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LongText Report for: 1W1I-pdb

Name Class
1W1I-pdb
HEADER    HYDROLASE/COMPLEX                       22-JUN-04   1W1I              
TITLE     CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPPIV OR CD26)          
TITLE    2  IN COMPLEX WITH ADENOSINE DEAMINASE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;                                   
COMPND   3 SYNONYM: DPP IV, T-CELL ACTIVATION ANTIGEN CD26, TP103,              
COMPND   4  ADENOSINE DEAMINASE COMPLEXING PROTEIN-2, ADABP;                    
COMPND   5 CHAIN: A, B, C, D;                                                   
COMPND   6 FRAGMENT: EXTRACELLULAR DOMAIN 39 - 766;                             
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ADENOSINE DEAMINASE;                                       
COMPND  11 SYNONYM: ADENOSINE AMINOHYDROLASE;                                   
COMPND  12 CHAIN: E, F, G, H;                                                   
COMPND  13 EC: 3.5.4.4                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   3 EXPRESSION_SYSTEM_STRAIN: SF9 CELLS;                                 
SOURCE   4 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE   5 EXPRESSION_SYSTEM_PLASMID: PFASTBACHTC;                              
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGAN: KIDNEY;                                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  11 ORGANISM_COMMON: BOVINE;                                             
SOURCE  12 TISSUE: INTESTINAL MUCOSA;                                           
SOURCE  13 OTHER_DETAILS: SIGMA, TYPE VI, FROM CALF INTESTINAL MUCOSA           
KEYWDS    DIPETIDYL PEPTIDASE IV, DPPIV, CD26, ALPHA/BETA-HYDROLASE             
KEYWDS   2 FOLD, BETA-PROPELLER FOLD, PROTEIN-PROTEIN COMPLEX,                  
KEYWDS   3 ADENOSINE DEAMINASE, ADA, SERINE PROTEASE, AMINOPEPTIDASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN                          
REVDAT   1   02-SEP-04 1W1I    0                                                
JRNL        AUTH   W.A.WEIHOFEN,J.LIU,W.REUTTER,W.SAENGER,H.FAN                 
JRNL        TITL   CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV                 
JRNL        TITL 2 (DPPIV OR CD26) IN COMPLEX WITH ADENOSINE DEAMINASE          
JRNL        TITL 3 REVEALS A HIGHLY AMPHIPHILIC INTERFACE                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. 3.03 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC 5.1.9999                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3   REFINEMENT TARGET : MAXIMUM LIKELIHOOD                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.46                          
REMARK   3   NUMBER OF REFLECTIONS             : 98926                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.22445                         
REMARK   3   R VALUE            (WORKING SET) : 0.22377                         
REMARK   3   FREE R VALUE                     : 0.25704                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) :  2.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2048                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.030                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.108                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6906                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.367                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 154                          
REMARK   3   BIN FREE R VALUE                    : 0.417                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 35087                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 790                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.459                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.45                                                 
REMARK   3    B22 (A**2) : -2.35                                                
REMARK   3    B33 (A**2) : -1.47                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 1.75                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.498         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.378         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.957        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A): 41313 ; 0.008 ; 0.021          
REMARK   3   BOND LENGTHS OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   BOND ANGLES REFINED      (DEGREES): 63508 ; 1.340 ; 1.930          
REMARK   3   BOND ANGLES OTHERS       (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):  8614 ; 5.963 ; 7.500          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):  1772 ;34.827 ;24.108          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):  5999 ;19.946 ;15.000          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):   184 ;19.790 ;15.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):  5519 ; 0.116 ; 0.200          
REMARK   3   GENERAL PLANES REFINED ATOMS   (A): 45884 ; 0.003 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED CONTACTS REFINED    (A): 17208 ; 0.232 ; 0.300          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION REFINED     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  NULL ;  NULL ;  NULL          
REMARK   3   H-BOND (X...Y) REFINED         (A):  1927 ; 0.187 ; 0.500          
REMARK   3   SYMMETRY VDW REFINED           (A):    58 ; 0.275 ; 0.300          
REMARK   3   SYMMETRY H-BOND REFINED        (A):     7 ; 0.282 ; 0.500          
REMARK   3   H-BOND (X...Y) REFINED         (A):  1927 ; 0.187 ; 0.500          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2): 21822 ; 0.646 ; 2.000            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2): 34915 ; 1.141 ; 3.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2): 17155 ; 0.608 ; 2.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2): 15310 ; 1.053 ; 3.000            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   1                                
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    4                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     40       A      70      1                      
REMARK   3           1     B     40       B      70      1                      
REMARK   3           1     C     40       C      70      1                      
REMARK   3           1     D     40       D      70      1                      
REMARK   3           2     A     74       A     281      1                      
REMARK   3           2     B     74       B     281      1                      
REMARK   3           2     C     74       C     281      1                      
REMARK   3           2     D     74       D     281      1                      
REMARK   3           3     A    296       A     331      1                      
REMARK   3           3     B    296       B     331      1                      
REMARK   3           3     C    296       C     331      1                      
REMARK   3           3     D    296       D     331      1                      
REMARK   3           4     A    347       A     764      1                      
REMARK   3           4     B    347       B     764      1                      
REMARK   3           4     C    347       C     764      1                      
REMARK   3           4     D    347       D     764      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   5696 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   5696 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    C    (A):   5696 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   5696 ;  0.02 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   5696 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   5696 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      1    C (A**2):   5696 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      1    D (A**2):   5696 ;  0.04 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   2                                
REMARK   3     CHAIN NAMES                    : E F G H                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    9                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E      6       E      55      1                      
REMARK   3           1     F      6       F      55      1                      
REMARK   3           1     G      6       G      55      1                      
REMARK   3           1     H      6       H      55      1                      
REMARK   3           2     E    217       E     237      1                      
REMARK   3           2     F    217       F     237      1                      
REMARK   3           2     G    217       G     237      1                      
REMARK   3           2     H    217       H     237      1                      
REMARK   3           3     E     85       E     108      1                      
REMARK   3           3     F     85       F     108      1                      
REMARK   3           3     G     85       G     108      1                      
REMARK   3           3     H     85       H     108      1                      
REMARK   3           4     E    144       E     215      1                      
REMARK   3           4     F    144       F     215      1                      
REMARK   3           4     G    144       G     215      1                      
REMARK   3           4     H    144       H     215      1                      
REMARK   3           5     E    119       E     126      1                      
REMARK   3           5     F    119       F     126      1                      
REMARK   3           5     G    119       G     126      1                      
REMARK   3           5     H    119       H     126      1                      
REMARK   3           6     E     57       E      72      1                      
REMARK   3           6     F     57       F      72      1                      
REMARK   3           6     G     57       G      72      1                      
REMARK   3           6     H     57       H      72      1                      
REMARK   3           7     E    241       E     280      1                      
REMARK   3           7     F    241       F     280      1                      
REMARK   3           7     G    241       G     280      1                      
REMARK   3           7     H    241       H     280      1                      
REMARK   3           8     E    338       E     351      1                      
REMARK   3           8     F    338       F     351      1                      
REMARK   3           8     G    338       G     351      1                      
REMARK   3           8     H    338       H     351      1                      
REMARK   3           9     E    284       E     335      1                      
REMARK   3           9     F    284       F     335      1                      
REMARK   3           9     G    284       G     335      1                      
REMARK   3           9     H    284       H     335      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    E    (A):   2372 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    F    (A):   2372 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    G    (A):   2372 ;  0.02 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    H    (A):   2372 ;  0.02 ;  0.05           
REMARK   3   TIGHT THERMAL      2    E (A**2):   2372 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      2    F (A**2):   2372 ;  0.04 ;  0.50           
REMARK   3   TIGHT THERMAL      2    G (A**2):   2372 ;  0.03 ;  0.50           
REMARK   3   TIGHT THERMAL      2    H (A**2):   2372 ;  0.03 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   :1.20                                           
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. RESIDUES 1-3 OF CHAINS E,F,G,H OF ADA            
REMARK   3   ARE DISORDERED                                                     
REMARK   4                                                                      
REMARK   4 1W1I COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 23-JUN-2004.                
REMARK 100 THE EBI ID CODE IS EBI-20204.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-2003                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY BEAMLINE BL1                 
REMARK 200  BEAMLINE                       : BL1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.914                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (165MM)                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100817                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.03                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.3                               
REMARK 200  DATA REDUNDANCY                : 2.3                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.03                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.4                                
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1N1M AND 1KRM                            
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA):NULL                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   1/2+X,1/2+Y,Z                                           
REMARK 290       4555   1/2-X,1/2+Y,-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       79.03250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       84.25200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.03250            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       84.25200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF   8 CHAIN(S). SEE REMARK 350 FOR                   
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TETRAMERIC                      
REMARK 300                                                                      
REMARK 300 THE COMPLEX DESCRIBED BY REMARK 350 BELOW IS OF THE                  
REMARK 300 TYPE A2B2, WHERE CHAINS A AND B ARE IN CONTACT                       
REMARK 300 WITH EACH OTHER, AND EACH OF THESE CHAINS IS IN TURN                 
REMARK 300 IN COMPLEX WITH CHAINS F AND E RESPECTIVELY.                         
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, F, B, E                            
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 BIOMOLECULE:  1                                                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, D, 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     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     GLN E     3                                                      
REMARK 465     PRO E   356                                                      
REMARK 465     ALA E   357                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     GLN F     3                                                      
REMARK 465     PRO F   356                                                      
REMARK 465     ALA F   357                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G     2                                                      
REMARK 465     GLN G     3                                                      
REMARK 465     PRO G   356                                                      
REMARK 465     ALA G   357                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     GLN H     3                                                      
REMARK 465     PRO H   356                                                      
REMARK 465     ALA H   357                                                      
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     TYR F 351    N                                                   
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 246   CA  -  CB  -  CG  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LEU B 300   N   -  CA  -  C   ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    LEU C 246   CA  -  CB  -  CG  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    LEU D 300   N   -  CA  -  C   ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    THR E 176   N   -  CA  -  C   ANGL. DEV. =  10.1 DEGREES          
REMARK 500    LEU E 325   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ALA E 350   CA  -  C   -  N   ANGL. DEV. = -46.1 DEGREES          
REMARK 500    ALA E 350   O   -  C   -  N   ANGL. DEV. = -52.0 DEGREES          
REMARK 500    TYR E 351   N   -  CA  -  C   ANGL. DEV. =  48.8 DEGREES          
REMARK 500    TYR E 351   N   -  CA  -  CB  ANGL. DEV. = -20.9 DEGREES          
REMARK 500    LEU F 325   CA  -  CB  -  CG  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ASP G  77   CB  -  CG  -  OD2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    LEU G 325   CA  -  CB  -  CG  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    PHE H 283   N   -  CA  -  C   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    LEU H 325   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                                                                      
REMARK 500   O    TYR E   240     N    THR E   242               2.01           
REMARK 500   N    TYR E   351     O    LEU F   347               1.94           
REMARK 500   N    TYR E   351     O    TYR F   348               2.04           
REMARK 500   OH   TYR F   240     OG   SER F   266               2.01           
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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500                                                                      
REMARK 500    GLU E 113     -110.89      9.19                                   
REMARK 500    HIS E 238      -82.49     70.89                                   
REMARK 500    ASP E 295      -84.12     70.19                                   
REMARK 500    HIS F 238      -94.10     63.18                                   
REMARK 500    ASP F 295      -86.03     70.27                                   
REMARK 500    HIS G 238     -102.28     74.03                                   
REMARK 500    ASP G 295      -83.50     69.55                                   
REMARK 500    HIS H 238      -84.52     64.82                                   
REMARK 500    ASP H 295      -84.36     70.94                                   
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 GLU F 337    ASP F 338                  149.62                       
REMARK 500 GLU H 113    PRO H 114                  149.40                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM ZN    ZN E 501  THE COORDINATION ANGLES ARE:          
REMARK 600  1 ASP   295E  OD1                                                   
REMARK 600  2 HIS    15E  NE2        75.6                                       
REMARK 600  3 HIS    17E  NE2        90.3 112.6                                 
REMARK 600  4 HIS   214E  NE2       162.3  87.4 101.1                           
REMARK 600                             1     2     3                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM ZN    ZN F 501  THE COORDINATION ANGLES ARE:          
REMARK 600  1 HIS    15F  NE2                                                   
REMARK 600  2 HIS    17F  NE2       105.8                                       
REMARK 600  3 ASP   295F  OD1        74.6  89.6                                 
REMARK 600  4 HIS   214F  NE2        84.6  97.0 159.2                           
REMARK 600                             1     2     3                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM ZN    ZN G 501  THE COORDINATION ANGLES ARE:          
REMARK 600  1 HIS   214G  NE2                                                   
REMARK 600  2 HIS    17G  NE2        99.4                                       
REMARK 600  3 ASP   295G  OD1       161.8  90.4                                 
REMARK 600  4 HIS    15G  NE2        85.6 111.3  76.5                           
REMARK 600                             1     2     3                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM ZN    ZN H 501  THE COORDINATION ANGLES ARE:          
REMARK 600  1 HIS    15H  NE2                                                   
REMARK 600  2 HIS    17H  NE2       108.1                                       
REMARK 600  3 HIS   214H  NE2        85.9  98.3                                 
REMARK 600  4 ASP   295H  OD1        75.7  88.3 161.5                           
REMARK 600                             1     2     3                            
REMARK 600                                                                      
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 SITE_DESCRIPTION: MAN BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 SITE_DESCRIPTION: AFL BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 SITE_DESCRIPTION: BMA BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN E                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN F                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN G                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 SITE_DESCRIPTION: ZN BINDING SITE FOR CHAIN H                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J2E   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL                               
REMARK 900  PEPTIDASE IV                                                        
REMARK 900 RELATED ID: 1N1M   RELATED DB: PDB                                   
REMARK 900  HUMAN DIPEPTIDYL PEPTIDASE IV/CD26 IN                               
REMARK 900  COMPLEX WITH ANINHIBITOR                                            
REMARK 900 RELATED ID: 1NU6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL                               
REMARK 900  PEPTIDASE IV (DPP-IV)                                               
REMARK 900 RELATED ID: 1NU8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL                               
REMARK 900  PEPTIDASE IV (DPP-IV)IN COMPLEX WITH                                
REMARK 900  DIPROTIN A (ILI)                                                    
REMARK 900 RELATED ID: 1PFQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN APO DIPEPTIDYL                           
REMARK 900  PEPTIDASE IV /CD26                                                  
REMARK 900 RELATED ID: 1KRM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BOVINE ADENOSINE                               
REMARK 900  DEAMINASE COMPLEXEDWITH 6-HYDROXYL-1,6-                             
REMARK 900  DIHYDROPURINE RIBOSIDE                                              
REMARK 900 RELATED ID: 1NDV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE                            
REMARK 900  COMPLEXED WITHFR117016                                              
REMARK 900 RELATED ID: 1NDW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE                            
REMARK 900  COMPLEXED WITHFR221647                                              
REMARK 900 RELATED ID: 1NDY   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE                            
REMARK 900  COMPLEXED WITHFR230513                                              
REMARK 900 RELATED ID: 1NDZ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ADENOSINE DEAMINASE                            
REMARK 900  COMPLEXED WITHFR235999                                              
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONFLICTS DESCRIBED WITH ANNOTATION FOR THIS                     
REMARK 999 REMARK HAS BEEN DESCRIBED IN J. PHARM. BIOMED. ANAL.                 
REMARK 999 14:1513-1519(1996). PUBMED ID: 8877857.                              
DBREF  1W1I A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  1W1I B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  1W1I C   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  1W1I D   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  1W1I E    1   357  UNP    P56658   ADA_BOVIN        0    356             
DBREF  1W1I F    1   357  UNP    P56658   ADA_BOVIN        0    356             
DBREF  1W1I G    1   357  UNP    P56658   ADA_BOVIN        0    356             
DBREF  1W1I H    1   357  UNP    P56658   ADA_BOVIN        0    356             
SEQADV 1W1I ASP E    8  UNP  P56658    ASN     7 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS E   32  UNP  P56658    ARG    31 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG E   33  UNP  P56658    LYS    32 CONFLICT SEE REMARK 999        
SEQADV 1W1I LEU E   47  UNP  P56658    GLN    46 CONFLICT                       
SEQADV 1W1I THR E   57  UNP  P56658    SER    56 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP E   60  UNP  P56658    GLU    59 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP E   77  UNP  P56658    GLU    76 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE E   79  UNP  P56658    VAL    78 CONFLICT SEE REMARK 999        
SEQADV 1W1I GLN E  199  UNP  P56658    LYS   198 VARIANT                        
SEQADV 1W1I THR E  246  UNP  P56658    ALA   245 VARIANT                        
SEQADV 1W1I ILE E  261  UNP  P56658    VAL   260 CONFLICT SEE REMARK 999        
SEQADV 1W1I ALA E  279  UNP  P56658    PRO   278 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE E  281  UNP  P56658    VAL   280 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS E  313  UNP  P56658    ASN   312 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP E  314  UNP  P56658    GLU   313 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG E  352  UNP  P56658    GLY   351 VARIANT                        
SEQADV 1W1I ASP F    8  UNP  P56658    ASN     7 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS F   32  UNP  P56658    ARG    31 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG F   33  UNP  P56658    LYS    32 CONFLICT SEE REMARK 999        
SEQADV 1W1I LEU F   47  UNP  P56658    GLN    46 CONFLICT                       
SEQADV 1W1I THR F   57  UNP  P56658    SER    56 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP F   60  UNP  P56658    GLU    59 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP F   77  UNP  P56658    GLU    76 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE F   79  UNP  P56658    VAL    78 CONFLICT SEE REMARK 999        
SEQADV 1W1I GLN F  199  UNP  P56658    LYS   198 VARIANT                        
SEQADV 1W1I THR F  246  UNP  P56658    ALA   245 VARIANT                        
SEQADV 1W1I ILE F  261  UNP  P56658    VAL   260 CONFLICT SEE REMARK 999        
SEQADV 1W1I ALA F  279  UNP  P56658    PRO   278 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE F  281  UNP  P56658    VAL   280 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS F  313  UNP  P56658    ASN   312 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP F  314  UNP  P56658    GLU   313 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG F  352  UNP  P56658    GLY   351 VARIANT                        
SEQADV 1W1I ASP G    8  UNP  P56658    ASN     7 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS G   32  UNP  P56658    ARG    31 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG G   33  UNP  P56658    LYS    32 CONFLICT SEE REMARK 999        
SEQADV 1W1I LEU G   47  UNP  P56658    GLN    46 CONFLICT                       
SEQADV 1W1I THR G   57  UNP  P56658    SER    56 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP G   60  UNP  P56658    GLU    59 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP G   77  UNP  P56658    GLU    76 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE G   79  UNP  P56658    VAL    78 CONFLICT SEE REMARK 999        
SEQADV 1W1I GLN G  199  UNP  P56658    LYS   198 VARIANT                        
SEQADV 1W1I THR G  246  UNP  P56658    ALA   245 VARIANT                        
SEQADV 1W1I ILE G  261  UNP  P56658    VAL   260 CONFLICT SEE REMARK 999        
SEQADV 1W1I ALA G  279  UNP  P56658    PRO   278 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE G  281  UNP  P56658    VAL   280 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS G  313  UNP  P56658    ASN   312 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP G  314  UNP  P56658    GLU   313 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG G  352  UNP  P56658    GLY   351 VARIANT                        
SEQADV 1W1I ASP H    8  UNP  P56658    ASN     7 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS H   32  UNP  P56658    ARG    31 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG H   33  UNP  P56658    LYS    32 CONFLICT SEE REMARK 999        
SEQADV 1W1I LEU H   47  UNP  P56658    GLN    46 CONFLICT                       
SEQADV 1W1I THR H   57  UNP  P56658    SER    56 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP H   60  UNP  P56658    GLU    59 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP H   77  UNP  P56658    GLU    76 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE H   79  UNP  P56658    VAL    78 CONFLICT SEE REMARK 999        
SEQADV 1W1I GLN H  199  UNP  P56658    LYS   198 VARIANT                        
SEQADV 1W1I THR H  246  UNP  P56658    ALA   245 VARIANT                        
SEQADV 1W1I ILE H  261  UNP  P56658    VAL   260 CONFLICT SEE REMARK 999        
SEQADV 1W1I ALA H  279  UNP  P56658    PRO   278 CONFLICT SEE REMARK 999        
SEQADV 1W1I ILE H  281  UNP  P56658    VAL   280 CONFLICT SEE REMARK 999        
SEQADV 1W1I LYS H  313  UNP  P56658    ASN   312 CONFLICT SEE REMARK 999        
SEQADV 1W1I ASP H  314  UNP  P56658    GLU   313 CONFLICT SEE REMARK 999        
SEQADV 1W1I ARG H  352  UNP  P56658    GLY   351 VARIANT                        
SEQRES   1 A  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 B  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 C  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 C  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 C  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 C  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 C  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 C  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 C  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 C  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 C  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 C  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 C  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 C  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 C  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 C  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 C  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 C  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 C  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 C  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 C  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 C  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 C  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 C  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 C  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 C  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 C  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 C  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 C  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 C  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 C  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 C  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 C  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 C  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 C  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 C  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 C  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 C  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 C  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 C  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 C  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 C  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 C  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 C  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 C  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 C  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 C  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 C  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 C  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 C  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 C  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 C  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 C  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 C  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 C  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 C  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 C  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 C  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 D  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 D  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 D  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 D  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 D  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 D  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 D  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 D  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 D  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 D  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 D  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 D  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 D  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 D  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 D  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 D  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 D  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 D  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 D  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 D  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 D  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 D  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 D  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 D  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 D  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 D  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 D  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 D  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 D  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 D  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 D  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 D  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 D  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 D  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 D  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 D  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 D  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 D  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 D  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 D  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 D  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 D  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 D  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 D  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 D  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 D  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 D  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 D  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 D  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 D  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 D  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 D  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 D  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 D  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 D  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 D  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 E  357  MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU          
SEQRES   2 E  357  LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR          
SEQRES   3 E  357  ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO          
SEQRES   4 E  357  ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET          
SEQRES   5 E  357  ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE          
SEQRES   6 E  357  ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA          
SEQRES   7 E  357  ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA          
SEQRES   8 E  357  LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO          
SEQRES   9 E  357  HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP          
SEQRES  10 E  357  ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL          
SEQRES  11 E  357  SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP          
SEQRES  12 E  357  PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG          
SEQRES  13 E  357  HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS          
SEQRES  14 E  357  LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU          
SEQRES  15 E  357  ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO          
SEQRES  16 E  357  GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY          
SEQRES  17 E  357  VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA          
SEQRES  18 E  357  ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU          
SEQRES  19 E  357  ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR          
SEQRES  20 E  357  LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU          
SEQRES  21 E  357  ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS          
SEQRES  22 E  357  PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP          
SEQRES  23 E  357  GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE          
SEQRES  24 E  357  PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS          
SEQRES  25 E  357  LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU          
SEQRES  26 E  357  ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP          
SEQRES  27 E  357  GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR          
SEQRES  28 E  357  ARG MET PRO SER PRO ALA                                      
SEQRES   1 F  357  MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU          
SEQRES   2 F  357  LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR          
SEQRES   3 F  357  ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO          
SEQRES   4 F  357  ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET          
SEQRES   5 F  357  ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE          
SEQRES   6 F  357  ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA          
SEQRES   7 F  357  ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA          
SEQRES   8 F  357  LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO          
SEQRES   9 F  357  HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP          
SEQRES  10 F  357  ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL          
SEQRES  11 F  357  SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP          
SEQRES  12 F  357  PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG          
SEQRES  13 F  357  HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS          
SEQRES  14 F  357  LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU          
SEQRES  15 F  357  ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO          
SEQRES  16 F  357  GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY          
SEQRES  17 F  357  VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA          
SEQRES  18 F  357  ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU          
SEQRES  19 F  357  ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR          
SEQRES  20 F  357  LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU          
SEQRES  21 F  357  ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS          
SEQRES  22 F  357  PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP          
SEQRES  23 F  357  GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE          
SEQRES  24 F  357  PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS          
SEQRES  25 F  357  LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU          
SEQRES  26 F  357  ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP          
SEQRES  27 F  357  GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR          
SEQRES  28 F  357  ARG MET PRO SER PRO ALA                                      
SEQRES   1 G  357  MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU          
SEQRES   2 G  357  LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR          
SEQRES   3 G  357  ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO          
SEQRES   4 G  357  ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET          
SEQRES   5 G  357  ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE          
SEQRES   6 G  357  ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA          
SEQRES   7 G  357  ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA          
SEQRES   8 G  357  LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO          
SEQRES   9 G  357  HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP          
SEQRES  10 G  357  ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL          
SEQRES  11 G  357  SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP          
SEQRES  12 G  357  PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG          
SEQRES  13 G  357  HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS          
SEQRES  14 G  357  LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU          
SEQRES  15 G  357  ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO          
SEQRES  16 G  357  GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY          
SEQRES  17 G  357  VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA          
SEQRES  18 G  357  ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU          
SEQRES  19 G  357  ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR          
SEQRES  20 G  357  LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU          
SEQRES  21 G  357  ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS          
SEQRES  22 G  357  PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP          
SEQRES  23 G  357  GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE          
SEQRES  24 G  357  PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS          
SEQRES  25 G  357  LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU          
SEQRES  26 G  357  ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP          
SEQRES  27 G  357  GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR          
SEQRES  28 G  357  ARG MET PRO SER PRO ALA                                      
SEQRES   1 H  357  MET ALA GLN THR PRO ALA PHE ASP LYS PRO LYS VAL GLU          
SEQRES   2 H  357  LEU HIS VAL HIS LEU ASP GLY ALA ILE LYS PRO GLU THR          
SEQRES   3 H  357  ILE LEU TYR TYR GLY LYS ARG ARG GLY ILE ALA LEU PRO          
SEQRES   4 H  357  ALA ASP THR PRO GLU GLU LEU LEU ASN ILE ILE GLY MET          
SEQRES   5 H  357  ASP LYS PRO LEU THR LEU PRO ASP PHE LEU ALA LYS PHE          
SEQRES   6 H  357  ASP TYR TYR MET PRO ALA ILE ALA GLY CYS ARG ASP ALA          
SEQRES   7 H  357  ILE LYS ARG ILE ALA TYR GLU PHE VAL GLU MET LYS ALA          
SEQRES   8 H  357  LYS ASP GLY VAL VAL TYR VAL GLU VAL ARG TYR SER PRO          
SEQRES   9 H  357  HIS LEU LEU ALA ASN SER LYS VAL GLU PRO ILE PRO TRP          
SEQRES  10 H  357  ASN GLN ALA GLU GLY ASP LEU THR PRO ASP GLU VAL VAL          
SEQRES  11 H  357  SER LEU VAL ASN GLN GLY LEU GLN GLU GLY GLU ARG ASP          
SEQRES  12 H  357  PHE GLY VAL LYS VAL ARG SER ILE LEU CYS CYS MET ARG          
SEQRES  13 H  357  HIS GLN PRO SER TRP SER SER GLU VAL VAL GLU LEU CYS          
SEQRES  14 H  357  LYS LYS TYR ARG GLU GLN THR VAL VAL ALA ILE ASP LEU          
SEQRES  15 H  357  ALA GLY ASP GLU THR ILE GLU GLY SER SER LEU PHE PRO          
SEQRES  16 H  357  GLY HIS VAL GLN ALA TYR ALA GLU ALA VAL LYS SER GLY          
SEQRES  17 H  357  VAL HIS ARG THR VAL HIS ALA GLY GLU VAL GLY SER ALA          
SEQRES  18 H  357  ASN VAL VAL LYS GLU ALA VAL ASP THR LEU LYS THR GLU          
SEQRES  19 H  357  ARG LEU GLY HIS GLY TYR HIS THR LEU GLU ASP THR THR          
SEQRES  20 H  357  LEU TYR ASN ARG LEU ARG GLN GLU ASN MET HIS PHE GLU          
SEQRES  21 H  357  ILE CYS PRO TRP SER SER TYR LEU THR GLY ALA TRP LYS          
SEQRES  22 H  357  PRO ASP THR GLU HIS ALA VAL ILE ARG PHE LYS ASN ASP          
SEQRES  23 H  357  GLN VAL ASN TYR SER LEU ASN THR ASP ASP PRO LEU ILE          
SEQRES  24 H  357  PHE LYS SER THR LEU ASP THR ASP TYR GLN MET THR LYS          
SEQRES  25 H  357  LYS ASP MET GLY PHE THR GLU GLU GLU PHE LYS ARG LEU          
SEQRES  26 H  357  ASN ILE ASN ALA ALA LYS SER SER PHE LEU PRO GLU ASP          
SEQRES  27 H  357  GLU LYS LYS GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR          
SEQRES  28 H  357  ARG MET PRO SER PRO ALA                                      
HET    NAG  A 800      14                                                       
HET    NAG  A 801      14                                                       
HET    AFL  A 802      10                                                       
HET    NAG  A 810      14                                                       
HET    NAG  A 811      14                                                       
HET    NAG  A 820      14                                                       
HET    NAG  A 821      14                                                       
HET    NAG  A 830      14                                                       
HET    NAG  A 831      14                                                       
HET    BMA  A 832      11                                                       
HET    MAN  A 833      11                                                       
HET    NAG  A 840      14                                                       
HET    NAG  A 850      14                                                       
HET    NDG  A 860      14                                                       
HET    NDG  A 870      14                                                       
HET    NAG  B 800      14                                                       
HET    AFL  B 802      10                                                       
HET    NAG  B 810      14                                                       
HET    NAG  B 820      14                                                       
HET    NAG  B 821      14                                                       
HET    NAG  B 830      14                                                       
HET    NAG  B 831      14                                                       
HET    BMA  B 832      11                                                       
HET    MAN  B 833      11                                                       
HET    NAG  B 840      14                                                       
HET    NAG  B 850      14                                                       
HET    NAG  B 851      14                                                       
HET    NDG  B 860      14                                                       
HET    NAG  B 870      14                                                       
HET    NAG  C 800      14                                                       
HET    NAG  C 801      14                                                       
HET    AFL  C 802      10                                                       
HET    NAG  C 810      14                                                       
HET    NAG  C 811      14                                                       
HET    NAG  C 820      14                                                       
HET    NAG  C 821      14                                                       
HET    NAG  C 830      14                                                       
HET    NAG  C 831      14                                                       
HET    BMA  C 832      11                                                       
HET    MAN  C 833      11                                                       
HET    NAG  C 840      14                                                       
HET    NAG  C 850      14                                                       
HET    NAG  C 851      14                                                       
HET    NAG  C 860      14                                                       
HET    NAG  C 870      14                                                       
HET    NAG  D 800      14                                                       
HET    AFL  D 802      10                                                       
HET    NAG  D 810      14                                                       
HET    NAG  D 820      14                                                       
HET    NAG  D 821      14                                                       
HET    NAG  D 830      14                                                       
HET    NAG  D 831      14                                                       
HET    BMA  D 832      11                                                       
HET    MAN  D 833      11                                                       
HET    NAG  D 840      14                                                       
HET    NAG  D 850      14                                                       
HET    NAG  D 851      14                                                       
HET    NAG  D 860      14                                                       
HET    NAG  D 870      14                                                       
HET     ZN  E 501       1                                                       
HET     ZN  F 501       1                                                       
HET     ZN  G 501       1                                                       
HET     ZN  H 501       1                                                       
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM      ZN ZINC ION                                                         
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     AFL BETA-L-FUCOSE                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     NAG NAG                                                              
FORMUL   9   ZN    4(ZN1 2+)                                                    
FORMUL  12  NAG    44(C8 H15 N1 O6)                                             
FORMUL  13  MAN    5(C6 H12 O6)                                                 
FORMUL  14  BMA    4(C6 H12 O6)                                                 
FORMUL  15  AFL    4(C6 H12 O5)                                                 
FORMUL  16  NDG    3(C8 H15 N1 O6)                                              
HELIX    1   1 THR A   44  ASN A   51  1                                   8    
HELIX    2   2 ASP A  200  VAL A  207  1                                   8    
HELIX    3   3 ASP A  274  LEU A  276  5                                   3    
HELIX    4   4 PRO A  290  ILE A  295  1                                   6    
HELIX    5   5 VAL A  341  GLN A  344  5                                   4    
HELIX    6   6 GLU A  421  MET A  425  5                                   5    
HELIX    7   7 ASN A  497  ASN A  506  1                                  10    
HELIX    8   8 ASN A  562  ASN A  572  1                                  11    
HELIX    9   9 GLY A  587  HIS A  592  1                                   6    
HELIX   10  10 ALA A  593  ASN A  595  5                                   3    
HELIX   11  11 THR A  600  MET A  616  1                                  17    
HELIX   12  12 SER A  630  GLY A  641  1                                  12    
HELIX   13  13 ARG A  658  TYR A  662  5                                   5    
HELIX   14  14 ASP A  663  GLY A  672  1                                  10    
HELIX   15  15 ASN A  679  ASN A  685  1                                   7    
HELIX   16  16 VAL A  688  VAL A  698  5                                  11    
HELIX   17  17 HIS A  712  VAL A  726  1                                  15    
HELIX   18  18 SER A  744  SER A  764  1                                  21    
HELIX   19  19 THR B   44  ASN B   51  1                                   8    
HELIX   20  20 ASP B  200  VAL B  207  1                                   8    
HELIX   21  21 ASP B  274  LEU B  276  5                                   3    
HELIX   22  22 PRO B  290  ILE B  295  1                                   6    
HELIX   23  23 LEU B  340  GLN B  344  5                                   5    
HELIX   24  24 GLU B  421  MET B  425  5                                   5    
HELIX   25  25 SER B  446  ASN B  450  5                                   5    
HELIX   26  26 ASN B  497  ASN B  506  1                                  10    
HELIX   27  27 ASN B  562  ASN B  572  1                                  11    
HELIX   28  28 GLY B  587  HIS B  592  1                                   6    
HELIX   29  29 ALA B  593  ASN B  595  5                                   3    
HELIX   30  30 THR B  600  MET B  616  1                                  17    
HELIX   31  31 SER B  630  GLY B  641  1                                  12    
HELIX   32  32 ARG B  658  TYR B  662  5                                   5    
HELIX   33  33 ASP B  663  GLY B  672  1                                  10    
HELIX   34  34 ASN B  679  ASN B  685  1                                   7    
HELIX   35  35 VAL B  688  VAL B  698  5                                  11    
HELIX   36  36 HIS B  712  VAL B  726  1                                  15    
HELIX   37  37 SER B  744  SER B  764  1                                  21    
HELIX   38  38 THR C   44  LYS C   50  1                                   7    
HELIX   39  39 ASP C  200  VAL C  207  1                                   8    
HELIX   40  40 ASP C  274  LEU C  276  5                                   3    
HELIX   41  41 PRO C  290  ILE C  295  1                                   6    
HELIX   42  42 VAL C  341  GLN C  344  5                                   4    
HELIX   43  43 GLU C  421  MET C  425  5                                   5    
HELIX   44  44 SER C  446  ASN C  450  5                                   5    
HELIX   45  45 ASN C  497  ASN C  506  1                                  10    
HELIX   46  46 ASN C  562  ASN C  572  1                                  11    
HELIX   47  47 GLY C  587  HIS C  592  1                                   6    
HELIX   48  48 ALA C  593  ASN C  595  5                                   3    
HELIX   49  49 THR C  600  MET C  616  1                                  17    
HELIX   50  50 SER C  630  GLY C  641  1                                  12    
HELIX   51  51 ARG C  658  TYR C  662  5                                   5    
HELIX   52  52 ASP C  663  GLY C  672  1                                  10    
HELIX   53  53 ASN C  679  ASN C  685  1                                   7    
HELIX   54  54 VAL C  688  VAL C  698  5                                  11    
HELIX   55  55 HIS C  712  GLY C  727  1                                  16    
HELIX   56  56 SER C  744  SER C  764  1                                  21    
HELIX   57  57 THR D   44  ASN D   51  1                                   8    
HELIX   58  58 ASP D  200  VAL D  207  1                                   8    
HELIX   59  59 ASP D  274  LEU D  276  5                                   3    
HELIX   60  60 PRO D  290  ILE D  295  1                                   6    
HELIX   61  61 VAL D  341  GLN D  344  5                                   4    
HELIX   62  62 GLU D  421  MET D  425  5                                   5    
HELIX   63  63 SER D  446  ASN D  450  5                                   5    
HELIX   64  64 ASN D  497  ASN D  506  1                                  10    
HELIX   65  65 ASN D  562  ASN D  572  1                                  11    
HELIX   66  66 GLY D  587  HIS D  592  1                                   6    
HELIX   67  67 ALA D  593  ASN D  595  5                                   3    
HELIX   68  68 THR D  600  MET D  616  1                                  17    
HELIX   69  69 SER D  630  GLY D  641  1                                  12    
HELIX   70  70 ARG D  658  TYR D  662  5                                   5    
HELIX   71  71 ASP D  663  GLY D  672  1                                  10    
HELIX   72  72 ASN D  679  ASN D  685  1                                   7    
HELIX   73  73 VAL D  688  VAL D  698  5                                  11    
HELIX   74  74 HIS D  712  GLY D  727  1                                  16    
HELIX   75  75 SER D  744  SER D  764  1                                  21    
HELIX   76  76 ASP E   19  ALA E   21  5                                   3    
HELIX   77  77 LYS E   23  GLY E   35  1                                  13    
HELIX   78  78 THR E   42  GLY E   51  1                                  10    
HELIX   79  79 THR E   57  ALA E   63  1                                   7    
HELIX   80  80 LYS E   64  ALA E   73  1                                  10    
HELIX   81  81 CYS E   75  ASP E   93  1                                  19    
HELIX   82  82 PRO E  104  ALA E  108  5                                   5    
HELIX   83  83 ILE E  115  GLN E  119  5                                   5    
HELIX   84  84 THR E  125  GLY E  145  1                                  21    
HELIX   85  85 GLN E  158  TYR E  172  1                                  15    
HELIX   86  86 GLY E  190  LEU E  193  5                                   4    
HELIX   87  87 PHE E  194  GLY E  208  1                                  15    
HELIX   88  88 SER E  220  THR E  230  1                                  11    
HELIX   89  89 TYR E  240  LEU E  243  5                                   4    
HELIX   90  90 ASP E  245  GLU E  255  1                                  11    
HELIX   91  91 CYS E  262  GLY E  270  1                                   9    
HELIX   92  92 HIS E  278  ASP E  286  1                                   9    
HELIX   93  93 THR E  303  ASP E  314  1                                  12    
HELIX   94  94 THR E  318  SER E  333  1                                  16    
HELIX   95  95 PRO E  336  TYR E  351  1                                  16    
HELIX   96  96 ASP F   19  ALA F   21  5                                   3    
HELIX   97  97 LYS F   23  GLY F   35  1                                  13    
HELIX   98  98 THR F   42  GLY F   51  1                                  10    
HELIX   99  99 THR F   57  ALA F   63  1                                   7    
HELIX  100 100 LYS F   64  ALA F   73  1                                  10    
HELIX  101 101 CYS F   75  ASP F   93  1                                  19    
HELIX  102 102 PRO F  104  ALA F  108  5                                   5    
HELIX  103 103 THR F  125  GLY F  145  1                                  21    
HELIX  104 104 GLN F  158  TYR F  172  1                                  15    
HELIX  105 105 GLY F  190  LEU F  193  5                                   4    
HELIX  106 106 PHE F  194  GLY F  208  1                                  15    
HELIX  107 107 SER F  220  THR F  230  1                                  11    
HELIX  108 108 TYR F  240  LEU F  243  5                                   4    
HELIX  109 109 ASP F  245  GLU F  255  1                                  11    
HELIX  110 110 CYS F  262  GLY F  270  1                                   9    
HELIX  111 111 HIS F  278  ASP F  286  1                                   9    
HELIX  112 112 THR F  303  ASP F  314  1                                  12    
HELIX  113 113 THR F  318  SER F  333  1                                  16    
HELIX  114 114 PRO F  336  ALA F  350  1                                  15    
HELIX  115 115 LEU G   18  ALA G   21  5                                   4    
HELIX  116 116 LYS G   23  GLY G   35  1                                  13    
HELIX  117 117 THR G   42  GLY G   51  1                                  10    
HELIX  118 118 THR G   57  ALA G   63  1                                   7    
HELIX  119 119 LYS G   64  ALA G   73  1                                  10    
HELIX  120 120 CYS G   75  ASP G   93  1                                  19    
HELIX  121 121 PRO G  104  ALA G  108  5                                   5    
HELIX  122 122 THR G  125  GLY G  145  1                                  21    
HELIX  123 123 GLN G  158  TYR G  172  1                                  15    
HELIX  124 124 GLY G  190  LEU G  193  5                                   4    
HELIX  125 125 PHE G  194  GLY G  208  1                                  15    
HELIX  126 126 SER G  220  THR G  230  1                                  11    
HELIX  127 127 TYR G  240  LEU G  243  5                                   4    
HELIX  128 128 ASP G  245  GLU G  255  1                                  11    
HELIX  129 129 CYS G  262  GLY G  270  1                                   9    
HELIX  130 130 HIS G  278  ASP G  286  1                                   9    
HELIX  131 131 THR G  303  ASP G  314  1                                  12    
HELIX  132 132 THR G  318  SER G  333  1                                  16    
HELIX  133 133 PRO G  336  ARG G  352  1                                  17    
HELIX  134 134 ASP H   19  ALA H   21  5                                   3    
HELIX  135 135 LYS H   23  GLY H   35  1                                  13    
HELIX  136 136 THR H   42  GLY H   51  1                                  10    
HELIX  137 137 THR H   57  ALA H   63  1                                   7    
HELIX  138 138 LYS H   64  ALA H   73  1                                  10    
HELIX  139 139 CYS H   75  ASP H   93  1                                  19    
HELIX  140 140 PRO H  104  ALA H  108  5                                   5    
HELIX  141 141 ILE H  115  GLN H  119  5                                   5    
HELIX  142 142 THR H  125  GLY H  145  1                                  21    
HELIX  143 143 GLN H  158  TYR H  172  1                                  15    
HELIX  144 144 GLY H  190  LEU H  193  5                                   4    
HELIX  145 145 PHE H  194  GLY H  208  1                                  15    
HELIX  146 146 SER H  220  THR H  230  1                                  11    
HELIX  147 147 TYR H  240  LEU H  243  5                                   4    
HELIX  148 148 ASP H  245  GLU H  255  1                                  11    
HELIX  149 149 CYS H  262  GLY H  270  1                                   9    
HELIX  150 150 VAL H  280  ASN H  285  1                                   6    
HELIX  151 151 THR H  303  ASP H  314  1                                  12    
HELIX  152 152 THR H  318  SER H  333  1                                  16    
HELIX  153 153 PRO H  336  TYR H  351  1                                  16    
SHEET    1  AA 2 LYS A  41  THR A  42  0                                        
SHEET    2  AA 2 VAL A 507  GLN A 508  1  N  GLN A 508   O  LYS A  41           
SHEET    1  AB 4 LEU A  60  TRP A  62  0                                        
SHEET    2  AB 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3  AB 4 ASN A  75  ASN A  80 -1  O  ASN A  75   N  GLN A  72           
SHEET    4  AB 4 SER A  86  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1  AC 4 ILE A 102  ILE A 107  0                                        
SHEET    2  AC 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3  AC 4 TYR A 128  ASP A 136 -1  O  THR A 129   N  VAL A 121           
SHEET    4  AC 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1  AD 4 TRP A 154  TRP A 157  0                                        
SHEET    2  AD 4 LEU A 164  TRP A 168 -1  O  ALA A 165   N  THR A 156           
SHEET    3  AD 4 ASP A 171  LYS A 175 -1  O  ASP A 171   N  TRP A 168           
SHEET    4  AD 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1  AE 3 ILE A 194  ASN A 196  0                                        
SHEET    2  AE 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3  AE 3 LEU A 214  TRP A 216 -1  O  TRP A 215   N  ALA A 224           
SHEET    1  AF 4 ILE A 194  ASN A 196  0                                        
SHEET    2  AF 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3  AF 4 THR A 265  ASN A 272 -1  O  THR A 265   N  ASN A 229           
SHEET    4  AF 4 ILE A 285  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1  AG 2 LEU A 235  PHE A 240  0                                        
SHEET    2  AG 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240           
SHEET    1  AH 4 HIS A 298  TRP A 305  0                                        
SHEET    2  AH 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3  AH 4 TYR A 322  TYR A 330 -1  O  TYR A 322   N  ARG A 317           
SHEET    4  AH 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1  AI 4 HIS A 298  TRP A 305  0                                        
SHEET    2  AI 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3  AI 4 TYR A 322  TYR A 330 -1  O  TYR A 322   N  ARG A 317           
SHEET    4  AI 4 TRP A 337  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1  AJ 4 HIS A 363  PHE A 364  0                                        
SHEET    2  AJ 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3  AJ 4 ARG A 382  GLN A 388 -1  O  HIS A 383   N  ILE A 375           
SHEET    4  AJ 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1  AK 4 VAL A 404  LEU A 410  0                                        
SHEET    2  AK 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  GLU A 408           
SHEET    3  AK 4 ASN A 430  GLN A 435 -1  O  ASN A 430   N  SER A 419           
SHEET    4  AK 4 ASP A 438  CYS A 444 -1  N  ASP A 438   O  GLN A 435           
SHEET    1  AL 4 TYR A 457  PHE A 461  0                                        
SHEET    2  AL 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3  AL 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4  AL 4 LYS A 489  GLU A 495 -1  O  LYS A 489   N  SER A 484           
SHEET    1  AM 8 SER A 511  LEU A 519  0                                        
SHEET    2  AM 8 THR A 522  LEU A 530 -1  O  THR A 522   N  LEU A 519           
SHEET    3  AM 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4  AM 8 TYR A 540  VAL A 546  1  O  PRO A 541   N  ILE A 574           
SHEET    5  AM 8 VAL A 619  TRP A 629  1  N  ASP A 620   O  TYR A 540           
SHEET    6  AM 8 CYS A 649  VAL A 653  1  O  CYS A 649   N  ILE A 626           
SHEET    7  AM 8 GLU A 699  GLY A 705  1  O  GLU A 699   N  GLY A 650           
SHEET    8  AM 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  LEU A 702           
SHEET    1  BA 2 LYS B  41  THR B  42  0                                        
SHEET    2  BA 2 VAL B 507  GLN B 508  1  N  GLN B 508   O  LYS B  41           
SHEET    1  BB 4 ARG B  61  TRP B  62  0                                        
SHEET    2  BB 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3  BB 4 ASN B  75  ASN B  80 -1  O  ASN B  75   N  GLN B  72           
SHEET    4  BB 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78           
SHEET    1  BC 4 ILE B 102  ILE B 107  0                                        
SHEET    2  BC 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3  BC 4 TYR B 128  ASP B 136 -1  O  THR B 129   N  VAL B 121           
SHEET    4  BC 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1  BD 4 TRP B 154  TRP B 157  0                                        
SHEET    2  BD 4 LEU B 164  TRP B 168 -1  O  ALA B 165   N  THR B 156           
SHEET    3  BD 4 ASP B 171  LYS B 175 -1  O  ASP B 171   N  TRP B 168           
SHEET    4  BD 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1  BE 3 ILE B 194  ASN B 196  0                                        
SHEET    2  BE 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3  BE 3 LEU B 214  TRP B 216 -1  O  TRP B 215   N  ALA B 224           
SHEET    1  BF 4 ILE B 194  ASN B 196  0                                        
SHEET    2  BF 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3  BF 4 THR B 265  ASN B 272 -1  O  THR B 265   N  ASN B 229           
SHEET    4  BF 4 SER B 284  ILE B 287 -1  O  ILE B 285   N  VAL B 270           
SHEET    1  BG 2 LEU B 235  PHE B 240  0                                        
SHEET    2  BG 2 LYS B 250  PRO B 255 -1  O  LYS B 250   N  PHE B 240           
SHEET    1  BH 7 HIS B 298  TRP B 305  0                                        
SHEET    2  BH 7 ARG B 310  ARG B 317 -1  O  SER B 312   N  THR B 304           
SHEET    3  BH 7 TYR B 322  TYR B 330 -1  O  TYR B 322   N  ARG B 317           
SHEET    4  BH 7 TRP B 337  ASN B 338 -1  O  ASN B 338   N  ASP B 329           
SHEET    5  BH 7 TYR B 322  TYR B 330 -1  O  ASP B 329   N  ASN B 338           
SHEET    6  BH 7 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    7  BH 7 TYR B 322  TYR B 330 -1  O  SER B 323   N  GLU B 347           
SHEET    1  BI 4 HIS B 363  PHE B 364  0                                        
SHEET    2  BI 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3  BI 4 ARG B 382  GLN B 388 -1  O  HIS B 383   N  ILE B 375           
SHEET    4  BI 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1  BJ 4 VAL B 404  LEU B 410  0                                        
SHEET    2  BJ 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  GLU B 408           
SHEET    3  BJ 4 ASN B 430  GLN B 435 -1  O  ASN B 430   N  SER B 419           
SHEET    4  BJ 4 ASP B 438  CYS B 444 -1  N  ASP B 438   O  GLN B 435           
SHEET    1  BK 4 TYR B 457  PHE B 461  0                                        
SHEET    2  BK 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3  BK 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4  BK 4 LYS B 489  GLU B 495 -1  O  LYS B 489   N  SER B 484           
SHEET    1  BL 8 SER B 511  LEU B 519  0                                        
SHEET    2  BL 8 THR B 522  LEU B 530 -1  O  THR B 522   N  LEU B 519           
SHEET    3  BL 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4  BL 8 TYR B 540  ASP B 545  1  O  PRO B 541   N  ILE B 574           
SHEET    5  BL 8 VAL B 619  TRP B 629  1  N  ASP B 620   O  TYR B 540           
SHEET    6  BL 8 CYS B 649  VAL B 653  1  O  CYS B 649   N  ILE B 626           
SHEET    7  BL 8 GLU B 699  GLY B 705  1  O  GLU B 699   N  GLY B 650           
SHEET    8  BL 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  LEU B 702           
SHEET    1  CA 2 LYS C  41  THR C  42  0                                        
SHEET    2  CA 2 VAL C 507  GLN C 508  1  N  GLN C 508   O  LYS C  41           
SHEET    1  CB 4 ARG C  61  TRP C  62  0                                        
SHEET    2  CB 4 GLU C  67  LYS C  71 -1  O  LEU C  69   N  ARG C  61           
SHEET    3  CB 4 ILE C  76  ASN C  80 -1  O  LEU C  77   N  TYR C  70           
SHEET    4  CB 4 SER C  86  LEU C  90 -1  O  SER C  87   N  VAL C  78           
SHEET    1  CC 4 ILE C 102  ILE C 107  0                                        
SHEET    2  CC 4 PHE C 113  LYS C 122 -1  O  LEU C 115   N  SER C 106           
SHEET    3  CC 4 TYR C 128  ASP C 136 -1  O  THR C 129   N  VAL C 121           
SHEET    4  CC 4 GLN C 141  LEU C 142 -1  O  GLN C 141   N  ASP C 136           
SHEET    1  CD 4 TRP C 154  TRP C 157  0                                        
SHEET    2  CD 4 LEU C 164  TRP C 168 -1  O  ALA C 165   N  THR C 156           
SHEET    3  CD 4 ASP C 171  LYS C 175 -1  O  ASP C 171   N  TRP C 168           
SHEET    4  CD 4 TYR C 183  ARG C 184 -1  O  TYR C 183   N  VAL C 174           
SHEET    1  CE 7 ILE C 194  ASN C 196  0                                        
SHEET    2  CE 7 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3  CE 7 LEU C 214  TRP C 216 -1  O  TRP C 215   N  ALA C 224           
SHEET    4  CE 7 PHE C 222  ASN C 229 -1  O  ALA C 224   N  TRP C 215           
SHEET    5  CE 7 SER C 284  GLN C 286                                           
SHEET    6  CE 7 THR C 265  ASN C 272 -1  O  VAL C 270   N  ILE C 285           
SHEET    7  CE 7 PHE C 222  ASN C 229 -1  O  LEU C 223   N  VAL C 271           
SHEET    1  CF 2 LEU C 235  PHE C 240  0                                        
SHEET    2  CF 2 LYS C 250  PRO C 255 -1  O  LYS C 250   N  PHE C 240           
SHEET    1  CG 7 HIS C 298  TRP C 305  0                                        
SHEET    2  CG 7 ARG C 310  ARG C 317 -1  O  SER C 312   N  THR C 304           
SHEET    3  CG 7 TYR C 322  TYR C 330 -1  O  TYR C 322   N  ARG C 317           
SHEET    4  CG 7 TRP C 337  CYS C 339 -1  O  ASN C 338   N  ASP C 329           
SHEET    5  CG 7 TYR C 322  TYR C 330 -1  O  ASP C 329   N  ASN C 338           
SHEET    6  CG 7 HIS C 345  MET C 348 -1  O  HIS C 345   N  MET C 325           
SHEET    7  CG 7 TYR C 322  TYR C 330 -1  O  SER C 323   N  GLU C 347           
SHEET    1  CH 4 HIS C 363  PHE C 364  0                                        
SHEET    2  CH 4 SER C 370  SER C 376 -1  O  TYR C 372   N  HIS C 363           
SHEET    3  CH 4 ARG C 382  GLN C 388 -1  O  HIS C 383   N  ILE C 375           
SHEET    4  CH 4 CYS C 394  PHE C 396 -1  O  THR C 395   N  TYR C 386           
SHEET    1  CI 4 VAL C 404  LEU C 410  0                                        
SHEET    2  CI 4 TYR C 414  SER C 419 -1  O  TYR C 416   N  GLU C 408           
SHEET    3  CI 4 ASN C 430  GLN C 435 -1  O  ASN C 430   N  SER C 419           
SHEET    4  CI 4 ASP C 438  CYS C 444 -1  N  ASP C 438   O  GLN C 435           
SHEET    1  CJ 4 TYR C 457  PHE C 461  0                                        
SHEET    2  CJ 4 TYR C 467  CYS C 472 -1  O  GLN C 469   N  SER C 460           
SHEET    3  CJ 4 LEU C 479  SER C 484 -1  O  LEU C 479   N  CYS C 472           
SHEET    4  CJ 4 LYS C 489  GLU C 495 -1  O  LYS C 489   N  SER C 484           
SHEET    1  CK 8 SER C 511  LEU C 519  0                                        
SHEET    2  CK 8 THR C 522  LEU C 530 -1  O  THR C 522   N  LEU C 519           
SHEET    3  CK 8 ILE C 574  PHE C 578 -1  O  VAL C 575   N  ILE C 529           
SHEET    4  CK 8 TYR C 540  VAL C 546  1  O  PRO C 541   N  ILE C 574           
SHEET    5  CK 8 VAL C 619  TRP C 629  1  N  ASP C 620   O  TYR C 540           
SHEET    6  CK 8 CYS C 649  VAL C 653  1  O  CYS C 649   N  ILE C 626           
SHEET    7  CK 8 GLU C 699  GLY C 705  1  O  GLU C 699   N  GLY C 650           
SHEET    8  CK 8 GLN C 731  TYR C 735  1  O  GLN C 731   N  LEU C 702           
SHEET    1  DA 4 ARG D  61  TRP D  62  0                                        
SHEET    2  DA 4 GLU D  67  GLN D  72 -1  O  LEU D  69   N  ARG D  61           
SHEET    3  DA 4 ASN D  75  ASN D  80 -1  O  ASN D  75   N  GLN D  72           
SHEET    4  DA 4 SER D  86  LEU D  90 -1  O  SER D  87   N  VAL D  78           
SHEET    1  DB 4 ILE D 102  ILE D 107  0                                        
SHEET    2  DB 4 PHE D 113  LYS D 122 -1  O  LEU D 115   N  SER D 106           
SHEET    3  DB 4 TYR D 128  ASP D 136 -1  O  THR D 129   N  VAL D 121           
SHEET    4  DB 4 GLN D 141  LEU D 142 -1  O  GLN D 141   N  ASP D 136           
SHEET    1  DC 4 TRP D 154  TRP D 157  0                                        
SHEET    2  DC 4 LEU D 164  TRP D 168 -1  O  ALA D 165   N  THR D 156           
SHEET    3  DC 4 ASP D 171  LYS D 175 -1  O  ASP D 171   N  TRP D 168           
SHEET    4  DC 4 TYR D 183  ARG D 184 -1  O  TYR D 183   N  VAL D 174           
SHEET    1  DD 7 ILE D 194  ASN D 196  0                                        
SHEET    2  DD 7 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3  DD 7 LEU D 214  TRP D 216 -1  O  TRP D 215   N  ALA D 224           
SHEET    4  DD 7 PHE D 222  ASN D 229 -1  O  ALA D 224   N  TRP D 215           
SHEET    5  DD 7 ILE D 285  GLN D 286                                           
SHEET    6  DD 7 THR D 265  ASN D 272 -1  O  VAL D 270   N  ILE D 285           
SHEET    7  DD 7 PHE D 222  ASN D 229 -1  O  LEU D 223   N  VAL D 271           
SHEET    1  DE 2 LEU D 235  PHE D 240  0                                        
SHEET    2  DE 2 LYS D 250  PRO D 255 -1  O  LYS D 250   N  PHE D 240           
SHEET    1  DF 7 HIS D 298  TRP D 305  0                                        
SHEET    2  DF 7 ARG D 310  ARG D 317 -1  O  SER D 312   N  THR D 304           
SHEET    3  DF 7 TYR D 322  TYR D 330 -1  O  TYR D 322   N  ARG D 317           
SHEET    4  DF 7 TRP D 337  CYS D 339 -1  O  ASN D 338   N  ASP D 329           
SHEET    5  DF 7 TYR D 322  TYR D 330 -1  O  ASP D 329   N  ASN D 338           
SHEET    6  DF 7 GLU D 347  MET D 348 -1  O  GLU D 347   N  SER D 323           
SHEET    7  DF 7 TYR D 322  TYR D 330 -1  O  SER D 323   N  GLU D 347           
SHEET    1  DG 4 HIS D 363  PHE D 364  0                                        
SHEET    2  DG 4 SER D 370  SER D 376 -1  O  TYR D 372   N  HIS D 363           
SHEET    3  DG 4 ARG D 382  GLN D 388 -1  O  HIS D 383   N  ILE D 375           
SHEET    4  DG 4 THR D 395  PHE D 396 -1  O  THR D 395   N  TYR D 386           
SHEET    1  DH 4 VAL D 404  LEU D 410  0                                        
SHEET    2  DH 4 TYR D 414  SER D 419 -1  O  TYR D 416   N  GLU D 408           
SHEET    3  DH 4 ASN D 430  GLN D 435 -1  O  ASN D 430   N  SER D 419           
SHEET    4  DH 4 ASP D 438  CYS D 444 -1  N  ASP D 438   O  GLN D 435           
SHEET    1  DI 4 TYR D 457  PHE D 461  0                                        
SHEET    2  DI 4 TYR D 467  CYS D 472 -1  O  GLN D 469   N  SER D 460           
SHEET    3  DI 4 LEU D 479  SER D 484 -1  O  LEU D 479   N  CYS D 472           
SHEET    4  DI 4 LYS D 489  GLU D 495 -1  O  LYS D 489   N  SER D 484           
SHEET    1  DJ 8 SER D 511  LEU D 519  0                                        
SHEET    2  DJ 8 THR D 522  LEU D 530 -1  O  THR D 522   N  LEU D 519           
SHEET    3  DJ 8 ILE D 574  PHE D 578 -1  O  VAL D 575   N  ILE D 529           
SHEET    4  DJ 8 TYR D 540  VAL D 546  1  O  PRO D 541   N  ILE D 574           
SHEET    5  DJ 8 VAL D 619  TRP D 629  1  N  ASP D 620   O  TYR D 540           
SHEET    6  DJ 8 CYS D 649  VAL D 653  1  O  CYS D 649   N  ILE D 626           
SHEET    7  DJ 8 GLU D 699  GLY D 705  1  O  GLU D 699   N  GLY D 650           
SHEET    8  DJ 8 GLN D 731  TYR D 735  1  O  GLN D 731   N  LEU D 702           
SHEET    1  EA 8 LYS E  11  HIS E  17  0                                        
SHEET    2  EA 8 VAL E  95  TYR E 102  1  N  VAL E  96   O  LYS E  11           
SHEET    3  EA 8 LYS E 147  MET E 155  1  O  LYS E 147   N  VAL E  98           
SHEET    4  EA 8 VAL E 177  ALA E 183  1  N  VAL E 178   O  SER E 150           
SHEET    5  EA 8 HIS E 210  ALA E 215  1  O  HIS E 210   N  ILE E 180           
SHEET    6  EA 8 ARG E 235  HIS E 238  1  O  ARG E 235   N  VAL E 213           
SHEET    7  EA 8 HIS E 258  ILE E 261  1  O  HIS E 258   N  LEU E 236           
SHEET    8  EA 8 TYR E 290  LEU E 292  1  O  SER E 291   N  ILE E 261           
SHEET    1  FA 8 LYS F  11  HIS F  17  0                                        
SHEET    2  FA 8 VAL F  95  TYR F 102  1  N  VAL F  96   O  LYS F  11           
SHEET    3  FA 8 LYS F 147  MET F 155  1  O  LYS F 147   N  VAL F  98           
SHEET    4  FA 8 VAL F 177  ALA F 183  1  N  VAL F 178   O  SER F 150           
SHEET    5  FA 8 HIS F 210  ALA F 215  1  O  HIS F 210   N  ILE F 180           
SHEET    6  FA 8 ARG F 235  HIS F 238  1  O  ARG F 235   N  VAL F 213           
SHEET    7  FA 8 HIS F 258  ILE F 261  1  O  HIS F 258   N  LEU F 236           
SHEET    8  FA 8 TYR F 290  LEU F 292  1  O  SER F 291   N  ILE F 261           
SHEET    1  GA 8 LYS G  11  GLU G  13  0                                        
SHEET    2  GA 8 VAL G  95  TYR G 102  1  N  VAL G  96   O  LYS G  11           
SHEET    3  GA 8 LYS G 147  MET G 155  1  O  LYS G 147   N  VAL G  98           
SHEET    4  GA 8 VAL G 177  ALA G 183  1  N  VAL G 178   O  SER G 150           
SHEET    5  GA 8 HIS G 210  ALA G 215  1  O  HIS G 210   N  ILE G 180           
SHEET    6  GA 8 ARG G 235  HIS G 238  1  O  ARG G 235   N  VAL G 213           
SHEET    7  GA 8 HIS G 258  ILE G 261  1  O  HIS G 258   N  LEU G 236           
SHEET    8  GA 8 TYR G 290  LEU G 292  1  O  SER G 291   N  ILE G 261           
SHEET    1  HA 8 LYS H  11  HIS H  17  0                                        
SHEET    2  HA 8 VAL H  95  TYR H 102  1  N  VAL H  96   O  LYS H  11           
SHEET    3  HA 8 LYS H 147  MET H 155  1  O  LYS H 147   N  VAL H  98           
SHEET    4  HA 8 VAL H 177  ALA H 183  1  N  VAL H 178   O  SER H 150           
SHEET    5  HA 8 HIS H 210  ALA H 215  1  O  HIS H 210   N  ILE H 180           
SHEET    6  HA 8 ARG H 235  HIS H 238  1  O  ARG H 235   N  VAL H 213           
SHEET    7  HA 8 HIS H 258  ILE H 261  1  O  HIS H 258   N  LEU H 236           
SHEET    8  HA 8 ASN H 289  LEU H 292  1  O  ASN H 289   N  PHE H 259           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555        
SSBOND   2 CYS A  385    CYS A  394                          1555   1555        
SSBOND   3 CYS A  444    CYS A  447                          1555   1555        
SSBOND   4 CYS A  454    CYS A  472                          1555   1555        
SSBOND   5 CYS A  649    CYS A  762                          1555   1555        
SSBOND   6 CYS B  328    CYS B  339                          1555   1555        
SSBOND   7 CYS B  385    CYS B  394                          1555   1555        
SSBOND   8 CYS B  444    CYS B  447                          1555   1555        
SSBOND   9 CYS B  454    CYS B  472                          1555   1555        
SSBOND  10 CYS B  649    CYS B  762                          1555   1555        
SSBOND  11 CYS C  328    CYS C  339                          1555   1555        
SSBOND  12 CYS C  385    CYS C  394                          1555   1555        
SSBOND  13 CYS C  444    CYS C  447                          1555   1555        
SSBOND  14 CYS C  454    CYS C  472                          1555   1555        
SSBOND  15 CYS C  649    CYS C  762                          1555   1555        
SSBOND  16 CYS D  328    CYS D  339                          1555   1555        
SSBOND  17 CYS D  385    CYS D  394                          1555   1555        
SSBOND  18 CYS D  444    CYS D  447                          1555   1555        
SSBOND  19 CYS D  454    CYS D  472                          1555   1555        
SSBOND  20 CYS D  649    CYS D  762                          1555   1555        
LINK         ND2 ASN A  85                 C1  NAG A 800     1555   1555        
LINK         ND2 ASN A  92                 C1  NDG A 870     1555   1555        
LINK         ND2 ASN A 150                 C1  NAG A 810     1555   1555        
LINK         ND2 ASN A 219                 C1  NAG A 820     1555   1555        
LINK         ND2 ASN A 229                 C1  NAG A 830     1555   1555        
LINK         ND2 ASN A 281                 C1  NAG A 840     1555   1555        
LINK         ND2 ASN A 321                 C1  NAG A 850     1555   1555        
LINK         ND2 ASN A 520                 C1  NDG A 860     1555   1555        
LINK         O6  NAG A 800                 C1  AFL A 802     1555   1555        
LINK         O4  NAG A 800                 C1  NAG A 801     1555   1555        
LINK         O4  NAG A 810                 C1  NAG A 811     1555   1555        
LINK         O4  NAG A 820                 C1  NAG A 821     1555   1555        
LINK         O4  NAG A 830                 C1  NAG A 831     1555   1555        
LINK         O4  NAG A 831                 C1  BMA A 832     1555   1555        
LINK         O3  BMA A 832                 C1  MAN A 833     1555   1555        
LINK         ND2 ASN B  85                 C1  NAG B 800     1555   1555        
LINK         ND2 ASN B  92                 C1  NAG B 870     1555   1555        
LINK         ND2 ASN B 150                 C1  NAG B 810     1555   1555        
LINK         ND2 ASN B 219                 C1  NAG B 820     1555   1555        
LINK         ND2 ASN B 229                 C1  NAG B 830     1555   1555        
LINK         ND2 ASN B 281                 C1  NAG B 840     1555   1555        
LINK         ND2 ASN B 321                 C1  NAG B 850     1555   1555        
LINK         ND2 ASN B 520                 C1  NDG B 860     1555   1555        
LINK         O6  NAG B 800                 C1  AFL B 802     1555   1555        
LINK         O4  NAG B 820                 C1  NAG B 821     1555   1555        
LINK         O4  NAG B 830                 C1  NAG B 831     1555   1555        
LINK         O4  NAG B 831                 C1  BMA B 832     1555   1555        
LINK         O3  BMA B 832                 C1  MAN B 833     1555   1555        
LINK         O4  NAG B 850                 C1  NAG B 851     1555   1555        
LINK         ND2 ASN C  85                 C1  NAG C 800     1555   1555        
LINK         ND2 ASN C  92                 C1  NAG C 870     1555   1555        
LINK         ND2 ASN C 150                 C1  NAG C 810     1555   1555        
LINK         ND2 ASN C 219                 C1  NAG C 820     1555   1555        
LINK         ND2 ASN C 229                 C1  NAG C 830     1555   1555        
LINK         ND2 ASN C 281                 C1  NAG C 840     1555   1555        
LINK         ND2 ASN C 321                 C1  NAG C 850     1555   1555        
LINK         ND2 ASN C 520                 C1  NAG C 860     1555   1555        
LINK         O4  NAG C 800                 C1  NAG C 801     1555   1555        
LINK         O6  NAG C 800                 C1  AFL C 802     1555   1555        
LINK         O4  NAG C 810                 C1  NAG C 811     1555   1555        
LINK         O4  NAG C 820                 C1  NAG C 821     1555   1555        
LINK         O4  NAG C 830                 C1  NAG C 831     1555   1555        
LINK         O4  NAG C 831                 C1  BMA C 832     1555   1555        
LINK         O3  BMA C 832                 C1  MAN C 833     1555   1555        
LINK         O4  NAG C 850                 C1  NAG C 851     1555   1555        
LINK         ND2 ASN D  85                 C1  NAG D 800     1555   1555        
LINK         ND2 ASN D  92                 C1  NAG D 870     1555   1555        
LINK         ND2 ASN D 150                 C1  NAG D 810     1555   1555        
LINK         ND2 ASN D 219                 C1  NAG D 820     1555   1555        
LINK         ND2 ASN D 229                 C1  NAG D 830     1555   1555        
LINK         ND2 ASN D 281                 C1  NAG D 840     1555   1555        
LINK         ND2 ASN D 321                 C1  NAG D 850     1555   1555        
LINK         ND2 ASN D 520                 C1  NAG D 860     1555   1555        
LINK         O6  NAG D 800                 C1  AFL D 802     1555   1555        
LINK         O4  NAG D 820                 C1  NAG D 821     1555   1555        
LINK         O4  NAG D 830                 C1  NAG D 831     1555   1555        
LINK         O4  NAG D 831                 C1  BMA D 832     1555   1555        
LINK         O3  BMA D 832                 C1  MAN D 833     1555   1555        
LINK         O4  NAG D 850                 C1  NAG D 851     1555   1555        
LINK        ZN    ZN E 501                 NE2 HIS E 214     1555   1555        
LINK        ZN    ZN E 501                 NE2 HIS E  17     1555   1555        
LINK        ZN    ZN E 501                 NE2 HIS E  15     1555   1555        
LINK        ZN    ZN E 501                 OD1 ASP E 295     1555   1555        
LINK        ZN    ZN F 501                 NE2 HIS F  15     1555   1555        
LINK        ZN    ZN F 501                 NE2 HIS F 214     1555   1555        
LINK        ZN    ZN F 501                 OD1 ASP F 295     1555   1555        
LINK        ZN    ZN F 501                 NE2 HIS F  17     1555   1555        
LINK        ZN    ZN G 501                 NE2 HIS G  15     1555   1555        
LINK        ZN    ZN G 501                 OD1 ASP G 295     1555   1555        
LINK        ZN    ZN G 501                 NE2 HIS G  17     1555   1555        
LINK        ZN    ZN G 501                 NE2 HIS G 214     1555   1555        
LINK        ZN    ZN H 501                 OD1 ASP H 295     1555   1555        
LINK        ZN    ZN H 501                 NE2 HIS H 214     1555   1555        
LINK        ZN    ZN H 501                 NE2 HIS H  17     1555   1555        
LINK        ZN    ZN H 501                 NE2 HIS H  15     1555   1555        
CISPEP   1 GLY A  474    PRO A  475          0        -0.04                     
CISPEP   2 GLY B  474    PRO B  475          0         0.13                     
CISPEP   3 GLY C  474    PRO C  475          0        -0.87                     
CISPEP   4 GLY D  474    PRO D  475          0         0.40                     
CISPEP   5 GLU E  121    GLY E  122          0         4.78                     
CISPEP   6 GLU F  121    GLY F  122          0         4.97                     
CISPEP   7 GLU G  121    GLY G  122          0         6.05                     
CISPEP   8 GLU H  121    GLY H  122          0         5.80                     
SITE     1 AC1  3 ASN A  85  SER A  86  SER A  87                               
SITE     1 AC4  2 ARG A 147  ASN A 150                                          
SITE     1 AC5  1 ARG A 147                                                     
SITE     1 AC6  3 ASN A 219  THR A 221  GLU A 309                               
SITE     1 AC7  2 TYR A 330  GLU A 332                                          
SITE     1 AC8  4 ILE A 194  ASN A 229  THR A 231  GLU A 232                    
SITE     1 AC9  3 ARG F  33  ARG F  34  GLY F  35                               
SITE     1 BC1  2 ARG F  34  GLY F  35                                          
SITE     1 BC2  2 GLY F  35  ILE F  36                                          
SITE     1 BC3  2 TRP A 187  ASN A 281                                          
SITE     1 BC4  4 ILE A 319  ASN A 321  SER A 349  ARG A 596                    
SITE     1 BC6  2 ASN A 520  ARG A 581                                          
SITE     1 BC7  3 GLU A  73  ASN A  75  ASN A  92                               
SITE     1 BC8  2 ASN B  85  SER B  87                                          
SITE     1 BC9  3 TYR B  83  SER C 412  ASP C 413                               
SITE     1 CC1  2 ILE B 148  ASN B 150                                          
SITE     1 CC2  4 ASN B 219  THR B 221  GLN B 308  GLU B 309                    
SITE     1 CC3  2 THR B 221  GLU B 332                                          
SITE     1 CC4  4 ASN B 229  THR B 231  GLU B 232  ARG E  33                    
SITE     1 CC5  4 THR B 231  ARG E  33  ARG E  34  GLY E  35                    
SITE     1 CC6  1 GLY E  35                                                     
SITE     1 CC7  2 GLY E  35  ILE E  36                                          
SITE     1 CC8  3 ASN A 450  TRP B 187  ASN B 281                               
SITE     1 CC9  1 ASN B 321                                                     
SITE     1 DC2  2 ASN B 520  ARG B 581                                          
SITE     1 DC3  5 GLU B  73  ASN B  74  ASN B  75  ASN B  92                    
SITE     2 DC3  5 ARG F 352                                                     
SITE     1 DC4  4 GLU C  67  ASN C  85  SER C  86  SER C  87                    
SITE     1 DC6  1 TYR C  83                                                     
SITE     1 DC7  3 ARG C 147  ILE C 148  ASN C 150                               
SITE     1 DC8  1 ARG C 147                                                     
SITE     1 DC9  4 ASN C 219  THR C 221  GLN C 308  GLU C 309                    
SITE     1 FC1  2 GLU C 309  GLU C 332                                          
SITE     1 FC2  5 ILE C 194  ASN C 229  THR C 231  GLU C 232                    
SITE     2 FC2  5 ARG G  33                                                     
SITE     1 FC3  3 ARG G  33  ARG G  34  GLY G  35                               
SITE     1 FC4  1 GLY G  35                                                     
SITE     1 FC5  1 ILE G  36                                                     
SITE     1 FC7  1 ASN C 321                                                     
SITE     1 FC9  2 ASN C 520  ARG C 581                                          
SITE     1 GC1  3 GLU C  73  ASN C  75  ASN C  92                               
SITE     1 GC2  3 ASN D  85  SER D  86  SER D  87                               
SITE     1 GC3  1 GLU B 521                                                     
SITE     1 GC4  2 ARG D 147  ASN D 150                                          
SITE     1 GC5  4 ASN D 219  THR D 221  GLN D 308  GLU D 309                    
SITE     1 GC6  2 GLU D 309  TYR D 330                                          
SITE     1 GC7  3 ASN D 229  THR D 231  GLU D 232                               
SITE     1 GC8  3 ARG H  33  ARG H  34  GLY H  35                               
SITE     1 GC9  1 GLY H  35                                                     
SITE     1 HC2  3 ASN C 450  TRP D 187  ASN D 281                               
SITE     1 HC3  3 ASN D 321  SER D 349  ARG D 596                               
SITE     1 HC4  1 GLU D 677                                                     
SITE     1 HC5  2 ASN D 520  ARG D 581                                          
SITE     1 HC6  3 GLU D  73  ASN D  75  ASN D  92                               
SITE     1 HC7  4 HIS E  15  HIS E  17  HIS E 214  ASP E 295                    
SITE     1 HC8  4 HIS F  15  HIS F  17  HIS F 214  ASP F 295                    
SITE     1 HC9  4 HIS G  15  HIS G  17  HIS G 214  ASP G 295                    
SITE     1 IC1  5 HIS H  15  HIS H  17  HIS H 214  HIS H 238                    
SITE     2 IC1  5 ASP H 295                                                     
CRYST1  158.065  168.504  236.842  90.00 100.54  90.00 C 1 2 1      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      0.006327  0.000000  0.001177        0.00000                         
SCALE2      0.000000  0.005935  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004295        0.00000                         
TER    5964      PRO A 766                                                      
TER   11928      PRO B 766                                                      
TER   17892      PRO C 766                                                      
TER   23856      PRO D 766                                                      
TER   26666      SER E 355                                                      
TER   29475      SER F 355                                                      
TER   32285      SER G 355                                                      
TER   35095      SER H 355                                                      
MASTER      660    0   63  153  231    0   59    635877    8  879  336          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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