GenomeNet

Database: PDB
Entry: 5CYY
LinkDB: 5CYY
Original site: 5CYY 
HEADER    MEMBRANE PROTEIN                        31-JUL-15   5CYY              
TITLE     STRUCTURE OF THE C-TERMINAL DOMAINS OF DIPZ FROM MYCOBACTERIUM        
TITLE    2 TUBERCULOSIS                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DIPZ;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 361-695;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: ATCC 25618 / H37RV;                                          
SOURCE   5 GENE: DIPZ, RV2874, MTCY274.05;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    THIOREDOXIN, CARBOHYDRATE BINDING MODULE, REDOX, STRUCTURAL GENOMICS, 
KEYWDS   2 PSI-BIOLOGY, MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS        
KEYWDS   3 PROJECT, XMTB, MEMBRANE PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.GOLDSTONE,P.METCALF,E.N.BAKER,MYCOBACTERIUM TUBERCULOSIS          
AUTHOR   2 STRUCTURAL PROTEOMICS PROJECT (XMTB)                                 
REVDAT   2   18-APR-18 5CYY    1       JRNL   REMARK                            
REVDAT   1   13-JAN-16 5CYY    0                                                
JRNL        AUTH   D.C.GOLDSTONE,P.METCALF,E.N.BAKER                            
JRNL        TITL   STRUCTURE OF THE ECTODOMAIN OF THE ELECTRON TRANSPORTER      
JRNL        TITL 2 RV2874 FROM MYCOBACTERIUM TUBERCULOSIS REVEALS A             
JRNL        TITL 3 THIOREDOXIN-LIKE DOMAIN COMBINED WITH A CARBOHYDRATE-BINDING 
JRNL        TITL 4 MODULE.                                                      
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  72    40 2016              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   26894533                                                     
JRNL        DOI    10.1107/S2059798315021488                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 73019                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7296                            
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 42.4011 -  6.8267    0.83     2170   249  0.1522 0.1750        
REMARK   3     2  6.8267 -  5.4221    0.86     2170   239  0.1441 0.1891        
REMARK   3     3  5.4221 -  4.7378    0.87     2151   246  0.1314 0.1893        
REMARK   3     4  4.7378 -  4.3051    0.87     2165   231  0.1202 0.1740        
REMARK   3     5  4.3051 -  3.9967    0.88     2165   241  0.1396 0.1791        
REMARK   3     6  3.9967 -  3.7613    0.88     2157   244  0.1570 0.1982        
REMARK   3     7  3.7613 -  3.5730    0.89     2177   236  0.1692 0.2277        
REMARK   3     8  3.5730 -  3.4175    0.89     2193   228  0.1829 0.2623        
REMARK   3     9  3.4175 -  3.2860    0.90     2199   246  0.1872 0.2215        
REMARK   3    10  3.2860 -  3.1727    0.90     2196   244  0.1802 0.2472        
REMARK   3    11  3.1727 -  3.0735    0.90     2172   255  0.1954 0.2289        
REMARK   3    12  3.0735 -  2.9857    0.91     2194   228  0.1996 0.2475        
REMARK   3    13  2.9857 -  2.9071    0.91     2204   265  0.1975 0.2586        
REMARK   3    14  2.9071 -  2.8362    0.91     2193   239  0.2055 0.2622        
REMARK   3    15  2.8362 -  2.7717    0.92     2222   249  0.1977 0.2848        
REMARK   3    16  2.7717 -  2.7127    0.92     2207   263  0.2043 0.2814        
REMARK   3    17  2.7127 -  2.6585    0.92     2203   244  0.2127 0.2931        
REMARK   3    18  2.6585 -  2.6083    0.92     2229   223  0.2057 0.2868        
REMARK   3    19  2.6083 -  2.5617    0.92     2230   253  0.2091 0.2711        
REMARK   3    20  2.5617 -  2.5183    0.92     2212   260  0.2034 0.2689        
REMARK   3    21  2.5183 -  2.4777    0.92     2228   245  0.2100 0.3117        
REMARK   3    22  2.4777 -  2.4396    0.92     2205   252  0.2086 0.2571        
REMARK   3    23  2.4396 -  2.4037    0.92     2242   221  0.2138 0.2904        
REMARK   3    24  2.4037 -  2.3699    0.92     2207   268  0.2266 0.2899        
REMARK   3    25  2.3699 -  2.3378    0.92     2214   236  0.2309 0.3149        
REMARK   3    26  2.3378 -  2.3075    0.92     2201   253  0.2435 0.3302        
REMARK   3    27  2.3075 -  2.2786    0.91     2182   260  0.2481 0.2931        
REMARK   3    28  2.2786 -  2.2512    0.90     2165   240  0.2843 0.3350        
REMARK   3    29  2.2512 -  2.2250    0.88     2095   218  0.3864 0.4504        
REMARK   3    30  2.2250 -  2.2000    0.89     2175   220  0.3331 0.3967        
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)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.410           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.37                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.38                          
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      :  0.008          10246                                  
REMARK   3   ANGLE     :  1.088          14018                                  
REMARK   3   CHIRALITY :  0.041           1567                                  
REMARK   3   PLANARITY :  0.005           1836                                  
REMARK   3   DIHEDRAL  : 11.694           3601                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CYY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212385.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73550                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.570                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 0.1M NA-CITRATE PH 5.6,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       54.98600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.21900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.76250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.21900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       54.98600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.76250            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 465     TYR A   338                                                      
REMARK 465     TYR A   339                                                      
REMARK 465     HIS A   340                                                      
REMARK 465     HIS A   341                                                      
REMARK 465     HIS A   342                                                      
REMARK 465     HIS A   343                                                      
REMARK 465     HIS A   344                                                      
REMARK 465     HIS A   345                                                      
REMARK 465     ASP A   346                                                      
REMARK 465     TYR A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     ILE A   349                                                      
REMARK 465     PRO A   350                                                      
REMARK 465     THR A   351                                                      
REMARK 465     THR A   352                                                      
REMARK 465     GLU A   353                                                      
REMARK 465     ASN A   354                                                      
REMARK 465     LEU A   355                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     PHE A   357                                                      
REMARK 465     GLN A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     ALA A   360                                                      
REMARK 465     ILE A   361                                                      
REMARK 465     SER A   362                                                      
REMARK 465     MET B   336                                                      
REMARK 465     SER B   337                                                      
REMARK 465     TYR B   338                                                      
REMARK 465     TYR B   339                                                      
REMARK 465     HIS B   340                                                      
REMARK 465     HIS B   341                                                      
REMARK 465     HIS B   342                                                      
REMARK 465     HIS B   343                                                      
REMARK 465     HIS B   344                                                      
REMARK 465     HIS B   345                                                      
REMARK 465     ASP B   346                                                      
REMARK 465     TYR B   347                                                      
REMARK 465     ASP B   348                                                      
REMARK 465     ILE B   349                                                      
REMARK 465     PRO B   350                                                      
REMARK 465     THR B   351                                                      
REMARK 465     THR B   352                                                      
REMARK 465     GLU B   353                                                      
REMARK 465     ASN B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     TYR B   356                                                      
REMARK 465     PHE B   357                                                      
REMARK 465     GLN B   358                                                      
REMARK 465     GLY B   359                                                      
REMARK 465     ALA B   360                                                      
REMARK 465     ILE B   361                                                      
REMARK 465     SER B   362                                                      
REMARK 465     ARG B   650                                                      
REMARK 465     ASP B   651                                                      
REMARK 465     GLY B   652                                                      
REMARK 465     LYS B   653                                                      
REMARK 465     PRO B   654                                                      
REMARK 465     MET C   336                                                      
REMARK 465     SER C   337                                                      
REMARK 465     TYR C   338                                                      
REMARK 465     TYR C   339                                                      
REMARK 465     HIS C   340                                                      
REMARK 465     HIS C   341                                                      
REMARK 465     HIS C   342                                                      
REMARK 465     HIS C   343                                                      
REMARK 465     HIS C   344                                                      
REMARK 465     HIS C   345                                                      
REMARK 465     ASP C   346                                                      
REMARK 465     TYR C   347                                                      
REMARK 465     ASP C   348                                                      
REMARK 465     ILE C   349                                                      
REMARK 465     PRO C   350                                                      
REMARK 465     THR C   351                                                      
REMARK 465     THR C   352                                                      
REMARK 465     GLU C   353                                                      
REMARK 465     ASN C   354                                                      
REMARK 465     LEU C   355                                                      
REMARK 465     TYR C   356                                                      
REMARK 465     PHE C   357                                                      
REMARK 465     GLN C   358                                                      
REMARK 465     GLY C   359                                                      
REMARK 465     ALA C   360                                                      
REMARK 465     ILE C   361                                                      
REMARK 465     SER C   362                                                      
REMARK 465     MET D   336                                                      
REMARK 465     SER D   337                                                      
REMARK 465     TYR D   338                                                      
REMARK 465     TYR D   339                                                      
REMARK 465     HIS D   340                                                      
REMARK 465     HIS D   341                                                      
REMARK 465     HIS D   342                                                      
REMARK 465     HIS D   343                                                      
REMARK 465     HIS D   344                                                      
REMARK 465     HIS D   345                                                      
REMARK 465     ASP D   346                                                      
REMARK 465     TYR D   347                                                      
REMARK 465     ASP D   348                                                      
REMARK 465     ILE D   349                                                      
REMARK 465     PRO D   350                                                      
REMARK 465     THR D   351                                                      
REMARK 465     THR D   352                                                      
REMARK 465     GLU D   353                                                      
REMARK 465     ASN D   354                                                      
REMARK 465     LEU D   355                                                      
REMARK 465     TYR D   356                                                      
REMARK 465     PHE D   357                                                      
REMARK 465     GLN D   358                                                      
REMARK 465     GLY D   359                                                      
REMARK 465     ALA D   360                                                      
REMARK 465     ILE D   361                                                      
REMARK 465     ARG D   650                                                      
REMARK 465     ASP D   651                                                      
REMARK 465     GLY D   652                                                      
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 564    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 628    CE   NZ                                             
REMARK 470     LYS A 653    CE   NZ                                             
REMARK 470     ARG A 673    NE   CZ   NH1  NH2                                  
REMARK 470     GLN B 393    CD   OE1  NE2                                       
REMARK 470     LYS B 416    CE   NZ                                             
REMARK 470     LYS B 480    CD   CE   NZ                                        
REMARK 470     ARG B 564    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B 672    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     ARG B 682    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 685    CG   CD   CE   NZ                                   
REMARK 470     ARG C 564    CD   NE   CZ   NH1  NH2                             
REMARK 470     TYR C 672    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     GLN D 452    CD   OE1  NE2                                       
REMARK 470     ASP D 624    CG   OD1  OD2                                       
REMARK 470     LYS D 653    CG   CD   CE   NZ                                   
REMARK 470     TYR D 672    CD1  CD2  CE1  CE2  CZ   OH                         
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   OD2  ASP C   543     O    HOH C   701              2.19            
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    ASP A 494       54.50   -102.37                                   
REMARK 500    TYR A 497       18.69     56.54                                   
REMARK 500    ASN A 580       36.91   -140.41                                   
REMARK 500    THR A 664     -165.96   -162.64                                   
REMARK 500    ASN B 372       66.41   -100.42                                   
REMARK 500    CYS B 397       51.93   -141.27                                   
REMARK 500    ASP B 494       55.08   -106.03                                   
REMARK 500    TYR B 497       18.88     57.00                                   
REMARK 500    ARG B 506      -18.92   -140.50                                   
REMARK 500    LYS B 545       78.50   -153.64                                   
REMARK 500    ALA B 565       45.78    -75.62                                   
REMARK 500    ALA B 566       47.33   -141.52                                   
REMARK 500    ASP B 621      -88.42    -96.76                                   
REMARK 500    ALA B 633     -179.28   -171.97                                   
REMARK 500    CYS C 397       61.41   -154.25                                   
REMARK 500    ASP C 494       57.25   -103.44                                   
REMARK 500    ALA C 565       44.63    -75.00                                   
REMARK 500    ALA C 566       34.17   -140.26                                   
REMARK 500    ASP C 614     -156.61   -145.86                                   
REMARK 500    CYS D 397       57.40   -140.70                                   
REMARK 500    ASP D 494       50.51   -108.34                                   
REMARK 500    LYS D 545       83.60   -152.80                                   
REMARK 500    PRO D 553      132.81    -36.13                                   
REMARK 500    THR D 556       30.69    -93.76                                   
REMARK 500    THR D 557        1.48   -159.93                                   
REMARK 500    ASN D 580       35.44   -140.04                                   
REMARK 500    PRO D 663      127.20    -39.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HYX   RELATED DB: PDB                                   
REMARK 900 2HYX IS A SHORTER CONSTRUCT                                          
DBREF  5CYY A  361   695  UNP    P9WG63   DIPZ_MYCTU     361    695             
DBREF  5CYY B  361   695  UNP    P9WG63   DIPZ_MYCTU     361    695             
DBREF  5CYY C  361   695  UNP    P9WG63   DIPZ_MYCTU     361    695             
DBREF  5CYY D  361   695  UNP    P9WG63   DIPZ_MYCTU     361    695             
SEQADV 5CYY MET A  336  UNP  P9WG63              INITIATING METHIONINE          
SEQADV 5CYY SER A  337  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR A  338  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR A  339  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS A  340  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS A  341  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS A  342  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS A  343  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS A  344  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS A  345  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP A  346  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR A  347  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP A  348  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ILE A  349  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PRO A  350  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR A  351  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR A  352  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLU A  353  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASN A  354  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY LEU A  355  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR A  356  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PHE A  357  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLN A  358  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLY A  359  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ALA A  360  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY MET B  336  UNP  P9WG63              INITIATING METHIONINE          
SEQADV 5CYY SER B  337  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR B  338  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR B  339  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS B  340  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS B  341  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS B  342  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS B  343  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS B  344  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS B  345  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP B  346  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR B  347  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP B  348  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ILE B  349  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PRO B  350  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR B  351  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR B  352  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLU B  353  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASN B  354  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY LEU B  355  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR B  356  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PHE B  357  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLN B  358  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLY B  359  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ALA B  360  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY MET C  336  UNP  P9WG63              INITIATING METHIONINE          
SEQADV 5CYY SER C  337  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR C  338  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR C  339  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS C  340  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS C  341  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS C  342  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS C  343  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS C  344  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS C  345  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP C  346  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR C  347  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP C  348  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ILE C  349  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PRO C  350  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR C  351  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR C  352  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLU C  353  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASN C  354  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY LEU C  355  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR C  356  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PHE C  357  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLN C  358  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLY C  359  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ALA C  360  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY MET D  336  UNP  P9WG63              INITIATING METHIONINE          
SEQADV 5CYY SER D  337  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR D  338  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR D  339  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS D  340  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS D  341  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS D  342  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS D  343  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS D  344  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY HIS D  345  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP D  346  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR D  347  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASP D  348  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ILE D  349  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PRO D  350  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR D  351  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY THR D  352  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLU D  353  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ASN D  354  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY LEU D  355  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY TYR D  356  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY PHE D  357  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLN D  358  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY GLY D  359  UNP  P9WG63              EXPRESSION TAG                 
SEQADV 5CYY ALA D  360  UNP  P9WG63              EXPRESSION TAG                 
SEQRES   1 A  360  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A  360  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE          
SEQRES   3 A  360  SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY          
SEQRES   4 A  360  GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS          
SEQRES   5 A  360  SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA          
SEQRES   6 A  360  PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO          
SEQRES   7 A  360  GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS          
SEQRES   8 A  360  VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN          
SEQRES   9 A  360  CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN          
SEQRES  10 A  360  ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS          
SEQRES  11 A  360  THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL          
SEQRES  12 A  360  ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE          
SEQRES  13 A  360  ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG          
SEQRES  14 A  360  ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR          
SEQRES  15 A  360  GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR          
SEQRES  16 A  360  ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP          
SEQRES  17 A  360  ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR          
SEQRES  18 A  360  THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO          
SEQRES  19 A  360  GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY          
SEQRES  20 A  360  GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP          
SEQRES  21 A  360  TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG          
SEQRES  22 A  360  GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP          
SEQRES  23 A  360  GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS          
SEQRES  24 A  360  ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR          
SEQRES  25 A  360  VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER          
SEQRES  26 A  360  GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG          
SEQRES  27 A  360  LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY          
SEQRES  28 A  360  LEU GLN VAL PHE SER PHE THR TYR GLY                          
SEQRES   1 B  360  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 B  360  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE          
SEQRES   3 B  360  SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY          
SEQRES   4 B  360  GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS          
SEQRES   5 B  360  SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA          
SEQRES   6 B  360  PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO          
SEQRES   7 B  360  GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS          
SEQRES   8 B  360  VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN          
SEQRES   9 B  360  CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN          
SEQRES  10 B  360  ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS          
SEQRES  11 B  360  THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL          
SEQRES  12 B  360  ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE          
SEQRES  13 B  360  ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG          
SEQRES  14 B  360  ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR          
SEQRES  15 B  360  GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR          
SEQRES  16 B  360  ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP          
SEQRES  17 B  360  ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR          
SEQRES  18 B  360  THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO          
SEQRES  19 B  360  GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY          
SEQRES  20 B  360  GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP          
SEQRES  21 B  360  TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG          
SEQRES  22 B  360  GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP          
SEQRES  23 B  360  GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS          
SEQRES  24 B  360  ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR          
SEQRES  25 B  360  VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER          
SEQRES  26 B  360  GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG          
SEQRES  27 B  360  LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY          
SEQRES  28 B  360  LEU GLN VAL PHE SER PHE THR TYR GLY                          
SEQRES   1 C  360  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 C  360  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE          
SEQRES   3 C  360  SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY          
SEQRES   4 C  360  GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS          
SEQRES   5 C  360  SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA          
SEQRES   6 C  360  PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO          
SEQRES   7 C  360  GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS          
SEQRES   8 C  360  VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN          
SEQRES   9 C  360  CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN          
SEQRES  10 C  360  ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS          
SEQRES  11 C  360  THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL          
SEQRES  12 C  360  ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE          
SEQRES  13 C  360  ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG          
SEQRES  14 C  360  ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR          
SEQRES  15 C  360  GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR          
SEQRES  16 C  360  ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP          
SEQRES  17 C  360  ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR          
SEQRES  18 C  360  THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO          
SEQRES  19 C  360  GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY          
SEQRES  20 C  360  GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP          
SEQRES  21 C  360  TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG          
SEQRES  22 C  360  GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP          
SEQRES  23 C  360  GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS          
SEQRES  24 C  360  ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR          
SEQRES  25 C  360  VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER          
SEQRES  26 C  360  GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG          
SEQRES  27 C  360  LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY          
SEQRES  28 C  360  LEU GLN VAL PHE SER PHE THR TYR GLY                          
SEQRES   1 D  360  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 D  360  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA ILE          
SEQRES   3 D  360  SER THR GLY THR GLU ILE ARG GLU GLN LEU ASN LEU GLY          
SEQRES   4 D  360  GLY ILE VAL ASN ALA GLN ASN ALA GLN LEU SER ASN CYS          
SEQRES   5 D  360  SER ASP GLY ALA ALA GLN LEU GLU SER CYS GLY THR ALA          
SEQRES   6 D  360  PRO ASP LEU LYS GLY ILE THR GLY TRP LEU ASN THR PRO          
SEQRES   7 D  360  GLY ASN LYS PRO ILE ASP LEU LYS SER LEU ARG GLY LYS          
SEQRES   8 D  360  VAL VAL LEU ILE ASP PHE TRP ALA TYR SER CYS ILE ASN          
SEQRES   9 D  360  CYS GLN ARG ALA ILE PRO HIS VAL VAL GLY TRP TYR GLN          
SEQRES  10 D  360  ALA TYR LYS ASP SER GLY LEU ALA VAL ILE GLY VAL HIS          
SEQRES  11 D  360  THR PRO GLU TYR ALA PHE GLU LYS VAL PRO GLY ASN VAL          
SEQRES  12 D  360  ALA LYS GLY ALA ALA ASN LEU GLY ILE SER TYR PRO ILE          
SEQRES  13 D  360  ALA LEU ASP ASN ASN TYR ALA THR TRP THR ASN TYR ARG          
SEQRES  14 D  360  ASN ARG TYR TRP PRO ALA GLU TYR LEU ILE ASP ALA THR          
SEQRES  15 D  360  GLY THR VAL ARG HIS ILE LYS PHE GLY GLU GLY ASP TYR          
SEQRES  16 D  360  ASN VAL THR GLU THR LEU VAL ARG GLN LEU LEU ASN ASP          
SEQRES  17 D  360  ALA LYS PRO GLY VAL LYS LEU PRO GLN PRO SER SER THR          
SEQRES  18 D  360  THR THR PRO ASP LEU THR PRO ARG ALA ALA LEU THR PRO          
SEQRES  19 D  360  GLU THR TYR PHE GLY VAL GLY LYS VAL VAL ASN TYR GLY          
SEQRES  20 D  360  GLY GLY GLY ALA TYR ASP GLU GLY SER ALA VAL PHE ASP          
SEQRES  21 D  360  TYR PRO PRO SER LEU ALA ALA ASN SER PHE ALA LEU ARG          
SEQRES  22 D  360  GLY ARG TRP ALA LEU ASP TYR GLN GLY ALA THR SER ASP          
SEQRES  23 D  360  GLY ASN ASP ALA ALA ILE LYS LEU ASN TYR HIS ALA LYS          
SEQRES  24 D  360  ASP VAL TYR ILE VAL VAL GLY GLY THR GLY THR LEU THR          
SEQRES  25 D  360  VAL VAL ARG ASP GLY LYS PRO ALA THR LEU PRO ILE SER          
SEQRES  26 D  360  GLY PRO PRO THR THR HIS GLN VAL VAL ALA GLY TYR ARG          
SEQRES  27 D  360  LEU ALA SER GLU THR LEU GLU VAL ARG PRO SER LYS GLY          
SEQRES  28 D  360  LEU GLN VAL PHE SER PHE THR TYR GLY                          
FORMUL   5  HOH   *486(H2 O)                                                    
HELIX    1 AA1 GLN A  383  CYS A  387  5                                   5    
HELIX    2 AA2 THR A  412  LYS A  416  5                                   5    
HELIX    3 AA3 ASP A  419  ARG A  424  5                                   6    
HELIX    4 AA4 CYS A  437  LYS A  455  1                                  19    
HELIX    5 AA5 TYR A  469  LYS A  473  5                                   5    
HELIX    6 AA6 VAL A  474  LEU A  485  1                                  12    
HELIX    7 AA7 TYR A  497  TYR A  503  1                                   7    
HELIX    8 AA8 ASP A  529  LYS A  545  1                                  17    
HELIX    9 AA9 PRO A  553  THR A  557  5                                   5    
HELIX   10 AB1 GLN B  383  CYS B  387  5                                   5    
HELIX   11 AB2 THR B  412  LYS B  416  5                                   5    
HELIX   12 AB3 ASP B  419  ARG B  424  5                                   6    
HELIX   13 AB4 CYS B  437  LYS B  455  1                                  19    
HELIX   14 AB5 TYR B  469  LYS B  473  5                                   5    
HELIX   15 AB6 VAL B  474  LEU B  485  1                                  12    
HELIX   16 AB7 TYR B  497  TYR B  503  1                                   7    
HELIX   17 AB8 ASP B  529  LYS B  545  1                                  17    
HELIX   18 AB9 PRO B  553  THR B  557  5                                   5    
HELIX   19 AC1 GLN C  383  CYS C  387  5                                   5    
HELIX   20 AC2 THR C  412  LYS C  416  5                                   5    
HELIX   21 AC3 ASP C  419  ARG C  424  5                                   6    
HELIX   22 AC4 CYS C  437  LYS C  455  1                                  19    
HELIX   23 AC5 TYR C  469  LYS C  473  5                                   5    
HELIX   24 AC6 VAL C  474  GLY C  486  1                                  13    
HELIX   25 AC7 TYR C  497  TYR C  503  1                                   7    
HELIX   26 AC8 ASP C  529  LYS C  545  1                                  17    
HELIX   27 AC9 PRO C  553  THR C  557  5                                   5    
HELIX   28 AD1 GLN D  383  CYS D  387  5                                   5    
HELIX   29 AD2 THR D  412  LYS D  416  5                                   5    
HELIX   30 AD3 ASP D  419  ARG D  424  5                                   6    
HELIX   31 AD4 CYS D  437  LYS D  455  1                                  19    
HELIX   32 AD5 TYR D  469  LYS D  473  5                                   5    
HELIX   33 AD6 VAL D  474  GLY D  486  1                                  13    
HELIX   34 AD7 TYR D  497  TYR D  503  1                                   7    
HELIX   35 AD8 ASP D  529  LYS D  545  1                                  17    
HELIX   36 AD9 PRO D  553  THR D  557  5                                   5    
SHEET    1 AA1 2 GLY A 364  THR A 365  0                                        
SHEET    2 AA1 2 TYR B 507  TRP B 508  1  O  TRP B 508   N  GLY A 364           
SHEET    1 AA2 6 GLY A 408  LEU A 410  0                                        
SHEET    2 AA2 6 ILE A 491  LEU A 493 -1  O  LEU A 493   N  GLY A 408           
SHEET    3 AA2 6 LEU A 459  HIS A 465  1  N  GLY A 463   O  ALA A 492           
SHEET    4 AA2 6 VAL A 427  TRP A 433  1  N  VAL A 427   O  ALA A 460           
SHEET    5 AA2 6 ALA A 510  ILE A 514 -1  O  ILE A 514   N  VAL A 428           
SHEET    6 AA2 6 VAL A 520  PHE A 525 -1  O  HIS A 522   N  LEU A 513           
SHEET    1 AA3 2 TYR A 507  TRP A 508  0                                        
SHEET    2 AA3 2 GLY B 364  THR B 365  1  O  GLY B 364   N  TRP A 508           
SHEET    1 AA4 4 GLY A 590  PHE A 594  0                                        
SHEET    2 AA4 4 ALA A 618  SER A 620  0                                        
SHEET    3 AA4 4 GLN A 688  GLY A 695 -1  O  VAL A 689   N  ALA A 618           
SHEET    4 AA4 4 THR A 571  TYR A 572 -1  N  THR A 571   O  PHE A 692           
SHEET    1 AA5 6 GLY A 590  PHE A 594  0                                        
SHEET    2 AA5 6 PHE A 605  LEU A 613 -1  O  TRP A 611   N  ALA A 592           
SHEET    3 AA5 6 ALA A 626  GLY A 641 -1  O  LYS A 628   N  ALA A 606           
SHEET    4 AA5 6 THR A 664  PRO A 683 -1  O  VAL A 668   N  VAL A 636           
SHEET    5 AA5 6 GLY A 644  ARG A 650 -1  N  VAL A 649   O  GLU A 680           
SHEET    6 AA5 6 LYS A 653  ILE A 659 -1  O  LEU A 657   N  LEU A 646           
SHEET    1 AA6 6 THR A 571  TYR A 572  0                                        
SHEET    2 AA6 6 GLN A 688  GLY A 695 -1  O  PHE A 692   N  THR A 571           
SHEET    3 AA6 6 ALA A 626  GLY A 641 -1  N  VAL A 639   O  PHE A 690           
SHEET    4 AA6 6 THR A 664  PRO A 683 -1  O  VAL A 668   N  VAL A 636           
SHEET    5 AA6 6 GLY A 644  ARG A 650 -1  N  VAL A 649   O  GLU A 680           
SHEET    6 AA6 6 LYS A 653  ILE A 659 -1  O  LEU A 657   N  LEU A 646           
SHEET    1 AA7 6 GLY B 408  LEU B 410  0                                        
SHEET    2 AA7 6 ILE B 491  LEU B 493 -1  O  LEU B 493   N  GLY B 408           
SHEET    3 AA7 6 LEU B 459  HIS B 465  1  N  HIS B 465   O  ALA B 492           
SHEET    4 AA7 6 VAL B 427  TRP B 433  1  N  VAL B 427   O  ALA B 460           
SHEET    5 AA7 6 ALA B 510  ILE B 514 -1  O  ILE B 514   N  VAL B 428           
SHEET    6 AA7 6 VAL B 520  PHE B 525 -1  O  ARG B 521   N  LEU B 513           
SHEET    1 AA8 4 GLY B 590  PHE B 594  0                                        
SHEET    2 AA8 4 ALA B 618  SER B 620  0                                        
SHEET    3 AA8 4 GLN B 688  GLY B 695 -1  O  VAL B 689   N  ALA B 618           
SHEET    4 AA8 4 THR B 571  TYR B 572 -1  N  THR B 571   O  PHE B 692           
SHEET    1 AA9 6 GLY B 590  PHE B 594  0                                        
SHEET    2 AA9 6 SER B 604  LEU B 613 -1  O  GLY B 609   N  PHE B 594           
SHEET    3 AA9 6 ALA B 626  GLY B 641 -1  O  ASN B 630   N  SER B 604           
SHEET    4 AA9 6 THR B 664  PRO B 683 -1  O  ALA B 675   N  ALA B 633           
SHEET    5 AA9 6 GLY B 644  VAL B 648 -1  N  THR B 647   O  ARG B 682           
SHEET    6 AA9 6 THR B 656  ILE B 659 -1  O  ILE B 659   N  GLY B 644           
SHEET    1 AB1 6 THR B 571  TYR B 572  0                                        
SHEET    2 AB1 6 GLN B 688  GLY B 695 -1  O  PHE B 692   N  THR B 571           
SHEET    3 AB1 6 ALA B 626  GLY B 641 -1  N  VAL B 639   O  PHE B 690           
SHEET    4 AB1 6 THR B 664  PRO B 683 -1  O  ALA B 675   N  ALA B 633           
SHEET    5 AB1 6 GLY B 644  VAL B 648 -1  N  THR B 647   O  ARG B 682           
SHEET    6 AB1 6 THR B 656  ILE B 659 -1  O  ILE B 659   N  GLY B 644           
SHEET    1 AB2 2 GLY C 364  THR C 365  0                                        
SHEET    2 AB2 2 TYR D 507  TRP D 508  1  O  TRP D 508   N  GLY C 364           
SHEET    1 AB3 5 ILE C 491  LEU C 493  0                                        
SHEET    2 AB3 5 LEU C 459  HIS C 465  1  N  HIS C 465   O  ALA C 492           
SHEET    3 AB3 5 VAL C 427  TRP C 433  1  N  VAL C 427   O  ALA C 460           
SHEET    4 AB3 5 ALA C 510  ILE C 514 -1  O  ILE C 514   N  VAL C 428           
SHEET    5 AB3 5 VAL C 520  PHE C 525 -1  O  ARG C 521   N  LEU C 513           
SHEET    1 AB4 2 TYR C 507  TRP C 508  0                                        
SHEET    2 AB4 2 GLY D 364  THR D 365  1  O  GLY D 364   N  TRP C 508           
SHEET    1 AB5 4 GLY C 590  PHE C 594  0                                        
SHEET    2 AB5 4 ALA C 618  SER C 620  0                                        
SHEET    3 AB5 4 GLN C 688  GLY C 695 -1  O  VAL C 689   N  ALA C 618           
SHEET    4 AB5 4 THR C 571  TYR C 572 -1  N  THR C 571   O  PHE C 692           
SHEET    1 AB6 6 GLY C 590  PHE C 594  0                                        
SHEET    2 AB6 6 SER C 604  LEU C 613 -1  O  LEU C 613   N  GLY C 590           
SHEET    3 AB6 6 ALA C 626  GLY C 641 -1  O  ALA C 626   N  ARG C 608           
SHEET    4 AB6 6 THR C 664  PRO C 683 -1  O  VAL C 668   N  VAL C 636           
SHEET    5 AB6 6 GLY C 644  ARG C 650 -1  N  VAL C 649   O  GLU C 680           
SHEET    6 AB6 6 LYS C 653  ILE C 659 -1  O  ILE C 659   N  GLY C 644           
SHEET    1 AB7 6 THR C 571  TYR C 572  0                                        
SHEET    2 AB7 6 GLN C 688  GLY C 695 -1  O  PHE C 692   N  THR C 571           
SHEET    3 AB7 6 ALA C 626  GLY C 641 -1  N  TYR C 637   O  THR C 693           
SHEET    4 AB7 6 THR C 664  PRO C 683 -1  O  VAL C 668   N  VAL C 636           
SHEET    5 AB7 6 GLY C 644  ARG C 650 -1  N  VAL C 649   O  GLU C 680           
SHEET    6 AB7 6 LYS C 653  ILE C 659 -1  O  ILE C 659   N  GLY C 644           
SHEET    1 AB8 6 GLY D 408  LEU D 410  0                                        
SHEET    2 AB8 6 ILE D 491  LEU D 493 -1  O  LEU D 493   N  GLY D 408           
SHEET    3 AB8 6 LEU D 459  HIS D 465  1  N  HIS D 465   O  ALA D 492           
SHEET    4 AB8 6 VAL D 427  TRP D 433  1  N  VAL D 427   O  ALA D 460           
SHEET    5 AB8 6 ALA D 510  ILE D 514 -1  O  ILE D 514   N  VAL D 428           
SHEET    6 AB8 6 VAL D 520  PHE D 525 -1  O  ARG D 521   N  LEU D 513           
SHEET    1 AB9 4 GLY D 590  PHE D 594  0                                        
SHEET    2 AB9 4 ALA D 618  SER D 620  0                                        
SHEET    3 AB9 4 GLN D 688  GLY D 695 -1  O  VAL D 689   N  ALA D 618           
SHEET    4 AB9 4 THR D 571  TYR D 572 -1  N  THR D 571   O  PHE D 692           
SHEET    1 AC1 6 GLY D 590  PHE D 594  0                                        
SHEET    2 AC1 6 SER D 604  LEU D 613 -1  O  GLY D 609   N  PHE D 594           
SHEET    3 AC1 6 ALA D 626  GLY D 641 -1  O  LYS D 628   N  ALA D 606           
SHEET    4 AC1 6 THR D 664  PRO D 683 -1  O  LEU D 679   N  LEU D 629           
SHEET    5 AC1 6 GLY D 644  VAL D 649 -1  N  THR D 647   O  ARG D 682           
SHEET    6 AC1 6 ALA D 655  ILE D 659 -1  O  ILE D 659   N  GLY D 644           
SHEET    1 AC2 6 THR D 571  TYR D 572  0                                        
SHEET    2 AC2 6 GLN D 688  GLY D 695 -1  O  PHE D 692   N  THR D 571           
SHEET    3 AC2 6 ALA D 626  GLY D 641 -1  N  VAL D 639   O  SER D 691           
SHEET    4 AC2 6 THR D 664  PRO D 683 -1  O  LEU D 679   N  LEU D 629           
SHEET    5 AC2 6 GLY D 644  VAL D 649 -1  N  THR D 647   O  ARG D 682           
SHEET    6 AC2 6 ALA D 655  ILE D 659 -1  O  ILE D 659   N  GLY D 644           
SSBOND   1 CYS A  387    CYS A  397                          1555   1555  2.03  
SSBOND   2 CYS B  387    CYS B  397                          1555   1555  2.03  
SSBOND   3 CYS C  387    CYS C  397                          1555   1555  2.03  
SSBOND   4 CYS C  437    CYS C  440                          1555   1555  2.05  
SSBOND   5 CYS D  387    CYS D  397                          1555   1555  2.03  
SSBOND   6 CYS D  437    CYS D  440                          1555   1555  2.05  
CISPEP   1 TRP A  508    PRO A  509          0       -12.18                     
CISPEP   2 TRP B  508    PRO B  509          0       -12.87                     
CISPEP   3 TRP C  508    PRO C  509          0       -10.91                     
CISPEP   4 TRP D  508    PRO D  509          0        -8.61                     
CRYST1  109.972  117.525  122.438  90.00  90.00  90.00 P 21 21 21   16          
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      0.009093  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008509  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008167        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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