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Database: PDB
Entry: 3EDI
LinkDB: 3EDI
Original site: 3EDI 
HEADER    HYDROLASE                               03-SEP-08   3EDI              
TITLE     CRYSTAL STRUCTURE OF TOLLOID-LIKE PROTEASE 1 (TLL-1)                  
TITLE    2 PROTEASE DOMAIN                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOLLOID-LIKE PROTEIN 1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEASE DOMAIN;                                           
COMPND   5 SYNONYM: TLL-1;                                                      
COMPND   6 EC: 3.4.24.-;                                                        
COMPND   7 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: TLL1, TLL;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24A                                    
KEYWDS    DISORDERED CYSTEINE-RICH LOOP, ALTERNATIVE SPLICING,                  
KEYWDS   2 CALCIUM, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, EGF-LIKE            
KEYWDS   3 DOMAIN, GLYCOPROTEIN, HYDROLASE, METAL-BINDING,                      
KEYWDS   4 METALLOPROTEASE, POLYMORPHISM, PROTEASE, SECRETED, ZINC,             
KEYWDS   5 ZYMOGEN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MAC SWEENEY                                                         
REVDAT   3   24-FEB-09 3EDI    1       VERSN                                    
REVDAT   2   23-SEP-08 3EDI    1       AUTHOR JRNL                              
REVDAT   1   16-SEP-08 3EDI    0                                                
JRNL        AUTH   A.MAC SWEENEY,S.G.PARRADO,D.VINZENZ,A.BERNARDI,              
JRNL        AUTH 2 A.HEIN,U.BODENDORF,P.ERBEL,C.LOGEL,B.GERHARTZ                
JRNL        TITL   STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF            
JRNL        TITL 2 BONE MORPHOGENETIC PROTEIN 1/TOLLOID-LIKE                    
JRNL        TITL 3 METALLOPROTEASES                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 41791                          
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) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2090                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2237                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 118                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1598                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 283                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.14000                                             
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.08000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.064         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.058         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.033         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.836         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1657 ; 0.016 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2242 ; 1.473 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   201 ; 6.135 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    87 ;28.716 ;22.184       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   271 ;12.887 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;16.797 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   234 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1284 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   819 ; 0.288 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1138 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   211 ; 0.256 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.034 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    45 ; 0.365 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    26 ; 0.591 ; 0.200       
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):  1010 ; 1.843 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1592 ; 2.747 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   723 ; 4.873 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   644 ; 5.070 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1733 ; 4.479 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   285 ; 7.680 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1620 ; 5.158 ; 3.000       
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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3EDI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049186.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9999                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41793                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.04400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.66                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
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: 1DLE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 200MM LITHIUM              
REMARK 280  SULPHATE, 100MM BIS-TRIS-HCL, PH 7.5, VAPOR DIFFUSION,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.46150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A    61                                                      
REMARK 465     CYS A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     CYS A    64                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     LYS A    82                                                      
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     TYR A  59    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  78    OG                                                  
REMARK 470     MET A 159    CG   SD   CE                                        
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    HOH A   477     O    HOH A   487              1.53            
REMARK 500   O    HOH A   483     O    HOH A   487              1.66            
REMARK 500   O    HOH A   478     O    HOH A   487              1.67            
REMARK 500   O    HOH A   495     O    HOH A   496              1.76            
REMARK 500   CE   MET A    29     O    HOH A   493              1.79            
REMARK 500   O    HOH A   409     O    HOH A   486              1.93            
REMARK 500   O    HOH A   405     O    HOH A   438              2.07            
REMARK 500   O    HOH A   243     O    HOH A   494              2.07            
REMARK 500   O    HOH A   330     O    HOH A   377              2.12            
REMARK 500   SD   MET A    29     O    HOH A   493              2.13            
REMARK 500   NH1  ARG A   170     O1   SO4 A   214              2.15            
REMARK 500   O    HOH A   405     O    HOH A   475              2.17            
REMARK 500   O    HOH A   221     O    HOH A   455              2.19            
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   S    DMS A   215     O    HOH A   386     2546     0.77            
REMARK 500   O    HOH A   474     O    HOH A   498     2555     1.68            
REMARK 500   O    HOH A   238     O    HOH A   497     2556     1.70            
REMARK 500   C2   DMS A   215     O    HOH A   386     2546     1.77            
REMARK 500   O    HOH A   474     O    HOH A   492     2555     1.81            
REMARK 500   C1   DMS A   215     O    HOH A   386     2546     2.08            
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    SER A  49      -71.89   -110.69                                   
REMARK 500    TYR A  59        8.83    -68.02                                   
REMARK 500    CYS A  84       37.99    -91.54                                   
REMARK 500    HIS A 112      -30.08   -131.56                                   
REMARK 500    PHE A 160       -2.33     69.46                                   
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 A 376        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH A 425        DISTANCE =  5.14 ANGSTROMS                       
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 A 210  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  65   SG                                                     
REMARK 620 2 HIS A  92   NE2 122.8                                              
REMARK 620 3 HIS A  96   NE2 109.1 100.9                                        
REMARK 620 4 HIS A 102   NE2 112.1 110.6  97.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 211  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 189   OE1                                                    
REMARK 620 2 ACE A 201   O    79.9                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 201                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 210                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 211                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 212                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 213                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 214                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 215                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EDG   RELATED DB: PDB                                   
REMARK 900 BMP-1                                                                
REMARK 900 RELATED ID: 3EDH   RELATED DB: PDB                                   
REMARK 900 DMSO                                                                 
REMARK 900 RELATED ID: 1DLE   RELATED DB: PDB                                   
REMARK 900 ASTACIN                                                              
DBREF  3EDI A    1   200  UNP    O43897   TLL1_HUMAN     148    348             
SEQRES   1 A  201  ALA ALA THR SER ARG THR GLU ARG ILE TRP PRO GLY GLY          
SEQRES   2 A  201  VAL ILE PRO TYR VAL ILE GLY GLY ASN PHE THR GLY SER          
SEQRES   3 A  201  GLN ARG ALA MET PHE LYS GLN ALA MET ARG HIS TRP GLU          
SEQRES   4 A  201  LYS HIS THR CYS VAL THR PHE ILE GLU ARG SER ASP GLU          
SEQRES   5 A  201  GLU SER TYR ILE VAL PHE THR TYR ARG PRO CYS GLY CYS          
SEQRES   6 A  201  CYS SER TYR VAL GLY ARG ARG GLY ASN GLY PRO GLN ALA          
SEQRES   7 A  201  ILE SER ILE GLY LYS ASN CYS ASP LYS PHE GLY ILE VAL          
SEQRES   8 A  201  VAL HIS GLU LEU GLY HIS VAL ILE GLY PHE TRP HIS GLU          
SEQRES   9 A  201  HIS THR ARG PRO ASP ARG ASP ASN HIS VAL THR ILE ILE          
SEQRES  10 A  201  ARG GLU ASN ILE GLN PRO GLY GLN GLU TYR ASN PHE LEU          
SEQRES  11 A  201  LYS MET GLU PRO GLY GLU VAL ASN SER LEU GLY GLU ARG          
SEQRES  12 A  201  TYR ASP PHE ASP SER ILE MET HIS TYR ALA ARG ASN THR          
SEQRES  13 A  201  PHE SER ARG GLY MET PHE LEU ASP THR ILE LEU PRO SER          
SEQRES  14 A  201  ARG ASP ASP ASN GLY ILE ARG PRO ALA ILE GLY GLN ARG          
SEQRES  15 A  201  THR ARG LEU SER LYS GLY ASP ILE ALA GLN ALA ARG LYS          
SEQRES  16 A  201  LEU TYR ARG CYS PRO ALA                                      
HET    ACE  A 201       3                                                       
HET     ZN  A 210       1                                                       
HET     ZN  A 211       1                                                       
HET    SO4  A 212       5                                                       
HET    SO4  A 213       5                                                       
HET    SO4  A 214       5                                                       
HET    DMS  A 215       4                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  ACE    C2 H4 O                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   8  DMS    C2 H6 O S                                                    
FORMUL   9  HOH   *283(H2 O)                                                    
HELIX    1   1 ARG A    5  ILE A    9  5                                   5    
HELIX    2   2 TRP A   10  GLY A   12  5                                   3    
HELIX    3   3 THR A   23  THR A   41  1                                  19    
HELIX    4   4 LYS A   86  GLY A   99  1                                  14    
HELIX    5   5 HIS A  102  ARG A  106  5                                   5    
HELIX    6   6 ASP A  108  ASN A  111  5                                   4    
HELIX    7   7 ARG A  117  ILE A  120  5                                   4    
HELIX    8   8 GLN A  124  LEU A  129  5                                   6    
HELIX    9   9 GLU A  132  VAL A  134  5                                   5    
HELIX   10  10 SER A  183  TYR A  194  1                                  12    
SHEET    1   A 4 THR A  44  GLU A  47  0                                        
SHEET    2   A 4 VAL A  14  ILE A  19  1  N  ILE A  15   O  THR A  44           
SHEET    3   A 4 ILE A  55  THR A  58  1  O  ILE A  55   N  PRO A  16           
SHEET    4   A 4 GLN A  75  SER A  78  1  O  ILE A  77   N  VAL A  56           
SHEET    1   B 2 VAL A 113  ILE A 115  0                                        
SHEET    2   B 2 ILE A 164  PRO A 166 -1  O  LEU A 165   N  THR A 114           
SSBOND   1 CYS A   42    CYS A  198                          1555   1555  2.05  
LINK         N   ALA A   1                 C   ACE A 201     1555   1555  1.42  
LINK         SG  CYS A  65                ZN    ZN A 210     1555   1555  2.26  
LINK         NE2 HIS A  92                ZN    ZN A 210     1555   1555  2.04  
LINK         NE2 HIS A  96                ZN    ZN A 210     1555   1555  2.08  
LINK         NE2 HIS A 102                ZN    ZN A 210     1555   1555  2.02  
LINK         OE1 GLN A 189                ZN    ZN A 211     1555   1555  2.40  
LINK         O   ACE A 201                ZN    ZN A 211     1555   1555  2.30  
SITE     1 AC1  6 ALA A   1  ALA A   2  GLU A 103  ARG A 106                    
SITE     2 AC1  6 SER A 136  GLN A 189                                          
SITE     1 AC2  4 CYS A  65  HIS A  92  HIS A  96  HIS A 102                    
SITE     1 AC3  5 GLU A 103  GLN A 189  HOH A 236  HOH A 240                    
SITE     2 AC3  5 HOH A 247                                                     
SITE     1 AC4  3 HIS A  36  LYS A  39  HIS A  40                               
SITE     1 AC5  8 SER A   4  ARG A   5  THR A   6  ARG A 151                    
SITE     2 AC5  8 HOH A 258  HOH A 287  HOH A 362  HOH A 370                    
SITE     1 AC6  5 SER A 167  ARG A 168  ARG A 170  HOH A 279                    
SITE     2 AC6  5 HOH A 437                                                     
SITE     1 AC7  6 TYR A  17  LYS A  31  ARG A  35  GLU A  38                    
SITE     2 AC7  6 PHE A  45  HOH A 414                                          
CRYST1   41.281   58.923   47.444  90.00 104.62  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024224  0.000000  0.006320        0.00000                         
SCALE2      0.000000  0.016971  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021783        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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