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Database: PDB
Entry: 5AMA
LinkDB: 5AMA
Original site: 5AMA 
HEADER    HYDROLASE                               10-MAR-15   5AMA              
TITLE     CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-DOMAIN IN  
TITLE    2 COMPLEX WITH AMYLOID-BETA 1-16                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N DOMAIN, UNP RESIDUES 30-658;                             
COMPND   5 EC: 3.4.15.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 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    METALLOPROTEASE, AMYLOID- BETA, HYDROLASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MASUYER,K.M.LARMUTH,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA            
REVDAT   4   20-JUN-18 5AMA    1       REMARK LINK                              
REVDAT   3   06-APR-16 5AMA    1       JRNL                                     
REVDAT   2   20-JAN-16 5AMA    1       JRNL                                     
REVDAT   1   13-JAN-16 5AMA    0                                                
JRNL        AUTH   K.M.LARMUTH,G.MASUYER,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA   
JRNL        TITL   THE KINETIC AND STRUCTURAL CHARACTERISATION OF AMYLOID-BETA  
JRNL        TITL 2 METABOLISM BY HUMAN ANGIOTENSIN-1- CONVERTING ENZYME (ACE)   
JRNL        REF    FEBS J.                       V. 283  1060 2016              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   26748546                                                     
JRNL        DOI    10.1111/FEBS.13647                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
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) : 113.48                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 267318                         
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13921                           
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) : 15422                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 789                          
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19755                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 608                                     
REMARK   3   SOLVENT ATOMS            : 1890                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.90000                                             
REMARK   3    B22 (A**2) : 0.36000                                              
REMARK   3    B33 (A**2) : 0.43000                                              
REMARK   3    B12 (A**2) : -0.30000                                             
REMARK   3    B13 (A**2) : -0.04000                                             
REMARK   3    B23 (A**2) : 0.07000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.118         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.095         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21006 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 19141 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28563 ; 1.388 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44035 ; 0.973 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2424 ; 5.952 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1059 ;35.218 ;23.787       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3207 ;12.896 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   132 ;16.695 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2990 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23566 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5172 ; 0.002 ; 0.020       
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):  9720 ; 0.939 ; 2.060       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  9719 ; 0.939 ; 2.060       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12130 ; 1.592 ; 3.082       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11286 ; 1.202 ; 2.286       
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  : 1                                          
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): -12.6330  46.3797 -29.1702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0044 T22:   0.0104                                     
REMARK   3      T33:   0.0269 T12:  -0.0002                                     
REMARK   3      T13:  -0.0105 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0218 L22:   0.0095                                     
REMARK   3      L33:   0.0330 L12:   0.0099                                     
REMARK   3      L13:   0.0205 L23:   0.0163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:   0.0120 S13:  -0.0079                       
REMARK   3      S21:   0.0013 S22:   0.0096 S23:  -0.0068                       
REMARK   3      S31:   0.0013 S32:   0.0172 S33:  -0.0107                       
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. ONLY DI-PEPTIDE ASP-SER (7-8) VISIBLE FOR AMYLOID-       
REMARK   3  BETA ( PRODUCT OF CLEAVAGE REACTION BY ACE)                         
REMARK   4                                                                      
REMARK   4 5AMA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290063277.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-OCT-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   : 281258                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.420                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 1.600                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8000                             
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     (%) : 82.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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): 2.95                     
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: 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 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: 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: 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: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 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 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     THR C   133                                                      
REMARK 465     ALA C   134                                                      
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     THR D   133                                                      
REMARK 465     ALA D   134                                                      
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     LEU B 129    CG   CD1  CD2                                       
REMARK 470     THR B 133    OG1  CG2                                            
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 135    OG1  CG2                                            
REMARK 470     GLU C 609    CG   CD   OE1  OE2                                  
REMARK 470     ILE C 611    CG1  CG2  CD1                                       
REMARK 470     ASP C 612    CG   OD1  OD2                                       
REMARK 470     ASP D  13    CG   OD1  OD2                                       
REMARK 470     GLU D  14    CG   CD   OE1  OE2                                  
REMARK 470     TRP D  80    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D  80    CZ3  CH2                                            
REMARK 470     PHE D  83    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR D  84    OG1  CG2                                            
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   C    ASP C   907     N    SER C   908              1.33            
REMARK 500   C    ASP D   907     N    SER D   908              1.34            
REMARK 500   C    ASP A   907     N    SER A   908              1.34            
REMARK 500   C    ASP B   907     N    SER B   908              1.34            
REMARK 500   O    HOH C  2365     O    HOH C  2366              2.11            
REMARK 500   OD2  ASP D   354     O    HOH D  2317              2.14            
REMARK 500   NH1  ARG D   151     O    HOH D  2138              2.16            
REMARK 500   O    HOH D  2323     O    HOH D  2324              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 541   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG B 541   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 541   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  45       78.23   -174.82                                   
REMARK 500    ASN A 203       58.92     38.58                                   
REMARK 500    ASP A 324     -128.59    -72.87                                   
REMARK 500    LYS A 341      -45.76   -133.49                                   
REMARK 500    ARG A 500      -39.11    -38.38                                   
REMARK 500    ASN B  45       75.09   -174.79                                   
REMARK 500    ALA B 134     -128.74   -113.32                                   
REMARK 500    ASP B 324     -171.52    -69.78                                   
REMARK 500    LYS B 341      -45.38   -133.38                                   
REMARK 500    ASN C  45       78.70   -172.10                                   
REMARK 500    ASN C 203       55.22     38.44                                   
REMARK 500    ASP C 324        2.05    -69.68                                   
REMARK 500    PRO C 608       41.71   -104.28                                   
REMARK 500    GLU C 609       71.14    -67.40                                   
REMARK 500    ALA D  12       48.60    -79.96                                   
REMARK 500    ALA D  17      -36.34   -147.66                                   
REMARK 500    ASN D  45       77.62   -175.74                                   
REMARK 500    GLN D  81      -13.21    108.74                                   
REMARK 500    PHE D  83     -103.20    -46.06                                   
REMARK 500    THR D  84      -74.65    -21.16                                   
REMARK 500    ASN D 203       58.09     37.24                                   
REMARK 500    LYS D 341      -45.16   -131.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  325     ARG A  326                 -143.39                    
REMARK 500 GLN D   82     PHE D   83                 -134.13                    
REMARK 500 PHE D   83     THR D   84                 -137.27                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C2019        DISTANCE =  6.02 ANGSTROMS                       
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     ASP A  907                                                       
REMARK 610     ASP B  907                                                       
REMARK 610     ASP C  907                                                       
REMARK 610     ASP D  907                                                       
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 105.5                                              
REMARK 620 3 GLU A 389   OE1  91.0 106.1                                        
REMARK 620 4 HOH A2320   O   116.2 128.0 103.0                                  
REMARK 620 5 HOH A2319   O    99.1  83.1 164.1  61.5                            
REMARK 620 N                    1     2     3     4                             
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 103.7                                              
REMARK 620 3 GLU B 389   OE1  90.9 107.2                                        
REMARK 620 4 HOH B2335   O   100.3  86.4 160.0                                  
REMARK 620 5 HOH B2336   O   115.9 131.4  99.6  60.6                            
REMARK 620 N                    1     2     3     4                             
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 105.2                                              
REMARK 620 3 GLU C 389   OE1  92.9 105.4                                        
REMARK 620 4 HOH C2365   O   100.2  84.3 161.2                                  
REMARK 620 5 HOH C2366   O   116.8 124.7 106.5  55.4                            
REMARK 620 N                    1     2     3     4                             
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 103.9                                              
REMARK 620 3 GLU D 389   OE1  89.8 104.9                                        
REMARK 620 4 HOH D2323   O    98.8  88.6 161.9                                  
REMARK 620 5 HOH D2324   O   114.7 131.6 103.4  58.5                            
REMARK 620 N                    1     2     3     4                             
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 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 1200                
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 P6G B 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G C 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 1200                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G D 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G D 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 1205                
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  A1101 through NAG A1102 bound to ASN A 45                           
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  A1103 through NAG A1104 bound to ASN A 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG A1100 bound   
REMARK 800  to ASN A 480                                                        
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  B1102 through NAG B1103 bound to ASN B 45                           
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  B1104 through BMA B1106 bound to ASN B 416                          
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  B1100 through FUC B1101 bound to ASN B 480                          
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  C1102 through NAG C1103 bound to ASN C 45                           
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  C1104 through FUL C1107 bound to ASN C 416                          
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  C1100 through FUC C1101 bound to ASN C 480                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Mono-Saccharide NAG D1102 bound   
REMARK 800  to ASN D 45                                                         
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  D1103 through FUC D1106 bound to ASN D 416                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
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: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide ASP A 907 and SER A    
REMARK 800  908                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide ASP B 907 and SER B    
REMARK 800  908                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide ASP C 907 and SER C    
REMARK 800  908                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide ASP D 907 and SER D    
REMARK 800  908                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 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               
DBREF  5AMA A    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AMA B    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AMA C    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AMA D    1   629  UNP    P12821   ACE_HUMAN       30    658             
SEQADV 5AMA GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AMA GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AMA GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AMA GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AMA GLN A  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AMA GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AMA ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AMA LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AMA LEU A  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AMA LEU B  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AMA GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AMA GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AMA GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AMA GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AMA GLN B  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AMA GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AMA ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AMA LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AMA LEU C  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AMA GLN C    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AMA GLN C   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AMA GLN C   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AMA GLN C  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AMA GLN C  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AMA GLN C  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AMA ARG C  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AMA LEU C  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AMA LEU D  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AMA GLN D    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AMA GLN D   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AMA GLN D   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AMA GLN D  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AMA GLN D  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AMA GLN D  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AMA ARG D  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AMA 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 5AMA ASN A   45  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN A  416  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN A  480  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN B   45  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN B  416  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN B  480  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN C   45  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN C  416  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN C  480  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN D   45  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN D  416  ASN  GLYCOSYLATION SITE                                 
MODRES 5AMA ASN D  480  ASN  GLYCOSYLATION SITE                                 
HET    ASP  A 907       8                                                       
HET    SER  A 908       7                                                       
HET     ZN  A1001       1                                                       
HET     CL  A1002       1                                                       
HET    NAG  A1100      14                                                       
HET    NAG  A1101      14                                                       
HET    NAG  A1102      14                                                       
HET    NAG  A1103      14                                                       
HET    NAG  A1104      14                                                       
HET    PEG  A1200       7                                                       
HET    PEG  A1201       7                                                       
HET    P6G  A1202      19                                                       
HET    PEG  A1204       7                                                       
HET    ASP  B 907       8                                                       
HET    SER  B 908       7                                                       
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  B1200       7                                                       
HET    PEG  B1201       7                                                       
HET    PEG  B1202       7                                                       
HET    P6G  B1203      19                                                       
HET    P6G  B1204      19                                                       
HET    ASP  C 907       8                                                       
HET    SER  C 908       7                                                       
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    FUL  C1107      10                                                       
HET    PEG  C1200       7                                                       
HET    PEG  C1201       7                                                       
HET    P6G  C1202      19                                                       
HET    ASP  D 907       8                                                       
HET    SER  D 908       7                                                       
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    MAN  D1105      11                                                       
HET    FUC  D1106      10                                                       
HET    PEG  D1200       7                                                       
HET    P6G  D1201      19                                                       
HET    PEG  D1202       7                                                       
HET    P6G  D1203      19                                                       
HET    PEG  D1205       7                                                       
HETNAM     ASP ASPARTIC ACID                                                    
HETNAM     SER SERINE                                                           
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   5  ASP    4(C4 H7 N O4)                                                
FORMUL   6  SER    4(C3 H7 N O3)                                                
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL   8   CL    4(CL 1-)                                                     
FORMUL   9  NAG    19(C8 H15 N O6)                                              
FORMUL  12  PEG    11(C4 H10 O3)                                                
FORMUL  14  P6G    6(C12 H26 O7)                                                
FORMUL  20  FUC    4(C6 H12 O5)                                                 
FORMUL  22  BMA    2(C6 H12 O6)                                                 
FORMUL  34  FUL    C6 H12 O5                                                    
FORMUL  44  MAN    C6 H12 O6                                                    
FORMUL  50  HOH   *1890(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 ILE A   79  PHE A   83  5                                   5    
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 PHE A  435  SER A  451  1                                  17    
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  SER B  400  1                                  17    
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  GLY B  452  1                                  19    
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  ASN B  588  1                                  22    
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  ILE C  408  1                                  25    
HELIX   79  79 ASP C  417  ILE C  433  1                                  17    
HELIX   80  80 ALA C  434  SER C  451  1                                  18    
HELIX   81  81 PRO C  455  SER C  457  5                                   3    
HELIX   82  82 ARG C  458  GLY C  472  1                                  15    
HELIX   83  83 PHE C  484  LYS C  489  5                                   6    
HELIX   84  84 TYR C  498  ALA C  519  1                                  22    
HELIX   85  85 PRO C  524  CYS C  528  5                                   5    
HELIX   86  86 SER C  533  GLY C  547  1                                  15    
HELIX   87  87 PRO C  551  GLY C  561  1                                  11    
HELIX   88  88 ALA C  567  ASN C  588  1                                  22    
HELIX   89  89 GLY C  610  VAL C  614  5                                   5    
HELIX   90  90 ASP D    2  GLN D    6  5                                   5    
HELIX   91  91 ALA D   17  THR D   44  1                                  28    
HELIX   92  92 THR D   47  GLU D   77  1                                  31    
HELIX   93  93 ASP D   85  ARG D   96  1                                  12    
HELIX   94  94 LEU D   98  LEU D  103  5                                   6    
HELIX   95  95 PRO D  104  ALA D  125  1                                  22    
HELIX   96  96 PRO D  141  SER D  150  1                                  10    
HELIX   97  97 SER D  152  GLN D  188  1                                  37    
HELIX   98  98 ASP D  193  TRP D  201  1                                   9    
HELIX   99  99 THR D  206  GLY D  238  1                                  33    
HELIX  100 100 TRP D  261  ASN D  263  5                                   3    
HELIX  101 101 ILE D  264  VAL D  269  1                                   6    
HELIX  102 102 VAL D  279  GLY D  287  1                                   9    
HELIX  103 103 GLN D  289  LEU D  304  1                                  16    
HELIX  104 104 PRO D  310  SER D  317  1                                   8    
HELIX  105 105 THR D  352  LYS D  373  1                                  22    
HELIX  106 106 PRO D  376  ARG D  380  5                                   5    
HELIX  107 107 ASN D  384  SER D  400  1                                  17    
HELIX  108 108 THR D  401  ILE D  408  1                                   8    
HELIX  109 109 ASP D  417  ILE D  433  1                                  17    
HELIX  110 110 ALA D  434  GLY D  452  1                                  19    
HELIX  111 111 PRO D  455  SER D  457  5                                   3    
HELIX  112 112 ARG D  458  GLY D  472  1                                  15    
HELIX  113 113 PHE D  484  LYS D  489  5                                   6    
HELIX  114 114 TYR D  498  ALA D  519  1                                  22    
HELIX  115 115 PRO D  524  CYS D  528  5                                   5    
HELIX  116 116 SER D  533  GLY D  547  1                                  15    
HELIX  117 117 PRO D  551  GLY D  561  1                                  11    
HELIX  118 118 ALA D  567  ASN D  588  1                                  22    
SHEET    1  AA 2 VAL A 127  CYS A 128  0                                        
SHEET    2  AA 2 CYS A 136  TRP A 137 -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 LYS B 126  CYS B 128  0                                        
SHEET    2  BA 2 CYS B 136  SER B 138 -1  O  TRP B 137   N  VAL B 127           
SHEET    1  BB 2 ILE B 248  PRO B 249  0                                        
SHEET    2  BB 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248           
SHEET    1  BC 2 SER B 333  ASP B 336  0                                        
SHEET    2  BC 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SHEET    1  CA 2 LYS C 126  CYS C 128  0                                        
SHEET    2  CA 2 CYS C 136  SER C 138 -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 ILE D 248  PRO D 249  0                                        
SHEET    2  DA 2 ILE D 473  CYS D 474  1  N  CYS D 474   O  ILE D 248           
SHEET    1  DB 2 SER D 333  ASP D 336  0                                        
SHEET    2  DB 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  2.06  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.08  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.07  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.08  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.05  
SSBOND   7 CYS C  128    CYS C  136                          1555   1555  2.06  
SSBOND   8 CYS C  330    CYS C  348                          1555   1555  2.09  
SSBOND   9 CYS C  516    CYS C  528                          1555   1555  2.03  
SSBOND  10 CYS D  128    CYS D  136                          1555   1555  2.06  
SSBOND  11 CYS D  330    CYS D  348                          1555   1555  2.07  
SSBOND  12 CYS D  516    CYS D  528                          1555   1555  2.03  
LINK         ND2 ASN A  45                 C1  NAG A1101     1555   1555  1.45  
LINK         NE2 HIS A 361                ZN    ZN A1001     1555   1555  2.06  
LINK         NE2 HIS A 365                ZN    ZN A1001     1555   1555  2.09  
LINK         OE1 GLU A 389                ZN    ZN A1001     1555   1555  1.97  
LINK         ND2 ASN A 416                 C1  NAG A1103     1555   1555  1.43  
LINK         ND2 ASN A 480                 C1  NAG A1100     1555   1555  1.45  
LINK         ND2 ASN B  45                 C1  NAG B1102     1555   1555  1.44  
LINK         NE2 HIS B 361                ZN    ZN B1001     1555   1555  2.09  
LINK         NE2 HIS B 365                ZN    ZN B1001     1555   1555  2.06  
LINK         OE1 GLU B 389                ZN    ZN B1001     1555   1555  1.97  
LINK         ND2 ASN B 416                 C1  NAG B1104     1555   1555  1.43  
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  2.08  
LINK         NE2 HIS C 365                ZN    ZN C1001     1555   1555  2.09  
LINK         OE1 GLU C 389                ZN    ZN C1001     1555   1555  1.96  
LINK         ND2 ASN C 416                 C1  NAG C1104     1555   1555  1.43  
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  2.09  
LINK         NE2 HIS D 365                ZN    ZN D1001     1555   1555  2.06  
LINK         OE1 GLU D 389                ZN    ZN D1001     1555   1555  1.94  
LINK         ND2 ASN D 416                 C1  NAG D1103     1555   1555  1.44  
LINK         ND2 ASN D 480                 C1  NAG D1100     1555   1555  1.47  
LINK        ZN    ZN A1001                 O   HOH A2320     1555   1555  2.18  
LINK        ZN    ZN A1001                 O   HOH A2319     1555   1555  2.21  
LINK         O4  NAG A1101                 C1  NAG A1102     1555   1555  1.45  
LINK         O4  NAG A1103                 C1  NAG A1104     1555   1555  1.44  
LINK        ZN    ZN B1001                 O   HOH B2335     1555   1555  2.35  
LINK        ZN    ZN B1001                 O   HOH B2336     1555   1555  2.20  
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  1.44  
LINK        ZN    ZN C1001                 O   HOH C2365     1555   1555  2.38  
LINK        ZN    ZN C1001                 O   HOH C2366     1555   1555  2.13  
LINK         O6  NAG C1100                 C1  FUC C1101     1555   1555  1.45  
LINK         O4  NAG C1102                 C1  NAG C1103     1555   1555  1.45  
LINK         O4  NAG C1104                 C1  NAG C1105     1555   1555  1.42  
LINK         O6  NAG C1104                 C1  FUL C1107     1555   1555  1.44  
LINK         O4  NAG C1105                 C1  BMA C1106     1555   1555  1.44  
LINK        ZN    ZN D1001                 O   HOH D2323     1555   1555  2.22  
LINK        ZN    ZN D1001                 O   HOH D2324     1555   1555  2.25  
LINK         O6  NAG D1100                 C1  FUC D1101     1555   1555  1.45  
LINK         O4  NAG D1103                 C1  NAG D1104     1555   1555  1.43  
LINK         O6  NAG D1103                 C1  FUC D1106     1555   1555  1.45  
LINK         O4  NAG D1104                 C1  MAN D1105     1555   1555  1.45  
CISPEP   1 ASP A  140    PRO A  141          0        12.04                     
CISPEP   2 TYR A  607    PRO A  608          0         4.84                     
CISPEP   3 ASP B  140    PRO B  141          0        10.57                     
CISPEP   4 TYR B  607    PRO B  608          0        -5.93                     
CISPEP   5 ASP C  140    PRO C  141          0        16.09                     
CISPEP   6 TYR C  607    PRO C  608          0        11.66                     
CISPEP   7 ASP D  140    PRO D  141          0        11.71                     
CISPEP   8 TYR D  607    PRO D  608          0        -1.69                     
SITE     1 AC1  5 HIS A 361  HIS A 365  GLU A 389  HOH A2319                    
SITE     2 AC1  5 HOH A2320                                                     
SITE     1 AC2  3 TYR A 202  PRO A 497  ARG A 500                               
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 10 GLN A 286  TRP A 288  HIS A 292  ARG A 295                    
SITE     2 AC5 10 PEG A1201  HOH A2270  GLN C 286  TRP C 288                    
SITE     3 AC5 10 HIS C 292  ILE C 408                                          
SITE     1 AC6  7 ALA A 334  HIS A 365  TYR A 369  HIS A 388                    
SITE     2 AC6  7 HOH A2143  HOH A2299  HOH A2424                               
SITE     1 AC7  5 HIS B 361  HIS B 365  GLU B 389  HOH B2335                    
SITE     2 AC7  5 HOH B2336                                                     
SITE     1 AC8  5 TYR B 202  PRO B 385  PRO B 497  ARG B 500                    
SITE     2 AC8  5 HOH B2203                                                     
SITE     1 AC9  4 ARG B  96  ASP B 189  GLY B 190  PHE B 191                    
SITE     1 BC1  6 TYR B 465  HOH B2384  HOH B2398  HOH B2478                    
SITE     2 BC1  6 ASP D 462  TYR D 465                                          
SITE     1 BC2  3 ARG B 295  VAL D 296  ILE D 408                               
SITE     1 BC3  7 GLN B 286  GLY B 287  TRP B 288  HIS B 292                    
SITE     2 BC3  7 GLN D 286  HIS D 292  ARG D 295                               
SITE     1 BC4 11 ALA B 334  HIS B 365  TYR B 369  HIS B 388                    
SITE     2 BC4 11 ASN B 494  HOH B2052  HOH B2118  HOH B2137                    
SITE     3 BC4 11 HOH B2313  HOH B2409  HOH B2482                               
SITE     1 BC5  5 HIS C 361  HIS C 365  GLU C 389  HOH C2365                    
SITE     2 BC5  5 HOH C2366                                                     
SITE     1 BC6  4 TYR C 202  PRO C 385  ARG C 500  HOH C2227                    
SITE     1 BC7  2 ASP C 189  GLY C 190                                          
SITE     1 BC8  3 ARG A 453  TYR A 465  TYR C 465                               
SITE     1 BC9 10 SER C  35  SER C  39  ALA C 334  HIS C 365                    
SITE     2 BC9 10 TYR C 369  HIS C 388  HOH C2342  HOH C2513                    
SITE     3 BC9 10 HOH C2514  HOH C2515                                          
SITE     1 CC1  5 HIS D 361  HIS D 365  GLU D 389  HOH D2323                    
SITE     2 CC1  5 HOH D2324                                                     
SITE     1 CC2  4 TYR D 202  PRO D 497  ARG D 500  HOH D2187                    
SITE     1 CC3  3 ASP D 189  GLY D 190  PHE D 191                               
SITE     1 CC4  8 PHE D 228  ARG D 231  ARG D 235  VAL D 268                    
SITE     2 CC4  8 VAL D 269  PRO D 270  PEG D1202  HOH D2201                    
SITE     1 CC5  1 P6G D1201                                                     
SITE     1 CC6  6 SER D  35  SER D  39  ALA D 334  TYR D 369                    
SITE     2 CC6  6 HIS D 388  HOH D2304                                          
SITE     1 CC7  4 PHE D 271  TRP D 580  GLN D 584  HOH D2467                    
SITE     1 CC8  6 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 CC8  6 ARG A 326  HOH A2421                                          
SITE     1 CC9  5 ASN A 416  GLY A 523  PRO A 524  GLN A 527                    
SITE     2 CC9  5 HOH A2423                                                     
SITE     1 DC1  5 ASN A 480  THR A 482  HIS A 483  ARG C 245                    
SITE     2 DC1  5 GLU C 596                                                     
SITE     1 DC2  5 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     2 DC2  5 ARG B 326                                                     
SITE     1 DC3  7 GLU B 403  ASN B 416  GLU B 522  GLY B 523                    
SITE     2 DC3  7 PRO B 524  GLN B 527  HOH B2362                               
SITE     1 DC4  8 ASN B 480  THR B 482  HIS B 483  HOH B2404                    
SITE     2 DC4  8 HOH B2406  HOH B2476  ARG D 245  GLU D 596                    
SITE     1 DC5  7 ASN C  45  THR C  47  GLU C  49  ASN C  50                    
SITE     2 DC5  7 HOH C2508  HOH C2509  HOH C2510                               
SITE     1 DC6 10 GLN C   9  ASN C 416  GLU C 522  GLY C 523                    
SITE     2 DC6 10 PRO C 524  GLN C 527  HOH C2457  HOH C2459                    
SITE     3 DC6 10 HOH C2460  HOH C2512                                          
SITE     1 DC7  5 ARG A 245  GLU A 596  ASN C 480  THR C 482                    
SITE     2 DC7  5 HOH C2436                                                     
SITE     1 DC8  6 ASN D  45  THR D  47  GLU D  49  ASN D  50                    
SITE     2 DC8  6 ARG D 326  HOH D2461                                          
SITE     1 DC9  9 GLN D   9  PHE D  10  GLU D 403  ASN D 416                    
SITE     2 DC9  9 GLU D 522  PRO D 524  GLN D 527  HOH D2404                    
SITE     3 DC9  9 HOH D2464                                                     
SITE     1 EC1  7 ARG B 245  GLU B 596  THR D 478  ASN D 480                    
SITE     2 EC1  7 THR D 482  HOH D2385  HOH D2460                               
SITE     1 EC2 15 GLN A 259  HIS A 331  ALA A 332  THR A 358                    
SITE     2 EC2 15 GLU A 362  LYS A 489  HIS A 491  TYR A 498                    
SITE     3 EC2 15 TYR A 501  HOH A2247  HOH A2248  HOH A2298                    
SITE     4 EC2 15 HOH A2319  HOH A2320  HOH A3001                               
SITE     1 EC3 15 GLN B 259  HIS B 331  ALA B 332  THR B 358                    
SITE     2 EC3 15 GLU B 362  LYS B 489  HIS B 491  TYR B 498                    
SITE     3 EC3 15 TYR B 501  HOH B2256  HOH B2257  HOH B2312                    
SITE     4 EC3 15 HOH B2335  HOH B2336  HOH B3001                               
SITE     1 EC4 14 GLN C 259  HIS C 331  ALA C 332  THR C 358                    
SITE     2 EC4 14 HIS C 361  GLU C 362  LYS C 489  HIS C 491                    
SITE     3 EC4 14 TYR C 498  TYR C 501  HOH C2340  HOH C2341                    
SITE     4 EC4 14 HOH C2365  HOH C2438                                          
SITE     1 EC5 17 GLN D 259  HIS D 331  ALA D 332  THR D 358                    
SITE     2 EC5 17 HIS D 361  GLU D 362  PHE D 435  LYS D 489                    
SITE     3 EC5 17 HIS D 491  TYR D 498  TYR D 501  HOH D2241                    
SITE     4 EC5 17 HOH D2303  HOH D2322  HOH D2323  HOH D2324                    
SITE     5 EC5 17 HOH D2389                                                     
CRYST1   73.340  101.730  114.140  85.09  85.62  81.30 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      0.013635 -0.002086 -0.000890        0.00000                         
SCALE2      0.000000  0.009944 -0.000749        0.00000                         
SCALE3      0.000000  0.000000  0.008812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system