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Database: PDB
Entry: 1R1J
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Original site: 1R1J 
HEADER    HYDROLASE                               24-SEP-03   1R1J              
TITLE     STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND POTENT    
TITLE    2 INHIBITORS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEPRILYSIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, (RESIDUE 54-749);                    
COMPND   5 SYNONYM: NEUTRAL ENDOPEPTIDASE, NEP, ENKEPHALINASE, COMMON ACUTE     
COMPND   6 LYMPHOCYTIC LEUKEMIA ANTIGEN, CALLA, NEUTRAL ENDOPEPTIDASE 24.11,    
COMPND   7 CD10;                                                                
COMPND   8 EC: 3.4.24.11;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MME, EPN;                                                      
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZ-ALPHA                               
KEYWDS    ENKEPHALINASE, GLYCOPROTEIN, METALLOPROTEASE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.OEFNER,B.P.ROQUES,M.C.FOURNIE-ZALUSKI,G.E.DALE                      
REVDAT   4   29-JUL-20 1R1J    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-JUL-11 1R1J    1       VERSN                                    
REVDAT   2   24-FEB-09 1R1J    1       VERSN                                    
REVDAT   1   28-SEP-04 1R1J    0                                                
JRNL        AUTH   C.OEFNER,B.P.ROQUES,M.C.FOURNIE-ZALUSKI,G.E.DALE             
JRNL        TITL   STRUCTURAL ANALYSIS OF NEPRILYSIN WITH VARIOUS SPECIFIC AND  
JRNL        TITL 2 POTENT INHIBITORS.                                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  60   392 2004              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   14747736                                                     
JRNL        DOI    10.1107/S0907444903027410                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 29871                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1585                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4258                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 210                          
REMARK   3   BIN FREE R VALUE                    : 0.3530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5595                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.64000                                             
REMARK   3    B22 (A**2) : -0.64000                                             
REMARK   3    B33 (A**2) : 0.96000                                              
REMARK   3    B12 (A**2) : -0.32000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.486         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.297         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.319         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.121        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.881                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5793 ; 0.005 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5064 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7841 ; 0.718 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11824 ; 0.514 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   695 ; 8.783 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1037 ;23.360 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   842 ; 0.039 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6446 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1163 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1620 ; 0.286 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5530 ; 0.265 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     3 ; 0.735 ; 0.500       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   241 ; 0.198 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     5 ; 0.095 ; 0.500       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.125 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    30 ; 0.621 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    47 ; 0.313 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.762 ; 0.500       
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):  3461 ; 2.076 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5572 ; 3.214 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2332 ; 2.150 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2269 ; 3.377 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1R1J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020324.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC                              
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31584                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.66467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.33233            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.33233            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.66467            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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 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   NZ   LYS A   502     OE2  GLU A   505              1.52            
REMARK 500   OE1  GLU A   505     CD   GLU A   508              1.59            
REMARK 500   O    ASP A   128     NE2  GLN A   133              1.68            
REMARK 500   OE1  GLU A   505     CG   GLU A   508              1.69            
REMARK 500   OD1  ASN A    94     O    HOH A  2076              1.82            
REMARK 500   OE1  GLU A   505     OE1  GLU A   508              1.83            
REMARK 500   OD1  ASP A    73     OG1  THR A    75              2.02            
REMARK 500   O    GLY A   588     O    GLY A   593              2.09            
REMARK 500   OE1  GLU A   527     O    HOH A  2039              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE1  GLN A   175     C    ARG A   260     6555     1.46            
REMARK 500   OE1  GLN A   175     O    ARG A   260     6555     1.48            
REMARK 500   OE1  GLN A   175     N    LEU A   261     6555     2.01            
REMARK 500   CG   GLU A   171     OE2  GLU A   171     6555     2.16            
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    ASP A 604   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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    ASP A  81       86.89   -160.49                                   
REMARK 500    TRP A 181      133.99    -31.70                                   
REMARK 500    LEU A 199      -58.43     78.50                                   
REMARK 500    ASN A 316       23.00     47.27                                   
REMARK 500    LYS A 318      -95.79    -59.83                                   
REMARK 500    SER A 331        6.07    -67.82                                   
REMARK 500    LEU A 382     -162.72   -107.27                                   
REMARK 500    GLU A 505       51.26   -140.49                                   
REMARK 500    ALA A 539       44.53    -95.18                                   
REMARK 500    LEU A 602       90.78    -64.39                                   
REMARK 500    LYS A 736      139.03    -32.98                                   
REMARK 500    ASN A 737       15.28     51.78                                   
REMARK 500    VAL A 748      -72.41   -116.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TRP A  181     THR A  182                  146.21                    
REMARK 500 ALA A  429     ALA A  430                 -144.19                    
REMARK 500 PHE A  431     ALA A  432                 -149.12                    
REMARK 500 PHE A  564     SER A  565                  148.71                    
REMARK 500 ASN A  737     SER A  738                  137.52                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 583   NE2                                                    
REMARK 620 2 HIS A 587   NE2  94.9                                              
REMARK 620 3 GLU A 646   OE1  88.5 100.7                                        
REMARK 620 4 GLU A 646   OE2 140.6  88.2  52.4                                  
REMARK 620 5 OIR A2001   O19  85.0 176.0  75.3  89.4                            
REMARK 620 6 OIR A2001   S26 124.3  83.6 146.6  95.1  99.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DMT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1R1H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1R1I   RELATED DB: PDB                                   
DBREF  1R1J A   54   749  UNP    P08473   NEP_HUMAN       54    749             
SEQRES   1 A  696  GLY ILE CYS LYS SER SER ASP CYS ILE LYS SER ALA ALA          
SEQRES   2 A  696  ARG LEU ILE GLN ASN MET ASP ALA THR THR GLU PRO CYS          
SEQRES   3 A  696  THR ASP PHE PHE LYS TYR ALA CYS GLY GLY TRP LEU LYS          
SEQRES   4 A  696  ARG ASN VAL ILE PRO GLU THR SER SER ARG TYR GLY ASN          
SEQRES   5 A  696  PHE ASP ILE LEU ARG ASP GLU LEU GLU VAL VAL LEU LYS          
SEQRES   6 A  696  ASP VAL LEU GLN GLU PRO LYS THR GLU ASP ILE VAL ALA          
SEQRES   7 A  696  VAL GLN LYS ALA LYS ALA LEU TYR ARG SER CYS ILE ASN          
SEQRES   8 A  696  GLU SER ALA ILE ASP SER ARG GLY GLY GLU PRO LEU LEU          
SEQRES   9 A  696  LYS LEU LEU PRO ASP ILE TYR GLY TRP PRO VAL ALA THR          
SEQRES  10 A  696  GLU ASN TRP GLU GLN LYS TYR GLY ALA SER TRP THR ALA          
SEQRES  11 A  696  GLU LYS ALA ILE ALA GLN LEU ASN SER LYS TYR GLY LYS          
SEQRES  12 A  696  LYS VAL LEU ILE ASN LEU PHE VAL GLY THR ASP ASP LYS          
SEQRES  13 A  696  ASN SER VAL ASN HIS VAL ILE HIS ILE ASP GLN PRO ARG          
SEQRES  14 A  696  LEU GLY LEU PRO SER ARG ASP TYR TYR GLU CYS THR GLY          
SEQRES  15 A  696  ILE TYR LYS GLU ALA CYS THR ALA TYR VAL ASP PHE MET          
SEQRES  16 A  696  ILE SER VAL ALA ARG LEU ILE ARG GLN GLU GLU ARG LEU          
SEQRES  17 A  696  PRO ILE ASP GLU ASN GLN LEU ALA LEU GLU MET ASN LYS          
SEQRES  18 A  696  VAL MET GLU LEU GLU LYS GLU ILE ALA ASN ALA THR ALA          
SEQRES  19 A  696  LYS PRO GLU ASP ARG ASN ASP PRO MET LEU LEU TYR ASN          
SEQRES  20 A  696  LYS MET THR LEU ALA GLN ILE GLN ASN ASN PHE SER LEU          
SEQRES  21 A  696  GLU ILE ASN GLY LYS PRO PHE SER TRP LEU ASN PHE THR          
SEQRES  22 A  696  ASN GLU ILE MET SER THR VAL ASN ILE SER ILE THR ASN          
SEQRES  23 A  696  GLU GLU ASP VAL VAL VAL TYR ALA PRO GLU TYR LEU THR          
SEQRES  24 A  696  LYS LEU LYS PRO ILE LEU THR LYS TYR SER ALA ARG ASP          
SEQRES  25 A  696  LEU GLN ASN LEU MET SER TRP ARG PHE ILE MET ASP LEU          
SEQRES  26 A  696  VAL SER SER LEU SER ARG THR TYR LYS GLU SER ARG ASN          
SEQRES  27 A  696  ALA PHE ARG LYS ALA LEU TYR GLY THR THR SER GLU THR          
SEQRES  28 A  696  ALA THR TRP ARG ARG CYS ALA ASN TYR VAL ASN GLY ASN          
SEQRES  29 A  696  MET GLU ASN ALA VAL GLY ARG LEU TYR VAL GLU ALA ALA          
SEQRES  30 A  696  PHE ALA GLY GLU SER LYS HIS VAL VAL GLU ASP LEU ILE          
SEQRES  31 A  696  ALA GLN ILE ARG GLU VAL PHE ILE GLN THR LEU ASP ASP          
SEQRES  32 A  696  LEU THR TRP MET ASP ALA GLU THR LYS LYS ARG ALA GLU          
SEQRES  33 A  696  GLU LYS ALA LEU ALA ILE LYS GLU ARG ILE GLY TYR PRO          
SEQRES  34 A  696  ASP ASP ILE VAL SER ASN ASP ASN LYS LEU ASN ASN GLU          
SEQRES  35 A  696  TYR LEU GLU LEU ASN TYR LYS GLU ASP GLU TYR PHE GLU          
SEQRES  36 A  696  ASN ILE ILE GLN ASN LEU LYS PHE SER GLN SER LYS GLN          
SEQRES  37 A  696  LEU LYS LYS LEU ARG GLU LYS VAL ASP LYS ASP GLU TRP          
SEQRES  38 A  696  ILE SER GLY ALA ALA VAL VAL ASN ALA PHE TYR SER SER          
SEQRES  39 A  696  GLY ARG ASN GLN ILE VAL PHE PRO ALA GLY ILE LEU GLN          
SEQRES  40 A  696  PRO PRO PHE PHE SER ALA GLN GLN SER ASN SER LEU ASN          
SEQRES  41 A  696  TYR GLY GLY ILE GLY MET VAL ILE GLY HIS GLU ILE THR          
SEQRES  42 A  696  HIS GLY PHE ASP ASP ASN GLY ARG ASN PHE ASN LYS ASP          
SEQRES  43 A  696  GLY ASP LEU VAL ASP TRP TRP THR GLN GLN SER ALA SER          
SEQRES  44 A  696  ASN PHE LYS GLU GLN SER GLN CYS MET VAL TYR GLN TYR          
SEQRES  45 A  696  GLY ASN PHE SER TRP ASP LEU ALA GLY GLY GLN HIS LEU          
SEQRES  46 A  696  ASN GLY ILE ASN THR LEU GLY GLU ASN ILE ALA ASP ASN          
SEQRES  47 A  696  GLY GLY LEU GLY GLN ALA TYR ARG ALA TYR GLN ASN TYR          
SEQRES  48 A  696  ILE LYS LYS ASN GLY GLU GLU LYS LEU LEU PRO GLY LEU          
SEQRES  49 A  696  ASP LEU ASN HIS LYS GLN LEU PHE PHE LEU ASN PHE ALA          
SEQRES  50 A  696  GLN VAL TRP CYS GLY THR TYR ARG PRO GLU TYR ALA VAL          
SEQRES  51 A  696  ASN SER ILE LYS THR ASP VAL HIS SER PRO GLY ASN PHE          
SEQRES  52 A  696  ARG ILE ILE GLY THR LEU GLN ASN SER ALA GLU PHE SER          
SEQRES  53 A  696  GLU ALA PHE HIS CYS ARG LYS ASN SER TYR MET ASN PRO          
SEQRES  54 A  696  GLU LYS LYS CYS ARG VAL TRP                                  
MODRES 1R1J ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 1R1J ASN A  324  ASN  GLYCOSYLATION SITE                                 
MODRES 1R1J ASN A  627  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 752      14                                                       
HET    NAG  A 753      14                                                       
HET    NAG  A 754      14                                                       
HET     ZN  A1001       1                                                       
HET    OIR  A2001      28                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      ZN ZINC ION                                                         
HETNAM     OIR N-(3-PHENYL-2-SULFANYLPROPANOYL)PHENYLALANYLALANINE              
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  OIR    C21 H24 N2 O4 S                                              
FORMUL   7  HOH   *88(H2 O)                                                     
HELIX    1   1 SER A   58  MET A   72  1                                  15    
HELIX    2   2 ASP A   81  ASN A   94  1                                  14    
HELIX    3   3 ASN A  105  GLN A  122  1                                  18    
HELIX    4   4 ILE A  129  ASN A  144  1                                  16    
HELIX    5   5 ASN A  144  ARG A  151  1                                   8    
HELIX    6   6 GLY A  153  LYS A  158  1                                   6    
HELIX    7   7 LEU A  159  TYR A  164  5                                   6    
HELIX    8   8 TRP A  166  THR A  170  5                                   5    
HELIX    9   9 ASN A  172  TYR A  177  1                                   6    
HELIX   10  10 THR A  182  GLY A  195  1                                  14    
HELIX   11  11 SER A  227  CYS A  233  5                                   7    
HELIX   12  12 THR A  234  ILE A  236  5                                   3    
HELIX   13  13 TYR A  237  GLU A  259  1                                  23    
HELIX   14  14 ASP A  264  THR A  286  1                                  23    
HELIX   15  15 LYS A  288  ASN A  293  5                                   6    
HELIX   16  16 ASP A  294  TYR A  299  1                                   6    
HELIX   17  17 LEU A  304  PHE A  311  1                                   8    
HELIX   18  18 SER A  321  SER A  331  1                                  11    
HELIX   19  19 ALA A  347  THR A  359  1                                  13    
HELIX   20  20 SER A  362  VAL A  379  1                                  18    
HELIX   21  21 SER A  380  LEU A  382  5                                   3    
HELIX   22  22 SER A  383  SER A  389  1                                   7    
HELIX   23  23 ARG A  390  GLY A  399  1                                  10    
HELIX   24  24 ALA A  405  MET A  418  1                                  14    
HELIX   25  25 MET A  418  PHE A  431  1                                  14    
HELIX   26  26 GLU A  434  LEU A  454  1                                  21    
HELIX   27  27 ASP A  455  LEU A  457  5                                   3    
HELIX   28  28 ASP A  461  ILE A  475  1                                  15    
HELIX   29  29 ASP A  483  ASN A  488  1                                   6    
HELIX   30  30 ASN A  488  TYR A  496  1                                   9    
HELIX   31  31 GLU A  505  LYS A  523  1                                  19    
HELIX   32  32 GLY A  557  LEU A  559  5                                   3    
HELIX   33  33 SER A  569  GLY A  576  1                                   8    
HELIX   34  34 GLY A  576  HIS A  587  1                                  12    
HELIX   35  35 GLY A  588  ASP A  590  5                                   3    
HELIX   36  36 THR A  607  ASN A  627  1                                  21    
HELIX   37  37 TRP A  630  GLY A  634  5                                   5    
HELIX   38  38 THR A  643  GLY A  669  1                                  27    
HELIX   39  39 ASN A  680  VAL A  692  1                                  13    
HELIX   40  40 ARG A  698  ASP A  709  1                                  12    
HELIX   41  41 PRO A  713  ASN A  724  1                                  12    
HELIX   42  42 SER A  725  PHE A  732  1                                   8    
SHEET    1   A 2 ARG A 102  GLY A 104  0                                        
SHEET    2   A 2 GLY A 695  TYR A 697 -1  O  THR A 696   N  TYR A 103           
SHEET    1   B 4 ASN A 201  ASP A 207  0                                        
SHEET    2   B 4 ASN A 210  ASP A 219 -1  O  ASP A 219   N  ASN A 201           
SHEET    3   B 4 ASP A 342  VAL A 345  1  O  VAL A 344   N  ILE A 216           
SHEET    4   B 4 ASN A 300  THR A 303 -1  N  MET A 302   O  VAL A 343           
SHEET    1   C 3 LYS A 476  GLY A 480  0                                        
SHEET    2   C 3 GLN A 551  PRO A 555  1  O  PHE A 554   N  GLY A 480           
SHEET    3   C 3 PHE A 544  SER A 546 -1  N  SER A 546   O  GLN A 551           
SSBOND   1 CYS A   56    CYS A   61                          1555   1555  2.04  
SSBOND   2 CYS A   79    CYS A  734                          1555   1555  2.03  
SSBOND   3 CYS A   87    CYS A  694                          1555   1555  2.03  
SSBOND   4 CYS A  142    CYS A  410                          1555   1555  2.02  
SSBOND   5 CYS A  233    CYS A  241                          1555   1555  2.03  
SSBOND   6 CYS A  620    CYS A  746                          1555   1555  2.04  
LINK         ND2 ASN A 144                 C1  NAG A 752     1555   1555  1.44  
LINK         ND2 ASN A 324                 C1  NAG A 753     1555   1555  1.44  
LINK         ND2 ASN A 627                 C1  NAG A 754     1555   1555  1.44  
LINK         NE2 HIS A 583                ZN    ZN A1001     1555   1555  1.97  
LINK         NE2 HIS A 587                ZN    ZN A1001     1555   1555  2.04  
LINK         OE1 GLU A 646                ZN    ZN A1001     1555   1555  2.01  
LINK         OE2 GLU A 646                ZN    ZN A1001     1555   1555  2.71  
LINK        ZN    ZN A1001                 O19 OIR A2001     1555   1555  1.79  
LINK        ZN    ZN A1001                 S26 OIR A2001     1555   1555  2.39  
CISPEP   1 LYS A  318    PRO A  319          0        -3.29                     
CISPEP   2 PRO A  561    PRO A  562          0        11.29                     
CRYST1  107.458  107.458  111.997  90.00  90.00 120.00 P 32 2 1      6          
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      0.009306  0.005373  0.000000        0.00000                         
SCALE2      0.000000  0.010746  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008929        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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