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Database: PDB
Entry: 5MW5
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Original site: 5MW5 
HEADER    SIGNALING PROTEIN                       18-JAN-17   5MW5              
TITLE     HUMAN JAGGED2 C2-EGF2                                                 
CAVEAT     5MW5    NAG A 401 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN JAGGED-2;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HJ2;                                                        
COMPND   5 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: JAG2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL: SCHNEIDER 2;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEXS2-2                                   
KEYWDS    C2, EGF, NOTCH, SIGNALING, SIGNALING PROTEIN                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.SUCKLING,P.A.HANDFORD,S.M.LEA                                     
REVDAT   4   29-JUL-20 5MW5    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-SEP-17 5MW5    1       REMARK                                   
REVDAT   2   09-AUG-17 5MW5    1       JRNL                                     
REVDAT   1   14-JUN-17 5MW5    0                                                
JRNL        AUTH   R.J.SUCKLING,B.KORONA,P.WHITEMAN,C.CHILLAKURI,L.HOLT,        
JRNL        AUTH 2 P.A.HANDFORD,S.M.LEA                                         
JRNL        TITL   STRUCTURAL AND FUNCTIONAL DISSECTION OF THE INTERPLAY        
JRNL        TITL 2 BETWEEN LIPID AND NOTCH BINDING BY HUMAN NOTCH LIGANDS.      
JRNL        REF    EMBO J.                       V.  36  2204 2017              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   28572448                                                     
JRNL        DOI    10.15252/EMBJ.201796632                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 64.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11513                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 578                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 64.1095 -  4.2857    0.99     2845   144  0.2128 0.2375        
REMARK   3     2  4.2857 -  3.4018    0.99     2711   160  0.2144 0.2419        
REMARK   3     3  3.4018 -  2.9718    1.00     2704   140  0.2567 0.3284        
REMARK   3     4  2.9718 -  2.7001    1.00     2675   134  0.2963 0.3423        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.620           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2117                                  
REMARK   3   ANGLE     :  0.686           2859                                  
REMARK   3   CHIRALITY :  0.043            286                                  
REMARK   3   PLANARITY :  0.004            375                                  
REMARK   3   DIHEDRAL  : 18.914           1239                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MW5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003096.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.3                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11513                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
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: 5MV7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM DIHYDROGEN           
REMARK 280  PHOSPHATE, VAPOR DIFFUSION, TEMPERATURE 293K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       24.13300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.67600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.93900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       49.67600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.13300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.93900            
REMARK 290   SMTRY3   4  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 TOTAL BURIED SURFACE AREA: 420 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 15870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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     GLY A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     ARG A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     THR A    57                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     PRO A   107                                                      
REMARK 465     ALA A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     ALA A   110                                                      
REMARK 465     ALA A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     ASP A   113                                                      
REMARK 465     ARG A   114                                                      
REMARK 465     ALA A   115                                                      
REMARK 465     ARG A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     ARG A   118                                                      
REMARK 465     ALA A   119                                                      
REMARK 465     ARG A   120                                                      
REMARK 465     ALA A   121                                                      
REMARK 465     GLY A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     SER A   311                                                      
REMARK 465     HIS A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     HIS A   314                                                      
REMARK 465     HIS A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A 156   C     PRO A 157   N       0.138                       
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    ARG A 140      -58.88     71.64                                   
REMARK 500    HIS A 168      117.38   -162.01                                   
REMARK 500    ARG A 177     -145.80   -103.44                                   
REMARK 500    VAL A 187      -55.99   -122.53                                   
REMARK 500    SER A 204      169.47     73.71                                   
REMARK 500    ASP A 216     -150.09   -150.38                                   
REMARK 500    CYS A 249      106.89    -59.20                                   
REMARK 500    ASN A 250      105.27    -57.52                                   
REMARK 500    VAL A 283      -91.11   -103.71                                   
REMARK 500    VAL A 288      -59.81   -126.54                                   
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                              CA A 404  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  50   O                                                      
REMARK 620 2 ASP A  51   OD1  70.7                                              
REMARK 620 3 ASP A 150   OD2 112.7  79.6                                        
REMARK 620 4 ASP A 152   OD1 147.1  76.4  60.9                                  
REMARK 620 5 ASP A 152   OD2 145.6 121.7 101.4  56.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  51   OD2                                                    
REMARK 620 2 ASP A  65   OD1  91.3                                              
REMARK 620 3 GLU A  66   O    72.7 100.4                                        
REMARK 620 4 ASP A  68   OD1 114.7 152.9  94.8                                  
REMARK 620 5 ASP A  68   OD2  69.1 148.5  97.0  48.7                            
REMARK 620 6 HOH A 524   O   160.4  79.2  92.0  77.9 126.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  51   OD1                                                    
REMARK 620 2 ASP A  51   OD2  55.1                                              
REMARK 620 3 ASP A  68   OD2 132.2  77.2                                        
REMARK 620 4 ASP A 150   OD1  99.2  97.7  88.5                                  
REMARK 620 5 ASP A 150   OD2  80.4 124.4 137.1  54.9                            
REMARK 620 6 TRP A 151   O   154.0 147.4  71.5  90.7  86.0                      
REMARK 620 7 ASP A 152   OD1  75.6 124.5 141.9 115.2  60.6  78.5                
REMARK 620 N                    1     2     3     4     5     6                 
DBREF  5MW5 A   27   309  UNP    Q9Y219   JAG2_HUMAN      27    309             
SEQADV 5MW5 GLY A  310  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 SER A  311  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  312  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  313  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  314  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  315  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  316  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  317  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  318  UNP  Q9Y219              EXPRESSION TAG                 
SEQADV 5MW5 HIS A  319  UNP  Q9Y219              EXPRESSION TAG                 
SEQRES   1 A  293  MET GLY TYR PHE GLU LEU GLN LEU SER ALA LEU ARG ASN          
SEQRES   2 A  293  VAL ASN GLY GLU LEU LEU SER GLY ALA CYS CYS ASP GLY          
SEQRES   3 A  293  ASP GLY ARG THR THR ARG ALA GLY GLY CYS GLY HIS ASP          
SEQRES   4 A  293  GLU CYS ASP THR TYR VAL ARG VAL CYS LEU LYS GLU TYR          
SEQRES   5 A  293  GLN ALA LYS VAL THR PRO THR GLY PRO CYS SER TYR GLY          
SEQRES   6 A  293  HIS GLY ALA THR PRO VAL LEU GLY GLY ASN SER PHE TYR          
SEQRES   7 A  293  LEU PRO PRO ALA GLY ALA ALA GLY ASP ARG ALA ARG ALA          
SEQRES   8 A  293  ARG ALA ARG ALA GLY GLY ASP GLN ASP PRO GLY LEU VAL          
SEQRES   9 A  293  VAL ILE PRO PHE GLN PHE ALA TRP PRO ARG SER PHE THR          
SEQRES  10 A  293  LEU ILE VAL GLU ALA TRP ASP TRP ASP ASN ASP THR THR          
SEQRES  11 A  293  PRO ASN GLU GLU LEU LEU ILE GLU ARG VAL SER HIS ALA          
SEQRES  12 A  293  GLY MET ILE ASN PRO GLU ASP ARG TRP LYS SER LEU HIS          
SEQRES  13 A  293  PHE SER GLY HIS VAL ALA HIS LEU GLU LEU GLN ILE ARG          
SEQRES  14 A  293  VAL ARG CYS ASP GLU ASN TYR TYR SER ALA THR CYS ASN          
SEQRES  15 A  293  LYS PHE CYS ARG PRO ARG ASN ASP PHE PHE GLY HIS TYR          
SEQRES  16 A  293  THR CYS ASP GLN TYR GLY ASN LYS ALA CYS MET ASP GLY          
SEQRES  17 A  293  TRP MET GLY LYS GLU CYS LYS GLU ALA VAL CYS LYS GLN          
SEQRES  18 A  293  GLY CYS ASN LEU LEU HIS GLY GLY CYS THR VAL PRO GLY          
SEQRES  19 A  293  GLU CYS ARG CYS SER TYR GLY TRP GLN GLY ARG PHE CYS          
SEQRES  20 A  293  ASP GLU CYS VAL PRO TYR PRO GLY CYS VAL HIS GLY SER          
SEQRES  21 A  293  CYS VAL GLU PRO TRP GLN CYS ASN CYS GLU THR ASN TRP          
SEQRES  22 A  293  GLY GLY LEU LEU CYS ASP LYS ASP LEU ASN GLY SER HIS          
SEQRES  23 A  293  HIS HIS HIS HIS HIS HIS HIS                                  
HET    NAG  A 401      14                                                       
HET     CA  A 402       1                                                       
HET     CA  A 403       1                                                       
HET     CA  A 404       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3   CA    3(CA 2+)                                                     
FORMUL   6  HOH   *43(H2 O)                                                     
HELIX    1 AA1 ASN A  158  GLU A  160  5                                   3    
SHEET    1 AA1 3 SER A 102  TYR A 104  0                                        
SHEET    2 AA1 3 GLY A  28  ARG A  38 -1  N  LEU A  37   O  PHE A 103           
SHEET    3 AA1 3 LEU A 129  PHE A 134 -1  O  PHE A 134   N  GLY A  28           
SHEET    1 AA2 4 SER A 102  TYR A 104  0                                        
SHEET    2 AA2 4 GLY A  28  ARG A  38 -1  N  LEU A  37   O  PHE A 103           
SHEET    3 AA2 4 HIS A 189  CYS A 198 -1  O  ARG A 195   N  GLU A  31           
SHEET    4 AA2 4 LYS A 179  SER A 184 -1  N  LEU A 181   O  LEU A 192           
SHEET    1 AA3 4 GLY A  91  ALA A  94  0                                        
SHEET    2 AA3 4 THR A  69  LYS A  76 -1  N  VAL A  73   O  GLY A  93           
SHEET    3 AA3 4 SER A 141  ASP A 150 -1  O  ILE A 145   N  CYS A  74           
SHEET    4 AA3 4 LEU A 162  MET A 171 -1  O  ILE A 163   N  ALA A 148           
SHEET    1 AA4 2 TYR A 202  TYR A 203  0                                        
SHEET    2 AA4 2 LYS A 209  PHE A 210 -1  O  LYS A 209   N  TYR A 203           
SHEET    1 AA5 3 ARG A 214  ASP A 216  0                                        
SHEET    2 AA5 3 GLY A 219  CYS A 223 -1  O  TYR A 221   N  ARG A 214           
SHEET    3 AA5 3 LYS A 229  CYS A 231 -1  O  ALA A 230   N  THR A 222           
SHEET    1 AA6 2 TRP A 235  MET A 236  0                                        
SHEET    2 AA6 2 GLU A 242  ALA A 243 -1  O  GLU A 242   N  MET A 236           
SHEET    1 AA7 2 GLY A 254  GLY A 255  0                                        
SHEET    2 AA7 2 ARG A 263  CYS A 264 -1  O  ARG A 263   N  GLY A 255           
SHEET    1 AA8 2 TRP A 268  GLN A 269  0                                        
SHEET    2 AA8 2 GLU A 275  CYS A 276 -1  O  GLU A 275   N  GLN A 269           
SHEET    1 AA9 2 GLY A 285  SER A 286  0                                        
SHEET    2 AA9 2 ASN A 294  CYS A 295 -1  O  ASN A 294   N  SER A 286           
SHEET    1 AB1 2 TRP A 299  GLY A 300  0                                        
SHEET    2 AB1 2 LYS A 306  ASP A 307 -1  O  LYS A 306   N  GLY A 300           
SSBOND   1 CYS A   49    CYS A   62                          1555   1555  2.03  
SSBOND   2 CYS A   50    CYS A   67                          1555   1555  2.03  
SSBOND   3 CYS A   74    CYS A   88                          1555   1555  2.03  
SSBOND   4 CYS A  198    CYS A  207                          1555   1555  2.03  
SSBOND   5 CYS A  211    CYS A  223                          1555   1555  2.04  
SSBOND   6 CYS A  231    CYS A  240                          1555   1555  2.03  
SSBOND   7 CYS A  245    CYS A  256                          1555   1555  2.04  
SSBOND   8 CYS A  249    CYS A  262                          1555   1555  2.03  
SSBOND   9 CYS A  264    CYS A  273                          1555   1555  2.03  
SSBOND  10 CYS A  276    CYS A  287                          1555   1555  2.03  
SSBOND  11 CYS A  282    CYS A  293                          1555   1555  2.03  
SSBOND  12 CYS A  295    CYS A  304                          1555   1555  2.03  
LINK         ND2 ASN A 153                 C1  NAG A 401     1555   1555  1.40  
LINK         O   CYS A  50                CA    CA A 404     1555   1555  2.31  
LINK         OD2 ASP A  51                CA    CA A 402     1555   1555  2.38  
LINK         OD1 ASP A  51                CA    CA A 403     1555   1555  2.35  
LINK         OD2 ASP A  51                CA    CA A 403     1555   1555  2.40  
LINK         OD1 ASP A  51                CA    CA A 404     1555   1555  2.36  
LINK         OD1 ASP A  65                CA    CA A 402     1555   1555  2.42  
LINK         O   GLU A  66                CA    CA A 402     1555   1555  2.40  
LINK         OD1 ASP A  68                CA    CA A 402     1555   1555  2.46  
LINK         OD2 ASP A  68                CA    CA A 402     1555   1555  2.81  
LINK         OD2 ASP A  68                CA    CA A 403     1555   1555  2.35  
LINK         OD1 ASP A 150                CA    CA A 403     1555   1555  2.35  
LINK         OD2 ASP A 150                CA    CA A 403     1555   1555  2.41  
LINK         OD2 ASP A 150                CA    CA A 404     1555   1555  2.44  
LINK         O   TRP A 151                CA    CA A 403     1555   1555  2.49  
LINK         OD1 ASP A 152                CA    CA A 403     1555   1555  2.33  
LINK         OD1 ASP A 152                CA    CA A 404     1555   1555  2.28  
LINK         OD2 ASP A 152                CA    CA A 404     1555   1555  2.38  
LINK        CA    CA A 402                 O   HOH A 524     1555   1555  2.44  
CISPEP   1 LEU A  105    PRO A  106          0         1.21                     
CRYST1   48.266   83.878   99.352  90.00  90.00  90.00 P 21 21 21    4          
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      0.020719  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011922  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010065        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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