GenomeNet

Database: PDB
Entry: 2XZL
LinkDB: 2XZL
Original site: 2XZL 
HEADER    HYDROLASE/RNA                           26-NOV-10   2XZL              
TITLE     UPF1-RNA COMPLEX                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-DEPENDENT HELICASE NAM7;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CH DOMAIN AND HELICASE DOMAIN, RESIDUES 54-850;            
COMPND   5 SYNONYM: UP FRAMESHIFT FACTOR 1, NONSENSE-MEDIATED MRNA DECAY PROTEIN
COMPND   6 1, NUCLEAR ACCOMODATION OF MITOCHONDRIA 7 PROTEIN, UP-FRAMESHIFT     
COMPND   7 SUPPRESSOR 1;                                                        
COMPND   8 EC: 3.6.4.13;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: 5- R(*UP*UP*UP*UP*UP*UP*UP*UP*U) -3;                       
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD PLYSS;                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET;                                      
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  13 ORGANISM_TAXID: 32630                                                
KEYWDS    HYDROLASE-RNA COMPLEX, NMD, RNA DEGRADATION, ALLOSTERIC REGULATION    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHAKRABARTI,U.JAYACHANDRAN,F.BONNEAU,F.FIORINI,C.BASQUIN,S.DOMCKE,  
AUTHOR   2 H.LE HIR,E.CONTI                                                     
REVDAT   2   20-DEC-23 2XZL    1       REMARK LINK                              
REVDAT   1   30-MAR-11 2XZL    0                                                
JRNL        AUTH   S.CHAKRABARTI,U.JAYACHANDRAN,F.BONNEAU,F.FIORINI,C.BASQUIN,  
JRNL        AUTH 2 S.DOMCKE,H.LE HIR,E.CONTI                                    
JRNL        TITL   MOLECULAR MECHANISMS FOR THE RNA-DEPENDENT ATPASE ACTIVITY   
JRNL        TITL 2 OF UPF1 AND ITS REGULATION BY UPF2.                          
JRNL        REF    MOL.CELL                      V.  41   693 2011              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   21419344                                                     
JRNL        DOI    10.1016/J.MOLCEL.2011.02.010                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33972                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1725                            
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 41.8883 -  5.1678    0.94     3174   177  0.1984 0.2275        
REMARK   3     2  5.1678 -  4.1030    0.97     3157   204  0.1566 0.1823        
REMARK   3     3  4.1030 -  3.5847    0.98     3243   170  0.1750 0.2122        
REMARK   3     4  3.5847 -  3.2570    0.98     3215   185  0.2012 0.2488        
REMARK   3     5  3.2570 -  3.0237    0.98     3247   175  0.2151 0.3016        
REMARK   3     6  3.0237 -  2.8454    0.98     3215   172  0.2235 0.2717        
REMARK   3     7  2.8454 -  2.7030    0.98     3265   167  0.2234 0.3128        
REMARK   3     8  2.7030 -  2.5853    0.99     3257   160  0.2168 0.2832        
REMARK   3     9  2.5853 -  2.4858    0.99     3233   152  0.2106 0.2521        
REMARK   3    10  2.4858 -  2.4000    0.99     3241   163  0.2145 0.2687        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 41.69                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.450           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27860                                             
REMARK   3    B22 (A**2) : -0.17500                                             
REMARK   3    B33 (A**2) : 0.45360                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.07570                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           6059                                  
REMARK   3   ANGLE     :  0.667           8237                                  
REMARK   3   CHIRALITY :  0.047            970                                  
REMARK   3   PLANARITY :  0.003           1002                                  
REMARK   3   DIHEDRAL  : 13.700           2208                                  
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: RESIDUES 138-143, 157-159, 213-224 261    
REMARK   3  -262 AND 283-291 ARE DISORDERED                                     
REMARK   4                                                                      
REMARK   4 2XZL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-NOV-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290046404.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : LN2 COOLED FIXED-EXIT SI(111)      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : LN2-COOLED DYNAMICALLY BENDABLE    
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33993                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
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: PDB ENTRY 2WJV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES PH 6.0, 200MM AMMONIUM          
REMARK 280  ACETATE, 20% PEG 3350                                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       57.05850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    49                                                      
REMARK 465     ALA A    50                                                      
REMARK 465     ALA A    51                                                      
REMARK 465     SER A    52                                                      
REMARK 465     MET A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     PRO A    55                                                      
REMARK 465     SER A    56                                                      
REMARK 465     ALA A    57                                                      
REMARK 465     SER A    58                                                      
REMARK 465     ASP A    59                                                      
REMARK 465     ALA A   138                                                      
REMARK 465     LYS A   139                                                      
REMARK 465     SER A   140                                                      
REMARK 465     GLU A   141                                                      
REMARK 465     ALA A   142                                                      
REMARK 465     VAL A   143                                                      
REMARK 465     ASN A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     ASN A   159                                                      
REMARK 465     ILE A   213                                                      
REMARK 465     ASN A   214                                                      
REMARK 465     ASP A   215                                                      
REMARK 465     ILE A   216                                                      
REMARK 465     ASP A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     PRO A   219                                                      
REMARK 465     GLU A   220                                                      
REMARK 465     GLU A   221                                                      
REMARK 465     GLN A   222                                                      
REMARK 465     GLU A   223                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     LEU A   262                                                      
REMARK 465     LEU A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     THR A   285                                                      
REMARK 465     PHE A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     ASN A   289                                                      
REMARK 465     GLU A   290                                                      
REMARK 465     LEU A   291                                                      
REMARK 465     SER A   323                                                      
REMARK 465     PHE A   324                                                      
REMARK 465     GLN A   325                                                      
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  68    OD1  OD2                                            
REMARK 470     LYS A  71    CD   CE   NZ                                        
REMARK 470     ASP A 114    CG   OD1  OD2                                       
REMARK 470     VAL A 119    CG1  CG2                                            
REMARK 470     GLU A 121    OE1  OE2                                            
REMARK 470     TYR A 123    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 124    CG   OD1  ND2                                       
REMARK 470     LYS A 128    NZ                                                  
REMARK 470     VAL A 136    CG1  CG2                                            
REMARK 470     SER A 137    OG                                                  
REMARK 470     VAL A 144    CG1  CG2                                            
REMARK 470     THR A 155    OG1  CG2                                            
REMARK 470     LYS A 156    CG   CD   CE   NZ                                   
REMARK 470     TRP A 160    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 160    CZ3  CH2                                            
REMARK 470     ASP A 161    CG   OD1  OD2                                       
REMARK 470     THR A 162    OG1  CG2                                            
REMARK 470     ASP A 163    CG   OD1  OD2                                       
REMARK 470     GLN A 164    CD   OE1  NE2                                       
REMARK 470     GLU A 170    CD   OE1  OE2                                       
REMARK 470     ASP A 171    OD1  OD2                                            
REMARK 470     LYS A 187    CE   NZ                                             
REMARK 470     ARG A 191    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     LYS A 204    CG   CD   CE   NZ                                   
REMARK 470     ARG A 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 208    CG   OD1  ND2                                       
REMARK 470     LYS A 209    CD   CE   NZ                                        
REMARK 470     ASP A 210    CG   OD1  OD2                                       
REMARK 470     THR A 212    OG1  CG2                                            
REMARK 470     LEU A 230    CG   CD1  CD2                                       
REMARK 470     GLN A 233    CD   OE1  NE2                                       
REMARK 470     LEU A 256    CD1  CD2                                            
REMARK 470     LYS A 257    CD   CE   NZ                                        
REMARK 470     GLU A 258    OE1  OE2                                            
REMARK 470     GLN A 260    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 263    CD   OE1  OE2                                       
REMARK 470     LEU A 271    CD1  CD2                                            
REMARK 470     ASN A 275    OD1  ND2                                            
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     VAL A 293    CG1  CG2                                            
REMARK 470     GLU A 298    OE1  OE2                                            
REMARK 470     GLU A 312    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 319    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 320    CD1  CD2                                            
REMARK 470     ASN A 322    CG   OD1  ND2                                       
REMARK 470     ASP A 326    CG   OD1  OD2                                       
REMARK 470     PHE A 328    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     GLU A 331    CD   OE1  OE2                                       
REMARK 470     LYS A 333    CE   NZ                                             
REMARK 470     SER A 335    OG                                                  
REMARK 470     LYS A 336    CG   CD   CE   NZ                                   
REMARK 470     THR A 337    OG1  CG2                                            
REMARK 470     GLU A 350    CD   OE1  OE2                                       
REMARK 470     ASP A 363    CG   OD1  OD2                                       
REMARK 470     LYS A 372    CG   CD   CE   NZ                                   
REMARK 470     GLN A 387    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 390    CG   OD1  OD2                                       
REMARK 470     ASP A 394    CG   OD1  OD2                                       
REMARK 470     LYS A 399    CG   CD   CE   NZ                                   
REMARK 470     GLU A 400    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 405    CG   OD1  ND2                                       
REMARK 470     ASN A 415    OD1  ND2                                            
REMARK 470     LYS A 478    CD   CE   NZ                                        
REMARK 470     ASP A 489    CG   OD1  OD2                                       
REMARK 470     GLU A 491    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 496    OD1  ND2                                            
REMARK 470     ARG A 505    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 508    CG   CD   CE   NZ                                   
REMARK 470     LYS A 512    CG   CD   CE   NZ                                   
REMARK 470     LYS A 516    CE   NZ                                             
REMARK 470     LYS A 518    CD   CE   NZ                                        
REMARK 470     ASP A 519    CG   OD1  OD2                                       
REMARK 470     GLU A 520    CD   OE1  OE2                                       
REMARK 470     LYS A 530    CG   CD   CE   NZ                                   
REMARK 470     ARG A 531    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 534    CG   CD   CE   NZ                                   
REMARK 470     LYS A 538    CD   CE   NZ                                        
REMARK 470     GLU A 542    CD   OE1  OE2                                       
REMARK 470     LYS A 546    CG   CD   CE   NZ                                   
REMARK 470     LYS A 560    CG   CD   CE   NZ                                   
REMARK 470     ASP A 563    CG   OD1  OD2                                       
REMARK 470     LYS A 565    CG   CD   CE   NZ                                   
REMARK 470     GLU A 573    CD   OE1  OE2                                       
REMARK 470     GLU A 581    CD   OE1  OE2                                       
REMARK 470     ARG A 609    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 610    CG   CD   CE   NZ                                   
REMARK 470     LYS A 617    CE   NZ                                             
REMARK 470     ARG A 633    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 654    CD   OE1  OE2                                       
REMARK 470     GLU A 664    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 672    CD   CE   NZ                                        
REMARK 470     ARG A 690    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 733    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 752    CG   OD1  OD2                                       
REMARK 470     LYS A 756    CE   NZ                                             
REMARK 470     GLU A 782    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 783    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 790    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 817    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 830    CD   OE1  OE2                                       
REMARK 470     ASP A 840    CG   OD1  OD2                                       
REMARK 470     GLN A 848    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 850    CG1  CG2                                            
REMARK 470       U B   9    C5'  C4'  O4'  C3'  O3'  C2'  O2'                   
REMARK 470       U B   9    C1'  N1   C2   O2   N3   C4   O4                    
REMARK 470       U B   9    C5   C6                                             
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 117       90.42    -61.83                                   
REMARK 500    ASN A 124      -81.85    -68.69                                   
REMARK 500    ASP A 210     -164.96   -125.72                                   
REMARK 500    SER A 259     -161.45   -110.11                                   
REMARK 500    HIS A 264       78.23   -118.50                                   
REMARK 500    ASN A 275       31.34     72.47                                   
REMARK 500    PRO A 404      150.23    -48.14                                   
REMARK 500    LEU A 562       59.37    -93.34                                   
REMARK 500    VAL A 587       39.58    -92.00                                   
REMARK 500    VAL A 778      -52.77     75.87                                   
REMARK 500    ALA A 780      104.82   -162.19                                   
REMARK 500    ASN A 841       59.86   -146.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1PE A 1857                                                       
REMARK 610     1PE A 1858                                                       
REMARK 610     1PE A 1859                                                       
REMARK 610     1PE A 1860                                                       
REMARK 610     1PE A 1861                                                       
REMARK 610     1PE A 1862                                                       
REMARK 610     1PE A 1863                                                       
REMARK 610     1PE A 1864                                                       
REMARK 610     1PE A 1865                                                       
REMARK 610     1PE A 1866                                                       
REMARK 610     1PE A 1867                                                       
REMARK 610     1PE A 1868                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1851  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  62   SG                                                     
REMARK 620 2 CYS A  65   SG  115.9                                              
REMARK 620 3 CYS A  84   SG  111.2 108.5                                        
REMARK 620 4 HIS A  94   ND1 113.7 111.5  93.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1852  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  76   SG                                                     
REMARK 620 2 CYS A  79   SG  107.9                                              
REMARK 620 3 HIS A  98   NE2 115.5  90.2                                        
REMARK 620 4 HIS A 104   ND1 101.1 125.4 117.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1853  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 122   SG                                                     
REMARK 620 2 CYS A 125   SG  120.9                                              
REMARK 620 3 CYS A 148   SG  106.4 100.3                                        
REMARK 620 4 CYS A 152   SG   94.3 112.5 124.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1856  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 437   OG1                                                    
REMARK 620 2 ADP A1854   O2B  88.1                                              
REMARK 620 3 HOH A2038   O    88.6 171.4                                        
REMARK 620 4 HOH A2047   O    86.1  77.8  94.0                                  
REMARK 620 5 HOH A2090   O    93.4  88.4  99.8 166.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF A1855  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A1854   O1B                                                    
REMARK 620 2 ALF A1855   F1   93.0                                              
REMARK 620 3 ALF A1855   F2   90.6  89.6                                        
REMARK 620 4 ALF A1855   F3   88.0  90.8 178.5                                  
REMARK 620 5 ALF A1855   F4   88.8 178.3  90.2  89.3                            
REMARK 620 6 HOH A2051   O   164.1 102.8  91.3  90.0  75.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1852                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1853                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1854                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 1855                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1856                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1857                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1858                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1859                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1860                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1861                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1862                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1863                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1864                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1865                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1866                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1867                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 1868                
DBREF  2XZL A   54   850  UNP    P30771   NAM7_YEAST      54    850             
DBREF  2XZL B    1     9  PDB    2XZL     2XZL             1      9             
SEQADV 2XZL GLY A   49  UNP  P30771              EXPRESSION TAG                 
SEQADV 2XZL ALA A   50  UNP  P30771              EXPRESSION TAG                 
SEQADV 2XZL ALA A   51  UNP  P30771              EXPRESSION TAG                 
SEQADV 2XZL SER A   52  UNP  P30771              EXPRESSION TAG                 
SEQADV 2XZL MET A   53  UNP  P30771              EXPRESSION TAG                 
SEQRES   1 A  802  GLY ALA ALA SER MET SER PRO SER ALA SER ASP ASN SER          
SEQRES   2 A  802  CYS ALA TYR CYS GLY ILE ASP SER ALA LYS CYS VAL ILE          
SEQRES   3 A  802  LYS CYS ASN SER CYS LYS LYS TRP PHE CYS ASN THR LYS          
SEQRES   4 A  802  ASN GLY THR SER SER SER HIS ILE VAL ASN HIS LEU VAL          
SEQRES   5 A  802  LEU SER HIS HIS ASN VAL VAL SER LEU HIS PRO ASP SER          
SEQRES   6 A  802  ASP LEU GLY ASP THR VAL LEU GLU CYS TYR ASN CYS GLY          
SEQRES   7 A  802  ARG LYS ASN VAL PHE LEU LEU GLY PHE VAL SER ALA LYS          
SEQRES   8 A  802  SER GLU ALA VAL VAL VAL LEU LEU CYS ARG ILE PRO CYS          
SEQRES   9 A  802  ALA GLN THR LYS ASN ALA ASN TRP ASP THR ASP GLN TRP          
SEQRES  10 A  802  GLN PRO LEU ILE GLU ASP ARG GLN LEU LEU SER TRP VAL          
SEQRES  11 A  802  ALA GLU GLN PRO THR GLU GLU GLU LYS LEU LYS ALA ARG          
SEQRES  12 A  802  LEU ILE THR PRO SER GLN ILE SER LYS LEU GLU ALA LYS          
SEQRES  13 A  802  TRP ARG SER ASN LYS ASP ALA THR ILE ASN ASP ILE ASP          
SEQRES  14 A  802  ALA PRO GLU GLU GLN GLU ALA ILE PRO PRO LEU LEU LEU          
SEQRES  15 A  802  ARG TYR GLN ASP ALA TYR GLU TYR GLN ARG SER TYR GLY          
SEQRES  16 A  802  PRO LEU ILE LYS LEU GLU ALA ASP TYR ASP LYS GLN LEU          
SEQRES  17 A  802  LYS GLU SER GLN ALA LEU GLU HIS ILE SER VAL SER TRP          
SEQRES  18 A  802  SER LEU ALA LEU ASN ASN ARG HIS LEU ALA SER PHE THR          
SEQRES  19 A  802  LEU SER THR PHE GLU SER ASN GLU LEU LYS VAL ALA ILE          
SEQRES  20 A  802  GLY ASP GLU MET ILE LEU TRP TYR SER GLY MET GLN HIS          
SEQRES  21 A  802  PRO ASP TRP GLU GLY ARG GLY TYR ILE VAL ARG LEU PRO          
SEQRES  22 A  802  ASN SER PHE GLN ASP THR PHE THR LEU GLU LEU LYS PRO          
SEQRES  23 A  802  SER LYS THR PRO PRO PRO THR HIS LEU THR THR GLY PHE          
SEQRES  24 A  802  THR ALA GLU PHE ILE TRP LYS GLY THR SER TYR ASP ARG          
SEQRES  25 A  802  MET GLN ASP ALA LEU LYS LYS PHE ALA ILE ASP LYS LYS          
SEQRES  26 A  802  SER ILE SER GLY TYR LEU TYR TYR LYS ILE LEU GLY HIS          
SEQRES  27 A  802  GLN VAL VAL ASP ILE SER PHE ASP VAL PRO LEU PRO LYS          
SEQRES  28 A  802  GLU PHE SER ILE PRO ASN PHE ALA GLN LEU ASN SER SER          
SEQRES  29 A  802  GLN SER ASN ALA VAL SER HIS VAL LEU GLN ARG PRO LEU          
SEQRES  30 A  802  SER LEU ILE GLN GLY PRO PRO GLY THR GLY LYS THR VAL          
SEQRES  31 A  802  THR SER ALA THR ILE VAL TYR HIS LEU SER LYS ILE HIS          
SEQRES  32 A  802  LYS ASP ARG ILE LEU VAL CYS ALA PRO SER ASN VAL ALA          
SEQRES  33 A  802  VAL ASP HIS LEU ALA ALA LYS LEU ARG ASP LEU GLY LEU          
SEQRES  34 A  802  LYS VAL VAL ARG LEU THR ALA LYS SER ARG GLU ASP VAL          
SEQRES  35 A  802  GLU SER SER VAL SER ASN LEU ALA LEU HIS ASN LEU VAL          
SEQRES  36 A  802  GLY ARG GLY ALA LYS GLY GLU LEU LYS ASN LEU LEU LYS          
SEQRES  37 A  802  LEU LYS ASP GLU VAL GLY GLU LEU SER ALA SER ASP THR          
SEQRES  38 A  802  LYS ARG PHE VAL LYS LEU VAL ARG LYS THR GLU ALA GLU          
SEQRES  39 A  802  ILE LEU ASN LYS ALA ASP VAL VAL CYS CYS THR CYS VAL          
SEQRES  40 A  802  GLY ALA GLY ASP LYS ARG LEU ASP THR LYS PHE ARG THR          
SEQRES  41 A  802  VAL LEU ILE ASP GLU SER THR GLN ALA SER GLU PRO GLU          
SEQRES  42 A  802  CYS LEU ILE PRO ILE VAL LYS GLY ALA LYS GLN VAL ILE          
SEQRES  43 A  802  LEU VAL GLY ASP HIS GLN GLN LEU GLY PRO VAL ILE LEU          
SEQRES  44 A  802  GLU ARG LYS ALA ALA ASP ALA GLY LEU LYS GLN SER LEU          
SEQRES  45 A  802  PHE GLU ARG LEU ILE SER LEU GLY HIS VAL PRO ILE ARG          
SEQRES  46 A  802  LEU GLU VAL GLN TYR ARG MET ASN PRO TYR LEU SER GLU          
SEQRES  47 A  802  PHE PRO SER ASN MET PHE TYR GLU GLY SER LEU GLN ASN          
SEQRES  48 A  802  GLY VAL THR ILE GLU GLN ARG THR VAL PRO ASN SER LYS          
SEQRES  49 A  802  PHE PRO TRP PRO ILE ARG GLY ILE PRO MET MET PHE TRP          
SEQRES  50 A  802  ALA ASN TYR GLY ARG GLU GLU ILE SER ALA ASN GLY THR          
SEQRES  51 A  802  SER PHE LEU ASN ARG ILE GLU ALA MET ASN CYS GLU ARG          
SEQRES  52 A  802  ILE ILE THR LYS LEU PHE ARG ASP GLY VAL LYS PRO GLU          
SEQRES  53 A  802  GLN ILE GLY VAL ILE THR PRO TYR GLU GLY GLN ARG ALA          
SEQRES  54 A  802  TYR ILE LEU GLN TYR MET GLN MET ASN GLY SER LEU ASP          
SEQRES  55 A  802  LYS ASP LEU TYR ILE LYS VAL GLU VAL ALA SER VAL ASP          
SEQRES  56 A  802  ALA PHE GLN GLY ARG GLU LYS ASP TYR ILE ILE LEU SER          
SEQRES  57 A  802  CYS VAL ARG ALA ASN GLU GLN GLN ALA ILE GLY PHE LEU          
SEQRES  58 A  802  ARG ASP PRO ARG ARG LEU ASN VAL GLY LEU THR ARG ALA          
SEQRES  59 A  802  LYS TYR GLY LEU VAL ILE LEU GLY ASN PRO ARG SER LEU          
SEQRES  60 A  802  ALA ARG ASN THR LEU TRP ASN HIS LEU LEU ILE HIS PHE          
SEQRES  61 A  802  ARG GLU LYS GLY CYS LEU VAL GLU GLY THR LEU ASP ASN          
SEQRES  62 A  802  LEU GLN LEU CYS THR VAL GLN LEU VAL                          
SEQRES   1 B    9    U   U   U   U   U   U   U   U   U                          
HET     ZN  A1851       1                                                       
HET     ZN  A1852       1                                                       
HET     ZN  A1853       1                                                       
HET    ADP  A1854      27                                                       
HET    ALF  A1855       5                                                       
HET     MG  A1856       1                                                       
HET    1PE  A1857      10                                                       
HET    1PE  A1858      13                                                       
HET    1PE  A1859       7                                                       
HET    1PE  A1860       7                                                       
HET    1PE  A1861      10                                                       
HET    1PE  A1862       7                                                       
HET    1PE  A1863       7                                                       
HET    1PE  A1864       7                                                       
HET    1PE  A1865       7                                                       
HET    1PE  A1866       7                                                       
HET    1PE  A1867       7                                                       
HET    1PE  A1868       7                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   3   ZN    3(ZN 2+)                                                     
FORMUL   6  ADP    C10 H15 N5 O10 P2                                            
FORMUL   7  ALF    AL F4 1-                                                     
FORMUL   8   MG    MG 2+                                                        
FORMUL   9  1PE    12(C10 H22 O6)                                               
FORMUL  21  HOH   *96(H2 O)                                                     
HELIX    1   1 SER A   93  HIS A  103  1                                  11    
HELIX    2   2 ASP A  161  TRP A  165  5                                   5    
HELIX    3   3 GLU A  185  ALA A  190  5                                   6    
HELIX    4   4 THR A  194  ARG A  206  1                                  13    
HELIX    5   5 ASP A  234  GLU A  258  1                                  25    
HELIX    6   6 GLY A  355  ASP A  371  1                                  17    
HELIX    7   7 SER A  376  GLY A  385  1                                  10    
HELIX    8   8 ASN A  410  LEU A  421  1                                  12    
HELIX    9   9 GLY A  435  LYS A  452  1                                  18    
HELIX   10  10 SER A  461  LEU A  475  1                                  15    
HELIX   11  11 ALA A  484  GLU A  488  5                                   5    
HELIX   12  12 VAL A  494  LEU A  497  5                                   4    
HELIX   13  13 ALA A  498  ARG A  505  1                                   8    
HELIX   14  14 GLY A  509  GLY A  522  1                                  14    
HELIX   15  15 SER A  525  LYS A  546  1                                  22    
HELIX   16  16 VAL A  555  ASP A  559  5                                   5    
HELIX   17  17 GLU A  573  ALA A  577  5                                   5    
HELIX   18  18 SER A  578  VAL A  587  1                                  10    
HELIX   19  19 GLU A  608  ALA A  614  1                                   7    
HELIX   20  20 SER A  619  LEU A  627  1                                   9    
HELIX   21  21 ASN A  641  TYR A  653  1                                  13    
HELIX   22  22 ASN A  702  ASP A  719  1                                  18    
HELIX   23  23 LYS A  722  GLU A  724  5                                   3    
HELIX   24  24 TYR A  732  GLY A  747  1                                  16    
HELIX   25  25 ASP A  750  LYS A  756  1                                   7    
HELIX   26  26 VAL A  762  GLN A  766  1                                   5    
HELIX   27  27 ILE A  786  ARG A  790  5                                   5    
HELIX   28  28 ASP A  791  THR A  800  1                                  10    
HELIX   29  29 ASN A  811  ALA A  816  1                                   6    
HELIX   30  30 ASN A  818  GLY A  832  1                                  15    
SHEET    1  AA 3 TRP A  82  CYS A  84  0                                        
SHEET    2  AA 3 VAL A  73  CYS A  76 -1  O  ILE A  74   N  PHE A  83           
SHEET    3  AA 3 VAL A 107  LEU A 109 -1  O  SER A 108   N  LYS A  75           
SHEET    1  AB 3 VAL A 145  CYS A 148  0                                        
SHEET    2  AB 3 LEU A 133  VAL A 136 -1  O  GLY A 134   N  LEU A 147           
SHEET    3  AB 3 GLN A 166  PRO A 167 -1  O  GLN A 166   N  PHE A 135           
SHEET    1  AC 6 VAL A 267  LEU A 271  0                                        
SHEET    2  AC 6 HIS A 277  PHE A 281 -1  O  LEU A 278   N  SER A 270           
SHEET    3  AC 6 PHE A 328  LEU A 332 -1  O  PHE A 328   N  PHE A 281           
SHEET    4  AC 6 TRP A 311  ARG A 319 -1  O  TYR A 316   N  GLU A 331           
SHEET    5  AC 6 GLU A 298  TYR A 303 -1  O  MET A 299   N  GLY A 315           
SHEET    6  AC 6 PHE A 347  PHE A 351 -1  O  THR A 348   N  TRP A 302           
SHEET    1  AD 7 VAL A 479  ARG A 481  0                                        
SHEET    2  AD 7 VAL A 549  THR A 553  1  O  VAL A 549   N  VAL A 480           
SHEET    3  AD 7 ILE A 455  ALA A 459  1  O  ILE A 455   N  VAL A 550           
SHEET    4  AD 7 THR A 568  ILE A 571  1  O  THR A 568   N  LEU A 456           
SHEET    5  AD 7 GLN A 592  GLY A 597  1  O  GLN A 592   N  VAL A 569           
SHEET    6  AD 7 LEU A 425  GLN A 429  1  O  SER A 426   N  LEU A 595           
SHEET    7  AD 7 ILE A 632  ARG A 633  1  O  ILE A 632   N  GLN A 429           
SHEET    1  AE 2 VAL A 636  GLN A 637  0                                        
SHEET    2  AE 2 GLN A 658  ASN A 659  1  O  GLN A 658   N  GLN A 637           
SHEET    1  AF 7 GLU A 758  SER A 761  0                                        
SHEET    2  AF 7 ILE A 726  THR A 730  1  O  ILE A 726   N  GLU A 758           
SHEET    3  AF 7 LYS A 770  SER A 776  1  O  TYR A 772   N  GLY A 727           
SHEET    4  AF 7 ALA A 802  GLY A 810  1  N  LYS A 803   O  LYS A 770           
SHEET    5  AF 7 MET A 682  ALA A 686  1  O  MET A 683   N  ILE A 808           
SHEET    6  AF 7 LEU A 834  THR A 838  1  O  VAL A 835   N  ALA A 686           
SHEET    7  AF 7 ASN A 841  LEU A 844 -1  O  ASN A 841   N  THR A 838           
SHEET    1  AG 2 GLU A 692  ILE A 693  0                                        
SHEET    2  AG 2 PHE A 700  LEU A 701 -1  O  LEU A 701   N  GLU A 692           
LINK         SG  CYS A  62                ZN    ZN A1851     1555   1555  2.47  
LINK         SG  CYS A  65                ZN    ZN A1851     1555   1555  2.57  
LINK         SG  CYS A  76                ZN    ZN A1852     1555   1555  2.52  
LINK         SG  CYS A  79                ZN    ZN A1852     1555   1555  2.66  
LINK         SG  CYS A  84                ZN    ZN A1851     1555   1555  2.56  
LINK         ND1 HIS A  94                ZN    ZN A1851     1555   1555  2.20  
LINK         NE2 HIS A  98                ZN    ZN A1852     1555   1555  2.21  
LINK         ND1 HIS A 104                ZN    ZN A1852     1555   1555  2.27  
LINK         SG  CYS A 122                ZN    ZN A1853     1555   1555  2.66  
LINK         SG  CYS A 125                ZN    ZN A1853     1555   1555  2.59  
LINK         SG  CYS A 148                ZN    ZN A1853     1555   1555  2.65  
LINK         SG  CYS A 152                ZN    ZN A1853     1555   1555  2.56  
LINK         OG1 THR A 437                MG    MG A1856     1555   1555  2.40  
LINK         O1B ADP A1854                AL   ALF A1855     1555   1555  2.16  
LINK         O2B ADP A1854                MG    MG A1856     1555   1555  2.52  
LINK        AL   ALF A1855                 O   HOH A2051     1555   1555  2.25  
LINK        MG    MG A1856                 O   HOH A2038     1555   1555  2.55  
LINK        MG    MG A1856                 O   HOH A2047     1555   1555  2.77  
LINK        MG    MG A1856                 O   HOH A2090     1555   1555  2.51  
CISPEP   1 ILE A  150    PRO A  151          0         3.43                     
SITE     1 AC1  4 CYS A  62  CYS A  65  CYS A  84  HIS A  94                    
SITE     1 AC2  4 CYS A  76  CYS A  79  HIS A  98  HIS A 104                    
SITE     1 AC3  4 CYS A 122  CYS A 125  CYS A 148  CYS A 152                    
SITE     1 AC4 15 GLN A 408  GLN A 413  GLY A 433  THR A 434                    
SITE     2 AC4 15 GLY A 435  LYS A 436  THR A 437  VAL A 438                    
SITE     3 AC4 15 TYR A 638  ARG A 639  GLU A 769  ALF A1855                    
SITE     4 AC4 15  MG A1856  HOH A2090  HOH A2091                               
SITE     1 AC5 11 PRO A 432  GLY A 433  LYS A 436  GLN A 601                    
SITE     2 AC5 11 ARG A 639  GLY A 767  ARG A 801  ADP A1854                    
SITE     3 AC5 11  MG A1856  HOH A2047  HOH A2051                               
SITE     1 AC6  6 THR A 437  ADP A1854  ALF A1855  HOH A2038                    
SITE     2 AC6  6 HOH A2047  HOH A2090                                          
SITE     1 AC7  3 GLY A 377  TYR A 381  ARG A 678                               
SITE     1 AC8  5 GLY A 720  LYS A 722  GLN A 725  ASP A 771                    
SITE     2 AC8  5 TYR A 804                                                     
SITE     1 AC9 10 ALA A 369  ILE A 370  SER A 671  LYS A 672                    
SITE     2 AC9 10 PHE A 673  TRP A 675  PRO A 676  ILE A 677                    
SITE     3 AC9 10 ARG A 678  1PE A1863                                          
SITE     1 BC1  5 PHE A 647  ASN A 650  MET A 651  HIS A 823                    
SITE     2 BC1  5 HIS A 827                                                     
SITE     1 BC2  3 GLN A 362  ASN A 841  GLN A 843                               
SITE     1 BC3  7 ARG A 829  LEU A 834  LEU A 844  CYS A 845                    
SITE     2 BC3  7 VAL A 847  LEU A 849  HOH A2086                               
SITE     1 BC4  9 ASN A 641  ILE A 663  THR A 667  TRP A 675                    
SITE     2 BC4  9 ILE A 677  GLY A 679  ILE A 680  PRO A 681                    
SITE     3 BC4  9 1PE A1859                                                     
SITE     1 BC5  9 HIS A 419  ARG A 423  LEU A 425  SER A 426                    
SITE     2 BC5  9 LEU A 427  HIS A 629  VAL A 630  PRO A 631                    
SITE     3 BC5  9 ILE A 632                                                     
SITE     1 BC6  5 PHE A 393  HIS A 451  ASP A 453  LYS A 591                    
SITE     2 BC6  5 GLN A 592                                                     
SITE     1 BC7  5 SER A 412  ASN A 415  ALA A 416  ILE A 632                    
SITE     2 BC7  5 ARG A 633                                                     
SITE     1 BC8  5 LYS A 367  ASP A 371  LYS A 373  THR A 564                    
SITE     2 BC8  5 LYS A 588                                                     
SITE     1 BC9  4 LYS A 372  ILE A 375  SER A 376  GLY A 589                    
CRYST1   64.135  114.117   65.730  90.00 110.24  90.00 P 1 21 1      2          
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      0.015592  0.000000  0.005749        0.00000                         
SCALE2      0.000000  0.008763  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016215        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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