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Database: PDB
Entry: 6HY7
LinkDB: 6HY7
Original site: 6HY7 
HEADER    TOXIN                                   19-OCT-18   6HY7              
TITLE     CRYSTAL STRUCTURE OF ALPHA9 NACHR EXTRACELLULAR DOMAIN IN COMPLEX WITH
TITLE    2 ALPHA-CONOTOXIN RGIA                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9;           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NICOTINIC ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9,NACHR      
COMPND   5 ALPHA-9;                                                             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: ALPHA9 NACHR;                                         
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ALPHA-CONOTOXIN RGIA;                                      
COMPND  10 CHAIN: B;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: ALPHA CONOTOXIN RGIA                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CHRNA9, NACHRA9;                                               
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPICZA;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: CONUS REGIUS;                                   
SOURCE  13 ORGANISM_COMMON: CROWN CONE;                                         
SOURCE  14 ORGANISM_TAXID: 101314                                               
KEYWDS    ALPHA9, ION CHANNEL, NACHR, ACETYLCHOLINE, CONOTOXIN, RGIA,           
KEYWDS   2 ANTAGONIST, TOXIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GIASTAS,M.ZOURIDAKIS                                                
REVDAT   3   21-AUG-19 6HY7    1       REMARK                                   
REVDAT   2   05-JUN-19 6HY7    1       JRNL                                     
REVDAT   1   22-MAY-19 6HY7    0                                                
JRNL        AUTH   M.ZOURIDAKIS,A.PAPAKYRIAKOU,I.A.IVANOV,I.E.KASHEVEROV,       
JRNL        AUTH 2 V.TSETLIN,S.TZARTOS,P.GIASTAS                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE MONOMERIC EXTRACELLULAR DOMAIN OF   
JRNL        TITL 2 ALPHA 9 NICOTINIC RECEPTOR SUBUNIT IN COMPLEX WITH           
JRNL        TITL 3 ALPHA-CONOTOXIN RGIA: MOLECULAR DYNAMICS INSIGHTS INTO RGIA  
JRNL        TITL 4 BINDING TO ALPHA 9 ALPHA 10 NICOTINIC RECEPTORS.             
JRNL        REF    FRONT PHARMACOL               V.  10   474 2019              
JRNL        REFN                   ESSN 1663-9812                               
JRNL        PMID   31118896                                                     
JRNL        DOI    10.3389/FPHAR.2019.00474                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.190                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23319                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1175                            
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 42.4410 -  4.5178    1.00     2799   148  0.1629 0.2155        
REMARK   3     2  4.5178 -  3.5865    1.00     2803   146  0.1585 0.1996        
REMARK   3     3  3.5865 -  3.1333    1.00     2819   147  0.1879 0.2685        
REMARK   3     4  3.1333 -  2.8469    1.00     2796   150  0.2158 0.2943        
REMARK   3     5  2.8469 -  2.6429    1.00     2796   154  0.2240 0.2459        
REMARK   3     6  2.6429 -  2.4871    1.00     2784   144  0.2579 0.3036        
REMARK   3     7  2.4871 -  2.3625    1.00     2773   149  0.3045 0.3815        
REMARK   3     8  2.3625 -  2.2597    0.92     2574   137  0.3367 0.4247        
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)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.210           
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      :  0.009           1907                                  
REMARK   3   ANGLE     :  1.053           2605                                  
REMARK   3   CHIRALITY :  0.057            285                                  
REMARK   3   PLANARITY :  0.006            338                                  
REMARK   3   DIHEDRAL  : 12.979           1125                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 30 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  67.6098  13.2357  73.0118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4624 T22:   0.3860                                     
REMARK   3      T33:   0.3505 T12:   0.0563                                     
REMARK   3      T13:  -0.0748 T23:   0.1041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5228 L22:   0.4617                                     
REMARK   3      L33:   0.2898 L12:   0.4832                                     
REMARK   3      L13:  -0.2678 L23:  -0.3197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0316 S12:  -0.2325 S13:  -0.1215                       
REMARK   3      S21:   0.6959 S22:   0.0642 S23:   0.2177                       
REMARK   3      S31:   0.2956 S32:  -0.2096 S33:  -0.0157                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 94 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  73.7436  20.4667  57.9758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3470 T22:   0.3121                                     
REMARK   3      T33:   0.3372 T12:   0.0518                                     
REMARK   3      T13:   0.0375 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6982 L22:   1.6279                                     
REMARK   3      L33:   0.2650 L12:  -0.0506                                     
REMARK   3      L13:   0.2308 L23:  -0.2772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1131 S12:  -0.0687 S13:  -0.1707                       
REMARK   3      S21:  -0.2150 S22:   0.0710 S23:  -0.2395                       
REMARK   3      S31:   0.3195 S32:   0.1497 S33:   0.0001                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 162 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  70.8167  27.6604  50.6058              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3051 T22:   0.3302                                     
REMARK   3      T33:   0.3367 T12:   0.0166                                     
REMARK   3      T13:   0.0448 T23:  -0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0306 L22:   1.1551                                     
REMARK   3      L33:   0.8268 L12:   0.0525                                     
REMARK   3      L13:   0.0697 L23:  -0.0734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1148 S12:   0.0098 S13:  -0.0038                       
REMARK   3      S21:  -0.1601 S22:   0.0595 S23:  -0.2142                       
REMARK   3      S31:   0.1856 S32:  -0.0370 S33:  -0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 163 THROUGH 213 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  75.2237  34.0925  46.8283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2666 T22:   0.2943                                     
REMARK   3      T33:   0.3450 T12:  -0.0093                                     
REMARK   3      T13:   0.0509 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5215 L22:   0.4837                                     
REMARK   3      L33:   1.6917 L12:   0.0771                                     
REMARK   3      L13:   0.6843 L23:  -0.6981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0156 S12:   0.1131 S13:   0.1431                       
REMARK   3      S21:  -0.1435 S22:   0.0218 S23:  -0.1600                       
REMARK   3      S31:   0.1825 S32:   0.2015 S33:  -0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 13 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  50.1525  30.3403  53.3105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6669 T22:   0.4466                                     
REMARK   3      T33:   0.6410 T12:  -0.0507                                     
REMARK   3      T13:  -0.1110 T23:  -0.0558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1359 L22:  -0.0005                                     
REMARK   3      L33:   0.0776 L12:  -0.0115                                     
REMARK   3      L13:   0.1180 L23:   0.0197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3296 S12:  -0.4419 S13:   0.7194                       
REMARK   3      S21:  -0.3803 S22:  -0.0246 S23:   0.9025                       
REMARK   3      S31:  -0.7106 S32:   0.7931 S33:   0.0002                       
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 6HY7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012510.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12622                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.434                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.260                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 1.1900                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
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  <I/SIGMA(I)> 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: PHASER                                                
REMARK 200 STARTING MODEL: 4UXU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 10000, 100MM HEPES, PH 7.5,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K                     
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       31.82300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.26500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.82300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.26500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     SER A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     HIS A   218                                                      
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     ASP A  99    CB   CG   OD1  OD2                                  
REMARK 470     ASP A 100    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 101    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 104    CB   CG   CD   OE1  OE2                             
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   SG   CYS A   130     SG   CYS A   144              1.68            
REMARK 500   N    ASP A    91     O    HOH A   401              1.95            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B  10   CD1   TYR B  10   CE1     0.100                       
REMARK 500    TYR B  10   CE1   TYR B  10   CZ     -0.111                       
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    LEU A  67       46.13   -107.36                                   
REMARK 500    TYR A  74       46.30   -141.59                                   
REMARK 500    SER A  79      136.99   -176.47                                   
REMARK 500    ASN A  96       43.83    -92.03                                   
REMARK 500    ASP A 140       74.81   -150.81                                   
REMARK 500    MET A 183       59.67   -142.26                                   
REMARK 500    CYS B   8      -98.37   -115.06                                   
REMARK 500    ARG B   9      -87.65     51.46                                   
REMARK 500    ARG B  11      -16.03   -179.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 301 bound   
REMARK 800  to ASN A 32                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 302 bound   
REMARK 800  to ASN A 145                                                        
DBREF  6HY7 A    1   212  UNP    Q9UGM1   ACHA9_HUMAN     26    237             
DBREF  6HY7 B    1    13  UNP    P0C1D0   CA1A_CONRE      20     32             
SEQADV 6HY7 HIS A  213  UNP  Q9UGM1              EXPRESSION TAG                 
SEQADV 6HY7 HIS A  214  UNP  Q9UGM1              EXPRESSION TAG                 
SEQADV 6HY7 HIS A  215  UNP  Q9UGM1              EXPRESSION TAG                 
SEQADV 6HY7 HIS A  216  UNP  Q9UGM1              EXPRESSION TAG                 
SEQADV 6HY7 HIS A  217  UNP  Q9UGM1              EXPRESSION TAG                 
SEQADV 6HY7 HIS A  218  UNP  Q9UGM1              EXPRESSION TAG                 
SEQRES   1 A  218  ALA ASP GLY LYS TYR ALA GLN LYS LEU PHE ASN ASP LEU          
SEQRES   2 A  218  PHE GLU ASP TYR SER ASN ALA LEU ARG PRO VAL GLU ASP          
SEQRES   3 A  218  THR ASP LYS VAL LEU ASN VAL THR LEU GLN ILE THR LEU          
SEQRES   4 A  218  SER GLN ILE LYS ASP MET ASP GLU ARG ASN GLN ILE LEU          
SEQRES   5 A  218  THR ALA TYR LEU TRP ILE ARG GLN ILE TRP HIS ASP ALA          
SEQRES   6 A  218  TYR LEU THR TRP ASP ARG ASP GLN TYR ASP GLY LEU ASP          
SEQRES   7 A  218  SER ILE ARG ILE PRO SER ASP LEU VAL TRP ARG PRO ASP          
SEQRES   8 A  218  ILE VAL LEU TYR ASN LYS ALA ASP ASP GLU SER SER GLU          
SEQRES   9 A  218  PRO VAL ASN THR ASN VAL VAL LEU ARG TYR ASP GLY LEU          
SEQRES  10 A  218  ILE THR TRP ASP ALA PRO ALA ILE THR LYS SER SER CYS          
SEQRES  11 A  218  VAL VAL ASP VAL THR TYR PHE PRO PHE ASP ASN GLN GLN          
SEQRES  12 A  218  CYS ASN LEU THR PHE GLY SER TRP THR TYR ASN GLY ASN          
SEQRES  13 A  218  GLN VAL ASP ILE PHE ASN ALA LEU ASP SER GLY ASP LEU          
SEQRES  14 A  218  SER ASP PHE ILE GLU ASP VAL GLU TRP GLU VAL HIS GLY          
SEQRES  15 A  218  MET PRO ALA VAL LYS ASN VAL ILE SER TYR GLY CYS CYS          
SEQRES  16 A  218  SER GLU PRO TYR PRO ASP VAL THR PHE THR LEU LEU LEU          
SEQRES  17 A  218  LYS ARG ARG SER HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B   13  GLY CYS CYS SER ASP PRO ARG CYS ARG TYR ARG CYS AAR          
MODRES 6HY7 AAR B   13  ARG  MODIFIED RESIDUE                                   
HET    AAR  B  13      12                                                       
HET    NAG  A 301      14                                                       
HET    NAG  A 302      14                                                       
HET    EDO  A 303      10                                                       
HETNAM     AAR ARGININEAMIDE                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  AAR    C6 H16 N5 O 1+                                               
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6  HOH   *50(H2 O)                                                     
HELIX    1 AA1 ASP A    2  GLU A   15  1                                  14    
HELIX    2 AA2 ASP A   70  TYR A   74  5                                   5    
HELIX    3 AA3 ASP A   85  VAL A   87  5                                   3    
HELIX    4 AA4 GLY B    1  ASP B    5  5                                   5    
SHEET    1   A 6 VAL A 158  ASN A 162  0                                        
SHEET    2   A 6 LEU A  31  ILE A  42  1                                        
SHEET    3   A 6 ILE A  51  HIS A  63 -1                                        
SHEET    4   A 6 LEU A 117  SER A 129 -1                                        
SHEET    5   A 6 ASN A 109  ARG A 113 -1                                        
SHEET    6   A 6 SER A  79  PRO A  83 -1                                        
SHEET    1   B 2 ASP A  44  ASP A  46  0                                        
SHEET    2   B 2 ILE A  51  THR A  53 -1                                        
SHEET    1   C 4 ILE A  92  LEU A  94  0                                        
SHEET    2   C 4 ASN A 141  SER A 150 -1                                        
SHEET    3   C 4 TYR A 199  ARG A 210 -1                                        
SHEET    4   C 4 TRP A 178  ILE A 190 -1                                        
SHEET    1   D 2 CYS A 130  ASP A 133  0                                        
SHEET    2   D 2 ASN A 141  CYS A 144 -1                                        
SSBOND   1 CYS A  194    CYS A  195                          1555   1555  2.07  
SSBOND   2 CYS B    2    CYS B    8                          1555   1555  2.05  
SSBOND   3 CYS B    3    CYS B   12                          1555   1555  2.05  
LINK         ND2 ASN A  32                 C1  NAG A 301     1555   1555  1.44  
LINK         ND2 ASN A 145                 C1  NAG A 302     1555   1555  1.44  
LINK         C   CYS B  12                 N   AAR B  13     1555   1555  1.33  
CISPEP   1 PHE A  137    PRO A  138          0        -4.81                     
SITE     1 AC1  2 TYR A 192  SER A 196                                          
SITE     1 AC2  5 VAL A  30  ASN A  32  ARG A  48  PHE A 161                    
SITE     2 AC2  5 HOH A 437                                                     
SITE     1 AC3  6 GLN A 143  ASN A 145  VAL A 186  ASN A 188                    
SITE     2 AC3  6 THR A 203  HOH A 406                                          
CRYST1   63.646   82.530   49.474  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015712  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012117  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020213        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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