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Database: PDB
Entry: 3I08
LinkDB: 3I08
Original site: 3I08 
HEADER    SIGNALING PROTEIN                       24-JUN-09   3I08              
TITLE     CRYSTAL STRUCTURE OF THE S1-CLEAVED NOTCH1 NEGATIVE                   
TITLE    2 REGULATORY REGION (NRR)                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: NOTCH1 NRR (RESIDUES 1446-1665);                           
COMPND   5 SYNONYM: NOTCH 1, HN1, TRANSLOCATION-ASSOCIATED NOTCH                
COMPND   6 PROTEIN TAN-1, NOTCH 1 EXTRACELLULAR TRUNCATION, NOTCH 1             
COMPND   7 INTRACELLULAR DOMAIN;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: NOTCH1 NRR (RESIDUES 1666-1734);                           
COMPND  13 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: HUMAN NOTCH1, NOTCH1, TAN1;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYSS;                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET 15B;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: HN1 NRR FULL-LENGTH;                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HUMAN NOTCH1, NOTCH1, TAN1;                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3) PLYSS;                       
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PET 15B;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: HN1 NRR FULL-LENGTH                       
KEYWDS    SEA DOMAIN, LIN-12 NOTCH REPEAT, LNR, HETERODIMERIZATION              
KEYWDS   2 DOMAIN, HD, ACTIVATOR, ANK REPEAT, CALCIUM, CELL MEMBRANE,           
KEYWDS   3 DEVELOPMENTAL PROTEIN, DIFFERENTIATION, DISULFIDE BOND,              
KEYWDS   4 EGF-LIKE DOMAIN, GLYCOPROTEIN, MEMBRANE, METAL-BINDING,              
KEYWDS   5 NOTCH SIGNALING PATHWAY, NUCLEUS, PHOSPHOPROTEIN,                    
KEYWDS   6 POLYMORPHISM, RECEPTOR, TRANSCRIPTION, TRANSCRIPTION                 
KEYWDS   7 REGULATION, TRANSMEMBRANE, FURIN, T-ALL, LEUKEMIA,                   
KEYWDS   8 ONCOGENE, METALLOPROTEASE, GAMMA-SECRETASE, SIGNALING                
KEYWDS   9 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.R.GORDON,S.C.BLACKLOW                                               
REVDAT   1   01-SEP-09 3I08    0                                                
JRNL        AUTH   W.R.GORDON,D.VARDAR-ULU,S.L'HEUREUX,T.ASHWORTH,              
JRNL        AUTH 2 M.J.MALECKI,C.SANCHEZ-IRIZARRY,D.G.MCARTHUR,                 
JRNL        AUTH 3 G.HISTEN,J.L.MITCHELL,J.C.ASTER,S.C.BLACKLOW                 
JRNL        TITL   EFFECTS OF S1 CLEAVAGE ON THE STRUCTURE, SURFACE             
JRNL        TITL 2 EXPORT, AND SIGNALING ACTIVITY OF HUMAN NOTCH1 AND           
JRNL        TITL 3 NOTCH2.                                                      
JRNL        REF    PLOS ONE                      V.   4 E6613 2009              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   19701457                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0006613                                 
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0093                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.32                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11922                          
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) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 602                             
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 833                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 35                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3566                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 21                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 76.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -0.63000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.535         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.364         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.757        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3670 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4995 ; 1.734 ; 1.922       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   462 ; 6.961 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   193 ;39.809 ;25.337       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   545 ;20.882 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;18.421 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   518 ; 0.126 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2917 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2312 ; 0.737 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3677 ; 1.440 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1358 ; 1.662 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1318 ; 2.891 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B   1450       A    1529      2                      
REMARK   3           1     A   1450       A    1529      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    316 ; 0.030 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    277 ; 0.040 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):    316 ; 0.060 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    277 ; 0.070 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. U VALUES: REFINED INDIVIDUALLY                    
REMARK   4                                                                      
REMARK   4 3I08 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053800.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11928                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.13200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.51800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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: NOTCH1 NRR DELETION (3ETO)                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAOAC, 2.0 M NACL, 10%              
REMARK 280  GLYCEROL, PH 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE        
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      161.29300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       32.93400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       32.93400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      241.93950            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       32.93400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       32.93400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       80.64650            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       32.93400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.93400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      241.93950            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       32.93400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.93400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       80.64650            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      161.29300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 22690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000      -65.86800            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE PRECURSOR STRUCTURE WAS CLEAVED IN VITRO BY FURIN PROTEASE.      
REMARK 400 FURIN CLEAVES AT R1665 PRIMARILY, BUT A MINOR CLEAVAGE WAS           
REMARK 400 OBSERVED AT R1634 VIA MASS SPECTROMETRY OF THE CRYSTALLIZED          
REMARK 400 PROTEIN.                                                             
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  1446                                                      
REMARK 465     GLU A  1447                                                      
REMARK 465     GLU A  1448                                                      
REMARK 465     ARG A  1623                                                      
REMARK 465     GLU A  1624                                                      
REMARK 465     GLU A  1625                                                      
REMARK 465     GLU A  1626                                                      
REMARK 465     LEU A  1627                                                      
REMARK 465     ARG A  1628                                                      
REMARK 465     LYS A  1629                                                      
REMARK 465     HIS A  1630                                                      
REMARK 465     PRO A  1631                                                      
REMARK 465     ILE A  1632                                                      
REMARK 465     LYS A  1633                                                      
REMARK 465     ARG A  1634                                                      
REMARK 465     ALA A  1635                                                      
REMARK 465     ALA A  1636                                                      
REMARK 465     GLU A  1637                                                      
REMARK 465     GLY A  1638                                                      
REMARK 465     TRP A  1639                                                      
REMARK 465     ALA A  1640                                                      
REMARK 465     ALA A  1641                                                      
REMARK 465     PRO A  1642                                                      
REMARK 465     ASP A  1643                                                      
REMARK 465     ALA A  1644                                                      
REMARK 465     LEU A  1645                                                      
REMARK 465     LEU A  1646                                                      
REMARK 465     GLY A  1647                                                      
REMARK 465     GLN A  1648                                                      
REMARK 465     VAL A  1649                                                      
REMARK 465     LYS A  1650                                                      
REMARK 465     ALA A  1651                                                      
REMARK 465     SER A  1652                                                      
REMARK 465     LEU A  1653                                                      
REMARK 465     LEU A  1654                                                      
REMARK 465     PRO A  1655                                                      
REMARK 465     GLY A  1656                                                      
REMARK 465     GLY A  1657                                                      
REMARK 465     SER A  1658                                                      
REMARK 465     GLU A  1659                                                      
REMARK 465     GLY A  1660                                                      
REMARK 465     GLY A  1661                                                      
REMARK 465     ARG A  1662                                                      
REMARK 465     ARG A  1663                                                      
REMARK 465     ARG A  1664                                                      
REMARK 465     ARG A  1665                                                      
REMARK 465     GLU B  1666                                                      
REMARK 465     LEU B  1667                                                      
REMARK 465     ASP B  1668                                                      
REMARK 465     PRO B  1669                                                      
REMARK 465     PRO B  1730                                                      
REMARK 465     PRO B  1731                                                      
REMARK 465     PRO B  1732                                                      
REMARK 465     ALA B  1733                                                      
REMARK 465     GLN B  1734                                                      
REMARK 465     GLY C  1446                                                      
REMARK 465     GLU C  1447                                                      
REMARK 465     GLU C  1448                                                      
REMARK 465     ARG C  1623                                                      
REMARK 465     GLU C  1624                                                      
REMARK 465     GLU C  1625                                                      
REMARK 465     GLU C  1626                                                      
REMARK 465     LEU C  1627                                                      
REMARK 465     ARG C  1628                                                      
REMARK 465     LYS C  1629                                                      
REMARK 465     HIS C  1630                                                      
REMARK 465     PRO C  1631                                                      
REMARK 465     ILE C  1632                                                      
REMARK 465     LYS C  1633                                                      
REMARK 465     ARG C  1634                                                      
REMARK 465     ALA C  1635                                                      
REMARK 465     ALA C  1636                                                      
REMARK 465     GLU C  1637                                                      
REMARK 465     GLY C  1638                                                      
REMARK 465     TRP C  1639                                                      
REMARK 465     ALA C  1640                                                      
REMARK 465     ALA C  1641                                                      
REMARK 465     PRO C  1642                                                      
REMARK 465     ASP C  1643                                                      
REMARK 465     ALA C  1644                                                      
REMARK 465     LEU C  1645                                                      
REMARK 465     LEU C  1646                                                      
REMARK 465     GLY C  1647                                                      
REMARK 465     GLN C  1648                                                      
REMARK 465     VAL C  1649                                                      
REMARK 465     LYS C  1650                                                      
REMARK 465     ALA C  1651                                                      
REMARK 465     SER C  1652                                                      
REMARK 465     LEU C  1653                                                      
REMARK 465     LEU C  1654                                                      
REMARK 465     PRO C  1655                                                      
REMARK 465     GLY C  1656                                                      
REMARK 465     GLY C  1657                                                      
REMARK 465     SER C  1658                                                      
REMARK 465     GLU C  1659                                                      
REMARK 465     GLY C  1660                                                      
REMARK 465     GLY C  1661                                                      
REMARK 465     ARG C  1662                                                      
REMARK 465     ARG C  1663                                                      
REMARK 465     ARG C  1664                                                      
REMARK 465     ARG C  1665                                                      
REMARK 465     GLU D  1666                                                      
REMARK 465     LEU D  1667                                                      
REMARK 465     ASP D  1668                                                      
REMARK 465     PRO D  1669                                                      
REMARK 465     MET D  1670                                                      
REMARK 465     ASP D  1671                                                      
REMARK 465     PRO D  1730                                                      
REMARK 465     PRO D  1731                                                      
REMARK 465     PRO D  1732                                                      
REMARK 465     ALA D  1733                                                      
REMARK 465     GLN D  1734                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU A1452    CG   CD1  CD2                                       
REMARK 470     GLU A1454    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1526    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1584    CG   CD   OE1  OE2                                  
REMARK 470     MET B1670    CG   SD   CE                                        
REMARK 470     GLU C1454    CG   CD   OE1  OE2                                  
REMARK 470     GLU C1526    CG   CD   OE1  OE2                                  
REMARK 470     VAL D1672    CG1  CG2                                            
REMARK 470     ARG D1673    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1718    CG   CD   CE   NZ                                   
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    CYS A1550   CB    CYS A1550   SG     -0.097                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A1537   CA  -  CB  -  SG  ANGL. DEV. = -20.7 DEGREES          
REMARK 500    CYS A1550   CA  -  CB  -  SG  ANGL. DEV. = -21.9 DEGREES          
REMARK 500    CYS C1450   CA  -  CB  -  SG  ANGL. DEV. =   7.4 DEGREES          
REMARK 500    CYS C1537   CB  -  CA  -  C   ANGL. DEV. =   8.3 DEGREES          
REMARK 500    CYS C1537   CA  -  CB  -  SG  ANGL. DEV. = -18.9 DEGREES          
REMARK 500    CYS C1550   CA  -  CB  -  SG  ANGL. DEV. = -14.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A1451      -79.56    -73.04                                   
REMARK 500    GLU A1454      -60.58    105.30                                   
REMARK 500    ALA A1459      108.18    -53.77                                   
REMARK 500    SER A1465       98.10    -47.35                                   
REMARK 500    ASP A1486       80.50     50.29                                   
REMARK 500    GLN A1523       90.46    -52.50                                   
REMARK 500    ALA A1525       91.29     -7.48                                   
REMARK 500    GLU A1526      -66.88    -97.86                                   
REMARK 500    ASN A1551       62.40   -105.49                                   
REMARK 500    ARG A1569       69.10   -154.80                                   
REMARK 500    MET A1581      121.36    154.46                                   
REMARK 500    THR A1603     -151.69   -159.41                                   
REMARK 500    ASP A1610     -158.45    -98.78                                   
REMARK 500    MET A1616       83.80    -66.40                                   
REMARK 500    ASP B1671       37.65    -67.93                                   
REMARK 500    SER B1712       41.42   -163.76                                   
REMARK 500    PRO B1716       29.32    -75.30                                   
REMARK 500    THR B1726       30.65   -141.76                                   
REMARK 500    GLU C1451      -92.33    -68.01                                   
REMARK 500    GLU C1454      -62.24    104.62                                   
REMARK 500    ALA C1459      108.03    -51.26                                   
REMARK 500    SER C1465       99.81    -44.73                                   
REMARK 500    ASP C1486       78.80     47.76                                   
REMARK 500    ASP C1518       27.59     47.49                                   
REMARK 500    GLN C1523       90.74    -50.77                                   
REMARK 500    ARG C1524      108.99    -40.09                                   
REMARK 500    ALA C1525       89.51     -3.30                                   
REMARK 500    GLU C1526      -63.99    -98.93                                   
REMARK 500    ASP C1558       28.41     44.76                                   
REMARK 500    ARG C1569       70.41   -162.64                                   
REMARK 500    LEU C1580       64.60    -68.65                                   
REMARK 500    THR C1603     -156.70   -154.47                                   
REMARK 500    ASP C1610     -172.26    -62.77                                   
REMARK 500    ARG D1673      -74.73    -67.20                                   
REMARK 500    SER D1690     -164.21   -169.36                                   
REMARK 500    PRO D1716       51.67    -93.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASN A1461        24.2      L          L   OUTSIDE RANGE          
REMARK 500     CYS A1537        24.8      L          L   OUTSIDE RANGE          
REMARK 500     ASP B1671        24.7      L          L   OUTSIDE RANGE          
REMARK 500     ASN C1461        24.5      L          L   OUTSIDE RANGE          
REMARK 500     CYS C1537        23.3      L          L   OUTSIDE RANGE          
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   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1458   O                                                      
REMARK 620 2 ASN A1461   OD1  77.7                                              
REMARK 620 3 VAL A1463   O   145.7  76.0                                        
REMARK 620 4 SER A1465   OG  124.0 123.5  89.1                                  
REMARK 620 5 ASP A1476   OD1 116.1 127.5  66.1  91.7                            
REMARK 620 6 ASP A1479   OD2  78.0  66.5  71.5 156.0  67.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1666  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A1500   O                                                      
REMARK 620 2 HIS A1505   O   146.2                                              
REMARK 620 3 ASP A1507   OD1  96.1  92.8                                        
REMARK 620 4 ASP A1518   OD1  73.9 139.5  85.0                                  
REMARK 620 5 ASP A1518   OD2 125.6  88.1  79.0  51.8                            
REMARK 620 6 ASP A1521   OD2  89.6  84.2 173.4  93.5  95.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1667  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A1540   O                                                      
REMARK 620 2 ASP A1543   OD2  74.1                                              
REMARK 620 3 HIS A1545   O   146.7  73.2                                        
REMARK 620 4 ASP A1547   OD1 100.7 108.7  95.8                                  
REMARK 620 5 ASP A1558   OD1 128.0 148.4  80.2  90.5                            
REMARK 620 6 ASP A1558   OD2  73.3 140.3 132.3  99.1  54.7                      
REMARK 620 7 ASP A1561   OD2  83.1  70.2  79.9 175.7  88.8  84.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C1458   O                                                      
REMARK 620 2 ASN C1461   OD1  75.9                                              
REMARK 620 3 VAL C1463   O   144.3  74.5                                        
REMARK 620 4 SER C1465   OG  126.3 125.7  87.6                                  
REMARK 620 5 ASP C1476   OD1 120.6 124.5  64.0  88.9                            
REMARK 620 6 ASP C1479   OD2  76.4  65.9  73.6 154.8  68.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1666  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C1500   O                                                      
REMARK 620 2 ASP C1503   OD2  84.6                                              
REMARK 620 3 HIS C1505   O   147.7  63.1                                        
REMARK 620 4 ASP C1507   OD1  96.5 108.0  93.1                                  
REMARK 620 5 ASP C1518   OD1  77.2 160.6 134.9  81.0                            
REMARK 620 6 ASP C1518   OD2 127.0 147.4  85.0  78.9  49.9                      
REMARK 620 7 ASP C1521   OD2  90.0  78.2  84.3 171.4  95.0  92.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1667  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C1540   O                                                      
REMARK 620 2 ASP C1543   OD2  64.7                                              
REMARK 620 3 HIS C1545   O   144.1  79.6                                        
REMARK 620 4 ASP C1547   OD1  95.1 115.0  96.4                                  
REMARK 620 5 ASP C1558   OD1 135.8 148.0  78.0  90.0                            
REMARK 620 6 ASP C1558   OD2  83.8 138.1 129.0  93.6  52.1                      
REMARK 620 7 ASP C1561   OD2  86.7  57.0  76.5 169.9  95.5  96.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1666                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1667                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1668                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1                    
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1666                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1667                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ETO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OO4   RELATED DB: PDB                                   
DBREF  3I08 A 1447  1665  UNP    P46531   NOTC1_HUMAN   1446   1664             
DBREF  3I08 B 1666  1734  UNP    P46531   NOTC1_HUMAN   1666   1734             
DBREF  3I08 C 1447  1665  UNP    P46531   NOTC1_HUMAN   1446   1664             
DBREF  3I08 D 1666  1734  UNP    P46531   NOTC1_HUMAN   1666   1734             
SEQADV 3I08 GLY A 1446  UNP  P46531              EXPRESSION TAG                 
SEQADV 3I08 GLY C 1446  UNP  P46531              EXPRESSION TAG                 
SEQRES   1 A  220  GLY GLU GLU ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP          
SEQRES   2 A  220  ALA GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS          
SEQRES   3 A  220  ALA CYS GLY TRP ASP GLY GLY ASP CYS SER LEU ASN PHE          
SEQRES   4 A  220  ASN ASP PRO TRP LYS ASN CYS THR GLN SER LEU GLN CYS          
SEQRES   5 A  220  TRP LYS TYR PHE SER ASP GLY HIS CYS ASP SER GLN CYS          
SEQRES   6 A  220  ASN SER ALA GLY CYS LEU PHE ASP GLY PHE ASP CYS GLN          
SEQRES   7 A  220  ARG ALA GLU GLY GLN CYS ASN PRO LEU TYR ASP GLN TYR          
SEQRES   8 A  220  CYS LYS ASP HIS PHE SER ASP GLY HIS CYS ASP GLN GLY          
SEQRES   9 A  220  CYS ASN SER ALA GLU CYS GLU TRP ASP GLY LEU ASP CYS          
SEQRES  10 A  220  ALA GLU HIS VAL PRO GLU ARG LEU ALA ALA GLY THR LEU          
SEQRES  11 A  220  VAL VAL VAL VAL LEU MET PRO PRO GLU GLN LEU ARG ASN          
SEQRES  12 A  220  SER SER PHE HIS PHE LEU ARG GLU LEU SER ARG VAL LEU          
SEQRES  13 A  220  HIS THR ASN VAL VAL PHE LYS ARG ASP ALA HIS GLY GLN          
SEQRES  14 A  220  GLN MET ILE PHE PRO TYR TYR GLY ARG GLU GLU GLU LEU          
SEQRES  15 A  220  ARG LYS HIS PRO ILE LYS ARG ALA ALA GLU GLY TRP ALA          
SEQRES  16 A  220  ALA PRO ASP ALA LEU LEU GLY GLN VAL LYS ALA SER LEU          
SEQRES  17 A  220  LEU PRO GLY GLY SER GLU GLY GLY ARG ARG ARG ARG              
SEQRES   1 B   69  GLU LEU ASP PRO MET ASP VAL ARG GLY SER ILE VAL TYR          
SEQRES   2 B   69  LEU GLU ILE ASP ASN ARG GLN CYS VAL GLN ALA SER SER          
SEQRES   3 B   69  GLN CYS PHE GLN SER ALA THR ASP VAL ALA ALA PHE LEU          
SEQRES   4 B   69  GLY ALA LEU ALA SER LEU GLY SER LEU ASN ILE PRO TYR          
SEQRES   5 B   69  LYS ILE GLU ALA VAL GLN SER GLU THR VAL GLU PRO PRO          
SEQRES   6 B   69  PRO PRO ALA GLN                                              
SEQRES   1 C  220  GLY GLU GLU ALA CYS GLU LEU PRO GLU CYS GLN GLU ASP          
SEQRES   2 C  220  ALA GLY ASN LYS VAL CYS SER LEU GLN CYS ASN ASN HIS          
SEQRES   3 C  220  ALA CYS GLY TRP ASP GLY GLY ASP CYS SER LEU ASN PHE          
SEQRES   4 C  220  ASN ASP PRO TRP LYS ASN CYS THR GLN SER LEU GLN CYS          
SEQRES   5 C  220  TRP LYS TYR PHE SER ASP GLY HIS CYS ASP SER GLN CYS          
SEQRES   6 C  220  ASN SER ALA GLY CYS LEU PHE ASP GLY PHE ASP CYS GLN          
SEQRES   7 C  220  ARG ALA GLU GLY GLN CYS ASN PRO LEU TYR ASP GLN TYR          
SEQRES   8 C  220  CYS LYS ASP HIS PHE SER ASP GLY HIS CYS ASP GLN GLY          
SEQRES   9 C  220  CYS ASN SER ALA GLU CYS GLU TRP ASP GLY LEU ASP CYS          
SEQRES  10 C  220  ALA GLU HIS VAL PRO GLU ARG LEU ALA ALA GLY THR LEU          
SEQRES  11 C  220  VAL VAL VAL VAL LEU MET PRO PRO GLU GLN LEU ARG ASN          
SEQRES  12 C  220  SER SER PHE HIS PHE LEU ARG GLU LEU SER ARG VAL LEU          
SEQRES  13 C  220  HIS THR ASN VAL VAL PHE LYS ARG ASP ALA HIS GLY GLN          
SEQRES  14 C  220  GLN MET ILE PHE PRO TYR TYR GLY ARG GLU GLU GLU LEU          
SEQRES  15 C  220  ARG LYS HIS PRO ILE LYS ARG ALA ALA GLU GLY TRP ALA          
SEQRES  16 C  220  ALA PRO ASP ALA LEU LEU GLY GLN VAL LYS ALA SER LEU          
SEQRES  17 C  220  LEU PRO GLY GLY SER GLU GLY GLY ARG ARG ARG ARG              
SEQRES   1 D   69  GLU LEU ASP PRO MET ASP VAL ARG GLY SER ILE VAL TYR          
SEQRES   2 D   69  LEU GLU ILE ASP ASN ARG GLN CYS VAL GLN ALA SER SER          
SEQRES   3 D   69  GLN CYS PHE GLN SER ALA THR ASP VAL ALA ALA PHE LEU          
SEQRES   4 D   69  GLY ALA LEU ALA SER LEU GLY SER LEU ASN ILE PRO TYR          
SEQRES   5 D   69  LYS ILE GLU ALA VAL GLN SER GLU THR VAL GLU PRO PRO          
SEQRES   6 D   69  PRO PRO ALA GLN                                              
HET     CA  A   1       1                                                       
HET     CA  A1666       1                                                       
HET     CA  A1667       1                                                       
HET     CL  A1668       1                                                       
HET     CA  C   1       1                                                       
HET     CA  C1666       1                                                       
HET     CA  C1667       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5   CA    6(CA 2+)                                                     
FORMUL   8   CL    CL 1-                                                        
FORMUL  12  HOH   *21(H2 O)                                                     
HELIX    1   1 GLU A 1454  ALA A 1459  1                                   6    
HELIX    2   2 SER A 1465  ASN A 1469  5                                   5    
HELIX    3   3 ASN A 1470  ALA A 1472  5                                   3    
HELIX    4   4 CYS A 1473  GLY A 1478  1                                   6    
HELIX    5   5 THR A 1492  TYR A 1500  5                                   9    
HELIX    6   6 ASP A 1507  ASN A 1511  5                                   5    
HELIX    7   7 SER A 1512  ASP A 1521  5                                  10    
HELIX    8   8 ASN A 1530  ASP A 1539  1                                  10    
HELIX    9   9 ASP A 1547  ASN A 1551  5                                   5    
HELIX   10  10 SER A 1552  ASP A 1561  5                                  10    
HELIX   11  11 PRO A 1582  SER A 1589  1                                   8    
HELIX   12  12 SER A 1589  HIS A 1602  1                                  14    
HELIX   13  13 GLN B 1685  SER B 1690  1                                   6    
HELIX   14  14 SER B 1696  LEU B 1710  1                                  15    
HELIX   15  15 GLU C 1454  ALA C 1459  1                                   6    
HELIX   16  16 SER C 1465  ASN C 1469  5                                   5    
HELIX   17  17 TRP C 1475  ASP C 1479  5                                   5    
HELIX   18  18 ASP C 1486  CYS C 1491  5                                   6    
HELIX   19  19 THR C 1492  TYR C 1500  5                                   9    
HELIX   20  20 ASP C 1507  ASN C 1511  5                                   5    
HELIX   21  21 SER C 1512  ASP C 1521  5                                  10    
HELIX   22  22 ASN C 1530  PHE C 1541  1                                  12    
HELIX   23  23 ASP C 1547  ASN C 1551  5                                   5    
HELIX   24  24 SER C 1552  ASP C 1561  5                                  10    
HELIX   25  25 PRO C 1582  SER C 1589  1                                   8    
HELIX   26  26 SER C 1589  HIS C 1602  1                                  14    
HELIX   27  27 GLN D 1685  SER D 1690  1                                   6    
HELIX   28  28 SER D 1696  LEU D 1710  1                                  15    
SHEET    1   A 3 ASN A1604  PHE A1607  0                                        
SHEET    2   A 3 GLY B1674  ASP B1682 -1  O  ASP B1682   N  ASN A1604           
SHEET    3   A 3 ILE A1617  TYR A1620 -1  N  TYR A1620   O  GLY B1674           
SHEET    1   B 4 ASN A1604  PHE A1607  0                                        
SHEET    2   B 4 GLY B1674  ASP B1682 -1  O  ASP B1682   N  ASN A1604           
SHEET    3   B 4 THR A1574  LEU A1580 -1  N  LEU A1575   O  LEU B1679           
SHEET    4   B 4 LYS B1718  GLU B1725 -1  O  GLU B1720   N  VAL A1578           
SHEET    1   C 3 ASN C1604  PHE C1607  0                                        
SHEET    2   C 3 GLY D1674  ASP D1682 -1  O  GLU D1680   N  VAL C1606           
SHEET    3   C 3 ILE C1617  TYR C1620 -1  N  PHE C1618   O  ILE D1676           
SHEET    1   D 4 ASN C1604  PHE C1607  0                                        
SHEET    2   D 4 GLY D1674  ASP D1682 -1  O  GLU D1680   N  VAL C1606           
SHEET    3   D 4 LEU C1575  VAL C1579 -1  N  LEU C1575   O  LEU D1679           
SHEET    4   D 4 ILE D1719  SER D1724 -1  O  GLU D1720   N  VAL C1578           
SSBOND   1 CYS A 1450    CYS A 1473                          1555   1555  2.07  
SSBOND   2 CYS A 1455    CYS A 1468                          1555   1555  2.04  
SSBOND   3 CYS A 1464    CYS A 1480                          1555   1555  2.07  
SSBOND   4 CYS A 1491    CYS A 1515                          1555   1555  2.07  
SSBOND   5 CYS A 1497    CYS A 1510                          1555   1555  2.08  
SSBOND   6 CYS A 1506    CYS A 1522                          1555   1555  2.09  
SSBOND   7 CYS A 1529    CYS A 1555                          1555   1555  2.10  
SSBOND   8 CYS A 1537    CYS A 1550                          1555   1555  1.97  
SSBOND   9 CYS A 1546    CYS A 1562                          1555   1555  2.11  
SSBOND  10 CYS B 1686    CYS B 1693                          1555   1555  2.10  
SSBOND  11 CYS C 1450    CYS C 1473                          1555   1555  2.08  
SSBOND  12 CYS C 1455    CYS C 1468                          1555   1555  2.07  
SSBOND  13 CYS C 1464    CYS C 1480                          1555   1555  2.05  
SSBOND  14 CYS C 1491    CYS C 1515                          1555   1555  2.08  
SSBOND  15 CYS C 1497    CYS C 1510                          1555   1555  2.09  
SSBOND  16 CYS C 1506    CYS C 1522                          1555   1555  2.07  
SSBOND  17 CYS C 1529    CYS C 1555                          1555   1555  2.11  
SSBOND  18 CYS C 1537    CYS C 1550                          1555   1555  1.97  
SSBOND  19 CYS C 1546    CYS C 1562                          1555   1555  2.08  
SSBOND  20 CYS D 1686    CYS D 1693                          1555   1555  2.09  
LINK         O   ASP A1458                CA    CA A   1     1555   1555  2.47  
LINK         OD1 ASN A1461                CA    CA A   1     1555   1555  2.52  
LINK         O   VAL A1463                CA    CA A   1     1555   1555  2.52  
LINK         OG  SER A1465                CA    CA A   1     1555   1555  2.83  
LINK         OD1 ASP A1476                CA    CA A   1     1555   1555  2.29  
LINK         OD2 ASP A1479                CA    CA A   1     1555   1555  2.43  
LINK         O   TYR A1500                CA    CA A1666     1555   1555  2.42  
LINK         O   HIS A1505                CA    CA A1666     1555   1555  2.46  
LINK         OD1 ASP A1507                CA    CA A1666     1555   1555  2.13  
LINK         OD1 ASP A1518                CA    CA A1666     1555   1555  2.54  
LINK         OD2 ASP A1518                CA    CA A1666     1555   1555  2.53  
LINK         OD2 ASP A1521                CA    CA A1666     1555   1555  2.23  
LINK         O   HIS A1540                CA    CA A1667     1555   1555  2.50  
LINK         OD2 ASP A1543                CA    CA A1667     1555   1555  2.56  
LINK         O   HIS A1545                CA    CA A1667     1555   1555  2.23  
LINK         OD1 ASP A1547                CA    CA A1667     1555   1555  2.35  
LINK         OD1 ASP A1558                CA    CA A1667     1555   1555  2.32  
LINK         OD2 ASP A1558                CA    CA A1667     1555   1555  2.48  
LINK         OD2 ASP A1561                CA    CA A1667     1555   1555  2.70  
LINK         O   ASP C1458                CA    CA C   1     1555   1555  2.48  
LINK         OD1 ASN C1461                CA    CA C   1     1555   1555  2.60  
LINK         O   VAL C1463                CA    CA C   1     1555   1555  2.61  
LINK         OG  SER C1465                CA    CA C   1     1555   1555  2.76  
LINK         OD1 ASP C1476                CA    CA C   1     1555   1555  2.34  
LINK         OD2 ASP C1479                CA    CA C   1     1555   1555  2.48  
LINK         O   TYR C1500                CA    CA C1666     1555   1555  2.39  
LINK         OD2 ASP C1503                CA    CA C1666     1555   1555  2.92  
LINK         O   HIS C1505                CA    CA C1666     1555   1555  2.48  
LINK         OD1 ASP C1507                CA    CA C1666     1555   1555  2.20  
LINK         OD1 ASP C1518                CA    CA C1666     1555   1555  2.53  
LINK         OD2 ASP C1518                CA    CA C1666     1555   1555  2.66  
LINK         OD2 ASP C1521                CA    CA C1666     1555   1555  2.17  
LINK         O   HIS C1540                CA    CA C1667     1555   1555  2.46  
LINK         OD2 ASP C1543                CA    CA C1667     1555   1555  2.48  
LINK         O   HIS C1545                CA    CA C1667     1555   1555  2.28  
LINK         OD1 ASP C1547                CA    CA C1667     1555   1555  2.38  
LINK         OD1 ASP C1558                CA    CA C1667     1555   1555  2.59  
LINK         OD2 ASP C1558                CA    CA C1667     1555   1555  2.35  
LINK         OD2 ASP C1561                CA    CA C1667     1555   1555  2.57  
CISPEP   1 ASN A 1461    LYS A 1462          0       -20.74                     
CISPEP   2 ASN C 1461    LYS C 1462          0       -19.72                     
SITE     1 AC1  6 ASP A1458  ASN A1461  VAL A1463  SER A1465                    
SITE     2 AC1  6 ASP A1476  ASP A1479                                          
SITE     1 AC2  6 TYR A1500  ASP A1503  HIS A1505  ASP A1507                    
SITE     2 AC2  6 ASP A1518  ASP A1521                                          
SITE     1 AC3  6 HIS A1540  ASP A1543  HIS A1545  ASP A1547                    
SITE     2 AC3  6 ASP A1558  ASP A1561                                          
SITE     1 AC4  5 HIS A1471  TRP A1475  ASP A1486  PRO A1487                    
SITE     2 AC4  5 TRP A1488                                                     
SITE     1 AC5  6 ASP C1458  ASN C1461  VAL C1463  SER C1465                    
SITE     2 AC5  6 ASP C1476  ASP C1479                                          
SITE     1 AC6  6 TYR C1500  ASP C1503  HIS C1505  ASP C1507                    
SITE     2 AC6  6 ASP C1518  ASP C1521                                          
SITE     1 AC7  6 HIS C1540  ASP C1543  HIS C1545  ASP C1547                    
SITE     2 AC7  6 ASP C1558  ASP C1561                                          
CRYST1   65.868   65.868  322.586  90.00  90.00  90.00 P 43 21 2    16          
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      0.015182  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015182  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003100        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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