GenomeNet

Database: PDB
Entry: 4Q26
LinkDB: 4Q26
Original site: 4Q26 
HEADER    SUGAR BINDING PROTEIN                   07-APR-14   4Q26              
TITLE     CRYSTAL STRUCTURE OF GALECTIN-1 IN COMPLEX WITH N-ACETYLLACTOSAMINE   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GALECTIN-1;                                                
COMPND   3 CHAIN: A, B, G, H;                                                   
COMPND   4 SYNONYM: GAL-1, 14 KDA LAMININ-BINDING PROTEIN, HLBP14, 14 KDA       
COMPND   5 LECTIN, BETA-GALACTOSIDE-BINDING LECTIN L-14-I, GALAPTIN, HBL, HPL,  
COMPND   6 LACTOSE-BINDING LECTIN 1, LECTIN GALACTOSIDE-BINDING SOLUBLE 1,      
COMPND   7 PUTATIVE MAPK-ACTIVATING PROTEIN PM12, S-LAC LECTIN 1;               
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LGALS1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUGAR BINDING PROTEIN                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GRIMM,N.BERTLEFF-ZIESCHANG                                          
REVDAT   1   07-OCT-15 4Q26    0                                                
JRNL        AUTH   C.GRIMM,N.BERTLEFF-ZIESCHANG                                 
JRNL        TITL   CRYSTAL STRUCTURE OF GALECTIN-1 IN COMPLEX WITH              
JRNL        TITL 2 N-ACETYLLACTOSAMINE                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 129632                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.540                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 48.0511 -  3.3709    0.93     8964   141  0.1809 0.2063        
REMARK   3     2  3.3709 -  2.6757    1.00     9315   145  0.1483 0.1730        
REMARK   3     3  2.6757 -  2.3375    1.00     9270   146  0.1495 0.1845        
REMARK   3     4  2.3375 -  2.1237    1.00     9190   144  0.1268 0.2047        
REMARK   3     5  2.1237 -  1.9715    1.00     9184   144  0.1245 0.1752        
REMARK   3     6  1.9715 -  1.8553    1.00     9163   143  0.1241 0.1757        
REMARK   3     7  1.8553 -  1.7624    1.00     9153   144  0.1329 0.1816        
REMARK   3     8  1.7624 -  1.6856    1.00     9147   143  0.1442 0.2225        
REMARK   3     9  1.6856 -  1.6207    1.00     9075   142  0.1574 0.2257        
REMARK   3    10  1.6207 -  1.5648    1.00     9140   143  0.1729 0.2484        
REMARK   3    11  1.5648 -  1.5159    1.00     9105   143  0.2000 0.2333        
REMARK   3    12  1.5159 -  1.4725    1.00     9063   142  0.2442 0.2684        
REMARK   3    13  1.4725 -  1.4338    1.00     9130   143  0.2836 0.3342        
REMARK   3    14  1.4338 -  1.3990    0.96     8733   137  0.3656 0.3976        
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              : 0.43                                          
REMARK   3   B_SOL              : 45.46                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.620           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.48560                                             
REMARK   3    B22 (A**2) : 4.44180                                              
REMARK   3    B33 (A**2) : -1.95620                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
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      :  0.018           4519                                  
REMARK   3   ANGLE     :  2.023           6158                                  
REMARK   3   CHIRALITY :  0.132            689                                  
REMARK   3   PLANARITY :  0.010            819                                  
REMARK   3   DIHEDRAL  : 19.827           1696                                  
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 4Q26 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085509.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129682                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.399                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.023                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 16.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       33.19200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.75850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.19200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.75850            
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, 3, 4, 5, 6                                        
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 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 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 399  LIES ON A SPECIAL POSITION.                          
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    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLY G    -1                                                      
REMARK 465     MET G     0                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     GLY H    -1                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ALA H     1                                                      
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     CYS A   2    SG                                                  
REMARK 470     CYS B   2    SG                                                  
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  HH22  ARG G    18     O    HOH G   429              1.05            
REMARK 500  HH21  ARG G    18     O    HOH G   331              1.48            
REMARK 500   H    ALA A    75     O    HOH A   425              1.56            
REMARK 500   HZ1  LYS H   127     O    HOH H   347              1.58            
REMARK 500   OE2  GLU G    71     HB   NLC G   202              1.58            
REMARK 500   O    HOH G   431     O    HOH G   432              1.81            
REMARK 500   NH2  ARG G    18     O    HOH G   429              1.85            
REMARK 500   O    GLY G    82     O    HOH G   433              1.86            
REMARK 500   O    HOH A   356     O    HOH A   408              1.89            
REMARK 500   OE1  GLU A    74     O    HOH A   406              1.89            
REMARK 500   O    HOH H   329     O    HOH H   340              1.91            
REMARK 500   OD1  ASN B    50     O    HOH B   386              1.92            
REMARK 500   O    HOH G   308     O    HOH G   406              1.93            
REMARK 500   O    HOH B   402     O    HOH B   409              1.94            
REMARK 500   O    HOH A   397     O    HOH A   422              1.94            
REMARK 500   O    HOH G   360     O    HOH G   430              1.94            
REMARK 500   N    ASN G   113     O    HOH G   408              1.97            
REMARK 500   O    HOH A   365     O    HOH A   388              2.01            
REMARK 500   O    HIS G    52     O    HOH G   330              2.02            
REMARK 500   OD2  ASP H   102     O    HOH H   366              2.05            
REMARK 500   O    HOH A   329     O    HOH A   417              2.05            
REMARK 500   OD1  ASP G   123     O    HOH G   390              2.07            
REMARK 500   O    HOH G   385     O    HOH G   414              2.08            
REMARK 500   O    HOH G   378     O    HOH G   409              2.09            
REMARK 500   O    HOH H   401     O    HOH H   403              2.12            
REMARK 500   O    HOH H   377     O    HOH H   385              2.12            
REMARK 500   N    CYS B     2     O    HOH B   380              2.12            
REMARK 500   O    LEU G   114     O    HOH G   424              2.15            
REMARK 500   O    HOH G   411     O    HOH H   359              2.15            
REMARK 500   O    HOH G   398     O    HOH G   399              2.17            
REMARK 500   CA   ASN G   113     O    HOH G   408              2.18            
REMARK 500   O    HOH A   428     O    HOH A   431              2.18            
REMARK 500   O    HOH A   381     O    HOH A   414              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG H    20     O    HOH H   321     4455     0.72            
REMARK 500  HH22  ARG H    20     O    HOH H   321     4455     0.95            
REMARK 500   HB1  ALA A    75     HB3  ASP G   102     1655     1.33            
REMARK 500   CZ   ARG H    20     O    HOH H   321     4455     1.33            
REMARK 500  HH21  ARG H    20     O    HOH H   321     4455     1.40            
REMARK 500   O    HOH A   375     O    HOH B   361     4554     1.96            
REMARK 500   NH1  ARG H    20     O    HOH H   321     4455     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP G 123   C     ASP G 123   O       0.117                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE A 133   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    ASP G 125   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
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    ASN A  50       93.96   -162.74                                   
REMARK 500    PHE A 133       79.71   -116.49                                   
REMARK 500    PHE B  77       82.18   -150.45                                   
REMARK 500    PRO B  78       48.09    -94.12                                   
REMARK 500    PRO G  78       53.19    -93.16                                   
REMARK 500    PHE G 133       69.50   -114.25                                   
REMARK 500    ASP H  26       -2.59     71.75                                   
REMARK 500    ASN H  50       88.56   -156.39                                   
REMARK 500    ASN H  56       59.07     36.71                                   
REMARK 500    PRO H  78       51.90    -90.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP G  123     GLY G  124                  125.89                    
REMARK 500 PHE G  133     ASP G  134                 -136.65                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A 134        16.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP G 134         9.8      L          L   EXPECTING SP3           
REMARK 500    ALA H  75        17.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NLC A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NLC B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NLC G 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NLC H 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Q1P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Q1R   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Q27   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Q2F   RELATED DB: PDB                                   
DBREF  4Q26 A    0   134  UNP    P09382   LEG1_HUMAN       1    135             
DBREF  4Q26 B    0   134  UNP    P09382   LEG1_HUMAN       1    135             
DBREF  4Q26 G    0   134  UNP    P09382   LEG1_HUMAN       1    135             
DBREF  4Q26 H    0   134  UNP    P09382   LEG1_HUMAN       1    135             
SEQADV 4Q26 GLY A   -1  UNP  P09382              EXPRESSION TAG                 
SEQADV 4Q26 GLY B   -1  UNP  P09382              EXPRESSION TAG                 
SEQADV 4Q26 GLY G   -1  UNP  P09382              EXPRESSION TAG                 
SEQADV 4Q26 GLY H   -1  UNP  P09382              EXPRESSION TAG                 
SEQRES   1 A  136  GLY MET ALA CYS GLY LEU VAL ALA SER ASN LEU ASN LEU          
SEQRES   2 A  136  LYS PRO GLY GLU CME LEU ARG VAL ARG GLY GLU VAL ALA          
SEQRES   3 A  136  PRO ASP ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP          
SEQRES   4 A  136  SER ASN ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN          
SEQRES   5 A  136  ALA HIS GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS          
SEQRES   6 A  136  ASP GLY GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL          
SEQRES   7 A  136  PHE PRO PHE GLN PRO GLY SER VAL ALA GLU VAL CME ILE          
SEQRES   8 A  136  THR PHE ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP          
SEQRES   9 A  136  GLY TYR GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU          
SEQRES  10 A  136  ALA ILE ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE          
SEQRES  11 A  136  LYS CME VAL ALA PHE ASP                                      
SEQRES   1 B  136  GLY MET ALA CYS GLY LEU VAL ALA SER ASN LEU ASN LEU          
SEQRES   2 B  136  LYS PRO GLY GLU CME LEU ARG VAL ARG GLY GLU VAL ALA          
SEQRES   3 B  136  PRO ASP ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP          
SEQRES   4 B  136  SER ASN ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN          
SEQRES   5 B  136  ALA HIS GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS          
SEQRES   6 B  136  ASP GLY GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL          
SEQRES   7 B  136  PHE PRO PHE GLN PRO GLY SER VAL ALA GLU VAL CME ILE          
SEQRES   8 B  136  THR PHE ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP          
SEQRES   9 B  136  GLY TYR GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU          
SEQRES  10 B  136  ALA ILE ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE          
SEQRES  11 B  136  LYS CME VAL ALA PHE ASP                                      
SEQRES   1 G  136  GLY MET ALA CYS GLY LEU VAL ALA SER ASN LEU ASN LEU          
SEQRES   2 G  136  LYS PRO GLY GLU CME LEU ARG VAL ARG GLY GLU VAL ALA          
SEQRES   3 G  136  PRO ASP ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP          
SEQRES   4 G  136  SER ASN ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN          
SEQRES   5 G  136  ALA HIS GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS          
SEQRES   6 G  136  ASP GLY GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL          
SEQRES   7 G  136  PHE PRO PHE GLN PRO GLY SER VAL ALA GLU VAL CME ILE          
SEQRES   8 G  136  THR PHE ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP          
SEQRES   9 G  136  GLY TYR GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU          
SEQRES  10 G  136  ALA ILE ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE          
SEQRES  11 G  136  LYS CME VAL ALA PHE ASP                                      
SEQRES   1 H  136  GLY MET ALA CYS GLY LEU VAL ALA SER ASN LEU ASN LEU          
SEQRES   2 H  136  LYS PRO GLY GLU CME LEU ARG VAL ARG GLY GLU VAL ALA          
SEQRES   3 H  136  PRO ASP ALA LYS SER PHE VAL LEU ASN LEU GLY LYS ASP          
SEQRES   4 H  136  SER ASN ASN LEU CYS LEU HIS PHE ASN PRO ARG PHE ASN          
SEQRES   5 H  136  ALA HIS GLY ASP ALA ASN THR ILE VAL CYS ASN SER LYS          
SEQRES   6 H  136  ASP GLY GLY ALA TRP GLY THR GLU GLN ARG GLU ALA VAL          
SEQRES   7 H  136  PHE PRO PHE GLN PRO GLY SER VAL ALA GLU VAL CME ILE          
SEQRES   8 H  136  THR PHE ASP GLN ALA ASN LEU THR VAL LYS LEU PRO ASP          
SEQRES   9 H  136  GLY TYR GLU PHE LYS PHE PRO ASN ARG LEU ASN LEU GLU          
SEQRES  10 H  136  ALA ILE ASN TYR MET ALA ALA ASP GLY ASP PHE LYS ILE          
SEQRES  11 H  136  LYS CME VAL ALA PHE ASP                                      
MODRES 4Q26 CME A   16  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME A   88  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME A  130  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME B   16  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME B   88  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME B  130  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME G   16  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME G   88  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME G  130  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME H   16  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME H   88  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
MODRES 4Q26 CME H  130  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A  16      10                                                       
HET    CME  A  88      10                                                       
HET    CME  A 130      10                                                       
HET    CME  B  16      10                                                       
HET    CME  B  88      10                                                       
HET    CME  B 130      10                                                       
HET    CME  G  16      10                                                       
HET    CME  G  88      10                                                       
HET    CME  G 130      10                                                       
HET    CME  H  16      10                                                       
HET    CME  H  88      10                                                       
HET    CME  H 130      10                                                       
HET    NLC  A 201      51                                                       
HET    NLC  B 201      51                                                       
HET    GOL  G 201      14                                                       
HET    NLC  G 202      51                                                       
HET    NLC  H 201      51                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     NLC 2-(ACETYLAMINO)-2-DEOXY-4-O-BETA-D-GALACTOPYRANOSYL-             
HETNAM   2 NLC  ALPHA-D-GLUCOPYRANOSE                                           
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CME    12(C5 H11 N O3 S2)                                           
FORMUL   5  NLC    4(C14 H25 N O11)                                             
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *495(H2 O)                                                    
SHEET    1   A12 ALA A  67  TRP A  68  0                                        
SHEET    2   A12 ASP A  54  ASP A  64 -1  N  ASP A  64   O  ALA A  67           
SHEET    3   A12 ASN A  40  ALA A  51 -1  N  HIS A  44   O  ASN A  61           
SHEET    4   A12 LEU A  32  ASP A  37 -1  N  LYS A  36   O  ASN A  40           
SHEET    5   A12 ILE A 117  ALA A 122 -1  O  ALA A 121   N  ASN A  33           
SHEET    6   A12 VAL A   5  LEU A  11 -1  N  ALA A   6   O  MET A 120           
SHEET    7   A12 VAL B   5  LEU B  11 -1  O  SER B   7   N  VAL A   5           
SHEET    8   A12 ILE B 117  ALA B 122 -1  O  MET B 120   N  ALA B   6           
SHEET    9   A12 LEU B  32  ASP B  37 -1  N  ASN B  33   O  ALA B 121           
SHEET   10   A12 ASN B  40  ALA B  51 -1  O  PHE B  45   N  LEU B  32           
SHEET   11   A12 ASP B  54  ASP B  64 -1  O  ASN B  61   N  HIS B  44           
SHEET   12   A12 ALA B  67  TRP B  68 -1  O  ALA B  67   N  ASP B  64           
SHEET    1   B12 GLN A  72  ARG A  73  0                                        
SHEET    2   B12 ASP A  54  ASP A  64 -1  N  CYS A  60   O  GLN A  72           
SHEET    3   B12 ASN A  40  ALA A  51 -1  N  HIS A  44   O  ASN A  61           
SHEET    4   B12 LEU A  32  ASP A  37 -1  N  LYS A  36   O  ASN A  40           
SHEET    5   B12 ILE A 117  ALA A 122 -1  O  ALA A 121   N  ASN A  33           
SHEET    6   B12 VAL A   5  LEU A  11 -1  N  ALA A   6   O  MET A 120           
SHEET    7   B12 VAL B   5  LEU B  11 -1  O  SER B   7   N  VAL A   5           
SHEET    8   B12 ILE B 117  ALA B 122 -1  O  MET B 120   N  ALA B   6           
SHEET    9   B12 LEU B  32  ASP B  37 -1  N  ASN B  33   O  ALA B 121           
SHEET   10   B12 ASN B  40  ALA B  51 -1  O  PHE B  45   N  LEU B  32           
SHEET   11   B12 ASP B  54  ASP B  64 -1  O  ASN B  61   N  HIS B  44           
SHEET   12   B12 GLN B  72  ARG B  73 -1  O  GLN B  72   N  CYS B  60           
SHEET    1   C10 GLU A 105  PRO A 109  0                                        
SHEET    2   C10 ASN A  95  LYS A  99 -1  N  LEU A  96   O  PHE A 108           
SHEET    3   C10 VAL A  84  PHE A  91 -1  N  CME A  88   O  LYS A  99           
SHEET    4   C10 LEU A  17  VAL A  23 -1  N  LEU A  17   O  ILE A  89           
SHEET    5   C10 PHE A 126  PHE A 133 -1  O  LYS A 129   N  ARG A  20           
SHEET    6   C10 PHE B 126  ASP B 134 -1  O  LYS B 129   N  PHE A 133           
SHEET    7   C10 CME B  16  VAL B  23 -1  N  ARG B  20   O  LYS B 129           
SHEET    8   C10 VAL B  84  PHE B  91 -1  O  ALA B  85   N  GLY B  21           
SHEET    9   C10 ASN B  95  LYS B  99 -1  O  LYS B  99   N  CME B  88           
SHEET   10   C10 GLU B 105  PRO B 109 -1  O  PHE B 108   N  LEU B  96           
SHEET    1   D12 ALA G  67  TRP G  68  0                                        
SHEET    2   D12 ASP G  54  ASP G  64 -1  N  ASP G  64   O  ALA G  67           
SHEET    3   D12 ASN G  40  ALA G  51 -1  N  ARG G  48   O  THR G  57           
SHEET    4   D12 VAL G  31  ASP G  37 -1  N  LYS G  36   O  ASN G  40           
SHEET    5   D12 ILE G 117  ASP G 123 -1  O  ALA G 121   N  ASN G  33           
SHEET    6   D12 VAL G   5  LEU G  11 -1  N  ALA G   6   O  MET G 120           
SHEET    7   D12 VAL H   5  SER H   7 -1  O  SER H   7   N  VAL G   5           
SHEET    8   D12 TYR H 119  ALA H 122 -1  O  MET H 120   N  ALA H   6           
SHEET    9   D12 LEU H  32  ASP H  37 -1  N  ASN H  33   O  ALA H 121           
SHEET   10   D12 ASN H  40  ALA H  51 -1  O  ASN H  40   N  LYS H  36           
SHEET   11   D12 ASP H  54  ASP H  64 -1  O  ASN H  61   N  HIS H  44           
SHEET   12   D12 ALA H  67  TRP H  68 -1  O  ALA H  67   N  ASP H  64           
SHEET    1   E12 GLN G  72  GLU G  74  0                                        
SHEET    2   E12 ASP G  54  ASP G  64 -1  N  CYS G  60   O  GLN G  72           
SHEET    3   E12 ASN G  40  ALA G  51 -1  N  ARG G  48   O  THR G  57           
SHEET    4   E12 VAL G  31  ASP G  37 -1  N  LYS G  36   O  ASN G  40           
SHEET    5   E12 ILE G 117  ASP G 123 -1  O  ALA G 121   N  ASN G  33           
SHEET    6   E12 VAL G   5  LEU G  11 -1  N  ALA G   6   O  MET G 120           
SHEET    7   E12 VAL H   5  SER H   7 -1  O  SER H   7   N  VAL G   5           
SHEET    8   E12 TYR H 119  ALA H 122 -1  O  MET H 120   N  ALA H   6           
SHEET    9   E12 LEU H  32  ASP H  37 -1  N  ASN H  33   O  ALA H 121           
SHEET   10   E12 ASN H  40  ALA H  51 -1  O  ASN H  40   N  LYS H  36           
SHEET   11   E12 ASP H  54  ASP H  64 -1  O  ASN H  61   N  HIS H  44           
SHEET   12   E12 GLN H  72  GLU H  74 -1  O  GLN H  72   N  CYS H  60           
SHEET    1   F10 GLU G 105  PRO G 109  0                                        
SHEET    2   F10 ASN G  95  LYS G  99 -1  N  LEU G  96   O  PHE G 108           
SHEET    3   F10 SER G  83  PHE G  91 -1  N  CME G  88   O  LYS G  99           
SHEET    4   F10 LEU G  17  VAL G  23 -1  N  LEU G  17   O  ILE G  89           
SHEET    5   F10 PHE G 126  PHE G 133 -1  O  LYS G 127   N  GLU G  22           
SHEET    6   F10 PHE H 126  ASP H 134 -1  O  PHE H 133   N  LYS G 129           
SHEET    7   F10 CME H  16  VAL H  23 -1  N  CME H  16   O  ASP H 134           
SHEET    8   F10 VAL H  84  PHE H  91 -1  O  ALA H  85   N  GLY H  21           
SHEET    9   F10 ASN H  95  LYS H  99 -1  O  LYS H  99   N  CME H  88           
SHEET   10   F10 GLU H 105  PRO H 109 -1  O  PHE H 108   N  LEU H  96           
LINK         C   GLU A  15                 N   CME A  16     1555   1555  1.33  
LINK         C   CME A  16                 N   LEU A  17     1555   1555  1.32  
LINK         C  AVAL A  87                 N   CME A  88     1555   1555  1.32  
LINK         C  BVAL A  87                 N   CME A  88     1555   1555  1.31  
LINK         C   CME A  88                 N   ILE A  89     1555   1555  1.33  
LINK         C   LYS A 129                 N   CME A 130     1555   1555  1.33  
LINK         C   CME A 130                 N  AVAL A 131     1555   1555  1.32  
LINK         C   CME A 130                 N  BVAL A 131     1555   1555  1.32  
LINK         C   GLU B  15                 N   CME B  16     1555   1555  1.33  
LINK         C   CME B  16                 N   LEU B  17     1555   1555  1.31  
LINK         C  AVAL B  87                 N   CME B  88     1555   1555  1.33  
LINK         C  BVAL B  87                 N   CME B  88     1555   1555  1.33  
LINK         C   CME B  88                 N   ILE B  89     1555   1555  1.34  
LINK         C   LYS B 129                 N   CME B 130     1555   1555  1.37  
LINK         C   CME B 130                 N   VAL B 131     1555   1555  1.32  
LINK         C   GLU G  15                 N   CME G  16     1555   1555  1.34  
LINK         C   CME G  16                 N   LEU G  17     1555   1555  1.34  
LINK         C  AVAL G  87                 N   CME G  88     1555   1555  1.33  
LINK         C  BVAL G  87                 N   CME G  88     1555   1555  1.32  
LINK         C   CME G  88                 N   ILE G  89     1555   1555  1.33  
LINK         C   LYS G 129                 N   CME G 130     1555   1555  1.33  
LINK         C   CME G 130                 N  AVAL G 131     1555   1555  1.33  
LINK         C   CME G 130                 N  BVAL G 131     1555   1555  1.33  
LINK         C   GLU H  15                 N   CME H  16     1555   1555  1.33  
LINK         C   CME H  16                 N   LEU H  17     1555   1555  1.32  
LINK         C  AVAL H  87                 N   CME H  88     1555   1555  1.33  
LINK         C  BVAL H  87                 N   CME H  88     1555   1555  1.34  
LINK         C   CME H  88                 N   ILE H  89     1555   1555  1.32  
LINK         C   LYS H 129                 N   CME H 130     1555   1555  1.35  
LINK         C   CME H 130                 N  AVAL H 131     1555   1555  1.32  
LINK         C   CME H 130                 N  BVAL H 131     1555   1555  1.33  
SITE     1 AC1 16 HIS A  44  ASN A  46  ARG A  48  HIS A  52                    
SITE     2 AC1 16 ASN A  61  TRP A  68  GLU A  71  ARG A  73                    
SITE     3 AC1 16 HOH A 326  HOH A 339  HOH A 352  HOH A 403                    
SITE     4 AC1 16 HOH A 419  HOH A 421  HOH A 424  ASP H 102                    
SITE     1 AC2 17 ARG A  20  LYS A 129  ARG B  18  HIS B  44                    
SITE     2 AC2 17 ASN B  46  ARG B  48  HIS B  52  ASN B  61                    
SITE     3 AC2 17 GLU B  71  ARG B  73  ALA B 132  PHE B 133                    
SITE     4 AC2 17 ASP B 134  HOH B 311  HOH B 350  HOH B 377                    
SITE     5 AC2 17 HOH B 411                                                     
SITE     1 AC3  5 LEU G   9  PHE G 133  HOH G 352  LYS H 127                    
SITE     2 AC3  5 ILE H 128                                                     
SITE     1 AC4 12 HIS G  44  ASN G  46  ARG G  48  HIS G  52                    
SITE     2 AC4 12 ASN G  61  TRP G  68  GLU G  71  ARG G  73                    
SITE     3 AC4 12 HOH G 312  HOH G 327  HOH G 343  HOH G 377                    
SITE     1 AC5 16 ARG G  20  LYS G 129  ARG H  18  HIS H  44                    
SITE     2 AC5 16 ASN H  46  ARG H  48  HIS H  52  ASN H  61                    
SITE     3 AC5 16 GLU H  71  ARG H  73  ALA H 132  PHE H 133                    
SITE     4 AC5 16 ASP H 134  HOH H 308  HOH H 364  HOH H 365                    
CRYST1   66.384   85.517  116.076  90.00  90.00  90.00 P 21 21 2    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      0.015064  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011694  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008615        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system