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Database: PDB
Entry: 3IAI
LinkDB: 3IAI
Original site: 3IAI 
HEADER    LYASE                                   14-JUL-09   3IAI              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE TUMOR-ASSOCIATED     
TITLE    2 HUMAN CARBONIC ANHYDRASE IX                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 9;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: EXTRACELLULAR CATALYTIC DOMAIN;                            
COMPND   5 SYNONYM: CARBONIC ANHYDRASE IX, CA-IX, CAIX, CARBONATE DEHYDRATASE   
COMPND   6 IX, MEMBRANE ANTIGEN MN, P54/58N, RENAL CELL CARCINOMA-ASSOCIATED    
COMPND   7 ANTIGEN G250, RCC-ASSOCIATED ANTIGEN G250, PMW1;                     
COMPND   8 EC: 4.2.1.1;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CA9, G250, MN;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    CARBONIC ANHYDRASES, TRANSMEMBRANE PROTEINS, CELL MEMBRANE, CELL      
KEYWDS   2 PROJECTION, DISULFIDE BOND, GLYCOPROTEIN, LYASE, MEMBRANE, METAL-    
KEYWDS   3 BINDING, NUCLEUS, PHOSPHOPROTEIN, TRANSMEMBRANE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.ALTERIO,A.DI FIORE,G.DE SIMONE                                      
REVDAT   4   29-JUL-20 3IAI    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   13-JUL-11 3IAI    1       VERSN                                    
REVDAT   2   20-OCT-09 3IAI    1       JRNL                                     
REVDAT   1   08-SEP-09 3IAI    0                                                
JRNL        AUTH   V.ALTERIO,M.HILVO,A.DI FIORE,C.T.SUPURAN,P.PAN,S.PARKKILA,   
JRNL        AUTH 2 A.SCALONI,J.PASTOREK,S.PASTOREKOVA,C.PEDONE,A.SCOZZAFAVA,    
JRNL        AUTH 3 S.M.MONTI,G.DE SIMONE                                        
JRNL        TITL   CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE             
JRNL        TITL 2 TUMOR-ASSOCIATED HUMAN CARBONIC ANHYDRASE IX.                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106 16233 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19805286                                                     
JRNL        DOI    10.1073/PNAS.0908301106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 119944                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 6054                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7872                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 507                                     
REMARK   3   SOLVENT ATOMS            : 1662                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054169.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122974                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1RJ5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 77.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM DIHYDROGEN PHOSPHATE,     
REMARK 280  0.1 M SODIUM ACETATE, PH 4.0, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.63000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      139.26000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      104.44500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      174.07500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       34.81500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
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: C, D, 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 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 B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     PRO C     0                                                      
REMARK 465     ASP C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     PRO D     0                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     GLN D     2                                                      
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    PHE A  27       78.13   -119.49                                   
REMARK 500    PRO A  42       -7.16    -56.26                                   
REMARK 500    SER A  65     -176.95   -177.63                                   
REMARK 500    ARG A  86       78.68   -119.51                                   
REMARK 500    SER B  65      179.70    178.05                                   
REMARK 500    ASP B 227A      25.24   -145.72                                   
REMARK 500    SER C  65      178.46    176.02                                   
REMARK 500    ARG C  86       77.53   -117.82                                   
REMARK 500    ASP C 227A      24.49   -145.54                                   
REMARK 500    ASP C 238       48.94     36.51                                   
REMARK 500    PHE D  27       73.70   -119.19                                   
REMARK 500    SER D  65      180.00    179.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RJ5   RELATED DB: PDB                                   
REMARK 900 MURINE CARBONIC ANHYDRASE XIV                                        
DBREF  3IAI A    0B  261  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  3IAI B    1   261  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  3IAI C    1   261  UNP    Q16790   CAH9_HUMAN     137    391             
DBREF  3IAI D    1   261  UNP    Q16790   CAH9_HUMAN     137    391             
SEQADV 3IAI GLY A    0  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI PRO A    0A UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI SER A   41  UNP  Q16790    CYS   174 ENGINEERED                     
SEQADV 3IAI GLY B   -1  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI PRO B    0  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI SER B   41  UNP  Q16790    CYS   174 ENGINEERED                     
SEQADV 3IAI GLY C   -1  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI PRO C    0  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI SER C   41  UNP  Q16790    CYS   174 ENGINEERED                     
SEQADV 3IAI GLY D   -1  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI PRO D    0  UNP  Q16790              EXPRESSION TAG                 
SEQADV 3IAI SER D   41  UNP  Q16790    CYS   174 ENGINEERED                     
SEQRES   1 A  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 A  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 A  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 A  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 A  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 A  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 A  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 A  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 A  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 A  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 A  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 A  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 A  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 A  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 A  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 A  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 A  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 A  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 A  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 A  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
SEQRES   1 B  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 B  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 B  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 B  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 B  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 B  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 B  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 B  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 B  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 B  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 B  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 B  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 B  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 B  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 B  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 B  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 B  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 B  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 B  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 B  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
SEQRES   1 C  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 C  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 C  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 C  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 C  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 C  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 C  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 C  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 C  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 C  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 C  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 C  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 C  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 C  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 C  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 C  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 C  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 C  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 C  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 C  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
SEQRES   1 D  257  GLY PRO ASP GLN SER HIS TRP ARG TYR GLY GLY ASP PRO          
SEQRES   2 D  257  PRO TRP PRO ARG VAL SER PRO ALA CYS ALA GLY ARG PHE          
SEQRES   3 D  257  GLN SER PRO VAL ASP ILE ARG PRO GLN LEU ALA ALA PHE          
SEQRES   4 D  257  SER PRO ALA LEU ARG PRO LEU GLU LEU LEU GLY PHE GLN          
SEQRES   5 D  257  LEU PRO PRO LEU PRO GLU LEU ARG LEU ARG ASN ASN GLY          
SEQRES   6 D  257  HIS SER VAL GLN LEU THR LEU PRO PRO GLY LEU GLU MET          
SEQRES   7 D  257  ALA LEU GLY PRO GLY ARG GLU TYR ARG ALA LEU GLN LEU          
SEQRES   8 D  257  HIS LEU HIS TRP GLY ALA ALA GLY ARG PRO GLY SER GLU          
SEQRES   9 D  257  HIS THR VAL GLU GLY HIS ARG PHE PRO ALA GLU ILE HIS          
SEQRES  10 D  257  VAL VAL HIS LEU SER THR ALA PHE ALA ARG VAL ASP GLU          
SEQRES  11 D  257  ALA LEU GLY ARG PRO GLY GLY LEU ALA VAL LEU ALA ALA          
SEQRES  12 D  257  PHE LEU GLU GLU GLY PRO GLU GLU ASN SER ALA TYR GLU          
SEQRES  13 D  257  GLN LEU LEU SER ARG LEU GLU GLU ILE ALA GLU GLU GLY          
SEQRES  14 D  257  SER GLU THR GLN VAL PRO GLY LEU ASP ILE SER ALA LEU          
SEQRES  15 D  257  LEU PRO SER ASP PHE SER ARG TYR PHE GLN TYR GLU GLY          
SEQRES  16 D  257  SER LEU THR THR PRO PRO CYS ALA GLN GLY VAL ILE TRP          
SEQRES  17 D  257  THR VAL PHE ASN GLN THR VAL MET LEU SER ALA LYS GLN          
SEQRES  18 D  257  LEU HIS THR LEU SER ASP THR LEU TRP GLY PRO GLY ASP          
SEQRES  19 D  257  SER ARG LEU GLN LEU ASN PHE ARG ALA THR GLN PRO LEU          
SEQRES  20 D  257  ASN GLY ARG VAL ILE GLU ALA SER PHE PRO                      
MODRES 3IAI ASN A  213  ASN  GLYCOSYLATION SITE                                 
MODRES 3IAI ASN B  213  ASN  GLYCOSYLATION SITE                                 
MODRES 3IAI ASN C  213  ASN  GLYCOSYLATION SITE                                 
MODRES 3IAI ASN D  213  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    MAN  E   5      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    MAN  F   5      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    MAN  G   5      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    BMA  H   3      11                                                       
HET    MAN  H   4      11                                                       
HET    MAN  H   5      11                                                       
HET     ZN  A 262       1                                                       
HET    AZM  A 263      13                                                       
HET    GOL  A 300       6                                                       
HET    GOL  A 302       6                                                       
HET    GOL  A 303       6                                                       
HET    GOL  A 304       6                                                       
HET    GOL  A 305       6                                                       
HET    GOL  A 307       6                                                       
HET    GOL  A 301       6                                                       
HET    TRS  A 501       8                                                       
HET    PO4  A 601       5                                                       
HET    PO4  A 600       5                                                       
HET     ZN  B 262       1                                                       
HET    AZM  B 263      13                                                       
HET    GOL  B 300       6                                                       
HET    GOL  B 302       6                                                       
HET    GOL  B 303       6                                                       
HET    GOL  B 304       6                                                       
HET    GOL  B 306       6                                                       
HET    GOL  B 301       6                                                       
HET    TRS  B 501       8                                                       
HET    PO4  B 600       5                                                       
HET     ZN  C 262       1                                                       
HET    AZM  C 263      13                                                       
HET    GOL  C 301       6                                                       
HET    GOL  C 300       6                                                       
HET    GOL  C 302       6                                                       
HET    GOL  C 303       6                                                       
HET    GOL  C 304       6                                                       
HET    TRS  C 501       8                                                       
HET    PO4  C 600       5                                                       
HET     ZN  D 262       1                                                       
HET    AZM  D 263      13                                                       
HET    GOL  D 301       6                                                       
HET    GOL  D 300       6                                                       
HET    GOL  D 302       6                                                       
HET    GOL  D 303       6                                                       
HET    GOL  D 304       6                                                       
HET    GOL  D 306       6                                                       
HET    GOL  D 307       6                                                       
HET    TRS  D 501       8                                                       
HET    PO4  D 600       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM      ZN ZINC ION                                                         
HETNAM     AZM 5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   5  NAG    8(C8 H15 N O6)                                               
FORMUL   5  BMA    4(C6 H12 O6)                                                 
FORMUL   5  MAN    8(C6 H12 O6)                                                 
FORMUL   9   ZN    4(ZN 2+)                                                     
FORMUL  10  AZM    4(C4 H6 N4 O3 S2)                                            
FORMUL  11  GOL    25(C3 H8 O3)                                                 
FORMUL  18  TRS    4(C4 H12 N O3 1+)                                            
FORMUL  19  PO4    5(O4 P 3-)                                                   
FORMUL  51  HOH   *1662(H2 O)                                                   
HELIX    1   1 PRO A   15  SER A   20  1                                   6    
HELIX    2   2 PRO A   21  GLY A   25  5                                   5    
HELIX    3   3 ARG A   34  ALA A   38  5                                   5    
HELIX    4   4 ARG A  130  LEU A  135  1                                   6    
HELIX    5   5 ASN A  154  SER A  162  1                                   9    
HELIX    6   6 ARG A  163  ALA A  168  5                                   6    
HELIX    7   7 ASP A  180  LEU A  185  5                                   6    
HELIX    8   8 SER A  219  THR A  228  1                                  11    
HELIX    9   9 PRO B   15  SER B   20  1                                   6    
HELIX   10  10 PRO B   21  GLY B   25  5                                   5    
HELIX   11  11 ARG B   34  ALA B   38  5                                   5    
HELIX   12  12 ARG B  130  LEU B  135  1                                   6    
HELIX   13  13 ASN B  154  SER B  162  1                                   9    
HELIX   14  14 ARG B  163  ALA B  168  5                                   6    
HELIX   15  15 ASP B  180  LEU B  185  5                                   6    
HELIX   16  16 SER B  219  ASP B  227A 1                                  10    
HELIX   17  17 PRO C   15  SER C   20  1                                   6    
HELIX   18  18 PRO C   21  GLY C   25  5                                   5    
HELIX   19  19 ARG C   34  ALA C   38  5                                   5    
HELIX   20  20 ARG C  130  LEU C  135  1                                   6    
HELIX   21  21 ASN C  154  SER C  162  1                                   9    
HELIX   22  22 ARG C  163  ALA C  168  5                                   6    
HELIX   23  23 ASP C  180  LEU C  185  5                                   6    
HELIX   24  24 SER C  219  ASP C  227A 1                                  10    
HELIX   25  25 PRO D   15  SER D   20  1                                   6    
HELIX   26  26 PRO D   21  GLY D   25  5                                   5    
HELIX   27  27 ARG D   34  ALA D   38  5                                   5    
HELIX   28  28 ARG D  130  LEU D  135  1                                   6    
HELIX   29  29 ASN D  154  SER D  162  1                                   9    
HELIX   30  30 ARG D  163  ALA D  168  5                                   6    
HELIX   31  31 ASP D  180  LEU D  185  5                                   6    
HELIX   32  32 SER D  219  THR D  228  1                                  11    
SHEET    1   A 2 ASP A  32  ILE A  33  0                                        
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33           
SHEET    1   B10 ALA A  39  PHE A  40  0                                        
SHEET    2   B10 GLU A 257  ALA A 258  1  O  ALA A 258   N  ALA A  39           
SHEET    3   B10 TYR A 191  SER A 197 -1  N  GLN A 193   O  GLU A 257           
SHEET    4   B10 GLN A 205  PHE A 212 -1  O  VAL A 207   N  GLY A 196           
SHEET    5   B10 LEU A 141  GLU A 150  1  N  ALA A 145   O  THR A 210           
SHEET    6   B10 ALA A 116  SER A 124 -1  N  HIS A 122   O  ALA A 142           
SHEET    7   B10 ARG A  86  TRP A  97 -1  N  LEU A  91   O  VAL A 121           
SHEET    8   B10 VAL A  66  THR A  69 -1  N  LEU A  68   O  LEU A  93           
SHEET    9   B10 LEU A  57  ASN A  61 -1  N  ARG A  60   O  GLN A  67           
SHEET   10   B10 GLU A 173  VAL A 176 -1  O  VAL A 176   N  LEU A  57           
SHEET    1   C 6 GLU A  48  LEU A  50  0                                        
SHEET    2   C 6 GLU A  78  GLY A  82 -1  O  GLU A  78   N  LEU A  50           
SHEET    3   C 6 ARG A  86  TRP A  97 -1  O  TYR A  88   N  MET A  79           
SHEET    4   C 6 ALA A 116  SER A 124 -1  O  VAL A 121   N  LEU A  91           
SHEET    5   C 6 LEU A 141  GLU A 150 -1  O  ALA A 142   N  HIS A 122           
SHEET    6   C 6 VAL A 216  LEU A 218  1  O  VAL A 216   N  GLU A 149           
SHEET    1   D 2 ASP B  32  ILE B  33  0                                        
SHEET    2   D 2 THR B 108  VAL B 109  1  O  THR B 108   N  ILE B  33           
SHEET    1   E10 ALA B  39  PHE B  40  0                                        
SHEET    2   E10 GLU B 257  ALA B 258  1  O  ALA B 258   N  ALA B  39           
SHEET    3   E10 TYR B 191  SER B 197 -1  N  GLN B 193   O  GLU B 257           
SHEET    4   E10 GLN B 205  PHE B 212 -1  O  VAL B 207   N  GLY B 196           
SHEET    5   E10 LEU B 141  GLU B 150  1  N  ALA B 145   O  THR B 210           
SHEET    6   E10 ALA B 116  SER B 124 -1  N  ALA B 116   O  LEU B 148           
SHEET    7   E10 ARG B  86  TRP B  97 -1  N  LEU B  91   O  VAL B 121           
SHEET    8   E10 VAL B  66  THR B  69 -1  N  LEU B  68   O  LEU B  93           
SHEET    9   E10 LEU B  57  ASN B  61 -1  N  ARG B  60   O  GLN B  67           
SHEET   10   E10 GLU B 173  VAL B 176 -1  O  VAL B 176   N  LEU B  57           
SHEET    1   F 6 GLU B  48  LEU B  50  0                                        
SHEET    2   F 6 GLU B  78  GLY B  82 -1  O  GLU B  78   N  LEU B  50           
SHEET    3   F 6 ARG B  86  TRP B  97 -1  O  TYR B  88   N  MET B  79           
SHEET    4   F 6 ALA B 116  SER B 124 -1  O  VAL B 121   N  LEU B  91           
SHEET    5   F 6 LEU B 141  GLU B 150 -1  O  LEU B 148   N  ALA B 116           
SHEET    6   F 6 VAL B 216  LEU B 218  1  O  VAL B 216   N  GLU B 149           
SHEET    1   G 2 TRP B 230  GLY B 231  0                                        
SHEET    2   G 2 SER B 239  ARG B 240 -1  O  SER B 239   N  GLY B 231           
SHEET    1   H 2 ASP C  32  ILE C  33  0                                        
SHEET    2   H 2 THR C 108  VAL C 109  1  O  THR C 108   N  ILE C  33           
SHEET    1   I10 ALA C  39  PHE C  40  0                                        
SHEET    2   I10 GLU C 257  ALA C 258  1  O  ALA C 258   N  ALA C  39           
SHEET    3   I10 TYR C 191  SER C 197 -1  N  GLN C 193   O  GLU C 257           
SHEET    4   I10 GLN C 205  PHE C 212 -1  O  VAL C 207   N  GLY C 196           
SHEET    5   I10 LEU C 141  GLU C 150  1  N  ALA C 145   O  THR C 210           
SHEET    6   I10 ALA C 116  SER C 124 -1  N  HIS C 122   O  ALA C 142           
SHEET    7   I10 ARG C  86  TRP C  97 -1  N  LEU C  91   O  VAL C 121           
SHEET    8   I10 VAL C  66  THR C  69 -1  N  LEU C  68   O  LEU C  93           
SHEET    9   I10 LEU C  57  ASN C  61 -1  N  ARG C  60   O  GLN C  67           
SHEET   10   I10 GLU C 173  VAL C 176 -1  O  THR C 174   N  LEU C  59           
SHEET    1   J 6 GLU C  48  LEU C  50  0                                        
SHEET    2   J 6 GLU C  78  GLY C  82 -1  O  GLU C  78   N  LEU C  50           
SHEET    3   J 6 ARG C  86  TRP C  97 -1  O  TYR C  88   N  MET C  79           
SHEET    4   J 6 ALA C 116  SER C 124 -1  O  VAL C 121   N  LEU C  91           
SHEET    5   J 6 LEU C 141  GLU C 150 -1  O  ALA C 142   N  HIS C 122           
SHEET    6   J 6 VAL C 216  LEU C 218  1  O  VAL C 216   N  GLU C 149           
SHEET    1   K 2 ASP D  32  ILE D  33  0                                        
SHEET    2   K 2 THR D 108  VAL D 109  1  O  THR D 108   N  ILE D  33           
SHEET    1   L10 ALA D  39  PHE D  40  0                                        
SHEET    2   L10 GLU D 257  ALA D 258  1  O  ALA D 258   N  ALA D  39           
SHEET    3   L10 TYR D 191  SER D 197 -1  N  GLN D 193   O  GLU D 257           
SHEET    4   L10 GLN D 205  PHE D 212 -1  O  VAL D 207   N  GLY D 196           
SHEET    5   L10 LEU D 141  GLU D 150  1  N  ALA D 145   O  THR D 210           
SHEET    6   L10 ALA D 116  SER D 124 -1  N  ALA D 116   O  LEU D 148           
SHEET    7   L10 ARG D  86  TRP D  97 -1  N  LEU D  91   O  VAL D 121           
SHEET    8   L10 VAL D  66  THR D  69 -1  N  LEU D  68   O  LEU D  93           
SHEET    9   L10 LEU D  57  ASN D  61 -1  N  ARG D  60   O  GLN D  67           
SHEET   10   L10 GLU D 173  VAL D 176 -1  O  VAL D 176   N  LEU D  57           
SHEET    1   M 6 GLU D  48  LEU D  50  0                                        
SHEET    2   M 6 GLU D  78  GLY D  82 -1  O  GLU D  78   N  LEU D  50           
SHEET    3   M 6 ARG D  86  TRP D  97 -1  O  TYR D  88   N  MET D  79           
SHEET    4   M 6 ALA D 116  SER D 124 -1  O  VAL D 121   N  LEU D  91           
SHEET    5   M 6 LEU D 141  GLU D 150 -1  O  LEU D 148   N  ALA D 116           
SHEET    6   M 6 VAL D 216  LEU D 218  1  O  VAL D 216   N  GLU D 149           
SHEET    1   N 2 TRP D 230  GLY D 231  0                                        
SHEET    2   N 2 SER D 239  ARG D 240 -1  O  SER D 239   N  GLY D 231           
SSBOND   1 CYS A   23    CYS A  203                          1555   1555  2.05  
SSBOND   2 CYS B   23    CYS B  203                          1555   1555  2.05  
SSBOND   3 CYS C   23    CYS C  203                          1555   1555  2.05  
SSBOND   4 CYS D   23    CYS D  203                          1555   1555  2.04  
LINK         ND2 ASN A 213                 C1  NAG E   1     1555   1555  1.47  
LINK         ND2 ASN B 213                 C1  NAG F   1     1555   1555  1.47  
LINK         ND2 ASN C 213                 C1  NAG G   1     1555   1555  1.47  
LINK         ND2 ASN D 213                 C1  NAG H   1     1555   1555  1.47  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.38  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.38  
LINK         O3  BMA E   3                 C1  MAN E   4     1555   1555  1.42  
LINK         O6  BMA E   3                 C1  MAN E   5     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.38  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.39  
LINK         O3  BMA F   3                 C1  MAN F   4     1555   1555  1.41  
LINK         O6  BMA F   3                 C1  MAN F   5     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.38  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.39  
LINK         O3  BMA G   3                 C1  MAN G   4     1555   1555  1.41  
LINK         O6  BMA G   3                 C1  MAN G   5     1555   1555  1.45  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.38  
LINK         O4  NAG H   2                 C1  BMA H   3     1555   1555  1.39  
LINK         O3  BMA H   3                 C1  MAN H   4     1555   1555  1.42  
LINK         O6  BMA H   3                 C1  MAN H   5     1555   1555  1.45  
CISPEP   1 ASP A   10    PRO A   11          0         0.28                     
CISPEP   2 ASP A   10    PRO A   11          0         0.26                     
CISPEP   3 SER A   29    PRO A   30          0         0.32                     
CISPEP   4 LEU A   54B   PRO A   55          0         0.15                     
CISPEP   5 PRO A  201    PRO A  202          0         0.25                     
CISPEP   6 ASP B   10    PRO B   11          0         0.33                     
CISPEP   7 SER B   29    PRO B   30          0         0.02                     
CISPEP   8 LEU B   54B   PRO B   55          0        -0.13                     
CISPEP   9 PRO B  201    PRO B  202          0         0.18                     
CISPEP  10 ASP C   10    PRO C   11          0        -0.11                     
CISPEP  11 SER C   29    PRO C   30          0         0.12                     
CISPEP  12 LEU C   54B   PRO C   55          0        -0.08                     
CISPEP  13 PRO C  201    PRO C  202          0         0.46                     
CISPEP  14 ASP D   10    PRO D   11          0         0.11                     
CISPEP  15 SER D   29    PRO D   30          0        -0.06                     
CISPEP  16 LEU D   54B   PRO D   55          0         0.27                     
CISPEP  17 PRO D  201    PRO D  202          0         0.99                     
CRYST1  144.180  144.180  208.890  90.00  90.00 120.00 P 61         24          
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      0.006936  0.004004  0.000000        0.00000                         
SCALE2      0.000000  0.008009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004787        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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