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Database: PDB
Entry: 4UFB
LinkDB: 4UFB
Original site: 4UFB 
HEADER    HYDROLASE                               16-MAR-15   4UFB              
TITLE     CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN IN  
TITLE    2 COMPLEX WITH LYS-PRO                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N DOMAIN (UNP RESIDUES 30-657);                            
COMPND   5 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, HUMAN      
COMPND   6 ANGIOTENSIN-CONVERTING ENZYME N-DOMAIN;                              
COMPND   7 EC: 3.4.15.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: MINIMALLY GLYCOSYLATED MUTANT                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO K1                                  
KEYWDS    HYDROLASE, ANGIOTENSIN-CONVERTING ENZYME, METALLOPROTEASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MASUYER,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA                        
REVDAT   2   20-JUN-18 4UFB    1       REMARK LINK                              
REVDAT   1   07-OCT-15 4UFB    0                                                
JRNL        AUTH   G.MASUYER,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA               
JRNL        TITL   STRUCTURAL BASIS OF AC-SDKP HYDROLYSIS BY ANGIOTENSIN-I      
JRNL        TITL 2 CONVERTING ENZYME                                            
JRNL        REF    SCI.REP.                      V.   5 13742 2015              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   26403559                                                     
JRNL        DOI    10.1038/SREP13742                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 113.94                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 279271                         
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14577                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 20470                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1043                         
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19752                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 644                                     
REMARK   3   SOLVENT ATOMS            : 1611                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.92000                                             
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : 0.47000                                              
REMARK   3    B12 (A**2) : -0.47000                                             
REMARK   3    B13 (A**2) : -0.08000                                             
REMARK   3    B23 (A**2) : 0.14000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.130         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.122         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.043         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21103 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28725 ; 1.185 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2436 ; 5.273 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1061 ;34.871 ;23.770       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3213 ;13.370 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   131 ;17.054 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3010 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16369 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9738 ; 0.878 ; 2.002       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12158 ; 1.497 ; 2.995       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11365 ; 1.240 ; 2.223       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A  1204                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.8989  24.4251  -1.9263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0701 T22:   0.0381                                     
REMARK   3      T33:   0.0960 T12:   0.0400                                     
REMARK   3      T13:  -0.0627 T23:  -0.0444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1469 L22:   0.3725                                     
REMARK   3      L33:   0.3525 L12:   0.1762                                     
REMARK   3      L13:  -0.0715 L23:  -0.1393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0598 S12:   0.0020 S13:   0.0030                       
REMARK   3      S21:   0.0340 S22:  -0.0417 S23:   0.0154                       
REMARK   3      S31:   0.0124 S32:   0.0659 S33:  -0.0180                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B  1205                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8774  66.3664 -59.6195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0906 T22:   0.0357                                     
REMARK   3      T33:   0.0996 T12:   0.0305                                     
REMARK   3      T13:  -0.0747 T23:  -0.0298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3652 L22:   0.4507                                     
REMARK   3      L33:   0.2906 L12:   0.3168                                     
REMARK   3      L13:   0.1280 L23:  -0.0476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0080 S12:   0.1000 S13:  -0.0087                       
REMARK   3      S21:   0.1040 S22:   0.0920 S23:  -0.0226                       
REMARK   3      S31:  -0.0050 S32:   0.0479 S33:  -0.1000                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C  1202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7582  76.7828   1.1502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0534 T22:   0.0473                                     
REMARK   3      T33:   0.0672 T12:   0.0218                                     
REMARK   3      T13:  -0.0520 T23:  -0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5788 L22:   0.1081                                     
REMARK   3      L33:   0.1513 L12:  -0.0532                                     
REMARK   3      L13:   0.1498 L23:   0.0639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0275 S12:   0.0554 S13:  -0.0099                       
REMARK   3      S21:   0.0289 S22:   0.0032 S23:   0.0030                       
REMARK   3      S31:  -0.0180 S32:   0.0063 S33:   0.0243                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D  1202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.4847  18.1506 -56.4484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0719 T22:   0.0289                                     
REMARK   3      T33:   0.0737 T12:   0.0237                                     
REMARK   3      T13:  -0.0583 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3395 L22:   0.1241                                     
REMARK   3      L33:   0.2288 L12:  -0.0558                                     
REMARK   3      L13:  -0.0017 L23:   0.0434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0040 S12:   0.0526 S13:  -0.0335                       
REMARK   3      S21:   0.0587 S22:   0.0109 S23:  -0.0190                       
REMARK   3      S31:  -0.0243 S32:   0.0067 S33:  -0.0069                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 RIDING   
REMARK   3  POSITIONS. DI-PEPTIDE LYS-PRO IS PRODUCT OF AC-SDKP CLEAVAGE        
REMARK   3  REACTION BY ACE                                                     
REMARK   4                                                                      
REMARK   4 4UFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063348.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 293868                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3NXQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06 M DIVALENT CATIONS, 0.1 M           
REMARK 280  TRIS/BICINE PH 8.5, 30 % PEG550MME/PEG20000                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   130                                                      
REMARK 465     GLN A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     THR A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     GLU A   609                                                      
REMARK 465     GLY A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     VAL A   614                                                      
REMARK 465     THR A   615                                                      
REMARK 465     ASP A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     GLU A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     SER A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     PHE A   623                                                      
REMARK 465     VAL A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     GLU A   626                                                      
REMARK 465     TYR A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     GLN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     GLU B   609                                                      
REMARK 465     GLY B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     ASP B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     VAL B   614                                                      
REMARK 465     THR B   615                                                      
REMARK 465     ASP B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     ALA B   618                                                      
REMARK 465     GLU B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     SER B   621                                                      
REMARK 465     LYS B   622                                                      
REMARK 465     PHE B   623                                                      
REMARK 465     VAL B   624                                                      
REMARK 465     GLU B   625                                                      
REMARK 465     GLU B   626                                                      
REMARK 465     TYR B   627                                                      
REMARK 465     ASP B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 465     PRO C   130                                                      
REMARK 465     GLN C   131                                                      
REMARK 465     LYS C   132                                                      
REMARK 465     ILE C   611                                                      
REMARK 465     ASP C   612                                                      
REMARK 465     LEU C   613                                                      
REMARK 465     VAL C   614                                                      
REMARK 465     THR C   615                                                      
REMARK 465     ASP C   616                                                      
REMARK 465     GLU C   617                                                      
REMARK 465     ALA C   618                                                      
REMARK 465     GLU C   619                                                      
REMARK 465     ALA C   620                                                      
REMARK 465     SER C   621                                                      
REMARK 465     LYS C   622                                                      
REMARK 465     PHE C   623                                                      
REMARK 465     VAL C   624                                                      
REMARK 465     GLU C   625                                                      
REMARK 465     GLU C   626                                                      
REMARK 465     TYR C   627                                                      
REMARK 465     ASP C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     PRO D   130                                                      
REMARK 465     GLN D   131                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     LEU D   613                                                      
REMARK 465     VAL D   614                                                      
REMARK 465     THR D   615                                                      
REMARK 465     ASP D   616                                                      
REMARK 465     GLU D   617                                                      
REMARK 465     ALA D   618                                                      
REMARK 465     GLU D   619                                                      
REMARK 465     ALA D   620                                                      
REMARK 465     SER D   621                                                      
REMARK 465     LYS D   622                                                      
REMARK 465     PHE D   623                                                      
REMARK 465     VAL D   624                                                      
REMARK 465     GLU D   625                                                      
REMARK 465     GLU D   626                                                      
REMARK 465     TYR D   627                                                      
REMARK 465     ASP D   628                                                      
REMARK 465     LEU D   629                                                      
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     LEU A 129    CG   CD1  CD2                                       
REMARK 470     LYS A 341    CG   CD   CE   NZ                                   
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B   9    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 129    CG   CD1  CD2                                       
REMARK 470     THR B 133    OG1  CG2                                            
REMARK 470     THR B 135    OG1  CG2                                            
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 606    CG   OD1  ND2                                       
REMARK 470     LEU C 129    CG   CD1  CD2                                       
REMARK 470     THR C 133    OG1  CG2                                            
REMARK 470     GLU C 609    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 609    CG   CD   OE1  OE2                                  
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   O3   BMA B  1106     O    HOH B  2379              0.83            
REMARK 500   C    LYS C  1303     N    PRO C  1304              1.36            
REMARK 500   C    LYS B  1303     N    PRO B  1304              1.36            
REMARK 500   C    LYS A  1303     N    PRO A  1304              1.36            
REMARK 500   C    LYS D  1303     N    PRO D  1304              1.36            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  12       58.30    -91.27                                   
REMARK 500    ASN A  45       77.09   -171.29                                   
REMARK 500    VAL A 269      109.09    -58.72                                   
REMARK 500    ARG A 326      140.00    -39.51                                   
REMARK 500    ASN A 416       82.87    -62.00                                   
REMARK 500    ASN B  45       75.51   -172.92                                   
REMARK 500    LYS B  73      -75.51    -88.06                                   
REMARK 500    GLU B  74       -5.02    -59.52                                   
REMARK 500    ALA B 134     -160.40   -102.74                                   
REMARK 500    ASN C  45       76.52   -171.02                                   
REMARK 500    ASN D  45       75.98   -170.46                                   
REMARK 500    ALA D 134      -59.21   -131.67                                   
REMARK 500    ASN D 203       57.23     39.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     LYS A 1303                                                       
REMARK 610     LYS B 1303                                                       
REMARK 610     LYS C 1303                                                       
REMARK 610     LYS D 1303                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 361   NE2                                                    
REMARK 620 2 HIS A 365   NE2 106.4                                              
REMARK 620 3 GLU A 389   OE1  92.5  98.9                                        
REMARK 620 4 HOH A2270   O   116.3 129.1 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 361   NE2                                                    
REMARK 620 2 HIS B 365   NE2 104.4                                              
REMARK 620 3 GLU B 389   OE1  91.6 101.2                                        
REMARK 620 4 HOH B2260   O   113.9 132.6 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 361   NE2                                                    
REMARK 620 2 HIS C 365   NE2 106.6                                              
REMARK 620 3 GLU C 389   OE1  93.5 102.7                                        
REMARK 620 4 HOH C2299   O   115.3 126.9 105.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 361   NE2                                                    
REMARK 620 2 HIS D 365   NE2 107.0                                              
REMARK 620 3 GLU D 389   OE1  96.1  98.8                                        
REMARK 620 4 HOH D2304   O   112.4 130.7 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G C 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G D 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G D 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1102 through NAG A1103 bound to ASN A 45                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1104 through BMA A1106 bound to ASN A 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  A1100 through FUC A1101 bound to ASN A 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B1102 through NAG B1103 bound to ASN B 45                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B1104 through BMA B1106 bound to ASN B 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  B1100 through FUC B1101 bound to ASN B 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  C1102 through NAG C1103 bound to ASN C 45                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  C1104 through FUC C1107 bound to ASN C 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  C1100 through FUC C1101 bound to ASN C 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  D1102 through NAG D1103 bound to ASN D 45                           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  D1104 through FUC D1107 bound to ASN D 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Poly-Saccharide residues NAG      
REMARK 800  D1100 through FUC D1101 bound to ASN D 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide LYS A1303 and PRO      
REMARK 800  A1304                                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide LYS B1303 and PRO      
REMARK 800  B1304                                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide LYS C1303 and PRO      
REMARK 800  C1304                                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide LYS D1303 and PRO      
REMARK 800  D1304                                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UFA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN    
REMARK 900 IN COMPLEX WITH AC-SD                                                
REMARK 900 RELATED ID: 5AM8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN    
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 4-10                                    
REMARK 900 RELATED ID: 5AM9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN    
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 10-16                                   
REMARK 900 RELATED ID: 5AMA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN    
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 1-16                                    
REMARK 900 RELATED ID: 5AMB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN    
REMARK 900 IN COMPLEX WITH AMYLOID-BETA 35-42                                   
REMARK 900 RELATED ID: 5AMC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN    
REMARK 900 IN COMPLEX WITH AMYLOID-BETA FLUOROGENIC FRAGMENT 4-10               
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 P62328 RESIDUES 4-5                                                  
DBREF  4UFB A    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  4UFB B    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  4UFB C    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  4UFB D    1   628  UNP    P12821   ACE_HUMAN       30    657             
SEQADV 4UFB LEU A  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4UFB GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 4UFB GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 4UFB GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 4UFB GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 4UFB GLN A  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 4UFB GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 4UFB ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4UFB LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 4UFB LEU B  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4UFB GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 4UFB GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 4UFB GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 4UFB GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 4UFB GLN B  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 4UFB GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 4UFB ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4UFB LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 4UFB LEU C  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4UFB GLN C    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 4UFB GLN C   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 4UFB GLN C   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 4UFB GLN C  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 4UFB GLN C  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 4UFB GLN C  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 4UFB ARG C  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4UFB LEU C  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 4UFB LEU D  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4UFB GLN D    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 4UFB GLN D   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 4UFB GLN D   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 4UFB GLN D  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 4UFB GLN D  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 4UFB GLN D  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 4UFB ARG D  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4UFB LEU D  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQRES   1 A  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 A  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 A  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 A  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 A  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 A  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 A  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 A  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 A  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 A  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 A  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 A  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 A  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 A  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 A  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 A  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 A  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 A  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 A  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 A  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 A  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 A  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 A  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 A  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 A  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 A  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 A  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 A  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 A  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 A  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 A  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 A  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 A  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 A  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 A  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 A  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 A  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 A  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 A  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 A  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 A  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 A  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 A  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 A  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 A  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 A  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 A  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 A  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 A  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 B  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 B  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 B  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 B  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 B  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 B  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 B  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 B  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 B  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 B  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 B  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 B  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 B  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 B  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 B  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 B  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 B  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 B  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 B  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 B  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 B  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 B  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 B  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 B  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 B  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 B  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 B  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 B  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 B  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 B  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 B  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 B  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 B  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 B  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 B  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 B  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 B  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 B  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 B  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 B  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 B  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 B  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 B  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 B  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 B  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 B  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 B  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 B  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 B  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 C  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 C  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 C  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 C  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 C  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 C  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 C  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 C  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 C  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 C  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 C  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 C  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 C  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 C  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 C  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 C  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 C  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 C  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 C  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 C  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 C  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 C  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 C  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 C  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 C  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 C  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 C  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 C  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 C  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 C  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 C  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 C  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 C  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 C  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 C  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 C  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 C  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 C  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 C  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 C  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 C  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 C  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 C  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 C  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 C  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 C  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 C  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 C  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 C  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 D  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 D  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 D  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 D  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 D  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 D  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 D  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 D  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 D  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 D  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 D  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 D  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 D  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 D  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 D  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 D  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 D  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 D  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 D  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 D  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 D  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 D  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 D  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 D  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 D  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 D  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 D  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 D  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 D  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 D  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 D  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 D  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 D  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 D  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 D  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 D  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 D  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 D  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 D  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 D  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 D  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 D  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 D  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 D  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 D  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 D  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 D  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 D  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 D  629  GLU GLU TYR ASP LEU                                          
MODRES 4UFB ASN A   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN A  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN A  480  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN B   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN B  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN B  480  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN C   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN C  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN C  480  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN D   45  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN D  416  ASN  GLYCOSYLATION SITE                                 
MODRES 4UFB ASN D  480  ASN  GLYCOSYLATION SITE                                 
HET    LYS  A1303       9                                                       
HET    PRO  A1304       8                                                       
HET     ZN  A1001       1                                                       
HET     CL  A1002       1                                                       
HET    NAG  A1100      14                                                       
HET    FUC  A1101      10                                                       
HET    NAG  A1102      14                                                       
HET    NAG  A1103      14                                                       
HET    NAG  A1104      14                                                       
HET    NAG  A1105      14                                                       
HET    BMA  A1106      11                                                       
HET    PEG  A1200       7                                                       
HET    PEG  A1201       7                                                       
HET    P6G  A1202      19                                                       
HET    PEG  A1203       7                                                       
HET    P6G  A1204      19                                                       
HET    LYS  B1303       9                                                       
HET    PRO  B1304       8                                                       
HET     ZN  B1001       1                                                       
HET     CL  B1002       1                                                       
HET    NAG  B1100      14                                                       
HET    FUC  B1101      10                                                       
HET    NAG  B1102      14                                                       
HET    NAG  B1103      14                                                       
HET    NAG  B1104      14                                                       
HET    NAG  B1105      14                                                       
HET    BMA  B1106      11                                                       
HET    PEG  B1201       7                                                       
HET    PEG  B1202       7                                                       
HET    P6G  B1203      19                                                       
HET    PEG  B1204       7                                                       
HET    PEG  B1205       7                                                       
HET    LYS  C1303       9                                                       
HET    PRO  C1304       8                                                       
HET     ZN  C1001       1                                                       
HET     CL  C1002       1                                                       
HET    NAG  C1100      14                                                       
HET    FUC  C1101      10                                                       
HET    NAG  C1102      14                                                       
HET    NAG  C1103      14                                                       
HET    NAG  C1104      14                                                       
HET    NAG  C1105      14                                                       
HET    BMA  C1106      11                                                       
HET    FUC  C1107      10                                                       
HET    PEG  C1200       7                                                       
HET    PEG  C1201       7                                                       
HET    P6G  C1202      19                                                       
HET    LYS  D1303       9                                                       
HET    PRO  D1304       8                                                       
HET     ZN  D1001       1                                                       
HET     CL  D1002       1                                                       
HET    NAG  D1100      14                                                       
HET    FUC  D1101      10                                                       
HET    NAG  D1102      14                                                       
HET    NAG  D1103      14                                                       
HET    NAG  D1104      14                                                       
HET    NAG  D1105      14                                                       
HET    BMA  D1106      11                                                       
HET    FUC  D1107      10                                                       
HET    PEG  D1200       7                                                       
HET    P6G  D1201      19                                                       
HET    P6G  D1202      19                                                       
HETNAM     LYS LYSINE                                                           
HETNAM     PRO PROLINE                                                          
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   5  LYS    4(C6 H15 N2 O2 1+)                                           
FORMUL   6  PRO    4(C5 H9 N O2)                                                
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL   8   CL    4(CL 1-)                                                     
FORMUL   9  NAG    20(C8 H15 N O6)                                              
FORMUL   9  FUC    6(C6 H12 O5)                                                 
FORMUL  11  BMA    4(C6 H12 O6)                                                 
FORMUL  12  PEG    10(C4 H10 O3)                                                
FORMUL  14  P6G    6(C12 H26 O7)                                                
FORMUL  49  HOH   *1611(H2 O)                                                   
HELIX    1   1 ASP A    2  GLN A    6  5                                   5    
HELIX    2   2 ASP A   13  THR A   44  1                                  32    
HELIX    3   3 THR A   47  GLU A   77  1                                  31    
HELIX    4   4 PRO A   78  PHE A   83  5                                   6    
HELIX    5   5 ASP A   85  ARG A   96  1                                  12    
HELIX    6   6 LEU A   98  LEU A  103  5                                   6    
HELIX    7   7 PRO A  104  ALA A  125  1                                  22    
HELIX    8   8 PRO A  141  SER A  150  1                                  10    
HELIX    9   9 SER A  152  GLN A  188  1                                  37    
HELIX   10  10 ASP A  193  TRP A  201  1                                   9    
HELIX   11  11 THR A  206  GLY A  238  1                                  33    
HELIX   12  12 TRP A  261  ASN A  263  5                                   3    
HELIX   13  13 ILE A  264  VAL A  269  1                                   6    
HELIX   14  14 VAL A  279  GLN A  286  1                                   8    
HELIX   15  15 GLN A  289  LEU A  304  1                                  16    
HELIX   16  16 PRO A  310  SER A  317  1                                   8    
HELIX   17  17 THR A  352  LYS A  373  1                                  22    
HELIX   18  18 PRO A  376  ARG A  380  5                                   5    
HELIX   19  19 ASN A  384  ILE A  408  1                                  25    
HELIX   20  20 ASP A  417  ILE A  433  1                                  17    
HELIX   21  21 ALA A  434  SER A  451  1                                  18    
HELIX   22  22 PRO A  455  SER A  457  5                                   3    
HELIX   23  23 ARG A  458  GLY A  472  1                                  15    
HELIX   24  24 PHE A  484  LYS A  489  5                                   6    
HELIX   25  25 TYR A  498  ALA A  519  1                                  22    
HELIX   26  26 PRO A  524  CYS A  528  5                                   5    
HELIX   27  27 SER A  533  GLY A  547  1                                  15    
HELIX   28  28 PRO A  551  GLY A  561  1                                  11    
HELIX   29  29 ALA A  567  ASN A  588  1                                  22    
HELIX   30  30 ASP B    2  GLN B    6  5                                   5    
HELIX   31  31 ASP B   13  THR B   44  1                                  32    
HELIX   32  32 THR B   47  GLU B   77  1                                  31    
HELIX   33  33 ILE B   79  PHE B   83  5                                   5    
HELIX   34  34 ASP B   85  ARG B   96  1                                  12    
HELIX   35  35 LEU B   98  LEU B  103  5                                   6    
HELIX   36  36 PRO B  104  ALA B  125  1                                  22    
HELIX   37  37 PRO B  141  SER B  150  1                                  10    
HELIX   38  38 SER B  152  GLN B  188  1                                  37    
HELIX   39  39 ASP B  193  TRP B  201  1                                   9    
HELIX   40  40 THR B  206  GLY B  238  1                                  33    
HELIX   41  41 TRP B  261  ASN B  263  5                                   3    
HELIX   42  42 ILE B  264  VAL B  269  1                                   6    
HELIX   43  43 VAL B  279  GLN B  286  1                                   8    
HELIX   44  44 GLN B  289  LEU B  304  1                                  16    
HELIX   45  45 PRO B  310  SER B  317  1                                   8    
HELIX   46  46 THR B  352  LYS B  373  1                                  22    
HELIX   47  47 PRO B  376  ARG B  380  5                                   5    
HELIX   48  48 ASN B  384  THR B  401  1                                  18    
HELIX   49  49 THR B  401  ILE B  408  1                                   8    
HELIX   50  50 ASP B  417  ILE B  433  1                                  17    
HELIX   51  51 ALA B  434  SER B  451  1                                  18    
HELIX   52  52 PRO B  455  SER B  457  5                                   3    
HELIX   53  53 ARG B  458  GLY B  472  1                                  15    
HELIX   54  54 PHE B  484  LYS B  489  5                                   6    
HELIX   55  55 TYR B  498  ALA B  519  1                                  22    
HELIX   56  56 PRO B  524  CYS B  528  5                                   5    
HELIX   57  57 SER B  533  GLY B  547  1                                  15    
HELIX   58  58 PRO B  551  GLY B  561  1                                  11    
HELIX   59  59 ALA B  567  GLY B  589  1                                  23    
HELIX   60  60 ASP C    2  GLN C    6  5                                   5    
HELIX   61  61 ASP C   13  THR C   44  1                                  32    
HELIX   62  62 THR C   47  GLU C   77  1                                  31    
HELIX   63  63 ILE C   79  PHE C   83  5                                   5    
HELIX   64  64 ASP C   85  ARG C   96  1                                  12    
HELIX   65  65 LEU C   98  LEU C  103  5                                   6    
HELIX   66  66 PRO C  104  ALA C  125  1                                  22    
HELIX   67  67 PRO C  141  SER C  150  1                                  10    
HELIX   68  68 SER C  152  GLN C  188  1                                  37    
HELIX   69  69 ASP C  193  TRP C  201  1                                   9    
HELIX   70  70 THR C  206  GLY C  238  1                                  33    
HELIX   71  71 TRP C  261  ASN C  263  5                                   3    
HELIX   72  72 ILE C  264  VAL C  269  1                                   6    
HELIX   73  73 VAL C  279  GLN C  286  1                                   8    
HELIX   74  74 GLN C  289  LEU C  304  1                                  16    
HELIX   75  75 PRO C  310  SER C  317  1                                   8    
HELIX   76  76 THR C  352  LYS C  373  1                                  22    
HELIX   77  77 PRO C  376  ARG C  380  5                                   5    
HELIX   78  78 ASN C  384  SER C  400  1                                  17    
HELIX   79  79 THR C  401  ILE C  408  1                                   8    
HELIX   80  80 ASP C  417  ILE C  433  1                                  17    
HELIX   81  81 ALA C  434  SER C  451  1                                  18    
HELIX   82  82 PRO C  455  SER C  457  5                                   3    
HELIX   83  83 ARG C  458  GLY C  472  1                                  15    
HELIX   84  84 PHE C  484  LYS C  489  5                                   6    
HELIX   85  85 TYR C  498  ALA C  519  1                                  22    
HELIX   86  86 PRO C  524  CYS C  528  5                                   5    
HELIX   87  87 SER C  533  GLY C  547  1                                  15    
HELIX   88  88 PRO C  551  GLY C  561  1                                  11    
HELIX   89  89 ALA C  567  ASN C  588  1                                  22    
HELIX   90  90 ASP D    2  GLN D    6  5                                   5    
HELIX   91  91 ASP D   13  THR D   44  1                                  32    
HELIX   92  92 THR D   47  GLU D   77  1                                  31    
HELIX   93  93 ILE D   79  PHE D   83  5                                   5    
HELIX   94  94 ASP D   85  ARG D   96  1                                  12    
HELIX   95  95 LEU D   98  LEU D  103  5                                   6    
HELIX   96  96 PRO D  104  ALA D  125  1                                  22    
HELIX   97  97 PRO D  141  SER D  150  1                                  10    
HELIX   98  98 SER D  152  GLN D  188  1                                  37    
HELIX   99  99 ASP D  193  TRP D  201  1                                   9    
HELIX  100 100 THR D  206  GLY D  238  1                                  33    
HELIX  101 101 TRP D  261  ASN D  263  5                                   3    
HELIX  102 102 ILE D  264  VAL D  269  1                                   6    
HELIX  103 103 VAL D  279  GLN D  286  1                                   8    
HELIX  104 104 GLN D  289  LEU D  304  1                                  16    
HELIX  105 105 PRO D  310  SER D  317  1                                   8    
HELIX  106 106 THR D  352  LYS D  373  1                                  22    
HELIX  107 107 PRO D  376  ARG D  380  5                                   5    
HELIX  108 108 ASN D  384  THR D  401  1                                  18    
HELIX  109 109 THR D  401  ILE D  408  1                                   8    
HELIX  110 110 ASP D  417  ILE D  433  1                                  17    
HELIX  111 111 ALA D  434  SER D  451  1                                  18    
HELIX  112 112 PRO D  455  SER D  457  5                                   3    
HELIX  113 113 ARG D  458  GLY D  472  1                                  15    
HELIX  114 114 PHE D  484  LYS D  489  5                                   6    
HELIX  115 115 TYR D  498  ALA D  519  1                                  22    
HELIX  116 116 PRO D  524  CYS D  528  5                                   5    
HELIX  117 117 SER D  533  GLY D  547  1                                  15    
HELIX  118 118 PRO D  551  GLY D  561  1                                  11    
HELIX  119 119 ALA D  567  ASN D  588  1                                  22    
SHEET    1  AA 2 LYS A 126  CYS A 128  0                                        
SHEET    2  AA 2 CYS A 136  SER A 138 -1  O  TRP A 137   N  VAL A 127           
SHEET    1  AB 2 ILE A 248  PRO A 249  0                                        
SHEET    2  AB 2 ILE A 473  CYS A 474  1  N  CYS A 474   O  ILE A 248           
SHEET    1  AC 2 SER A 333  ASP A 336  0                                        
SHEET    2  AC 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335           
SHEET    1  BA 2 ILE B 248  PRO B 249  0                                        
SHEET    2  BA 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248           
SHEET    1  BB 2 SER B 333  ASP B 336  0                                        
SHEET    2  BB 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SHEET    1  CA 2 VAL C 127  CYS C 128  0                                        
SHEET    2  CA 2 CYS C 136  TRP C 137 -1  O  TRP C 137   N  VAL C 127           
SHEET    1  CB 2 ILE C 248  PRO C 249  0                                        
SHEET    2  CB 2 ILE C 473  CYS C 474  1  N  CYS C 474   O  ILE C 248           
SHEET    1  CC 2 SER C 333  ASP C 336  0                                        
SHEET    2  CC 2 PHE C 343  LYS C 346 -1  O  ARG C 344   N  TRP C 335           
SHEET    1  DA 2 LYS D 126  VAL D 127  0                                        
SHEET    2  DA 2 TRP D 137  SER D 138 -1  O  TRP D 137   N  VAL D 127           
SHEET    1  DB 2 ILE D 248  PRO D 249  0                                        
SHEET    2  DB 2 ILE D 473  CYS D 474  1  N  CYS D 474   O  ILE D 248           
SHEET    1  DC 2 SER D 333  ASP D 336  0                                        
SHEET    2  DC 2 PHE D 343  LYS D 346 -1  O  ARG D 344   N  TRP D 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.03  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.04  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.04  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.04  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03  
SSBOND   7 CYS C  128    CYS C  136                          1555   1555  2.03  
SSBOND   8 CYS C  330    CYS C  348                          1555   1555  2.05  
SSBOND   9 CYS C  516    CYS C  528                          1555   1555  2.03  
SSBOND  10 CYS D  128    CYS D  136                          1555   1555  2.04  
SSBOND  11 CYS D  330    CYS D  348                          1555   1555  2.04  
SSBOND  12 CYS D  516    CYS D  528                          1555   1555  2.02  
LINK         ND2 ASN A  45                 C1  NAG A1102     1555   1555  1.44  
LINK         NE2 HIS A 361                ZN    ZN A1001     1555   1555  2.03  
LINK         NE2 HIS A 365                ZN    ZN A1001     1555   1555  2.04  
LINK         OE1 GLU A 389                ZN    ZN A1001     1555   1555  2.01  
LINK         ND2 ASN A 416                 C1  NAG A1104     1555   1555  1.33  
LINK         ND2 ASN A 480                 C1  NAG A1100     1555   1555  1.55  
LINK         ND2 ASN B  45                 C1  NAG B1102     1555   1555  1.44  
LINK         NE2 HIS B 361                ZN    ZN B1001     1555   1555  2.10  
LINK         NE2 HIS B 365                ZN    ZN B1001     1555   1555  2.02  
LINK         OE1 GLU B 389                ZN    ZN B1001     1555   1555  1.97  
LINK         ND2 ASN B 416                 C1  NAG B1104     1555   1555  1.39  
LINK         ND2 ASN B 480                 C1  NAG B1100     1555   1555  1.45  
LINK         ND2 ASN C  45                 C1  NAG C1102     1555   1555  1.44  
LINK         NE2 HIS C 361                ZN    ZN C1001     1555   1555  2.07  
LINK         NE2 HIS C 365                ZN    ZN C1001     1555   1555  2.00  
LINK         OE1 GLU C 389                ZN    ZN C1001     1555   1555  1.91  
LINK         ND2 ASN C 416                 C1  NAG C1104     1555   1555  1.44  
LINK         ND2 ASN C 480                 C1  NAG C1100     1555   1555  1.45  
LINK         ND2 ASN D  45                 C1  NAG D1102     1555   1555  1.44  
LINK         NE2 HIS D 361                ZN    ZN D1001     1555   1555  2.08  
LINK         NE2 HIS D 365                ZN    ZN D1001     1555   1555  2.04  
LINK         OE1 GLU D 389                ZN    ZN D1001     1555   1555  2.01  
LINK         ND2 ASN D 416                 C1  NAG D1104     1555   1555  1.44  
LINK         ND2 ASN D 480                 C1  NAG D1100     1555   1555  1.45  
LINK        ZN    ZN A1001                 O   HOH A2270     1555   1555  2.00  
LINK         O6  NAG A1100                 C1  FUC A1101     1555   1555  1.45  
LINK         O4  NAG A1102                 C1  NAG A1103     1555   1555  1.45  
LINK         O4  NAG A1104                 C1  NAG A1105     1555   1555  1.44  
LINK         O4  NAG A1105                 C1  BMA A1106     1555   1555  1.45  
LINK        ZN    ZN B1001                 O   HOH B2260     1555   1555  2.08  
LINK         O6  NAG B1100                 C1  FUC B1101     1555   1555  1.45  
LINK         O4  NAG B1102                 C1  NAG B1103     1555   1555  1.45  
LINK         O4  NAG B1104                 C1  NAG B1105     1555   1555  1.44  
LINK         O4  NAG B1105                 C1  BMA B1106     1555   1555  1.45  
LINK        ZN    ZN C1001                 O   HOH C2299     1555   1555  2.09  
LINK         O6  NAG C1100                 C1  FUC C1101     1555   1555  1.44  
LINK         O4  NAG C1102                 C1  NAG C1103     1555   1555  1.45  
LINK         O4  NAG C1104                 C1  NAG C1105     1555   1555  1.44  
LINK         O6  NAG C1104                 C1  FUC C1107     1555   1555  1.45  
LINK         O4  NAG C1105                 C1  BMA C1106     1555   1555  1.45  
LINK        ZN    ZN D1001                 O   HOH D2304     1555   1555  2.11  
LINK         O6  NAG D1100                 C1  FUC D1101     1555   1555  1.45  
LINK         O4  NAG D1102                 C1  NAG D1103     1555   1555  1.45  
LINK         O4  NAG D1104                 C1  NAG D1105     1555   1555  1.44  
LINK         O6  NAG D1104                 C1  FUC D1107     1555   1555  1.45  
LINK         O4  NAG D1105                 C1  BMA D1106     1555   1555  1.45  
CISPEP   1 ASP A  140    PRO A  141          0         9.64                     
CISPEP   2 TYR A  607    PRO A  608          0        -3.48                     
CISPEP   3 ASP B  140    PRO B  141          0        10.02                     
CISPEP   4 TYR B  607    PRO B  608          0        -6.82                     
CISPEP   5 ASP C  140    PRO C  141          0        10.32                     
CISPEP   6 TYR C  607    PRO C  608          0        -0.08                     
CISPEP   7 ASP D  140    PRO D  141          0         9.59                     
CISPEP   8 TYR D  607    PRO D  608          0        -3.32                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  HOH A2270                    
SITE     1 AC2  5 TYR A 202  PRO A 385  PRO A 497  ARG A 500                    
SITE     2 AC2  5 HOH A2169                                                     
SITE     1 AC3  4 TRP A  80  ASP A 189  GLY A 190  PHE A 191                    
SITE     1 AC4  1 P6G A1202                                                     
SITE     1 AC5  6 GLN A 286  TRP A 288  HIS A 292  PEG A1201                    
SITE     2 AC5  6 TRP C 288  HIS C 292                                          
SITE     1 AC6  4 TYR A 369  HIS A 388  P6G A1204  HOH A2319                    
SITE     1 AC7  5 ALA A 334  TYR A 338  VAL A 377  ARG A 381                    
SITE     2 AC7  5 PEG A1203                                                     
SITE     1 AC8  4 HIS B 361  HIS B 365  GLU B 389  HOH B2260                    
SITE     1 AC9  5 TYR B 202  PRO B 385  PRO B 497  ARG B 500                    
SITE     2 AC9  5 HOH B2151                                                     
SITE     1 BC1  8 ARG B 453  TYR B 465  HOH B2308  HOH B2380                    
SITE     2 BC1  8 HOH B2381  HOH B2382  ASP D 462  TYR D 465                    
SITE     1 BC2  1 ILE D 408                                                     
SITE     1 BC3 10 GLN B 286  GLY B 287  TRP B 288  HIS B 292                    
SITE     2 BC3 10 VAL B 296  HOH B2384  GLN D 286  GLY D 287                    
SITE     3 BC3 10 HIS D 292  ARG D 295                                          
SITE     1 BC4  3 ALA B 334  PEG B1205  HOH B2386                               
SITE     1 BC5  5 TYR B 369  HIS B 388  GLU B 389  PEG B1204                    
SITE     2 BC5  5 HOH B2320                                                     
SITE     1 BC6  4 HIS C 361  HIS C 365  GLU C 389  HOH C2299                    
SITE     1 BC7  5 TYR C 202  PRO C 385  PRO C 497  ARG C 500                    
SITE     2 BC7  5 HOH C2174                                                     
SITE     1 BC8  4 ARG C  96  ASP C 189  GLY C 190  PHE C 191                    
SITE     1 BC9  3 ARG A 453  TYR A 465  TYR C 465                               
SITE     1 CC1  5 SER C  39  ALA C 334  TYR C 369  HIS C 388                    
SITE     2 CC1  5 HOH C2279                                                     
SITE     1 CC2  4 HIS D 361  HIS D 365  GLU D 389  HOH D2304                    
SITE     1 CC3  5 TYR D 202  PRO D 385  PRO D 497  ARG D 500                    
SITE     2 CC3  5 HOH D2170                                                     
SITE     1 CC4  3 ASP D 189  GLY D 190  PHE D 191                               
SITE     1 CC5  8 SER A  11  PHE D 228  ARG D 231  ARG D 235                    
SITE     2 CC5  8 VAL D 268  VAL D 269  HOH D2204  HOH D2428                    
SITE     1 CC6  5 SER D  39  ALA D 334  TYR D 338  TYR D 369                    
SITE     2 CC6  5 HIS D 388                                                     
SITE     1 CC7  5 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 CC7  5 ARG A 326                                                     
SITE     1 CC8  5 ASN A 416  GLU A 522  GLY A 523  PRO A 524                    
SITE     2 CC8  5 GLN A 527                                                     
SITE     1 CC9  6 GLU A 161  ASN A 480  THR A 482  HIS A 483                    
SITE     2 CC9  6 ARG C 245  GLU C 596                                          
SITE     1 DC1  3 ASN B  45  THR B  47  ASN B  50                               
SITE     1 DC2  6 ASN B 416  GLU B 522  PRO B 524  GLN B 527                    
SITE     2 DC2  6 HOH B2335  HOH B2379                                          
SITE     1 DC3  9 ASN B 480  THR B 482  HOH B2314  HOH B2316                    
SITE     2 DC3  9 HOH B2376  HOH B2377  HOH B2378  ARG D 245                    
SITE     3 DC3  9 GLU D 596                                                     
SITE     1 DC4  6 ASN C  45  THR C  47  ASN C  50  ARG C  53                    
SITE     2 DC4  6 ARG C 326  HOH C2428                                          
SITE     1 DC5 12 GLN C   9  PHE C  10  SER C  11  GLU C 403                    
SITE     2 DC5 12 ASN C 416  GLU C 522  PRO C 524  GLN C 527                    
SITE     3 DC5 12 HOH C2382  HOH C2385  HOH C2429  HOH C2431                    
SITE     1 DC6  6 ARG A 245  GLU A 596  ASN C 480  THR C 482                    
SITE     2 DC6  6 HOH C2361  HOH C2427                                          
SITE     1 DC7  3 ASN D  45  THR D  47  ASN D  50                               
SITE     1 DC8  8 SER D  11  ASN D 416  GLU D 522  PRO D 524                    
SITE     2 DC8  8 GLN D 527  HOH D2377  HOH D2426  HOH D2427                    
SITE     1 DC9  6 ARG B 245  GLU B 596  ASN D 480  THR D 482                    
SITE     2 DC9  6 HIS D 483  HOH D2359                                          
SITE     1 EC1 13 GLN A 259  HIS A 331  ALA A 332  HIS A 361                    
SITE     2 EC1 13 GLU A 362  LYS A 489  HIS A 491  TYR A 498                    
SITE     3 EC1 13 TYR A 501  HOH A2125  HOH A2207  HOH A2249                    
SITE     4 EC1 13 HOH A2270                                                     
SITE     1 EC2 12 GLN B 259  HIS B 331  ALA B 332  THR B 358                    
SITE     2 EC2 12 HIS B 361  GLU B 362  LYS B 489  HIS B 491                    
SITE     3 EC2 12 TYR B 498  TYR B 501  HOH B2195  HOH B2260                    
SITE     1 EC3 15 GLN C 259  HIS C 331  ALA C 332  THR C 358                    
SITE     2 EC3 15 HIS C 361  GLU C 362  LYS C 489  HIS C 491                    
SITE     3 EC3 15 TYR C 498  TYR C 501  HOH C2111  HOH C2226                    
SITE     4 EC3 15 HOH C2297  HOH C2299  HOH C2434                               
SITE     1 EC4 13 GLN D 259  HIS D 331  ALA D 332  THR D 358                    
SITE     2 EC4 13 GLU D 362  LYS D 489  HIS D 491  TYR D 498                    
SITE     3 EC4 13 TYR D 501  HOH D2219  HOH D2302  HOH D2304                    
SITE     4 EC4 13 HOH D2430                                                     
CRYST1   73.480  101.590  114.510  85.46  85.90  81.62 P 1           4          
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      0.013609 -0.002005 -0.000838        0.00000                         
SCALE2      0.000000  0.009950 -0.000695        0.00000                         
SCALE3      0.000000  0.000000  0.008777        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system