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Database: PDB
Entry: 5AMC
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HEADER    HYDROLASE                               10-MAR-15   5AMC              
TITLE     CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME N-           
TITLE    2 DOMAIN IN COMPLEX WITH AMYLOID-BETA FLUOROGENIC FRAGMENT 4-10        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N DOMAIN, UNP RESIDUES 30-658;                             
COMPND   5 EC: 3.4.15.1;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: MINIMALLY GLYCOSYLATED MUTANT;                        
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ANGIOTENSIN-CONVERTING ENZYME;                             
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: N DOMAIN, UNP RESIDUES 30-658;                             
COMPND  13 EC: 3.4.15.1;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES;                                                       
COMPND  16 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;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: CHO K1                                  
KEYWDS    HYDROLASE, ANGIOTENSIN-CONVERTING ENZYME, METALLOPROTEASE, AMYLOID-   
KEYWDS   2 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 5AMC    1       JRNL                                     
REVDAT   2   20-JAN-16 5AMC    1       JRNL                                     
REVDAT   1   13-JAN-16 5AMC    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.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.74                          
REMARK   3   NUMBER OF REFLECTIONS             : 163962                         
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) : 0.20934                         
REMARK   3   R VALUE            (WORKING SET) : 0.20772                         
REMARK   3   FREE R VALUE                     : 0.24169                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 8521                            
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) : 1.650                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.693                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7542                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 56.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.358                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 406                          
REMARK   3   BIN FREE R VALUE                    : 0.380                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 307                                     
REMARK   3   SOLVENT ATOMS            : 886                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.142                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.18                                                
REMARK   3    B22 (A**2) : 1.96                                                 
REMARK   3    B33 (A**2) : -0.43                                                
REMARK   3    B12 (A**2) : 1.49                                                 
REMARK   3    B13 (A**2) : 0.12                                                 
REMARK   3    B23 (A**2) : -1.05                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.109         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.107         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.542         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10550 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9581 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14364 ; 1.363 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 22046 ; 0.976 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1218 ; 5.843 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   532 ;35.181 ;23.797       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1606 ;13.005 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    66 ;15.416 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1505 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11858 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2604 ; 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):  4866 ; 1.593 ; 2.827       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4867 ; 1.593 ; 2.827       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6074 ; 2.414 ; 4.231       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5684 ; 1.877 ; 3.132       
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  : NULL                                       
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.                                                  
REMARK   3 ONLY DI-PEPTIDE GLY-NITROTYROSINE VISIBLE FOR AMYLOID-BETA           
REMARK   3 SYNTHETIC FRAGMENT (PRODUCT OF CLEAVAGE REACTION BY ACE)             
REMARK   4                                                                      
REMARK   4 5AMC 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-63279.                                       
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   : 172512                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.65                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.81                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY                : 3.0                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.40                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.71                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.30                               
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   (%): 57                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
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     LEU A 129    CG   CD1  CD2                                       
REMARK 470     THR B 133    OG1  CG2                                            
REMARK 470     ASN B 606    CG   OD1  ND2                                       
REMARK 470     GLU B 609    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA A    12     O    HOH A  2006              2.19            
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 B 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 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       76.66   -176.29                                   
REMARK 500    LYS A 341      -44.36   -132.95                                   
REMARK 500    ASN B  45       76.27   -178.46                                   
REMARK 500    ALA B 134      -92.66   -106.96                                   
REMARK 500    ALA B 250        0.03    -67.83                                   
REMARK 500    LYS B 341      -53.43   -130.03                                   
REMARK 500    ASP B 417     -156.27   -119.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2095        DISTANCE =  6.47 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG4 B 1611                                                       
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 365   NE2                                                    
REMARK 620 2 HOH A2339   O   146.6                                              
REMARK 620 3 HOH A2340   O    94.9  68.6                                        
REMARK 620 4 HIS A 361   NE2 102.4 108.9 100.7                                  
REMARK 620 5 GLU A 389   OE1  99.3  92.2 160.2  89.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 361   NE2                                                    
REMARK 620 2 HIS B 365   NE2 103.5                                              
REMARK 620 3 GLU B 389   OE1  90.2 100.2                                        
REMARK 620 4 HOH B2279   O   103.5  93.0 158.3                                  
REMARK 620 5 HOH B2280   O   108.2 146.3  90.8  69.2                            
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 A1611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B1611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
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: BC5                                                 
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: BC6                                                 
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: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR POLY-SACCHARIDE                   
REMARK 800  RESIDUES NAG B1615  THROUGH NAG B1616  BOUND TO ASN B  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 B1617  THROUGH BMA B1619  BOUND TO ASN B 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 B1613  THROUGH FUC B1614  BOUND TO ASN B 480           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-PEPTIDE                        
REMARK 800  GLY A 906  AND NIY A 907                                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR DI-PEPTIDE                        
REMARK 800  GLY B 906  AND NIY B 907                                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 5AM9   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
REMARK 900   N-DOMAIN IN COMPLEX WITH AMYLOID-BETA 10-16                        
REMARK 900 RELATED ID: 5AMA   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ANGIOTENSIN-1 CONVERTING ENZYME            
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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE TYROSINE IS A NITRO-TYROSINE                                     
DBREF  5AMC A    1   629  UNP    P12821   ACE_HUMAN       30    658             
DBREF  5AMC B    1   629  UNP    P12821   ACE_HUMAN       30    658             
SEQADV 5AMC GLN A    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AMC GLU A   13  UNP  P12821    ASP    42 CONFLICT                       
SEQADV 5AMC ASP A   14  UNP  P12821    GLU    43 CONFLICT                       
SEQADV 5AMC GLN A   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AMC GLN A   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AMC GLN A  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AMC GLN A  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AMC GLN A  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AMC ARG A  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AMC LEU A  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AMC LEU A  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQADV 5AMC GLN B    9  UNP  P12821    ASN    38 ENGINEERED MUTATION            
SEQADV 5AMC GLN B   25  UNP  P12821    ASN    54 ENGINEERED MUTATION            
SEQADV 5AMC GLN B   82  UNP  P12821    ASN   111 ENGINEERED MUTATION            
SEQADV 5AMC GLN B  117  UNP  P12821    ASN   146 ENGINEERED MUTATION            
SEQADV 5AMC GLN B  131  UNP  P12821    ASN   160 ENGINEERED MUTATION            
SEQADV 5AMC GLN B  289  UNP  P12821    ASN   318 ENGINEERED MUTATION            
SEQADV 5AMC ARG B  545  UNP  P12821    GLN   574 ENGINEERED MUTATION            
SEQADV 5AMC LEU B  576  UNP  P12821    PRO   605 ENGINEERED MUTATION            
SEQADV 5AMC LEU B  629  UNP  P12821    ARG   658 ENGINEERED MUTATION            
SEQRES   1 A  629  LEU ASP PRO GLY LEU GLN PRO GLY GLN PHE SER ALA GLU          
SEQRES   2 A  629  ASP 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    GLY  A 906       4                                                       
HET    NIY  A 907      16                                                       
HET    GLY  B 906       4                                                       
HET    NIY  B 907      16                                                       
HET     ZN  A1001       1                                                       
HET     CL  A1611       1                                                       
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    PEG  A1620       7                                                       
HET    PEG  A1621       7                                                       
HET    PEG  A1622       7                                                       
HET     ZN  B1001       1                                                       
HET    PG4  B1611      10                                                       
HET     CL  B1612       1                                                       
HET    NAG  B1613      14                                                       
HET    FUC  B1614      10                                                       
HET    NAG  B1615      14                                                       
HET    NAG  B1616      14                                                       
HET    NAG  B1617      14                                                       
HET    NAG  B1618      14                                                       
HET    BMA  B1619      11                                                       
HET    PEG  B1620       7                                                       
HET    P6G  B1621      19                                                       
HET    PEG  B1622       7                                                       
HET    PEG  B1623       7                                                       
HETNAM     GLY GLYCINE                                                          
HETNAM      ZN ZINC ION                                                         
HETNAM     NIY META-NITRO-TYROSINE                                              
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   5  GLY    2(C2 H5 N O2)                                                
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  NIY    2(C9 H10 N2 O5)                                              
FORMUL   5  NAG    10(C8 H15 N O6)                                              
FORMUL   6  PEG    6(C4 H10 O3)                                                 
FORMUL   7  PG4    C8 H18 O5                                                    
FORMUL   8  P6G    C12 H26 O7                                                   
FORMUL   9  FUC    3(C6 H12 O5)                                                 
FORMUL  10   CL    2(CL 1-)                                                     
FORMUL  11  BMA    2(C6 H12 O6)                                                 
FORMUL  12  HOH   *886(H2 O)                                                    
HELIX    1   1 ASP A    2  GLN A    6  5                                   5    
HELIX    2   2 GLU A   13  THR A   44  1                                  32    
HELIX    3   3 THR A   47  GLU A   77  1                                  31    
HELIX    4   4 ILE A   79  PHE A   83  5                                   5    
HELIX    5   5 ASP A   85  ARG A   96  1                                  12    
HELIX    6   6 LEU A   98  LEU A  103  5                                   6    
HELIX    7   7 PRO A  104  ALA A  125  1                                  22    
HELIX    8   8 PRO A  141  SER A  150  1                                  10    
HELIX    9   9 SER A  152  GLN A  188  1                                  37    
HELIX   10  10 ASP A  193  TRP A  201  1                                   9    
HELIX   11  11 THR A  206  GLY A  238  1                                  33    
HELIX   12  12 TRP A  261  ASN A  263  5                                   3    
HELIX   13  13 ILE A  264  VAL A  269  1                                   6    
HELIX   14  14 VAL A  279  GLN A  286  1                                   8    
HELIX   15  15 GLN A  289  LEU A  304  1                                  16    
HELIX   16  16 PRO A  310  SER A  317  1                                   8    
HELIX   17  17 THR A  352  LYS A  373  1                                  22    
HELIX   18  18 PRO A  376  ARG A  380  5                                   5    
HELIX   19  19 ASN A  384  SER A  400  1                                  17    
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 PHE A  435  SER A  451  1                                  17    
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  TYR B  372  1                                  21    
HELIX   48  48 PRO B  376  ARG B  380  5                                   5    
HELIX   49  49 ASN B  384  THR B  401  1                                  18    
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  SER B  451  1                                  18    
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    
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  2.05  
SSBOND   3 CYS A  516    CYS A  528                          1555   1555  2.04  
SSBOND   4 CYS B  128    CYS B  136                          1555   1555  2.05  
SSBOND   5 CYS B  330    CYS B  348                          1555   1555  2.05  
SSBOND   6 CYS B  516    CYS B  528                          1555   1555  2.03  
LINK         ND2 ASN A  45                 C1  NAG A1614     1555   1555  1.45  
LINK         ND2 ASN A 416                 C1  NAG A1616     1555   1555  1.44  
LINK         ND2 ASN A 480                 C1  NAG A1612     1555   1555  1.45  
LINK         C   GLY A 906                 N   NIY A 907     1555   1555  1.33  
LINK        ZN    ZN A1001                 O   HOH A2340     1555   1555  2.22  
LINK        ZN    ZN A1001                 NE2 HIS A 361     1555   1555  2.15  
LINK        ZN    ZN A1001                 OE1 GLU A 389     1555   1555  2.06  
LINK        ZN    ZN A1001                 NE2 HIS A 365     1555   1555  2.06  
LINK        ZN    ZN A1001                 O   HOH A2339     1555   1555  2.07  
LINK         O6  NAG A1612                 C1  FUC A1613     1555   1555  1.44  
LINK         O4  NAG A1614                 C1  NAG A1615     1555   1555  1.44  
LINK         O6  NAG A1616                 C1  FUC A1619     1555   1555  1.44  
LINK         O4  NAG A1616                 C1  NAG A1617     1555   1555  1.43  
LINK         O4  NAG A1617                 C1  BMA A1618     1555   1555  1.45  
LINK         ND2 ASN B  45                 C1  NAG B1615     1555   1555  1.44  
LINK         ND2 ASN B 416                 C1  NAG B1617     1555   1555  1.44  
LINK         ND2 ASN B 480                 C1  NAG B1613     1555   1555  1.44  
LINK         C   GLY B 906                 N   NIY B 907     1555   1555  1.32  
LINK        ZN    ZN B1001                 O   HOH B2280     1555   1555  2.13  
LINK        ZN    ZN B1001                 O   HOH B2279     1555   1555  1.92  
LINK        ZN    ZN B1001                 OE1 GLU B 389     1555   1555  1.88  
LINK        ZN    ZN B1001                 NE2 HIS B 365     1555   1555  2.12  
LINK        ZN    ZN B1001                 NE2 HIS B 361     1555   1555  2.13  
LINK         O6  NAG B1613                 C1  FUC B1614     1555   1555  1.45  
LINK         O4  NAG B1615                 C1  NAG B1616     1555   1555  1.44  
LINK         O4  NAG B1617                 C1  NAG B1618     1555   1555  1.45  
LINK         O4  NAG B1618                 C1  BMA B1619     1555   1555  1.45  
CISPEP   1 ASP A  140    PRO A  141          0        11.55                     
CISPEP   2 TYR A  607    PRO A  608          0         1.29                     
CISPEP   3 ASP B  140    PRO B  141          0        11.50                     
CISPEP   4 TYR B  607    PRO B  608          0         5.54                     
SITE     1 AC1  5 HIS A 361  HIS A 365  GLU A 389  HOH A2339                    
SITE     2 AC1  5 HOH A2340                                                     
SITE     1 AC2  5 TYR A 202  PRO A 385  PRO A 497  ARG A 500                    
SITE     2 AC2  5 HOH A2201                                                     
SITE     1 AC3  2 ARG A 381  HOH A2328                                          
SITE     1 AC4  3 ARG A  96  GLY A 190  PHE A 191                               
SITE     1 AC5  9 PHE A 228  ARG A 231  ARG A 235  MET A 267                    
SITE     2 AC5  9 VAL A 268  VAL A 269  ASN A 588  HOH A2248                    
SITE     3 AC5  9 HOH A2510                                                     
SITE     1 AC6  5 HIS B 361  HIS B 365  GLU B 389  HOH B2279                    
SITE     2 AC6  5 HOH B2280                                                     
SITE     1 AC7  8 ASP A 462  LEU A 466  HOH A2382  ARG B 453                    
SITE     2 AC7  8 TYR B 465  LEU B 466  HOH B2306  HOH B2373                    
SITE     1 AC8  4 TYR B 202  PRO B 497  ARG B 500  HOH B2152                    
SITE     1 AC9  1 VAL A 296                                                     
SITE     1 BC1  8 GLN A 286  GLY A 287  TRP A 288  HIS A 292                    
SITE     2 BC1  8 GLN B 286  GLY B 287  TRP B 288  HIS B 292                    
SITE     1 BC2  5 TYR B 369  HIS B 388  PEG B1623  HOH B2094                    
SITE     2 BC2  5 HOH B2255                                                     
SITE     1 BC3  3 ALA B 334  TRP B 335  PEG B1622                               
SITE     1 BC4  5 ASN A  45  THR A  47  GLU A  49  ASN A  50                    
SITE     2 BC4  5 ARG A  53                                                     
SITE     1 BC5  6 PHE A  10  GLU A 403  ASN A 416  PRO A 524                    
SITE     2 BC5  6 GLN A 527  HOH A2437                                          
SITE     1 BC6  6 THR A 478  ASN A 480  THR A 482  HOH A2416                    
SITE     2 BC6  6 ARG B 245  GLU B 596                                          
SITE     1 BC7  5 ASN B  45  THR B  47  GLU B  49  ASN B  50                    
SITE     2 BC7  5 ARG B 326                                                     
SITE     1 BC8  5 ASN B 416  GLU B 522  PRO B 524  GLN B 527                    
SITE     2 BC8  5 HOH B2335                                                     
SITE     1 BC9  6 ARG A 245  GLU A 596  THR B 478  ASN B 480                    
SITE     2 BC9  6 THR B 482  HOH B2374                                          
SITE     1 CC1 16 GLN A 259  SER A 260  HIS A 331  ALA A 332                    
SITE     2 CC1 16 GLU A 362  LYS A 489  HIS A 491  TYR A 498                    
SITE     3 CC1 16 TYR A 501  HOH A2262  HOH A2263  HOH A2334                    
SITE     4 CC1 16 HOH A2339  HOH A2340  HOH A2352  HOH A2379                    
SITE     1 CC2 18 GLN B 259  SER B 260  HIS B 331  ALA B 332                    
SITE     2 CC2 18 ASP B 354  HIS B 361  GLU B 362  LYS B 489                    
SITE     3 CC2 18 HIS B 491  TYR B 498  TYR B 501  HOH B2193                    
SITE     4 CC2 18 HOH B2197  HOH B2198  HOH B2199  HOH B2271                    
SITE     5 CC2 18 HOH B2274  HOH B2301                                          
CRYST1   73.029   76.470   83.158  88.78  64.25  75.64 P 1           1          
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      0.013693 -0.003506 -0.006987        0.00000                         
SCALE2      0.000000  0.013499  0.001344        0.00000                         
SCALE3      0.000000  0.000000  0.013417        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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