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Database: PDB
Entry: 2O60
LinkDB: 2O60
Original site: 2O60 
HEADER    METAL BINDING PROTEIN                   06-DEC-06   2O60              
TITLE     CALMODULIN BOUND TO PEPTIDE FROM NEURONAL NITRIC OXIDE SYNTHASE       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PEPTIDE CORRESPONDING TO CALMODULIN BINDING DOMAIN OF      
COMPND   8 NEURONAL NITRIC OXIDE SYNTHASE;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 GENE: CALM;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET 15B;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE 
SOURCE  14 OCCURS NATURALLY IN MICE. PEPTIDE IS ACETYLATED AT N-TERMINUS AND    
SOURCE  15 AMIDATED AT C-TERMINUS.                                              
KEYWDS    PROTEIN-PEPTIDE COMPLEX, METAL BINDING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.L.NG,T.ALBER,A.J.WAND                                               
REVDAT   4   18-OCT-17 2O60    1       REMARK                                   
REVDAT   3   13-JUL-11 2O60    1       VERSN                                    
REVDAT   2   24-FEB-09 2O60    1       VERSN                                    
REVDAT   1   25-DEC-07 2O60    0                                                
JRNL        AUTH   K.G.VALENTINE,H.L.NG,L.SCHNEEWEIS,J.K.KRANZ,K.K.FREDERICK,   
JRNL        AUTH 2 T.ALBER,A.J.WAND                                             
JRNL        TITL   CRYSTAL STRUCTURE OF CALMODULIN-NEURONAL NITRIC OXIDE        
JRNL        TITL 2 SYNTHASE COMPLEX                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22393                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1208                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1673                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1316                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 165                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : -0.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.47000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.097         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.100         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.061         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.231         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1357 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   922 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1812 ; 1.656 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2279 ; 1.505 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   166 ; 6.118 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    73 ;28.061 ;26.575       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   275 ;15.569 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;15.492 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   199 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1506 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   248 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   377 ; 0.249 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):   971 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   701 ; 0.187 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   642 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   111 ; 0.205 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    13 ; 0.120 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    14 ; 0.180 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    40 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   870 ; 1.190 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   345 ; 0.376 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1332 ; 1.659 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   549 ; 2.462 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   480 ; 3.473 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8605  27.5462   3.8680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2411 T22:  -0.2256                                     
REMARK   3      T33:  -0.1152 T12:  -0.0021                                     
REMARK   3      T13:   0.0124 T23:  -0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.8686 L22:  14.5695                                     
REMARK   3      L33:   8.0821 L12:   8.0799                                     
REMARK   3      L13:  -5.2600 L23:  -6.3935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2016 S12:   0.0898 S13:   0.4498                       
REMARK   3      S21:  -0.1786 S22:   0.0832 S23:   0.3548                       
REMARK   3      S31:  -0.2114 S32:  -0.1296 S33:  -0.2848                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    15        A    74                          
REMARK   3    RESIDUE RANGE :   A   402        A   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9667  14.9514   7.7495              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2202 T22:  -0.2354                                     
REMARK   3      T33:  -0.2127 T12:  -0.0281                                     
REMARK   3      T13:   0.0034 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5354 L22:   1.5874                                     
REMARK   3      L33:   2.7173 L12:   0.8993                                     
REMARK   3      L13:  -0.4872 L23:  -0.4774                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0779 S12:  -0.3399 S13:  -0.1187                       
REMARK   3      S21:   0.1246 S22:  -0.0891 S23:   0.0039                       
REMARK   3      S31:   0.0355 S32:   0.0010 S33:   0.0112                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    87        A   113                          
REMARK   3    RESIDUE RANGE :   A   404        A   404                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5459  23.9108  28.5946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0884 T22:   0.0647                                     
REMARK   3      T33:  -0.1699 T12:  -0.0480                                     
REMARK   3      T13:   0.0144 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3376 L22:   6.2374                                     
REMARK   3      L33:   9.4696 L12:  -1.4801                                     
REMARK   3      L13:   0.7177 L23:   4.8429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0284 S12:  -0.3325 S13:  -0.3957                       
REMARK   3      S21:   0.0669 S22:  -0.2693 S23:   0.2535                       
REMARK   3      S31:   0.1900 S32:  -0.8038 S33:   0.2977                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   114        A   148                          
REMARK   3    RESIDUE RANGE :   A   401        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8942  30.0739  25.8521              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0073 T22:   0.0310                                     
REMARK   3      T33:  -0.1920 T12:  -0.0541                                     
REMARK   3      T13:   0.0065 T23:   0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7054 L22:   4.1956                                     
REMARK   3      L33:   8.4771 L12:   0.7019                                     
REMARK   3      L13:   1.7822 L23:   2.4534                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0811 S12:  -0.0398 S13:  -0.0107                       
REMARK   3      S21:  -0.4631 S22:   0.0496 S23:  -0.2544                       
REMARK   3      S31:  -0.5391 S32:   0.2320 S33:   0.0316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B    18                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.0780  25.8618  16.2411              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1412 T22:  -0.1187                                     
REMARK   3      T33:  -0.1764 T12:  -0.0463                                     
REMARK   3      T13:   0.0187 T23:  -0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.9203 L22:   6.1158                                     
REMARK   3      L33:  10.7720 L12:   3.5856                                     
REMARK   3      L13:   8.9398 L23:   1.5948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1140 S12:   0.5108 S13:   0.1643                       
REMARK   3      S21:  -0.1650 S22:  -0.0512 S23:  -0.3938                       
REMARK   3      S31:  -0.2475 S32:   0.8270 S33:   0.1651                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    19        B    23                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8376  23.9608  12.8067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0856 T22:  -0.1145                                     
REMARK   3      T33:  -0.1097 T12:   0.0031                                     
REMARK   3      T13:  -0.0206 T23:  -0.0858                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.9457 L22:  18.5589                                     
REMARK   3      L33:  12.8341 L12:   8.9513                                     
REMARK   3      L13:  -3.8996 L23:  -7.2871                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2377 S12:  -0.5891 S13:   0.7842                       
REMARK   3      S21:   1.1991 S22:  -0.0952 S23:   1.7203                       
REMARK   3      S31:  -0.6701 S32:  -0.7266 S33:   0.3329                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2O60 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040730.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23547                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 74.536                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2 M SODIUM ACETATE,      
REMARK 280  0.1 M SODIUM CITRATE PH 5.6, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       33.56300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       16.46500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       33.56300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       16.46500            
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: 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 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     LYS B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A     7     O    HOH A   557              1.47            
REMARK 500   NZ   LYS A    13     O    HOH A   457              1.86            
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    MET A  72   CG  -  SD  -  CE  ANGL. DEV. = -10.2 DEGREES          
REMARK 500    GLN B  23   CA  -  C   -  N   ANGL. DEV. = -16.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A   2      -58.76    -24.83                                   
REMARK 500    MET A  76      -99.21    -86.11                                   
REMARK 500    LYS A  77     -130.32     51.57                                   
REMARK 500    ASP A  78     -125.77   -149.18                                   
REMARK 500    THR A  79     -162.96     57.02                                   
REMARK 500    ASP A  80       96.38     37.64                                   
REMARK 500    SER A  81      -73.29     79.97                                   
REMARK 500    GLU A  82     -159.18     55.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2O5G   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PEPTIDE IN CHAIN B IS ACETYLATED AT N-TERMINUS AND                   
REMARK 999 AMIDATED AT C-TERMINUS. ACE GROUP WAS NOT MODELED DUE                
REMARK 999 TO LACK OF ELECTRON DENSITY.                                         
DBREF  2O60 A    1   148  UNP    P62149   CALM_CHICK       1    148             
DBREF  2O60 B    1    23  UNP    Q9Z0J4   NOS1_MOUSE     725    747             
SEQRES   1 A  148  ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A  148  GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A  148  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A  148  GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP          
SEQRES   7 A  148  THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL          
SEQRES   8 A  148  PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU          
SEQRES   9 A  148  LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE          
SEQRES  11 A  148  ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN          
SEQRES  12 A  148  MET MET THR ALA LYS                                          
SEQRES   1 B   24  LYS ARG ARG ALA ILE GLY PHE LYS LYS LEU ALA GLU ALA          
SEQRES   2 B   24  VAL LYS PHE SER ALA LYS LEU MET GLY GLN NH2                  
HET    NH2  B  24       1                                                       
HET     CA  A 401       1                                                       
HET     CA  A 402       1                                                       
HET     CA  A 403       1                                                       
HET     CA  A 404       1                                                       
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NH2    H2 N                                                         
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *165(H2 O)                                                    
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 ASP A   64  MET A   76  1                                  13    
HELIX    5   5 GLU A   84  ASP A   93  1                                  10    
HELIX    6   6 SER A  101  LEU A  112  1                                  12    
HELIX    7   7 THR A  117  ARG A  126  1                                  10    
HELIX    8   8 TYR A  138  ALA A  147  1                                  10    
HELIX    9   9 GLY B    6  MET B   21  1                                  16    
SHEET    1   A 2 TYR A  99  ILE A 100  0                                        
SHEET    2   A 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
LINK         C   GLN B  23                 N   NH2 B  24     1555   1555  1.34  
SITE     1 AC1  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC1  6 GLU A 140  HOH A 432                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 410                                          
SITE     1 AC3  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC3  6 GLU A  31  HOH A 419                                          
SITE     1 AC4  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC4  6 GLU A 104  HOH A 476                                          
CRYST1   67.126   32.930   73.830  90.00  93.30  90.00 C 1 2 1       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      0.014897  0.000000  0.000859        0.00000                         
SCALE2      0.000000  0.030367  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013567        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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