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Database: PDB
Entry: 4BXK
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Original site: 4BXK 
HEADER    HYDROLASE                               12-JUL-13   4BXK              
TITLE     CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-           
TITLE    2 DOMAIN IN COMPLEX WITH A DOMAIN-SPECIFIC INHIBITOR                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N DOMAIN, RESIDUES 30-657;                                 
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                                                        
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, PROTEASE INHIBITOR                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.G.DOUGLAS,R.K.SHARMA,G.MASUYER,L.LUBBE,I.ZAMORA,K.R.ACHARYA,        
AUTHOR   2 K.CHIBALE,E.D.STURROCK                                               
REVDAT   4   13-NOV-13 4BXK    1       REMARK LINK   ATOM   ANISOU              
REVDAT   3   06-NOV-13 4BXK    1       JRNL                                     
REVDAT   2   25-SEP-13 4BXK    1       JRNL   LINK                              
REVDAT   1   18-SEP-13 4BXK    0                                                
JRNL        AUTH   R.G.DOUGLAS,R.K.SHARMA,G.MASUYER,L.LUBBE,I.ZAMORA,           
JRNL        AUTH 2 K.R.ACHARYA,K.CHIBALE,E.D.STURROCK                           
JRNL        TITL   FRAGMENT-BASED DESIGN FOR THE DEVELOPMENT OF N-DOMAIN        
JRNL        TITL 2 SELECTIVE ANGIOTENSIN-1 CONVERTING ENZYME INHIBITORS         
JRNL        REF    CLIN.SCI.                     V. 126   305 2014              
JRNL        REFN                   ISSN 0143-5221                               
JRNL        PMID   24015848                                                     
JRNL        DOI    10.1042/CS20130403                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.40                          
REMARK   3   NUMBER OF REFLECTIONS             : 69351                          
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) : 0.18825                         
REMARK   3   R VALUE            (WORKING SET) : 0.18653                         
REMARK   3   FREE R VALUE                     : 0.21965                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3660                            
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) : 2.200                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.257                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4914                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.277                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 257                          
REMARK   3   BIN FREE R VALUE                    : 0.315                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9919                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 329                                     
REMARK   3   SOLVENT ATOMS            : 409                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.232                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.29                                                
REMARK   3    B22 (A**2) : 0.12                                                 
REMARK   3    B33 (A**2) : 0.65                                                 
REMARK   3    B12 (A**2) : 1.99                                                 
REMARK   3    B13 (A**2) : 0.63                                                 
REMARK   3    B23 (A**2) : 0.08                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.272         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.844        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10576 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9612 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14406 ; 1.183 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22017 ; 0.807 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1220 ; 5.589 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   532 ;35.227 ;23.797       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1596 ;14.102 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;14.779 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1510 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11905 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2626 ; 0.001 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
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    30        A   610                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6645 -15.5400 -18.6678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0112 T22:   0.0974                                     
REMARK   3      T33:   0.0348 T12:  -0.0046                                     
REMARK   3      T13:  -0.0051 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3541 L22:   0.4082                                     
REMARK   3      L33:   0.0320 L12:  -0.1086                                     
REMARK   3      L13:  -0.0999 L23:   0.0415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0410 S12:  -0.0067 S13:  -0.0163                       
REMARK   3      S21:  -0.0534 S22:  -0.0332 S23:  -0.0029                       
REMARK   3      S31:  -0.0115 S32:  -0.0042 S33:  -0.0078                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    30        B   610                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0424  14.6842  18.7376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0270 T22:   0.0506                                     
REMARK   3      T33:   0.0314 T12:  -0.0226                                     
REMARK   3      T13:  -0.0092 T23:  -0.0203                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0653 L22:   0.5265                                     
REMARK   3      L33:   0.8745 L12:  -0.1821                                     
REMARK   3      L13:  -0.1475 L23:   0.3786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0105 S12:   0.0041 S13:  -0.0027                       
REMARK   3      S21:  -0.0005 S22:  -0.0109 S23:  -0.0074                       
REMARK   3      S31:   0.0057 S32:  -0.0611 S33:   0.0004                       
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. RESIDUES 130-132 ARE DISORDERED                  
REMARK   4                                                                      
REMARK   4 4BXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUL-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-57666.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-12                          
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                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 2M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73018                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.67                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY                : 3.9                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.85                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.60                               
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ILE A   611                                                      
REMARK 465     ASP A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     VAL A   614                                                      
REMARK 465     THR A   615                                                      
REMARK 465     ASP A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     ALA A   618                                                      
REMARK 465     GLU A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     SER A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     PHE A   623                                                      
REMARK 465     VAL A   624                                                      
REMARK 465     GLU A   625                                                      
REMARK 465     GLU A   626                                                      
REMARK 465     TYR A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     GLN B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     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 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     GLU A  56    CD   OE1  OE2                                       
REMARK 470     LEU A 129    CG   CD1  CD2                                       
REMARK 470     LYS A 341    CD   CE   NZ                                        
REMARK 470     LYS A 542    CE   NZ                                             
REMARK 470     GLU B  56    CD   OE1  OE2                                       
REMARK 470     LYS B 341    CD   CE   NZ                                        
REMARK 470     ARG B 413    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 542    CE   NZ                                             
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   O    CYS A   330     O    HOH A  2150              2.19            
REMARK 500   OG   SER B   260     OE1  GLU B   262              1.86            
REMARK 500   OG1  THR B   282     O    HOH B  2082              2.18            
REMARK 500   ND2  ASN B   480     C2   NAG B  1612              1.53            
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       80.04   -172.15                                   
REMARK 500    ASN A 203       64.45     30.04                                   
REMARK 500    ASP A 324     -173.56    -67.07                                   
REMARK 500    ALA B  12       49.65    -88.52                                   
REMARK 500    ASN B  45       79.68   -175.26                                   
REMARK 500    ALA B 134      -86.69    -73.52                                   
REMARK 500    GLN B 575      -53.86    -28.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 B  704                                                       
REMARK 610     P6G A  704                                                       
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 A1620  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 365   NE2                                                    
REMARK 620 2 1IU A1001   OAI  83.2                                              
REMARK 620 3 1IU A1001   OAH 131.5  66.2                                        
REMARK 620 4 HIS A 361   NE2 105.3  99.4 115.7                                  
REMARK 620 5 GLU A 389   OE1  99.7 167.3 103.5  91.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1619  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 365   NE2                                                    
REMARK 620 2 GLU B 389   OE1 107.1                                              
REMARK 620 3 1IU B1001   OAI  80.9 166.3                                        
REMARK 620 4 1IU B1001   OAH 137.8 102.0  65.7                                  
REMARK 620 5 HIS B 361   NE2 100.1  91.6  98.0 109.1                            
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 PEG A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1IU A1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A1620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1IU B1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1614  THROUGH NAG A1615  BOUND TO ASN A  45           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1616  THROUGH FUC A1619  BOUND TO ASN A 416           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG A1612  THROUGH FUC A1613  BOUND TO ASN A 480           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B1614  THROUGH NAG B1615  BOUND TO ASN B  45           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B1616  THROUGH BMA B1618  BOUND TO ASN B 416           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-DOMAIN WITH MUTATIONS N9Q, N25Q, N82Q, N117Q, N131Q,               
REMARK 999 N289Q, Q545R, P576L, R629L (SIMILAR CONSTRUCT TO PDB 3NXQ)           
DBREF  4BXK A    1   628  UNP    P12821   ACE_HUMAN       30    657             
DBREF  4BXK B    1   628  UNP    P12821   ACE_HUMAN       30    657             
SEQADV 4BXK LEU A  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4BXK GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 4BXK GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 4BXK GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 4BXK GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 4BXK GLN A  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 4BXK GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 4BXK ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4BXK LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 4BXK LEU B  629  UNP  P12821              EXPRESSION TAG                 
SEQADV 4BXK GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 4BXK GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 4BXK GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 4BXK GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 4BXK GLN B  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 4BXK GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 4BXK ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 4BXK LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQRES   1 A  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 A  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 A  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 A  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 A  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 A  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 A  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 A  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 A  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 A  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 A  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 A  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 A  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 A  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 A  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 A  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 A  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 A  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 A  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 A  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 A  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 A  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 A  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 A  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 A  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 A  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 A  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 A  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 A  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 A  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 A  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 A  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 A  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 A  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 A  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 A  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 A  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 A  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 A  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 A  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 A  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 A  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 A  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 A  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 A  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 A  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 A  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 A  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 A  629  GLU GLU TYR ASP LEU                                          
SEQRES   1 B  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA ASP          
SEQRES   2 B  629  GLU ALA GLY ALA GLN LEU PHE ALA GLN SER TYR GLN SER          
SEQRES   3 B  629  SER ALA GLU GLN VAL LEU PHE GLN SER VAL ALA ALA SER          
SEQRES   4 B  629  TRP ALA HIS ASP THR ASN ILE THR ALA GLU ASN ALA ARG          
SEQRES   5 B  629  ARG GLN GLU GLU ALA ALA LEU LEU SER GLN GLU PHE ALA          
SEQRES   6 B  629  GLU ALA TRP GLY GLN LYS ALA LYS GLU LEU TYR GLU PRO          
SEQRES   7 B  629  ILE TRP GLN GLN PHE THR ASP PRO GLN LEU ARG ARG ILE          
SEQRES   8 B  629  ILE GLY ALA VAL ARG THR LEU GLY SER ALA ASN LEU PRO          
SEQRES   9 B  629  LEU ALA LYS ARG GLN GLN TYR ASN ALA LEU LEU SER GLN          
SEQRES  10 B  629  MET SER ARG ILE TYR SER THR ALA LYS VAL CYS LEU PRO          
SEQRES  11 B  629  GLN LYS THR ALA THR CYS TRP SER LEU ASP PRO ASP LEU          
SEQRES  12 B  629  THR ASN ILE LEU ALA SER SER ARG SER TYR ALA MET LEU          
SEQRES  13 B  629  LEU PHE ALA TRP GLU GLY TRP HIS ASN ALA ALA GLY ILE          
SEQRES  14 B  629  PRO LEU LYS PRO LEU TYR GLU ASP PHE THR ALA LEU SER          
SEQRES  15 B  629  ASN GLU ALA TYR LYS GLN ASP GLY PHE THR ASP THR GLY          
SEQRES  16 B  629  ALA TYR TRP ARG SER TRP TYR ASN SER PRO THR PHE GLU          
SEQRES  17 B  629  ASP ASP LEU GLU HIS LEU TYR GLN GLN LEU GLU PRO LEU          
SEQRES  18 B  629  TYR LEU ASN LEU HIS ALA PHE VAL ARG ARG ALA LEU HIS          
SEQRES  19 B  629  ARG ARG TYR GLY ASP ARG TYR ILE ASN LEU ARG GLY PRO          
SEQRES  20 B  629  ILE PRO ALA HIS LEU LEU GLY ASP MET TRP ALA GLN SER          
SEQRES  21 B  629  TRP GLU ASN ILE TYR ASP MET VAL VAL PRO PHE PRO ASP          
SEQRES  22 B  629  LYS PRO ASN LEU ASP VAL THR SER THR MET LEU GLN GLN          
SEQRES  23 B  629  GLY TRP GLN ALA THR HIS MET PHE ARG VAL ALA GLU GLU          
SEQRES  24 B  629  PHE PHE THR SER LEU GLU LEU SER PRO MET PRO PRO GLU          
SEQRES  25 B  629  PHE TRP GLU GLY SER MET LEU GLU LYS PRO ALA ASP GLY          
SEQRES  26 B  629  ARG GLU VAL VAL CYS HIS ALA SER ALA TRP ASP PHE TYR          
SEQRES  27 B  629  ASN ARG LYS ASP PHE ARG ILE LYS GLN CYS THR ARG VAL          
SEQRES  28 B  629  THR MET ASP GLN LEU SER THR VAL HIS HIS GLU MET GLY          
SEQRES  29 B  629  HIS ILE GLN TYR TYR LEU GLN TYR LYS ASP LEU PRO VAL          
SEQRES  30 B  629  SER LEU ARG ARG GLY ALA ASN PRO GLY PHE HIS GLU ALA          
SEQRES  31 B  629  ILE GLY ASP VAL LEU ALA LEU SER VAL SER THR PRO GLU          
SEQRES  32 B  629  HIS LEU HIS LYS ILE GLY LEU LEU ASP ARG VAL THR ASN          
SEQRES  33 B  629  ASP THR GLU SER ASP ILE ASN TYR LEU LEU LYS MET ALA          
SEQRES  34 B  629  LEU GLU LYS ILE ALA PHE LEU PRO PHE GLY TYR LEU VAL          
SEQRES  35 B  629  ASP GLN TRP ARG TRP GLY VAL PHE SER GLY ARG THR PRO          
SEQRES  36 B  629  PRO SER ARG TYR ASN PHE ASP TRP TRP TYR LEU ARG THR          
SEQRES  37 B  629  LYS TYR GLN GLY ILE CYS PRO PRO VAL THR ARG ASN GLU          
SEQRES  38 B  629  THR HIS PHE ASP ALA GLY ALA LYS PHE HIS VAL PRO ASN          
SEQRES  39 B  629  VAL THR PRO TYR ILE ARG TYR PHE VAL SER PHE VAL LEU          
SEQRES  40 B  629  GLN PHE GLN PHE HIS GLU ALA LEU CYS LYS GLU ALA GLY          
SEQRES  41 B  629  TYR GLU GLY PRO LEU HIS GLN CYS ASP ILE TYR ARG SER          
SEQRES  42 B  629  THR LYS ALA GLY ALA LYS LEU ARG LYS VAL LEU ARG ALA          
SEQRES  43 B  629  GLY SER SER ARG PRO TRP GLN GLU VAL LEU LYS ASP MET          
SEQRES  44 B  629  VAL GLY LEU ASP ALA LEU ASP ALA GLN PRO LEU LEU LYS          
SEQRES  45 B  629  TYR PHE GLN LEU VAL THR GLN TRP LEU GLN GLU GLN ASN          
SEQRES  46 B  629  GLN GLN ASN GLY GLU VAL LEU GLY TRP PRO GLU TYR GLN          
SEQRES  47 B  629  TRP HIS PRO PRO LEU PRO ASP ASN TYR PRO GLU GLY ILE          
SEQRES  48 B  629  ASP LEU VAL THR ASP GLU ALA GLU ALA SER LYS PHE VAL          
SEQRES  49 B  629  GLU GLU TYR ASP LEU                                          
HET    PEG  A 701       7                                                       
HET    PEG  A 702       7                                                       
HET    PEG  A 703       7                                                       
HET    P6G  A 704      13                                                       
HET    1IU  A1001      33                                                       
HET    NAG  A1612      14                                                       
HET    FUC  A1613      10                                                       
HET    NAG  A1614      14                                                       
HET    NAG  A1615      14                                                       
HET    NAG  A1616      14                                                       
HET    NAG  A1617      14                                                       
HET    BMA  A1618      11                                                       
HET    FUC  A1619      10                                                       
HET     ZN  A1620       1                                                       
HET     CL  A1621       1                                                       
HET    PEG  B 701       7                                                       
HET    PG4  B 704      10                                                       
HET    P6G  B 709      19                                                       
HET    PEG  B 711       7                                                       
HET    1IU  B1001      33                                                       
HET    NAG  B1612      14                                                       
HET    NAG  B1614      14                                                       
HET    NAG  B1615      14                                                       
HET    NAG  B1616      14                                                       
HET    NAG  B1617      14                                                       
HET    BMA  B1618      11                                                       
HET     ZN  B1619       1                                                       
HET     CL  B1620       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     1IU [3-[[(2S)-1-AZANYL-1-OXIDANYLIDENE-PROPAN-2-                     
HETNAM   2 1IU  YL]AMINO]-2-METHYL-3-OXIDANYLIDENE-PROPYL]-                     
HETNAM   3 1IU  [(1R)-1-[[(2R)-2-AZANYL-3-(1H-1,2,3,4-TETRAZOL-                 
HETNAM   4 1IU  5-YL)PROPANOYL]AMINO]-2-PHENYL-ETHYL]                           
HETNAM   5 1IU  PHOSPHINIC ACID                                                 
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BMA BETA-D-MANNOSE                                                   
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   2   ZN    2(ZN 2+)                                                     
FORMUL   3  1IU    2(C19 H29 N8 O5 P)                                           
FORMUL   4  NAG    10(C8 H15 N O6)                                              
FORMUL   5  PEG    5(C4 H10 O3)                                                 
FORMUL   6  PG4    C8 H18 O5                                                    
FORMUL   7  P6G    2(C12 H26 O7)                                                
FORMUL   8  FUC    2(C6 H12 O5)                                                 
FORMUL   9   CL    2(CL 1-)                                                     
FORMUL  10  BMA    2(C6 H12 O6)                                                 
FORMUL  11  HOH   *409(H2 O)                                                    
HELIX    1   1 ASP A    2  GLN A    6  5                                   5    
HELIX    2   2 ASP A   13  THR A   44  1                                  32    
HELIX    3   3 THR A   47  GLU A   77  1                                  31    
HELIX    4   4 ILE A   79  PHE A   83  5                                   5    
HELIX    5   5 ASP A   85  ARG A   96  1                                  12    
HELIX    6   6 LEU A   98  LEU A  103  5                                   6    
HELIX    7   7 PRO A  104  ALA A  125  1                                  22    
HELIX    8   8 PRO A  141  SER A  150  1                                  10    
HELIX    9   9 SER A  152  GLN A  188  1                                  37    
HELIX   10  10 ASP A  193  SER A  200  1                                   8    
HELIX   11  11 TRP A  201  ASN A  203  5                                   3    
HELIX   12  12 THR A  206  GLY A  238  1                                  33    
HELIX   13  13 TRP A  261  ASN A  263  5                                   3    
HELIX   14  14 ILE A  264  VAL A  269  1                                   6    
HELIX   15  15 VAL A  279  GLY A  287  1                                   9    
HELIX   16  16 GLN A  289  LEU A  304  1                                  16    
HELIX   17  17 PRO A  310  SER A  317  1                                   8    
HELIX   18  18 THR A  352  TYR A  372  1                                  21    
HELIX   19  19 PRO A  376  ARG A  380  5                                   5    
HELIX   20  20 ASN A  384  SER A  400  1                                  17    
HELIX   21  21 THR A  401  ILE A  408  1                                   8    
HELIX   22  22 ASP A  417  ILE A  433  1                                  17    
HELIX   23  23 ALA A  434  SER A  451  1                                  18    
HELIX   24  24 PRO A  455  SER A  457  5                                   3    
HELIX   25  25 ARG A  458  GLY A  472  1                                  15    
HELIX   26  26 PHE A  484  LYS A  489  5                                   6    
HELIX   27  27 TYR A  498  ALA A  519  1                                  22    
HELIX   28  28 PRO A  524  CYS A  528  5                                   5    
HELIX   29  29 SER A  533  GLY A  547  1                                  15    
HELIX   30  30 PRO A  551  GLY A  561  1                                  11    
HELIX   31  31 ALA A  567  ASN A  588  1                                  22    
HELIX   32  32 ASP B    2  GLN B    6  5                                   5    
HELIX   33  33 ASP B   13  THR B   44  1                                  32    
HELIX   34  34 THR B   47  GLU B   77  1                                  31    
HELIX   35  35 ILE B   79  PHE B   83  5                                   5    
HELIX   36  36 ASP B   85  THR B   97  1                                  13    
HELIX   37  37 LEU B   98  LEU B  103  5                                   6    
HELIX   38  38 PRO B  104  ALA B  125  1                                  22    
HELIX   39  39 PRO B  141  SER B  150  1                                  10    
HELIX   40  40 SER B  152  GLN B  188  1                                  37    
HELIX   41  41 ASP B  193  TRP B  201  1                                   9    
HELIX   42  42 THR B  206  GLY B  238  1                                  33    
HELIX   43  43 TRP B  261  ASN B  263  5                                   3    
HELIX   44  44 ILE B  264  VAL B  269  1                                   6    
HELIX   45  45 VAL B  279  GLY B  287  1                                   9    
HELIX   46  46 GLN B  289  LEU B  304  1                                  16    
HELIX   47  47 PRO B  310  SER B  317  1                                   8    
HELIX   48  48 THR B  352  LYS B  373  1                                  22    
HELIX   49  49 PRO B  376  ARG B  380  5                                   5    
HELIX   50  50 ASN B  384  ILE B  408  1                                  25    
HELIX   51  51 ASP B  417  ILE B  433  1                                  17    
HELIX   52  52 PHE B  435  SER B  451  1                                  17    
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  ALA B  546  1                                  14    
HELIX   59  59 PRO B  551  GLY B  561  1                                  11    
HELIX   60  60 ALA B  567  GLY B  589  1                                  23    
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  CYS B 128  0                                        
SHEET    2  BA 2 CYS B 136  SER B 138 -1  O  TRP B 137   N  VAL B 127           
SHEET    1  BB 2 ILE B 248  PRO B 249  0                                        
SHEET    2  BB 2 ILE B 473  CYS B 474  1  N  CYS B 474   O  ILE B 248           
SHEET    1  BC 2 SER B 333  ASP B 336  0                                        
SHEET    2  BC 2 PHE B 343  LYS B 346 -1  O  ARG B 344   N  TRP B 335           
SSBOND   1 CYS A  128    CYS A  136                          1555   1555  2.05  
SSBOND   2 CYS A  330    CYS A  348                          1555   1555  2.07  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.06  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.11  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.04  
LINK         ND2 ASN A  45                 C1  NAG A1614     1555   1555  1.44  
LINK         ND2 ASN A 416                 C1  NAG A1616     1555   1555  1.45  
LINK         ND2 ASN A 480                 C1  NAG A1612     1555   1555  1.45  
LINK         O6  NAG A1612                 C1  FUC A1613     1555   1555  1.44  
LINK         O4  NAG A1614                 C1  NAG A1615     1555   1555  1.44  
LINK         O4  NAG A1616                 C1  NAG A1617     1555   1555  1.44  
LINK         O6  NAG A1616                 C1  FUC A1619     1555   1555  1.44  
LINK         O4  NAG A1617                 C1  BMA A1618     1555   1555  1.45  
LINK        ZN    ZN A1620                 OAH 1IU A1001     1555   1555  1.99  
LINK        ZN    ZN A1620                 NE2 HIS A 361     1555   1555  2.14  
LINK        ZN    ZN A1620                 OE1 GLU A 389     1555   1555  2.03  
LINK        ZN    ZN A1620                 NE2 HIS A 365     1555   1555  2.08  
LINK        ZN    ZN A1620                 OAI 1IU A1001     1555   1555  2.51  
LINK         ND2 ASN B  45                 C1  NAG B1614     1555   1555  1.45  
LINK         ND2 ASN B 416                 C1  NAG B1616     1555   1555  1.45  
LINK         ND2 ASN B 480                 C1  NAG B1612     1555   1555  1.44  
LINK         O4  NAG B1614                 C1  NAG B1615     1555   1555  1.44  
LINK         O4  NAG B1616                 C1  NAG B1617     1555   1555  1.45  
LINK         O4  NAG B1617                 C1  BMA B1618     1555   1555  1.45  
LINK        ZN    ZN B1619                 NE2 HIS B 361     1555   1555  2.12  
LINK        ZN    ZN B1619                 OAH 1IU B1001     1555   1555  2.11  
LINK        ZN    ZN B1619                 OAI 1IU B1001     1555   1555  2.43  
LINK        ZN    ZN B1619                 OE1 GLU B 389     1555   1555  2.08  
LINK        ZN    ZN B1619                 NE2 HIS B 365     1555   1555  2.11  
CISPEP   1 ASP A  140    PRO A  141          0         8.48                     
CISPEP   2 TYR A  607    PRO A  608          0        -4.71                     
CISPEP   3 ASP B  140    PRO B  141          0        12.58                     
CISPEP   4 TYR B  607    PRO B  608          0         2.54                     
SITE     1 AC1  2 TRP A 335  1IU A1001                                          
SITE     1 AC2  1 ARG A 344                                                     
SITE     1 AC3  1 PHE A 191                                                     
SITE     1 AC4  4 PHE A 228  ARG A 231  ARG A 235  VAL A 268                    
SITE     1 AC5 21 GLN A 259  HIS A 331  ALA A 332  SER A 333                    
SITE     2 AC5 21 ALA A 334  HIS A 361  GLU A 362  HIS A 365                    
SITE     3 AC5 21 TYR A 369  HIS A 388  GLU A 389  LYS A 489                    
SITE     4 AC5 21 PHE A 490  HIS A 491  TYR A 498  TYR A 501                    
SITE     5 AC5 21 PEG A 701   ZN A1620  HOH A2168  HOH A2170                    
SITE     6 AC5 21 HOH A2206                                                     
SITE     1 AC6  4 HIS A 361  HIS A 365  GLU A 389  1IU A1001                    
SITE     1 AC7  4 TYR A 202  PRO A 497  ARG A 500  HOH A2087                    
SITE     1 AC8  2 TRP B 335  1IU B1001                                          
SITE     1 AC9  7 TYR A 465  HOH A2187  ARG B 453  TYR B 465                    
SITE     2 AC9  7 LEU B 466  HOH B2129  HOH B2164                               
SITE     1 BC1 10 GLN A 286  GLY A 287  TRP A 288  HIS A 292                    
SITE     2 BC1 10 GLN B 286  GLY B 287  TRP B 288  HIS B 292                    
SITE     3 BC1 10 ARG B 295  PEG B 711                                          
SITE     1 BC2  3 VAL B 296  ILE B 408  P6G B 709                               
SITE     1 BC3 23 GLN B 259  HIS B 331  ALA B 332  SER B 333                    
SITE     2 BC3 23 ALA B 334  HIS B 361  GLU B 362  HIS B 365                    
SITE     3 BC3 23 TYR B 369  HIS B 388  GLU B 389  LYS B 489                    
SITE     4 BC3 23 PHE B 490  HIS B 491  TYR B 498  TYR B 501                    
SITE     5 BC3 23 PEG B 701   ZN B1619  HOH B2110  HOH B2115                    
SITE     6 BC3 23 HOH B2117  HOH B2142  HOH B2165                               
SITE     1 BC4  6 ARG A 245  GLU A 596  ASN B 480  THR B 482                    
SITE     2 BC4  6 HIS B 483  HOH B2166                                          
SITE     1 BC5  4 HIS B 361  HIS B 365  GLU B 389  1IU B1001                    
SITE     1 BC6  3 TYR B 202  PRO B 497  ARG B 500                               
SITE     1 BC7  3 ASN A  45  THR A  47  ASN A  50                               
SITE     1 BC8  5 GLU A 403  ASN A 416  GLU A 522  PRO A 524                    
SITE     2 BC8  5 GLN A 527                                                     
SITE     1 BC9  4 ASN A 480  THR A 482  ARG B 245  GLU B 596                    
SITE     1 CC1  4 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     1 CC2  3 ASN B 416  PRO B 524  GLN B 527                               
CRYST1   73.142   77.255   82.866  88.43  64.28  75.29 P 1           2          
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      0.013672 -0.003589 -0.006958        0.00000                         
SCALE2      0.000000  0.013383  0.001277        0.00000                         
SCALE3      0.000000  0.000000  0.013456        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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