLICT                       
SEQADV 6ZYF SER B  330  UNP  Q6P988    CYS   330 CONFLICT                       
SEQADV 6ZYF GLY B  452  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF THR B  453  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF LYS B  454  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS B  455  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS B  456  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS B  457  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS B  458  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS B  459  UNP  Q6P988              EXPRESSION TAG                 
SEQADV 6ZYF HIS B  460  UNP  Q6P988              EXPRESSION TAG                 
SEQRES   1 A  383  GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG          
SEQRES   2 A  383  LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP          
SEQRES   3 A  383  GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY          
SEQRES   4 A  383  SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR          
SEQRES   5 A  383  CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR          
SEQRES   6 A  383  MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR          
SEQRES   7 A  383  ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU          
SEQRES   8 A  383  ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO          
SEQRES   9 A  383  TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS          
SEQRES  10 A  383  SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE          
SEQRES  11 A  383  ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU          
SEQRES  12 A  383  SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER ALA ALA          
SEQRES  13 A  383  GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA          
SEQRES  14 A  383  GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL          
SEQRES  15 A  383  ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS          
SEQRES  16 A  383  GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS          
SEQRES  17 A  383  ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP          
SEQRES  18 A  383  ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN          
SEQRES  19 A  383  GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL          
SEQRES  20 A  383  TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP          
SEQRES  21 A  383  LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS          
SEQRES  22 A  383  LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR          
SEQRES  23 A  383  ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS          
SEQRES  24 A  383  ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS          
SEQRES  25 A  383  GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL          
SEQRES  26 A  383  LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP          
SEQRES  27 A  383  ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO          
SEQRES  28 A  383  LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO          
SEQRES  29 A  383  TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS          
SEQRES  30 A  383  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  383  GLU THR GLY SER ALA GLN GLN LEU ASN GLU ASP LEU ARG          
SEQRES   2 B  383  LEU HIS LEU LEU LEU ASN THR SER VAL THR CYS ASN ASP          
SEQRES   3 B  383  GLY SER PRO ALA GLY TYR TYR LEU LYS GLU SER ARG GLY          
SEQRES   4 B  383  SER ARG ARG TRP LEU LEU PHE LEU GLU GLY GLY TRP TYR          
SEQRES   5 B  383  CYS PHE ASN ARG GLU ASN CYS ASP SER ARG TYR ASP THR          
SEQRES   6 B  383  MET ARG ARG LEU MET SER SER ARG ASP TRP PRO ARG THR          
SEQRES   7 B  383  ARG THR GLY THR GLY ILE LEU SER SER GLN PRO GLU GLU          
SEQRES   8 B  383  ASN PRO TYR TRP TRP ASN ALA ASN MET VAL PHE ILE PRO          
SEQRES   9 B  383  TYR CYS SER SER ASP VAL TRP SER GLY ALA SER SER LYS          
SEQRES  10 B  383  SER GLU LYS ASN GLU TYR ALA PHE MET GLY ALA LEU ILE          
SEQRES  11 B  383  ILE GLN GLU VAL VAL ARG GLU LEU LEU GLY ARG GLY LEU          
SEQRES  12 B  383  SER GLY ALA LYS VAL LEU LEU LEU ALA GLY SER ALA ALA          
SEQRES  13 B  383  GLY GLY THR GLY VAL LEU LEU ASN VAL ASP ARG VAL ALA          
SEQRES  14 B  383  GLU GLN LEU GLU LYS LEU GLY TYR PRO ALA ILE GLN VAL          
SEQRES  15 B  383  ARG GLY LEU ALA ASP SER GLY TRP PHE LEU ASP ASN LYS          
SEQRES  16 B  383  GLN TYR ARG HIS THR ASP CYS VAL ASP THR ILE THR CYS          
SEQRES  17 B  383  ALA PRO THR GLU ALA ILE ARG ARG GLY ILE ARG TYR TRP          
SEQRES  18 B  383  ASN GLY VAL VAL PRO GLU ARG CYS ARG ARG GLN PHE GLN          
SEQRES  19 B  383  GLU GLY GLU GLU TRP ASN CYS PHE PHE GLY TYR LYS VAL          
SEQRES  20 B  383  TYR PRO THR LEU ARG SER PRO VAL PHE VAL VAL GLN TRP          
SEQRES  21 B  383  LEU PHE ASP GLU ALA GLN LEU THR VAL ASP ASN VAL HIS          
SEQRES  22 B  383  LEU THR GLY GLN PRO VAL GLN GLU GLY LEU ARG LEU TYR          
SEQRES  23 B  383  ILE GLN ASN LEU GLY ARG GLU LEU ARG HIS THR LEU LYS          
SEQRES  24 B  383  ASP VAL PRO ALA SER PHE ALA PRO ALA CYS LEU SER HIS          
SEQRES  25 B  383  GLU ILE ILE ILE ARG SER HIS TRP THR ASP VAL GLN VAL          
SEQRES  26 B  383  LYS GLY THR SER LEU PRO ARG ALA LEU HIS CYS TRP ASP          
SEQRES  27 B  383  ARG SER LEU HIS ASP SER HIS LYS ALA SER LYS THR PRO          
SEQRES  28 B  383  LEU LYS GLY CYS PRO VAL HIS LEU VAL ASP SER CYS PRO          
SEQRES  29 B  383  TRP PRO HIS CYS ASN PRO SER CYS PRO THR GLY THR LYS          
SEQRES  30 B  383  HIS HIS HIS HIS HIS HIS                                      
HET    NAG  A 501      14                                                       
HET    K4Q  A 502      15                                                       
HET    NAG  B 501      14                                                       
HET    K4Q  B 502      10                                                       
HET    EDO  B 503       4                                                       
HET    EDO  B 504       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     K4Q [(2~{S})-2-AZANYL-3-OXIDANYLIDENE-PROPYL] OCTANOATE              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  K4Q    2(C11 H21 N O3)                                              
FORMUL   7  EDO    2(C2 H6 O2)                                                  
FORMUL   9  HOH   *56(H2 O)                                                     
HELIX    1 AA1 ASN A  132  MET A  143  1                                  12    
HELIX    2 AA2 ARG A  144  SER A  148  5                                   5    
HELIX    3 AA3 THR A  159  SER A  163  5                                   5    
HELIX    4 AA4 MET A  203  GLY A  217  1                                  15    
HELIX    5 AA5 ARG A  218  ALA A  223  5                                   6    
HELIX    6 AA6 ALA A  232  LEU A  252  1                                  21    
HELIX    7 AA7 ALA A  286  ASN A  299  1                                  14    
HELIX    8 AA8 PRO A  303  ARG A  308  1                                   6    
HELIX    9 AA9 GLU A  314  PHE A  319  5                                   6    
HELIX   10 AB1 PHE A  320  TYR A  325  1                                   6    
HELIX   11 AB2 PRO A  326  LEU A  328  5                                   3    
HELIX   12 AB3 ASP A  340  ASP A  347  1                                   8    
HELIX   13 AB4 GLY A  359  LEU A  375  1                                  17    
HELIX   14 AB5 ARG A  394  ASP A  399  5                                   6    
HELIX   15 AB6 LEU A  407  LEU A  418  1                                  12    
HELIX   16 AB7 ASN B  132  MET B  143  1                                  12    
HELIX   17 AB8 ARG B  144  SER B  148  5                                   5    
HELIX   18 AB9 THR B  159  SER B  163  5                                   5    
HELIX   19 AC1 MET B  203  GLY B  217  1                                  15    
HELIX   20 AC2 ARG B  218  ALA B  223  5                                   6    
HELIX   21 AC3 ALA B  232  LEU B  252  1                                  21    
HELIX   22 AC4 ALA B  286  ASN B  299  1                                  14    
HELIX   23 AC5 PRO B  303  PHE B  310  1                                   8    
HELIX   24 AC6 GLU B  314  PHE B  319  5                                   6    
HELIX   25 AC7 PHE B  320  TYR B  325  1                                   6    
HELIX   26 AC8 PRO B  326  LEU B  328  5                                   3    
HELIX   27 AC9 GLU B  341  ASP B  347  1                                   7    
HELIX   28 AD1 GLN B  357  LYS B  376  1                                  20    
HELIX   29 AD2 ARG B  394  ASP B  399  5                                   6    
HELIX   30 AD3 LEU B  407  LEU B  418  1                                  12    
SHEET    1 AA110 THR A 155  ARG A 156  0                                        
SHEET    2 AA110 LEU A  89  LEU A  93 -1  N  LEU A  89   O  ARG A 156           
SHEET    3 AA110 GLY A 108  LYS A 112 -1  O  TYR A 109   N  HIS A  92           
SHEET    4 AA110 ASN A 176  ILE A 180 -1  O  PHE A 179   N  TYR A 110           
SHEET    5 AA110 ARG A 119  LEU A 124  1  N  LEU A 121   O  ASN A 176           
SHEET    6 AA110 VAL A 225  SER A 231  1  O  ALA A 229   N  LEU A 122           
SHEET    7 AA110 GLN A 258  ASP A 264  1  O  ARG A 260   N  LEU A 228           
SHEET    8 AA110 VAL A 332  VAL A 335  1  O  VAL A 335   N  ALA A 263           
SHEET    9 AA110 SER A 381  ALA A 383  1  O  PHE A 382   N  VAL A 334           
SHEET   10 AA110 HIS A 435  VAL A 437  1  O  LEU A 436   N  ALA A 383           
SHEET    1 AA2 2 GLN A 401  VAL A 402  0                                        
SHEET    2 AA2 2 THR A 405  SER A 406 -1  O  THR A 405   N  VAL A 402           
SHEET    1 AA310 THR B 155  ARG B 156  0                                        
SHEET    2 AA310 LEU B  89  LEU B  93 -1  N  LEU B  89   O  ARG B 156           
SHEET    3 AA310 GLY B 108  LYS B 112 -1  O  TYR B 109   N  HIS B  92           
SHEET    4 AA310 ASN B 176  ILE B 180 -1  O  PHE B 179   N  TYR B 110           
SHEET    5 AA310 ARG B 119  LEU B 124  1  N  PHE B 123   O  ILE B 180           
SHEET    6 AA310 VAL B 225  SER B 231  1  O  ALA B 229   N  LEU B 122           
SHEET    7 AA310 GLN B 258  ASP B 264  1  O  ARG B 260   N  LEU B 228           
SHEET    8 AA310 VAL B 332  VAL B 335  1  O  VAL B 335   N  ALA B 263           
SHEET    9 AA310 SER B 381  ALA B 383  1  O  PHE B 382   N  VAL B 334           
SHEET   10 AA310 HIS B 435  VAL B 437  1  O  LEU B 436   N  ALA B 383           
SHEET    1 AA4 2 PHE B 339  ASP B 340  0                                        
SHEET    2 AA4 2 LEU B 387  SER B 388  1  O  SER B 388   N  PHE B 339           
SHEET    1 AA5 2 GLN B 401  VAL B 402  0                                        
SHEET    2 AA5 2 THR B 405  SER B 406 -1  O  THR B 405   N  VAL B 402           
SSBOND   1 CYS A  101    CYS A  183                          1555   1555  2.03  
SSBOND   2 CYS A  130    CYS A  136                          1555   1555  2.03  
SSBOND   3 CYS A  279    CYS A  285                          1555   1555  2.03  
SSBOND   4 CYS A  306    CYS A  318                          1555   1555  2.03  
SSBOND   5 CYS A  386    CYS A  449                          1555   1555  2.03  
SSBOND   6 CYS A  413    CYS A  432                          1555   1555  2.03  
SSBOND   7 CYS A  440    CYS A  445                          1555   1555  2.03  
SSBOND   8 CYS B  101    CYS B  183                          1555   1555  2.03  
SSBOND   9 CYS B  130    CYS B  136                          1555   1555  2.03  
SSBOND  10 CYS B  279    CYS B  285                          1555   1555  2.03  
SSBOND  11 CYS B  306    CYS B  318                          1555   1555  2.03  
SSBOND  12 CYS B  386    CYS B  449                          1555   1555  2.03  
SSBOND  13 CYS B  413    CYS B  432                          1555   1555  2.03  
SSBOND  14 CYS B  440    CYS B  445                          1555   1555  2.03  
LINK         ND2 ASN A  96                 C1  NAG A 501     1555   1555  1.44  
LINK         ND2 ASN B  96                 C1  NAG B 501     1555   1555  1.44  
CRYST1   75.418  184.072   61.811  90.00  90.00  90.00 P 21 21 2     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      0.013259  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005433  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016178        0.00000                         
TER    2818      THR A 451                                                      
TER    5615      THR B 451                                                      
MASTER      484    0    6   30   26    0    0    6 5730    2   91   60          
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