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Database: PDB
Entry: 5AM9
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HEADER    HYDROLASE                               10-MAR-15   5AM9              
TITLE     CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-           
TITLE    2 DOMAIN IN COMPLEX WITH AMYLOID-BETA 10-16                            
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 SYNONYM: ACE, DIPEPTIDYL CARBOXYPEPTIDASE I, KININASE II, CD143,     
COMPND   6  ANGIOTENSIN-CONVERTING ENZYME, SOLUBLE FORM;                        
COMPND   7 EC: 3.2.1.-, 3.4.15.1;                                               
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: MINIMALLY GLYCOSYLATED MUTANT                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO K1                                  
KEYWDS    HYDROLASE, METALLOPROTEASE, AMYLOID- BETA                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MASUYER,K.M.LARMUTH,R.G.DOUGLAS,E.D.STURROCK,K.R.ACHARYA            
REVDAT   3   06-APR-16 5AM9    1       JRNL                                     
REVDAT   2   20-JAN-16 5AM9    1       JRNL                                     
REVDAT   1   13-JAN-16 5AM9    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,                      
REMARK   3                 STEINER,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) : 113.27                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.00                          
REMARK   3   NUMBER OF REFLECTIONS             : 277219                         
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) : 0.19835                         
REMARK   3   R VALUE            (WORKING SET) : 0.19674                         
REMARK   3   FREE R VALUE                     : 0.22907                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 14478                           
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) : 1.800                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.847                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 20272                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.366                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 1023                         
REMARK   3   BIN FREE R VALUE                    : 0.383                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19882                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 570                                     
REMARK   3   SOLVENT ATOMS            :   1649                                  
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.347                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.13                                                
REMARK   3    B22 (A**2) : -0.00                                                
REMARK   3    B33 (A**2) : 1.08                                                 
REMARK   3    B12 (A**2) : -0.14                                                
REMARK   3    B13 (A**2) : -0.03                                                
REMARK   3    B23 (A**2) : 0.05                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.125         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.626         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
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): 21170 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 19291 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28807 ; 1.454 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44389 ; 0.979 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2444 ; 5.961 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1073 ;35.368 ;23.784       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3242 ;13.097 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   134 ;18.082 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3022 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23752 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5224 ; 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):  9761 ; 1.113 ; 2.457       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  9760 ; 1.112 ; 2.457       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12189 ; 1.837 ; 3.677       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11409 ; 1.411 ; 2.720       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  1203                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1301  46.4750 -29.0133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0032 T22:   0.0057                                     
REMARK   3      T33:   0.0197 T12:   0.0009                                     
REMARK   3      T13:  -0.0079 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0182 L22:   0.0069                                     
REMARK   3      L33:   0.0307 L12:   0.0058                                     
REMARK   3      L13:   0.0207 L23:   0.0126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0028 S12:   0.0090 S13:  -0.0055                       
REMARK   3      S21:   0.0009 S22:   0.0055 S23:  -0.0037                       
REMARK   3      S31:   0.0030 S32:   0.0132 S33:  -0.0082                       
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          
REMARK   3   RIDING POSITIONS. FOR AMYLOID-BETA FRAGMENT 10-16, ONLY            
REMARK   3   DI-PEPTIDE PRODUCT OF THE ACE ENZYMATIC ACTIVITY WERE SEEN.        
REMARK   4                                                                      
REMARK   4 5AM9 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 PDBE ID CODE IS EBI-63276.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS-6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 291734                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.47                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.2                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.30                               
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     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.76                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.40                               
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                                        
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: 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 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: 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 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     LYS B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     ALA B   134                                                      
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     GLU C   617                                                      
REMARK 465     ALA C   618                                                      
REMARK 465     GLU C   619                                                      
REMARK 465     ALA C   620                                                      
REMARK 465     SER C   621                                                      
REMARK 465     LYS C   622                                                      
REMARK 465     PHE C   623                                                      
REMARK 465     VAL C   624                                                      
REMARK 465     GLU C   625                                                      
REMARK 465     GLU C   626                                                      
REMARK 465     TYR C   627                                                      
REMARK 465     ASP C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     PRO D   130                                                      
REMARK 465     GLN D   131                                                      
REMARK 465     LYS D   132                                                      
REMARK 465     LEU D   613                                                      
REMARK 465     VAL D   614                                                      
REMARK 465     THR D   615                                                      
REMARK 465     ASP D   616                                                      
REMARK 465     GLU D   617                                                      
REMARK 465     ALA D   618                                                      
REMARK 465     GLU D   619                                                      
REMARK 465     ALA D   620                                                      
REMARK 465     SER D   621                                                      
REMARK 465     LYS D   622                                                      
REMARK 465     PHE D   623                                                      
REMARK 465     VAL D   624                                                      
REMARK 465     GLU D   625                                                      
REMARK 465     GLU D   626                                                      
REMARK 465     TYR D   627                                                      
REMARK 465     ASP D   628                                                      
REMARK 465     LEU D   629                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A 129    CG   CD1  CD2                                       
REMARK 470     LYS A 341    CG   CD   CE   NZ                                   
REMARK 470     ARG A 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 130    CG   CD                                             
REMARK 470     GLN B 131    CG   CD   OE1  NE2                                  
REMARK 470     THR B 135    OG1  CG2                                            
REMARK 470     LEU C 129    CG   CD1  CD2                                       
REMARK 470     THR C 135    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   ND2  ASN B    45     O5   NAG B  1102              2.17            
REMARK 500   OG   SER D   149     O    HOH D  2113              2.20            
REMARK 500   OE1  GLU D   176     O    HOH D  2144              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 326   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 541   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP B 354   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B 541   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG C 541   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 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       73.96   -172.30                                   
REMARK 500    PHE A 271       72.04   -119.02                                   
REMARK 500    ASP A 324     -146.96    -79.73                                   
REMARK 500    ARG A 340       13.38     57.47                                   
REMARK 500    LYS A 341      -45.91   -130.00                                   
REMARK 500    ASN B  45       75.83   -169.02                                   
REMARK 500    LYS B 341      -48.06   -133.19                                   
REMARK 500    ASN C  45       78.27   -176.17                                   
REMARK 500    ASN C 606       70.44   -119.77                                   
REMARK 500    ASN D  45       79.47   -174.42                                   
REMARK 500    ALA D 134      -86.10   -123.69                                   
REMARK 500    LYS D 341      -46.08   -132.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP C  324     GLY C  325                  -37.61                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 105.1                                              
REMARK 620 3 GLU A 389   OE1  93.6 102.2                                        
REMARK 620 4 HOH A2273   O   117.5 125.8 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2273   O                                                      
REMARK 620 2 HIS B 365   NE2 130.0                                              
REMARK 620 3 GLU B 389   OE1 108.9 103.5                                        
REMARK 620 4 HIS B 361   NE2 113.6 101.8  92.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 365   NE2                                                    
REMARK 620 2 GLU C 389   OE1 103.4                                              
REMARK 620 3 HIS C 361   NE2 102.3  92.8                                        
REMARK 620 4 HOH C2329   O   125.7 113.0 114.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 361   NE2                                                    
REMARK 620 2 GLU D 389   OE1  91.8                                              
REMARK 620 3 HIS D 365   NE2 104.4 102.5                                        
REMARK 620 4 HOH D2277   O   115.8 107.7 127.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2205   O                                                      
REMARK 620 2 ASN B 263   OD1 168.6                                              
REMARK 620 3 HOH B2198   O    95.8  90.3                                        
REMARK 620 4 HOH B2207   O    96.6  74.0  87.2                                  
REMARK 620 5 ASP B 354   OD2  90.3  83.7 173.9  92.6                            
REMARK 620 6 GLU B 262   OE2  90.2 100.2  81.6 167.4  97.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 262   OE2                                                    
REMARK 620 2 ASN C 263   OD1 102.3                                              
REMARK 620 3 ASP C 354   OD2  99.5  84.8                                        
REMARK 620 4 HOH C2244   O    83.3  92.7 176.5                                  
REMARK 620 5 HOH C2250   O    92.5 165.1  91.0  90.8                            
REMARK 620 6 HOH C2252   O   169.3  76.7  91.0  86.1  89.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1003  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2208   O                                                      
REMARK 620 2 HOH A2211   O    92.2                                              
REMARK 620 3 HOH A2213   O    89.4  99.6                                        
REMARK 620 4 ASN A 263   OD1  91.8 175.8  79.2                                  
REMARK 620 5 ASP A 354   OD2 173.8  90.5  95.6  85.6                            
REMARK 620 6 GLU A 262   OE2  77.6  82.7 166.9  99.4  97.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D1003  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 262   OE2                                                    
REMARK 620 2 ASP D 354   OD2  92.6                                              
REMARK 620 3 ASN D 263   OD1  98.0  82.9                                        
REMARK 620 4 HOH D2202   O    91.0 170.5  87.8                                  
REMARK 620 5 HOH D2208   O   168.9  91.7  72.4  83.2                            
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 A1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA B1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN C1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA C1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C1202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN D1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA D1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G D1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D1202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D1203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D1204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1102  THROUGH NAG A1103  BOUND TO ASN A  45           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1104  THROUGH MAN A1106  BOUND TO ASN A 416           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1100  THROUGH FUL A1101  BOUND TO ASN A 480           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B1102  THROUGH NAG B1103  BOUND TO ASN B  45           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B1104  THROUGH MAN B1106  BOUND TO ASN B 416           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B1100  THROUGH FUC B1101  BOUND TO ASN B 480           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C1102  THROUGH NAG C1103  BOUND TO ASN C  45           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C1104  THROUGH FUC C1107  BOUND TO ASN C 416           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG C1100  THROUGH FUC C1101  BOUND TO ASN C 480           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG D1102  THROUGH NAG D1103  BOUND TO ASN D  45           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG D1104  THROUGH FUC D1107  BOUND TO ASN D 416           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG D1100  THROUGH FUC D1101  BOUND TO ASN D 480           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-PEPTIDE                        
REMARK 800  GLN A 915  AND LYS A 916                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-PEPTIDE                        
REMARK 800  GLU B 911  AND VAL B 912                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-PEPTIDE                        
REMARK 800  GLU C 911  AND VAL C 912                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-PEPTIDE                        
REMARK 800  GLN D 915  AND LYS D 916                                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UFA   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
REMARK 900   N-DOMAIN IN COMPLEX WITH AC-SD                                     
REMARK 900 RELATED ID: 4UFB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
REMARK 900   N-DOMAIN IN COMPLEX WITH LYS-PRO                                   
REMARK 900 RELATED ID: 5AM8   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
REMARK 900   N-DOMAIN IN COMPLEX WITH AMYLOID-BETA 4-10                         
REMARK 900 RELATED ID: 5AMA   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
REMARK 900   N-DOMAIN IN COMPLEX WITH AMYLOID-BETA 1-16                         
REMARK 900 RELATED ID: 5AMB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
REMARK 900   N-DOMAIN 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            
REMARK 900   N-DOMAIN IN COMPLEX WITH AMYLOID-BETA FLUOROGENIC                  
REMARK 900  FRAGMENT 4-10                                                       
DBREF  5AM9 A    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AM9 B    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AM9 C    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AM9 D    1   629  UNP    P12821   ACE_HUMAN       30    658             
SEQADV 5AM9 GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AM9 GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AM9 GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AM9 GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AM9 GLN A  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AM9 GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AM9 ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AM9 LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AM9 LEU A  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AM9 GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AM9 GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AM9 GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AM9 GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AM9 GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AM9 ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AM9 LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AM9 LEU B  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AM9 GLN C    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AM9 GLN C   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AM9 GLN C   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AM9 GLN C  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AM9 GLN C  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AM9 GLN C  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AM9 ARG C  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AM9 LEU C  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AM9 LEU C  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AM9 GLN D    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AM9 GLN D   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AM9 GLN D   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AM9 GLN D  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AM9 GLN D  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AM9 GLN D  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AM9 ARG D  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AM9 LEU D  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AM9 LEU D  629  UNP  P12821    ARG   658 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                                          
HET    GLN  A 915       9                                                       
HET    LYS  A 916      10                                                       
HET     ZN  A1001       1                                                       
HET     CL  A1002       1                                                       
HET     NA  A1003       1                                                       
HET    NAG  A1100      14                                                       
HET    FUL  A1101      10                                                       
HET    NAG  A1102      14                                                       
HET    NAG  A1103      14                                                       
HET    NAG  A1104      14                                                       
HET    NAG  A1105      14                                                       
HET    MAN  A1106      11                                                       
HET    PEG  A1200       7                                                       
HET    PEG  A1201       7                                                       
HET    P6G  A1202      19                                                       
HET    PEG  A1203       7                                                       
HET    GLU  B 911       9                                                       
HET    VAL  B 912       8                                                       
HET     ZN  B1001       1                                                       
HET     CL  B1002       1                                                       
HET     CA  B1003       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    MAN  B1106      11                                                       
HET    PEG  B1201       7                                                       
HET    PEG  B1202       7                                                       
HET    P6G  B1203      19                                                       
HET    P6G  B1204      19                                                       
HET    PEG  B1205       7                                                       
HET    GLU  C 911       9                                                       
HET    VAL  C 912       8                                                       
HET     ZN  C1001       1                                                       
HET     CL  C1002       1                                                       
HET     CA  C1003       1                                                       
HET    NAG  C1100      14                                                       
HET    FUC  C1101      10                                                       
HET    NAG  C1102      14                                                       
HET    NAG  C1103      14                                                       
HET    NAG  C1104      14                                                       
HET    NAG  C1105      14                                                       
HET    BMA  C1106      11                                                       
HET    FUC  C1107      10                                                       
HET    PEG  C1200       7                                                       
HET    PEG  C1201       7                                                       
HET    PEG  C1202       7                                                       
HET    PEG  C1203       7                                                       
HET    GLN  D 915       9                                                       
HET    LYS  D 916      10                                                       
HET     ZN  D1001       1                                                       
HET     CL  D1002       1                                                       
HET     NA  D1003       1                                                       
HET    NAG  D1100      14                                                       
HET    FUC  D1101      10                                                       
HET    NAG  D1102      14                                                       
HET    NAG  D1103      14                                                       
HET    NAG  D1104      14                                                       
HET    NAG  D1105      14                                                       
HET    BMA  D1106      11                                                       
HET    FUC  D1107      10                                                       
HET    PEG  D1200       7                                                       
HET    P6G  D1201      19                                                       
HET    PEG  D1202       7                                                       
HET    PEG  D1203       7                                                       
HET    PEG  D1204       7                                                       
HETNAM     GLN GLUTAMINE                                                        
HETNAM     LYS LYSINE                                                           
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     VAL VALINE                                                           
HETNAM      ZN ZINC ION                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM      CA CALCIUM ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   5  GLN    2(C5 H10 N2 O3)                                              
FORMUL   6  LYS    2(C6 H15 N2 O2 1+)                                           
FORMUL   7   ZN    4(ZN 2+)                                                     
FORMUL   8   CL    4(CL 1-)                                                     
FORMUL   9   NA    2(NA 1+)                                                     
FORMUL  10  NAG    20(C8 H15 N O6)                                              
FORMUL  10  FUL    C6 H12 O5                                                    
FORMUL  12  MAN    2(C6 H12 O6)                                                 
FORMUL  13  PEG    14(C4 H10 O3)                                                
FORMUL  16  GLU    2(C5 H9 N O4)                                                
FORMUL  17  VAL    2(C5 H11 N O2)                                               
FORMUL  20   CA    2(CA 2+)                                                     
FORMUL  21  FUC    5(C6 H12 O5)                                                 
FORMUL  25  P6G    4(C12 H26 O7)                                                
FORMUL  36  BMA    2(C6 H12 O6)                                                 
FORMUL  55  HOH   *1649(H2 O)                                                   
HELIX    1   1 ASP A    2  GLN A    6  5                                   5    
HELIX    2   2 ASP A   13  THR A   44  1                                  32    
HELIX    3   3 THR A   47  GLU A   77  1                                  31    
HELIX    4   4 PRO A   78  PHE A   83  5                                   6    
HELIX    5   5 ASP A   85  ARG A   96  1                                  12    
HELIX    6   6 LEU A   98  LEU A  103  5                                   6    
HELIX    7   7 PRO A  104  ALA A  125  1                                  22    
HELIX    8   8 PRO A  141  SER A  150  1                                  10    
HELIX    9   9 SER A  152  GLN A  188  1                                  37    
HELIX   10  10 ASP A  193  TRP A  201  1                                   9    
HELIX   11  11 THR A  206  GLY A  238  1                                  33    
HELIX   12  12 TRP A  261  ASN A  263  5                                   3    
HELIX   13  13 ILE A  264  VAL A  269  1                                   6    
HELIX   14  14 VAL A  279  GLN A  286  1                                   8    
HELIX   15  15 GLN A  289  LEU A  304  1                                  16    
HELIX   16  16 PRO A  310  SER A  317  1                                   8    
HELIX   17  17 THR A  352  TYR A  372  1                                  21    
HELIX   18  18 PRO A  376  ARG A  380  5                                   5    
HELIX   19  19 ASN A  384  THR A  401  1                                  18    
HELIX   20  20 THR A  401  ILE A  408  1                                   8    
HELIX   21  21 ASP A  417  ILE A  433  1                                  17    
HELIX   22  22 ALA A  434  SER A  451  1                                  18    
HELIX   23  23 PRO A  455  SER A  457  5                                   3    
HELIX   24  24 ARG A  458  GLY A  472  1                                  15    
HELIX   25  25 PHE A  484  LYS A  489  5                                   6    
HELIX   26  26 TYR A  498  ALA A  519  1                                  22    
HELIX   27  27 PRO A  524  CYS A  528  5                                   5    
HELIX   28  28 SER A  533  GLY A  547  1                                  15    
HELIX   29  29 PRO A  551  GLY A  561  1                                  11    
HELIX   30  30 ALA A  567  ASN A  588  1                                  22    
HELIX   31  31 ASP B    2  GLN B    6  5                                   5    
HELIX   32  32 ASP B   13  THR B   44  1                                  32    
HELIX   33  33 THR B   47  GLU B   77  1                                  31    
HELIX   34  34 ILE B   79  PHE B   83  5                                   5    
HELIX   35  35 ASP B   85  ARG B   96  1                                  12    
HELIX   36  36 LEU B   98  LEU B  103  5                                   6    
HELIX   37  37 PRO B  104  ALA B  125  1                                  22    
HELIX   38  38 PRO B  141  SER B  150  1                                  10    
HELIX   39  39 SER B  152  GLN B  188  1                                  37    
HELIX   40  40 ASP B  193  TRP B  201  1                                   9    
HELIX   41  41 THR B  206  GLY B  238  1                                  33    
HELIX   42  42 TRP B  261  ASN B  263  5                                   3    
HELIX   43  43 ILE B  264  VAL B  269  1                                   6    
HELIX   44  44 VAL B  279  GLN B  286  1                                   8    
HELIX   45  45 GLN B  289  LEU B  304  1                                  16    
HELIX   46  46 PRO B  310  SER B  317  1                                   8    
HELIX   47  47 THR B  352  LYS B  373  1                                  22    
HELIX   48  48 PRO B  376  ARG B  380  5                                   5    
HELIX   49  49 ASN B  384  SER B  400  1                                  17    
HELIX   50  50 THR B  401  ILE B  408  1                                   8    
HELIX   51  51 ASP B  417  ILE B  433  1                                  17    
HELIX   52  52 ALA B  434  GLY B  452  1                                  19    
HELIX   53  53 PRO B  455  SER B  457  5                                   3    
HELIX   54  54 ARG B  458  GLY B  472  1                                  15    
HELIX   55  55 PHE B  484  LYS B  489  5                                   6    
HELIX   56  56 TYR B  498  ALA B  519  1                                  22    
HELIX   57  57 PRO B  524  CYS B  528  5                                   5    
HELIX   58  58 SER B  533  GLY B  547  1                                  15    
HELIX   59  59 PRO B  551  GLY B  561  1                                  11    
HELIX   60  60 ALA B  567  ASN B  588  1                                  22    
HELIX   61  61 ASP C    2  GLN C    6  5                                   5    
HELIX   62  62 ASP C   13  THR C   44  1                                  32    
HELIX   63  63 THR C   47  GLU C   77  1                                  31    
HELIX   64  64 ILE C   79  PHE C   83  5                                   5    
HELIX   65  65 ASP C   85  ARG C   96  1                                  12    
HELIX   66  66 LEU C   98  LEU C  103  5                                   6    
HELIX   67  67 PRO C  104  ALA C  125  1                                  22    
HELIX   68  68 PRO C  141  SER C  150  1                                  10    
HELIX   69  69 SER C  152  GLN C  188  1                                  37    
HELIX   70  70 ASP C  193  TRP C  201  1                                   9    
HELIX   71  71 THR C  206  GLY C  238  1                                  33    
HELIX   72  72 TRP C  261  ASN C  263  5                                   3    
HELIX   73  73 ILE C  264  VAL C  269  1                                   6    
HELIX   74  74 VAL C  279  GLN C  286  1                                   8    
HELIX   75  75 GLN C  289  LEU C  304  1                                  16    
HELIX   76  76 PRO C  310  SER C  317  1                                   8    
HELIX   77  77 THR C  352  LYS C  373  1                                  22    
HELIX   78  78 PRO C  376  ARG C  380  5                                   5    
HELIX   79  79 ASN C  384  SER C  400  1                                  17    
HELIX   80  80 THR C  401  ILE C  408  1                                   8    
HELIX   81  81 ASP C  417  ILE C  433  1                                  17    
HELIX   82  82 ALA C  434  GLY C  452  1                                  19    
HELIX   83  83 PRO C  455  SER C  457  5                                   3    
HELIX   84  84 ARG C  458  GLY C  472  1                                  15    
HELIX   85  85 PHE C  484  LYS C  489  5                                   6    
HELIX   86  86 TYR C  498  ALA C  519  1                                  22    
HELIX   87  87 PRO C  524  CYS C  528  5                                   5    
HELIX   88  88 SER C  533  GLY C  547  1                                  15    
HELIX   89  89 PRO C  551  GLY C  561  1                                  11    
HELIX   90  90 ALA C  567  GLY C  589  1                                  23    
HELIX   91  91 ILE C  611  THR C  615  5                                   5    
HELIX   92  92 ASP D    2  GLN D    6  5                                   5    
HELIX   93  93 ASP D   13  THR D   44  1                                  32    
HELIX   94  94 THR D   47  GLU D   77  1                                  31    
HELIX   95  95 ILE D   79  PHE D   83  5                                   5    
HELIX   96  96 ASP D   85  ARG D   96  1                                  12    
HELIX   97  97 LEU D   98  LEU D  103  5                                   6    
HELIX   98  98 PRO D  104  ALA D  125  1                                  22    
HELIX   99  99 PRO D  141  SER D  150  1                                  10    
HELIX  100 100 SER D  152  GLN D  188  1                                  37    
HELIX  101 101 ASP D  193  TRP D  201  1                                   9    
HELIX  102 102 THR D  206  GLY D  238  1                                  33    
HELIX  103 103 TRP D  261  ASN D  263  5                                   3    
HELIX  104 104 ILE D  264  VAL D  269  1                                   6    
HELIX  105 105 VAL D  279  GLN D  286  1                                   8    
HELIX  106 106 GLN D  289  LEU D  304  1                                  16    
HELIX  107 107 PRO D  310  SER D  317  1                                   8    
HELIX  108 108 THR D  352  LYS D  373  1                                  22    
HELIX  109 109 PRO D  376  ARG D  380  5                                   5    
HELIX  110 110 ASN D  384  SER D  400  1                                  17    
HELIX  111 111 THR D  401  ILE D  408  1                                   8    
HELIX  112 112 ASP D  417  ILE D  433  1                                  17    
HELIX  113 113 ALA D  434  SER D  451  1                                  18    
HELIX  114 114 PRO D  455  SER D  457  5                                   3    
HELIX  115 115 ARG D  458  GLY D  472  1                                  15    
HELIX  116 116 PHE D  484  LYS D  489  5                                   6    
HELIX  117 117 TYR D  498  ALA D  519  1                                  22    
HELIX  118 118 PRO D  524  CYS D  528  5                                   5    
HELIX  119 119 SER D  533  GLY D  547  1                                  15    
HELIX  120 120 PRO D  551  GLY D  561  1                                  11    
HELIX  121 121 ALA D  567  ASN D  588  1                                  22    
SHEET    1  AA 2 LYS A 126  CYS A 128  0                                        
SHEET    2  AA 2 CYS A 136  SER A 138 -1  O  TRP A 137   N  VAL A 127           
SHEET    1  AB 2 ILE A 248  PRO A 249  0                                        
SHEET    2  AB 2 ILE A 473  CYS A 474  1  N  CYS A 474   O  ILE A 248           
SHEET    1  AC 2 SER A 333  ASP A 336  0                                        
SHEET    2  AC 2 PHE A 343  LYS A 346 -1  O  ARG A 344   N  TRP A 335           
SHEET    1  BA 2 LYS B 126  VAL B 127  0                                        
SHEET    2  BA 2 TRP B 137  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 LYS D 126  VAL D 127  0                                        
SHEET    2  DA 2 TRP D 137  SER D 138 -1  O  TRP D 137   N  VAL D 127           
SHEET    1  DB 2 ILE D 248  PRO D 249  0                                        
SHEET    2  DB 2 ILE D 473  CYS D 474  1  N  CYS D 474   O  ILE D 248           
SHEET    1  DC 2 SER D 333  ASP D 336  0                                        
SHEET    2  DC 2 PHE D 343  LYS D 346 -1  O  ARG D 344   N  TRP D 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.06  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.07  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.02  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.05  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.07  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03  
SSBOND   7 CYS C  128    CYS C  136                          1555   1555  2.07  
SSBOND   8 CYS C  330    CYS C  348                          1555   1555  2.03  
SSBOND   9 CYS C  516    CYS C  528                          1555   1555  2.04  
SSBOND  10 CYS D  128    CYS D  136                          1555   1555  2.04  
SSBOND  11 CYS D  330    CYS D  348                          1555   1555  2.02  
SSBOND  12 CYS D  516    CYS D  528                          1555   1555  2.04  
LINK         ND2 ASN A  45                 C1  NAG A1102     1555   1555  1.44  
LINK         ND2 ASN A 416                 C1  NAG A1104     1555   1555  1.44  
LINK         ND2 ASN A 480                 C1  NAG A1100     1555   1555  1.44  
LINK        ZN    ZN A1001                 NE2 HIS A 361     1555   1555  2.07  
LINK        ZN    ZN A1001                 NE2 HIS A 365     1555   1555  2.06  
LINK        ZN    ZN A1001                 OE1 GLU A 389     1555   1555  1.95  
LINK        ZN    ZN A1001                 O   HOH A2273     1555   1555  2.02  
LINK        NA    NA A1003                 OE2 GLU A 262     1555   1555  2.26  
LINK        NA    NA A1003                 OD2 ASP A 354     1555   1555  2.36  
LINK        NA    NA A1003                 OD1 ASN A 263     1555   1555  2.71  
LINK        NA    NA A1003                 O   HOH A2208     1555   1555  2.29  
LINK        NA    NA A1003                 O   HOH A2213     1555   1555  2.55  
LINK        NA    NA A1003                 O   HOH A2211     1555   1555  2.35  
LINK         O6  NAG A1100                 C1  FUL A1101     1555   1555  1.43  
LINK         O4  NAG A1102                 C1  NAG A1103     1555   1555  1.46  
LINK         O4  NAG A1104                 C1  NAG A1105     1555   1555  1.44  
LINK         O4  NAG A1105                 C1  MAN A1106     1555   1555  1.46  
LINK         ND2 ASN B  45                 C1  NAG B1102     1555   1555  1.42  
LINK         ND2 ASN B 416                 C1  NAG B1104     1555   1555  1.42  
LINK         ND2 ASN B 480                 C1  NAG B1100     1555   1555  1.45  
LINK        ZN    ZN B1001                 O   HOH B2273     1555   1555  2.07  
LINK        ZN    ZN B1001                 NE2 HIS B 365     1555   1555  2.09  
LINK        ZN    ZN B1001                 NE2 HIS B 361     1555   1555  2.07  
LINK        ZN    ZN B1001                 OE1 GLU B 389     1555   1555  1.95  
LINK        CA    CA B1003                 OD2 ASP B 354     1555   1555  2.47  
LINK        CA    CA B1003                 OD1 ASN B 263     1555   1555  2.65  
LINK        CA    CA B1003                 OE2 GLU B 262     1555   1555  2.11  
LINK        CA    CA B1003                 O   HOH B2207     1555   1555  2.67  
LINK        CA    CA B1003                 O   HOH B2205     1555   1555  2.46  
LINK        CA    CA B1003                 O   HOH B2198     1555   1555  2.35  
LINK         O6  NAG B1100                 C1  FUC B1101     1555   1555  1.45  
LINK         O4  NAG B1102                 C1  NAG B1103     1555   1555  1.44  
LINK         O4  NAG B1104                 C1  NAG B1105     1555   1555  1.44  
LINK         O4  NAG B1105                 C1  MAN B1106     1555   1555  1.46  
LINK         ND2 ASN C  45                 C1  NAG C1102     1555   1555  1.45  
LINK         ND2 ASN C 416                 C1  NAG C1104     1555   1555  1.44  
LINK         ND2 ASN C 480                 C1  NAG C1100     1555   1555  1.46  
LINK        ZN    ZN C1001                 NE2 HIS C 365     1555   1555  2.12  
LINK        ZN    ZN C1001                 NE2 HIS C 361     1555   1555  2.11  
LINK        ZN    ZN C1001                 OE1 GLU C 389     1555   1555  1.89  
LINK        ZN    ZN C1001                 O   HOH C2329     1555   1555  2.06  
LINK        CA    CA C1003                 OE2 GLU C 262     1555   1555  2.21  
LINK        CA    CA C1003                 O   HOH C2252     1555   1555  2.47  
LINK        CA    CA C1003                 O   HOH C2244     1555   1555  2.33  
LINK        CA    CA C1003                 OD2 ASP C 354     1555   1555  2.39  
LINK        CA    CA C1003                 O   HOH C2250     1555   1555  2.31  
LINK        CA    CA C1003                 OD1 ASN C 263     1555   1555  2.51  
LINK         O6  NAG C1100                 C1  FUC C1101     1555   1555  1.45  
LINK         O4  NAG C1102                 C1  NAG C1103     1555   1555  1.44  
LINK         O6  NAG C1104                 C1  FUC C1107     1555   1555  1.46  
LINK         O4  NAG C1104                 C1  NAG C1105     1555   1555  1.43  
LINK         O4  NAG C1105                 C1  BMA C1106     1555   1555  1.44  
LINK         ND2 ASN D  45                 C1  NAG D1102     1555   1555  1.44  
LINK         ND2 ASN D 416                 C1  NAG D1104     1555   1555  1.44  
LINK         ND2 ASN D 480                 C1  NAG D1100     1555   1555  1.46  
LINK        ZN    ZN D1001                 O   HOH D2277     1555   1555  2.00  
LINK        ZN    ZN D1001                 NE2 HIS D 365     1555   1555  2.04  
LINK        ZN    ZN D1001                 OE1 GLU D 389     1555   1555  1.94  
LINK        ZN    ZN D1001                 NE2 HIS D 361     1555   1555  2.13  
LINK        NA    NA D1003                 O   HOH D2208     1555   1555  2.45  
LINK        NA    NA D1003                 OD1 ASN D 263     1555   1555  2.89  
LINK        NA    NA D1003                 O   HOH D2202     1555   1555  2.00  
LINK        NA    NA D1003                 OD2 ASP D 354     1555   1555  2.37  
LINK        NA    NA D1003                 OE2 GLU D 262     1555   1555  2.22  
LINK         O6  NAG D1100                 C1  FUC D1101     1555   1555  1.44  
LINK         O4  NAG D1102                 C1  NAG D1103     1555   1555  1.45  
LINK         O6  NAG D1104                 C1  FUC D1107     1555   1555  1.44  
LINK         O4  NAG D1104                 C1  NAG D1105     1555   1555  1.44  
LINK         O4  NAG D1105                 C1  BMA D1106     1555   1555  1.44  
CISPEP   1 ASP A  140    PRO A  141          0        10.79                     
CISPEP   2 TYR A  607    PRO A  608          0        -6.97                     
CISPEP   3 ASP B  140    PRO B  141          0        12.80                     
CISPEP   4 TYR B  607    PRO B  608          0        -0.78                     
CISPEP   5 ASP C  140    PRO C  141          0        17.85                     
CISPEP   6 TYR C  607    PRO C  608          0         1.74                     
CISPEP   7 ASP D  140    PRO D  141          0        14.30                     
CISPEP   8 TYR D  607    PRO D  608          0         1.41                     
SITE     1 AC1  4 HIS A 361  HIS A 365  GLU A 389  HOH A2273                    
SITE     1 AC2  4 TYR A 202  PRO A 385  PRO A 497  ARG A 500                    
SITE     1 AC3  6 GLU A 262  ASN A 263  ASP A 354  HOH A2208                    
SITE     2 AC3  6 HOH A2211  HOH A2213                                          
SITE     1 AC4  3 ARG A  96  ASP A 189  PHE A 191                               
SITE     1 AC5  1 P6G A1202                                                     
SITE     1 AC6  8 GLN A 286  TRP A 288  HIS A 292  PEG A1201                    
SITE     2 AC6  8 GLN C 286  TRP C 288  HIS C 292  ILE C 408                    
SITE     1 AC7  3 ALA A 334  TYR A 369  HOH A2367                               
SITE     1 AC8  4 HIS B 361  HIS B 365  GLU B 389  HOH B2273                    
SITE     1 AC9  4 TYR B 202  PRO B 385  ARG B 500  HOH B2155                    
SITE     1 BC1  6 GLU B 262  ASN B 263  ASP B 354  HOH B2198                    
SITE     2 BC1  6 HOH B2205  HOH B2207                                          
SITE     1 BC2  6 ARG B 453  TYR B 465  HOH B2402  HOH B2403                    
SITE     2 BC2  6 ARG D 453  TYR D 465                                          
SITE     1 BC3  8 GLN B 286  TRP B 288  HIS B 292  HOH B2405                    
SITE     2 BC3  8 GLN D 286  GLY D 287  HIS D 292  ARG D 295                    
SITE     1 BC4  7 SER B  39  SER B 333  TRP B 335  TYR B 369                    
SITE     2 BC4  7 HIS B 388  HOH B2338  HOH B2407                               
SITE     1 BC5  3 ARG B  96  ASP B 189  GLY B 190                               
SITE     1 BC6  4 HIS C 361  HIS C 365  GLU C 389  HOH C2329                    
SITE     1 BC7  4 TYR C 202  PRO C 385  ARG C 500  HOH C2194                    
SITE     1 BC8  6 GLU C 262  ASN C 263  ASP C 354  HOH C2244                    
SITE     2 BC8  6 HOH C2250  HOH C2252                                          
SITE     1 BC9  2 ASP C 189  GLY C 190                                          
SITE     1 CC1  4 ARG A 453  TYR A 465  TYR C 465  HOH C2379                    
SITE     1 CC2  1 SER C  39                                                     
SITE     1 CC3  1 TYR C 369                                                     
SITE     1 CC4  4 HIS D 361  HIS D 365  GLU D 389  HOH D2277                    
SITE     1 CC5  4 TYR D 202  PRO D 385  PRO D 497  ARG D 500                    
SITE     1 CC6  5 GLU D 262  ASN D 263  ASP D 354  HOH D2202                    
SITE     2 CC6  5 HOH D2208                                                     
SITE     1 CC7  2 ASP D 189  PHE D 191                                          
SITE     1 CC8  9 PHE D 228  ARG D 231  ARG D 235  VAL D 268                    
SITE     2 CC8  9 VAL D 269  PRO D 270  ASN D 588  PEG D1202                    
SITE     3 CC8  9 HOH D2072                                                     
SITE     1 CC9  3 ARG D 235  P6G D1201  HOH D2401                               
SITE     1 DC1  4 SER D  39  ALA D 334  PEG D1204  HOH D2402                    
SITE     1 DC2  5 ALA D 334  TYR D 369  HIS D 388  GLU D 389                    
SITE     2 DC2  5 PEG D1203                                                     
SITE     1 DC3  6 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 DC3  6 ARG A 326  HOH A2364                                          
SITE     1 DC4  6 ASN A 416  GLU A 522  GLY A 523  PRO A 524                    
SITE     2 DC4  6 GLN A 527  HOH A2365                                          
SITE     1 DC5  6 GLU A 161  ASN A 480  THR A 482  HIS A 483                    
SITE     2 DC5  6 ARG C 245  GLU C 596                                          
SITE     1 DC6  4 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     1 DC7  7 ASN B 416  GLU B 522  GLY B 523  PRO B 524                    
SITE     2 DC7  7 GLN B 527  HOH B2400  HOH B2401                               
SITE     1 DC8 10 THR B 478  ASN B 480  THR B 482  HIS B 483                    
SITE     2 DC8 10 HOH B2333  HOH B2397  HOH B2398  HOH B2399                    
SITE     3 DC8 10 ARG D 245  GLU D 596                                          
SITE     1 DC9  5 ASN C  45  THR C  47  GLU C  49  ASN C  50                    
SITE     2 DC9  5 HOH C2461                                                     
SITE     1 EC1 13 GLN C   9  PHE C  10  SER C  11  ASN C 416                    
SITE     2 EC1 13 GLU C 522  PRO C 524  GLN C 527  HOH C2416                    
SITE     3 EC1 13 HOH C2418  HOH C2462  HOH C2463  HOH C2464                    
SITE     4 EC1 13 HOH C2465                                                     
SITE     1 EC2  5 ARG A 245  GLU A 596  THR C 478  ASN C 480                    
SITE     2 EC2  5 THR C 482                                                     
SITE     1 EC3  4 ASN D  45  THR D  47  GLU D  49  ASN D  50                    
SITE     1 EC4  9 PHE D  10  SER D  11  ASN D 416  GLU D 522                    
SITE     2 EC4  9 PRO D 524  GLN D 527  HOH D2351  HOH D2399                    
SITE     3 EC4  9 HOH D2400                                                     
SITE     1 EC5  8 ARG B 245  GLU B 596  THR D 478  ASN D 480                    
SITE     2 EC5  8 THR D 482  HIS D 483  HOH D2335  HOH D2398                    
SITE     1 EC6 19 GLN A 259  SER A 260  HIS A 331  ALA A 332                    
SITE     2 EC6 19 GLU A 362  LYS A 489  HIS A 491  TYR A 498                    
SITE     3 EC6 19 TYR A 501  HOH A2253  HOH A2267  HOH A2268                    
SITE     4 EC6 19 HOH A2272  HOH A2273  HOH A2293  HOH A2322                    
SITE     5 EC6 19 HOH A3001  HOH A3002  HOH A3003                               
SITE     1 EC7 14 GLN B 259  HIS B 331  ALA B 332  GLU B 362                    
SITE     2 EC7 14 LYS B 489  HIS B 491  TYR B 498  TYR B 501                    
SITE     3 EC7 14 HOH B2200  HOH B2266  HOH B2267  HOH B2272                    
SITE     4 EC7 14 HOH B2273  HOH B3001                                          
SITE     1 EC8 16 GLN C 259  HIS C 331  ALA C 332  GLU C 362                    
SITE     2 EC8 16 LYS C 489  HIS C 491  TYR C 498  TYR C 501                    
SITE     3 EC8 16 HOH C2304  HOH C2322  HOH C2323  HOH C2328                    
SITE     4 EC8 16 HOH C2329  HOH C2397  HOH C3001  HOH C3002                    
SITE     1 EC9 17 GLN D 259  HIS D 331  ALA D 332  GLU D 362                    
SITE     2 EC9 17 GLU D 431  LYS D 489  HIS D 491  TYR D 498                    
SITE     3 EC9 17 TYR D 501  PHE D 505  HOH D2205  HOH D2271                    
SITE     4 EC9 17 HOH D2272  HOH D2276  HOH D2277  HOH D2310                    
SITE     5 EC9 17 HOH D3001                                                     
CRYST1   73.348  101.800  113.950  85.04  85.55  81.88 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      0.013634 -0.001945 -0.000915        0.00000                         
SCALE2      0.000000  0.009923 -0.000761        0.00000                         
SCALE3      0.000000  0.000000  0.008828        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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