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Database: PDB
Entry: 4CTH
LinkDB: 4CTH
Original site: 4CTH 
HEADER    TRANSFERASE                             13-MAR-14   4CTH              
TITLE     NEPRILYSIN VARIANT G399V,G714K IN COMPLEX WITH PHOSPHORAMIDON         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEPRILYSIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 52-750;                     
COMPND   5 SYNONYM: ATRIOPEPTIDASE, COMMON ACUTE LYMPHOCYTIC LEUKEMIA ANTIGEN,  
COMPND   6 CALLA, ENKEPHALINASE, NEUTRAL ENDOPEPTIDASE 24.11, NEP, NEUTRAL      
COMPND   7 ENDOPEPTIDASE, SKIN FIBROBLAST ELASTASE, SFE, CD10;                  
COMPND   8 EC: 3.4.24.11;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    TRANSFERASE, AMYLOID BETA, ALZHEIMER'S DISEASE, ENZYME ENGINEERING    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.I.WEBSTER,M.BURRELL,L.OLSSON,S.B.FOWLER,S.DIGBY,A.SANDERCOCK,       
AUTHOR   2 A.SNIJDER,J.TEBBE,U.HAUPTS,J.GRUDZINSKA,L.JERMUTUS,C.ANDERSSON       
REVDAT   4   29-JUL-20 4CTH    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   08-MAY-19 4CTH    1       REMARK LINK                              
REVDAT   2   20-JUN-18 4CTH    1       REMARK                                   
REVDAT   1   13-AUG-14 4CTH    0                                                
JRNL        AUTH   C.I.WEBSTER,M.BURRELL,L.OLSSON,S.B.FOWLER,S.DIGBY,           
JRNL        AUTH 2 A.SANDERCOCK,A.SNIJDER,J.TEBBE,U.HAUPTS,J.GRUDZINSKA,        
JRNL        AUTH 3 L.JERMUTUS,C.ANDERSSON                                       
JRNL        TITL   ENGINEERING NEPRILYSIN ACTIVITY AND SPECIFICITY TO CREATE A  
JRNL        TITL 2 NOVEL THERAPEUTIC FOR ALZHEIMER'S DISEASE.                   
JRNL        REF    PLOS ONE                      V.   9 04001 2014              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   25089527                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0104001                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.1                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 42359                          
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)  : 0.212                          
REMARK   3   R VALUE            (WORKING SET)  : 0.210                          
REMARK   3   FREE R VALUE                      : 0.261                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2138                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.15                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.21                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.79                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3091                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.4115                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2920                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.4097                   
REMARK   3   BIN FREE R VALUE                        : 0.4434                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.53                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 171                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5611                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 128                                     
REMARK   3   SOLVENT ATOMS            : 325                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.37                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.16090                                             
REMARK   3    B22 (A**2) : -4.16090                                             
REMARK   3    B33 (A**2) : 8.32170                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.332               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.268               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.212               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.260               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.212               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5859   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7926   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2063   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 184    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 827    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5859   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 753    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7005   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.73                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.93                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.    
REMARK   3  RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=NAG ZN GOL.         
REMARK   3  NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=5973. NUMBER WITH        
REMARK   3  APPROX DEFAULT CCP4 ATOM TYPE=90. NUMBER TREATED BY BAD NON-        
REMARK   3  BONDED CONTACTS=1.                                                  
REMARK   4                                                                      
REMARK   4 4CTH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290059997.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.917                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42405                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.27000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 16.40                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DMT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP, PH 7.0, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP                                                        
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       75.29467            
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       37.64733            
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       37.64733            
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       75.29467            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 56830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.1 KCAL/MOL                        
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -75.29467            
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     HIS A    41                                                      
REMARK 465     HIS A    42                                                      
REMARK 465     HIS A    43                                                      
REMARK 465     HIS A    44                                                      
REMARK 465     HIS A    45                                                      
REMARK 465     HIS A    46                                                      
REMARK 465     HIS A    47                                                      
REMARK 465     HIS A    48                                                      
REMARK 465     HIS A    49                                                      
REMARK 465     HIS A    50                                                      
REMARK 465     TYR A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN A   324     O5   NAG A   753              2.12            
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    LEU A 199      -60.30     67.08                                   
REMARK 500    ASN A 210       87.60   -157.27                                   
REMARK 500    ASN A 309      -74.04    -67.65                                   
REMARK 500    ALA A 462      -38.13    -39.40                                   
REMARK 500    VAL A 541       75.94   -101.63                                   
REMARK 500    LEU A 559       52.55    -92.71                                   
REMARK 500    SER A 565      125.97   -170.68                                   
REMARK 500    ASP A 678       54.28    -91.88                                   
REMARK 500    VAL A 748      -75.62   -116.69                                   
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 A1750  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 583   NE2                                                    
REMARK 620 2 HIS A 587   NE2  97.6                                              
REMARK 620 3 GLU A 646   OE1 102.4 114.6                                        
REMARK 620 4 RDF A1759   O2P 117.9 124.2  98.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: GLYCOPEPTIDE ENZYME INHIBITOR                         
REMARK 630 MOLECULE NAME: N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-    
REMARK 630 LEUCYL-L-TRYPTOPHAN                                                  
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     RDF A  1759                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    RHA LEU TRP                                              
REMARK 630 DETAILS: NULL                                                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 G399V G714K ARE ENGINEERED MUTATIONS                                 
DBREF  4CTH A   51   749  UNP    P08473   NEP_HUMAN       52    750             
SEQADV 4CTH HIS A   41  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   42  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   43  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   44  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   45  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   46  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   47  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   48  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   49  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH HIS A   50  UNP  P08473              EXPRESSION TAG                 
SEQADV 4CTH VAL A  399  UNP  P08473    GLY   400 ENGINEERED MUTATION            
SEQADV 4CTH LYS A  714  UNP  P08473    GLY   715 ENGINEERED MUTATION            
SEQRES   1 A  709  HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS TYR ASP ASP          
SEQRES   2 A  709  GLY ILE CYS LYS SER SER ASP CYS ILE LYS SER ALA ALA          
SEQRES   3 A  709  ARG LEU ILE GLN ASN MET ASP ALA THR THR GLU PRO CYS          
SEQRES   4 A  709  THR ASP PHE PHE LYS TYR ALA CYS GLY GLY TRP LEU LYS          
SEQRES   5 A  709  ARG ASN VAL ILE PRO GLU THR SER SER ARG TYR GLY ASN          
SEQRES   6 A  709  PHE ASP ILE LEU ARG ASP GLU LEU GLU VAL VAL LEU LYS          
SEQRES   7 A  709  ASP VAL LEU GLN GLU PRO LYS THR GLU ASP ILE VAL ALA          
SEQRES   8 A  709  VAL GLN LYS ALA LYS ALA LEU TYR ARG SER CYS ILE ASN          
SEQRES   9 A  709  GLU SER ALA ILE ASP SER ARG GLY GLY GLU PRO LEU LEU          
SEQRES  10 A  709  LYS LEU LEU PRO ASP ILE TYR GLY TRP PRO VAL ALA THR          
SEQRES  11 A  709  GLU ASN TRP GLU GLN LYS TYR GLY ALA SER TRP THR ALA          
SEQRES  12 A  709  GLU LYS ALA ILE ALA GLN LEU ASN SER LYS TYR GLY LYS          
SEQRES  13 A  709  LYS VAL LEU ILE ASN LEU PHE VAL GLY THR ASP ASP LYS          
SEQRES  14 A  709  ASN SER VAL ASN HIS VAL ILE HIS ILE ASP GLN PRO ARG          
SEQRES  15 A  709  LEU GLY LEU PRO SER ARG ASP TYR TYR GLU CYS THR GLY          
SEQRES  16 A  709  ILE TYR LYS GLU ALA CYS THR ALA TYR VAL ASP PHE MET          
SEQRES  17 A  709  ILE SER VAL ALA ARG LEU ILE ARG GLN GLU GLU ARG LEU          
SEQRES  18 A  709  PRO ILE ASP GLU ASN GLN LEU ALA LEU GLU MET ASN LYS          
SEQRES  19 A  709  VAL MET GLU LEU GLU LYS GLU ILE ALA ASN ALA THR ALA          
SEQRES  20 A  709  LYS PRO GLU ASP ARG ASN ASP PRO MET LEU LEU TYR ASN          
SEQRES  21 A  709  LYS MET THR LEU ALA GLN ILE GLN ASN ASN PHE SER LEU          
SEQRES  22 A  709  GLU ILE ASN GLY LYS PRO PHE SER TRP LEU ASN PHE THR          
SEQRES  23 A  709  ASN GLU ILE MET SER THR VAL ASN ILE SER ILE THR ASN          
SEQRES  24 A  709  GLU GLU ASP VAL VAL VAL TYR ALA PRO GLU TYR LEU THR          
SEQRES  25 A  709  LYS LEU LYS PRO ILE LEU THR LYS TYR SER ALA ARG ASP          
SEQRES  26 A  709  LEU GLN ASN LEU MET SER TRP ARG PHE ILE MET ASP LEU          
SEQRES  27 A  709  VAL SER SER LEU SER ARG THR TYR LYS GLU SER ARG ASN          
SEQRES  28 A  709  ALA PHE ARG LYS ALA LEU TYR VAL THR THR SER GLU THR          
SEQRES  29 A  709  ALA THR TRP ARG ARG CYS ALA ASN TYR VAL ASN GLY ASN          
SEQRES  30 A  709  MET GLU ASN ALA VAL GLY ARG LEU TYR VAL GLU ALA ALA          
SEQRES  31 A  709  PHE ALA GLY GLU SER LYS HIS VAL VAL GLU ASP LEU ILE          
SEQRES  32 A  709  ALA GLN ILE ARG GLU VAL PHE ILE GLN THR LEU ASP ASP          
SEQRES  33 A  709  LEU THR TRP MET ASP ALA GLU THR LYS LYS ARG ALA GLU          
SEQRES  34 A  709  GLU LYS ALA LEU ALA ILE LYS GLU ARG ILE GLY TYR PRO          
SEQRES  35 A  709  ASP ASP ILE VAL SER ASN ASP ASN LYS LEU ASN ASN GLU          
SEQRES  36 A  709  TYR LEU GLU LEU ASN TYR LYS GLU ASP GLU TYR PHE GLU          
SEQRES  37 A  709  ASN ILE ILE GLN ASN LEU LYS PHE SER GLN SER LYS GLN          
SEQRES  38 A  709  LEU LYS LYS LEU ARG GLU LYS VAL ASP LYS ASP GLU TRP          
SEQRES  39 A  709  ILE SER GLY ALA ALA VAL VAL ASN ALA PHE TYR SER SER          
SEQRES  40 A  709  GLY ARG ASN GLN ILE VAL PHE PRO ALA GLY ILE LEU GLN          
SEQRES  41 A  709  PRO PRO PHE PHE SER ALA GLN GLN SER ASN SER LEU ASN          
SEQRES  42 A  709  TYR GLY GLY ILE GLY MET VAL ILE GLY HIS GLU ILE THR          
SEQRES  43 A  709  HIS GLY PHE ASP ASP ASN GLY ARG ASN PHE ASN LYS ASP          
SEQRES  44 A  709  GLY ASP LEU VAL ASP TRP TRP THR GLN GLN SER ALA SER          
SEQRES  45 A  709  ASN PHE LYS GLU GLN SER GLN CYS MET VAL TYR GLN TYR          
SEQRES  46 A  709  GLY ASN PHE SER TRP ASP LEU ALA GLY GLY GLN HIS LEU          
SEQRES  47 A  709  ASN GLY ILE ASN THR LEU GLY GLU ASN ILE ALA ASP ASN          
SEQRES  48 A  709  GLY GLY LEU GLY GLN ALA TYR ARG ALA TYR GLN ASN TYR          
SEQRES  49 A  709  ILE LYS LYS ASN GLY GLU GLU LYS LEU LEU PRO GLY LEU          
SEQRES  50 A  709  ASP LEU ASN HIS LYS GLN LEU PHE PHE LEU ASN PHE ALA          
SEQRES  51 A  709  GLN VAL TRP CYS GLY THR TYR ARG PRO GLU TYR ALA VAL          
SEQRES  52 A  709  ASN SER ILE LYS THR ASP VAL HIS SER PRO LYS ASN PHE          
SEQRES  53 A  709  ARG ILE ILE GLY THR LEU GLN ASN SER ALA GLU PHE SER          
SEQRES  54 A  709  GLU ALA PHE HIS CYS ARG LYS ASN SER TYR MET ASN PRO          
SEQRES  55 A  709  GLU LYS LYS CYS ARG VAL TRP                                  
MODRES 4CTH ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4CTH ASN A  324  ASN  GLYCOSYLATION SITE                                 
MODRES 4CTH ASN A  627  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 752      14                                                       
HET    NAG  A 753      14                                                       
HET    NAG  A 754      14                                                       
HET     ZN  A1750       1                                                       
HET    GOL  A1751       6                                                       
HET    GOL  A1752       6                                                       
HET    GOL  A1753       6                                                       
HET    GOL  A1754       6                                                       
HET    GOL  A1755       6                                                       
HET    GOL  A1756       6                                                       
HET    GOL  A1757       6                                                       
HET    GOL  A1758       6                                                       
HET    RDF  A1759      37                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      ZN ZINC ION                                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     RDF N-ALPHA-L-RHAMNOPYRANOSYLOXY(HYDROXYPHOSPHINYL)-L-               
HETNAM   2 RDF  LEUCYL-L-TRYPTOPHAN                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     RDF PHOSPHORAMIDON                                                   
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  GOL    8(C3 H8 O3)                                                  
FORMUL  14  RDF    C23 H34 N3 O10 P                                             
FORMUL  15  HOH   *325(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  GLU A  123  1                                  19    
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  LEU A  160  1                                   8    
HELIX    7   7 PRO A  161  TYR A  164  5                                   4    
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  ARG A  260  1                                  24    
HELIX   14  14 ASP A  264  THR A  286  1                                  23    
HELIX   15  15 LYS A  288  ARG A  292  5                                   5    
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 THR A  332  ASN A  334  5                                   3    
HELIX   20  20 ALA A  347  THR A  359  1                                  13    
HELIX   21  21 SER A  362  MET A  376  1                                  15    
HELIX   22  22 ASP A  377  LEU A  382  5                                   6    
HELIX   23  23 SER A  383  VAL A  399  1                                  17    
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 ALA A  432  GLU A  434  5                                   3    
HELIX   27  27 SER A  435  LEU A  454  1                                  20    
HELIX   28  28 ASP A  455  LEU A  457  5                                   3    
HELIX   29  29 ASP A  461  ALA A  474  1                                  14    
HELIX   30  30 ASP A  483  ASN A  488  1                                   6    
HELIX   31  31 ASN A  488  TYR A  496  1                                   9    
HELIX   32  32 GLU A  505  LYS A  524  1                                  20    
HELIX   33  33 LEU A  525  GLU A  527  5                                   3    
HELIX   34  34 GLY A  557  LEU A  559  5                                   3    
HELIX   35  35 SER A  569  GLY A  576  1                                   8    
HELIX   36  36 GLY A  576  HIS A  587  1                                  12    
HELIX   37  37 GLY A  588  ASP A  590  5                                   3    
HELIX   38  38 ASN A  592  ASN A  595  5                                   4    
HELIX   39  39 THR A  607  ASN A  627  1                                  21    
HELIX   40  40 TRP A  630  GLY A  634  5                                   5    
HELIX   41  41 THR A  643  GLY A  669  1                                  27    
HELIX   42  42 ASN A  680  TRP A  693  1                                  14    
HELIX   43  43 ARG A  698  ASP A  709  1                                  12    
HELIX   44  44 PRO A  713  ASN A  724  1                                  12    
HELIX   45  45 SER A  725  HIS A  733  1                                   9    
SHEET    1  AA 2 ARG A 102  GLY A 104  0                                        
SHEET    2  AA 2 GLY A 695  TYR A 697 -1  O  THR A 696   N  TYR A 103           
SHEET    1  AB 4 ASN A 201  ASP A 207  0                                        
SHEET    2  AB 4 ASN A 210  ASP A 219 -1  N  ASN A 210   O  ASP A 207           
SHEET    3  AB 4 ASP A 342  VAL A 345  1  O  ASP A 342   N  ILE A 216           
SHEET    4  AB 4 LYS A 301  THR A 303 -1  O  MET A 302   N  VAL A 343           
SHEET    1  AC 2 GLU A 314  ILE A 315  0                                        
SHEET    2  AC 2 LYS A 318  PRO A 319 -1  O  LYS A 318   N  ILE A 315           
SHEET    1  AD 3 LYS A 476  GLY A 480  0                                        
SHEET    2  AD 3 GLN A 551  PRO A 555  1  O  ILE A 552   N  ARG A 478           
SHEET    3  AD 3 PHE A 544  SER A 546 -1  O  PHE A 544   N  VAL A 553           
SSBOND   1 CYS A   56    CYS A   61                          1555   1555  2.04  
SSBOND   2 CYS A   79    CYS A  734                          1555   1555  2.04  
SSBOND   3 CYS A   87    CYS A  694                          1555   1555  2.08  
SSBOND   4 CYS A  142    CYS A  410                          1555   1555  2.04  
SSBOND   5 CYS A  233    CYS A  241                          1555   1555  2.06  
SSBOND   6 CYS A  620    CYS A  746                          1555   1555  2.06  
LINK         ND2 ASN A 144                 C1  NAG A 752     1555   1555  1.69  
LINK         ND2 ASN A 324                 C1  NAG A 753     1555   1555  1.26  
LINK         ND2 ASN A 627                 C1  NAG A 754     1555   1555  1.29  
LINK         NE2 HIS A 583                ZN    ZN A1750     1555   1555  1.98  
LINK         NE2 HIS A 587                ZN    ZN A1750     1555   1555  1.97  
LINK         OE1 GLU A 646                ZN    ZN A1750     1555   1555  1.95  
LINK        ZN    ZN A1750                 O2P RDF A1759     1555   1555  1.96  
CISPEP   1 PRO A  561    PRO A  562          0        10.39                     
CRYST1  108.799  108.799  112.942  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      0.009191  0.005307  0.000000        0.00000                         
SCALE2      0.000000  0.010613  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008854        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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