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Database: PDB
Entry: 1Y6W
LinkDB: 1Y6W
Original site: 1Y6W 
HEADER    CALCIUM-BINDING PROTEIN                 07-DEC-04   1Y6W              
TITLE     TRAPPED INTERMEDIATE OF CALMODULIN                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CAM;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM1, CALM2, CALM3;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PAED4                                     
KEYWDS    EF-HAND, CALCIUM-BINDING PROTEIN, ENGINEERED DISULFIDE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.GRABAREK                                                            
REVDAT   3   20-OCT-21 1Y6W    1       REMARK SEQADV LINK                       
REVDAT   2   24-FEB-09 1Y6W    1       VERSN                                    
REVDAT   1   01-MAR-05 1Y6W    0                                                
JRNL        AUTH   Z.GRABAREK                                                   
JRNL        TITL   STRUCTURE OF A TRAPPED INTERMEDIATE OF CALMODULIN: CALCIUM   
JRNL        TITL 2 REGULATION OF EF-HAND PROTEINS FROM A NEW PERSPECTIVE.       
JRNL        REF    J.MOL.BIOL.                   V. 346  1351 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15713486                                                     
JRNL        DOI    10.1016/J.JMB.2005.01.004                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1351678.820                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 10322                          
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 SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 492                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1553                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 79                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1137                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 56                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.76000                                             
REMARK   3    B22 (A**2) : -9.76000                                             
REMARK   3    B33 (A**2) : 19.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.22                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.860                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.540 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.560 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.870 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.120 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 38.89                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : HETERO.PARAM                                   
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : HETERO.TOP                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE N-TERMINAL DOMAIN IS LOCKED IN A      
REMARK   3  CLOSED CONFORMATION WITH A DISULFIDE BOND. THIS PREVENTS THE        
REMARK   3  GLUTAMATE IN THE 12TH POSITION OF THE LOOP FROM INTERACTING WITH    
REMARK   3  THE CALCIUM ION IN SITES I AND II. BOND ANGLES IN RESIDUES 60,      
REMARK   3  61, 94 AND 132 DEVIATE BY MORE THAN 6*RMSD RELATIVE TO THE          
REMARK   3  STANDARD DICTIONARY (SEE REMARK 500). THESE RESIDUES ARE LOCATED    
REMARK   3  IN THE CALCIUM BINDING LOOPS, THUS THEIR CONFORMATION IS            
REMARK   3  CONSTRAINED BY THE CALCIUM IONS.                                    
REMARK   4                                                                      
REMARK   4 1Y6W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000031191.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97896, 0.97919, 0.97129          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10558                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% (W/V) 2-METHYL-2,4-PENTANEDIOL,      
REMARK 280  10% (V/V) T-BUTANOL, 20 MM NA-CACODYLATE, 5 MM CACL2, PH 5.2,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
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       21.32000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       54.93750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       54.93750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       31.98000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       54.93750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       54.93750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       10.66000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       54.93750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.93750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       31.98000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       54.93750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.93750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       10.66000            
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       21.32000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LYS A   148                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  114   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  115   CG   CD   CE   NZ                                   
REMARK 480     LEU A  116   CG   CD1  CD2                                       
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    ASN A  42       66.41   -116.25                                   
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 149  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  82.1                                              
REMARK 620 3 ASP A  22   OD2 105.0  46.1                                        
REMARK 620 4 ASP A  24   OD2  82.4 110.5  74.5                                  
REMARK 620 5 THR A  26   O    83.1 159.0 153.8  82.1                            
REMARK 620 6 HOH A 602   O   107.1  84.6 114.6 163.5  85.6                      
REMARK 620 7 HOH A 606   O   157.2  91.3  56.7  79.6 107.8  93.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 150  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  56   OD2  53.7                                              
REMARK 620 3 ASP A  58   OD1 121.0 106.4                                        
REMARK 620 4 ASP A  58   OD2  71.7  75.8  49.4                                  
REMARK 620 5 ASN A  60   OD1  90.6 140.3  75.4  76.8                            
REMARK 620 6 THR A  62   O    71.8  92.6 160.9 141.2  91.2                      
REMARK 620 7 MPD A 400   O2  148.8 142.1  84.0 130.9  77.3  79.8                
REMARK 620 8 MPD A 400   O4  125.8  73.7  82.9 110.3 143.6 101.2  71.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 151  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  93   OD1                                                    
REMARK 620 2 ASP A  95   OD2  84.4                                              
REMARK 620 3 ASN A  97   OD1  83.7  72.2                                        
REMARK 620 4 TYR A  99   O    81.6 153.4  83.8                                  
REMARK 620 5 GLU A 104   OE1 105.5 131.4 154.6  74.5                            
REMARK 620 6 GLU A 104   OE2 100.0  80.6 152.2 124.0  50.9                      
REMARK 620 7 HOH A 611   O   166.7  88.3  83.5 100.6  87.7  89.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 152  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 129   OD1                                                    
REMARK 620 2 ASP A 131   OD1  83.9                                              
REMARK 620 3 ASP A 133   OD1  81.4  97.0                                        
REMARK 620 4 GLN A 135   O    79.0 162.2  75.8                                  
REMARK 620 5 GLU A 140   OE1 111.5 115.4 145.7  75.9                            
REMARK 620 6 GLU A 140   OE2  84.1  73.0 163.2 109.6  49.0                      
REMARK 620 7 HOH A 604   O   159.6  96.5  78.3  97.9  86.8 115.6                
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 149                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TBU A 500                 
DBREF  1Y6W A    1   148  UNP    P62158   CALM_HUMAN       1    148             
SEQADV 1Y6W MSE A   36  UNP  P62158    MET    36 MODIFIED RESIDUE               
SEQADV 1Y6W CYS A   41  UNP  P62158    GLN    41 ENGINEERED MUTATION            
SEQADV 1Y6W MSE A   51  UNP  P62158    MET    51 MODIFIED RESIDUE               
SEQADV 1Y6W ASN A   64  UNP  P62158    ASP    64 ENGINEERED MUTATION            
SEQADV 1Y6W MSE A   71  UNP  P62158    MET    71 MODIFIED RESIDUE               
SEQADV 1Y6W MSE A   72  UNP  P62158    MET    72 MODIFIED RESIDUE               
SEQADV 1Y6W CYS A   75  UNP  P62158    LYS    75 ENGINEERED MUTATION            
SEQADV 1Y6W MSE A   76  UNP  P62158    MET    76 MODIFIED RESIDUE               
SEQADV 1Y6W MSE A  109  UNP  P62158    MET   109 MODIFIED RESIDUE               
SEQADV 1Y6W MSE A  124  UNP  P62158    MET   124 MODIFIED RESIDUE               
SEQADV 1Y6W MSE A  144  UNP  P62158    MET   144 MODIFIED RESIDUE               
SEQADV 1Y6W MSE A  145  UNP  P62158    MET   145 MODIFIED RESIDUE               
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 MSE ARG SER LEU          
SEQRES   4 A  148  GLY CYS ASN PRO THR GLU ALA GLU LEU GLN ASP MSE ILE          
SEQRES   5 A  148  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASN PHE          
SEQRES   6 A  148  PRO GLU PHE LEU THR MSE MSE ALA ARG CYS MSE 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 MSE THR ASN LEU GLY GLU LYS LEU THR          
SEQRES  10 A  148  ASP GLU GLU VAL ASP GLU MSE 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  MSE MSE THR ALA LYS                                          
MODRES 1Y6W MSE A   36  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A   51  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A   71  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A   72  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A   76  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A  109  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A  124  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A  144  MET  SELENOMETHIONINE                                   
MODRES 1Y6W MSE A  145  MET  SELENOMETHIONINE                                   
HET    MSE  A  36       8                                                       
HET    MSE  A  51       8                                                       
HET    MSE  A  71       8                                                       
HET    MSE  A  72       8                                                       
HET    MSE  A  76       8                                                       
HET    MSE  A 109       8                                                       
HET    MSE  A 124       8                                                       
HET    MSE  A 144       8                                                       
HET    MSE  A 145       8                                                       
HET     CA  A 149       1                                                       
HET     CA  A 150       1                                                       
HET     CA  A 151       1                                                       
HET     CA  A 152       1                                                       
HET    MPD  A 400       8                                                       
HET    TBU  A 500       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     TBU TERTIARY-BUTYL ALCOHOL                                           
HETSYN     TBU 2-METHYL-2-PROPANOL                                              
FORMUL   1  MSE    9(C5 H11 N O2 SE)                                            
FORMUL   2   CA    4(CA 2+)                                                     
FORMUL   6  MPD    C6 H14 O2                                                    
FORMUL   7  TBU    C4 H10 O                                                     
FORMUL   8  HOH   *56(H2 O)                                                     
HELIX    1   1 THR A    5  ASP A   20  1                                  16    
HELIX    2   2 THR A   29  LEU A   39  1                                  11    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 PHE A   65  ASP A   93  1                                  29    
HELIX    5   5 SER A  101  GLY A  113  1                                  13    
HELIX    6   6 THR A  117  ASP A  129  1                                  13    
HELIX    7   7 TYR A  138  THR A  146  1                                   9    
SHEET    1   A 2 THR A  26  THR A  28  0                                        
SHEET    2   A 2 THR A  62  ASN A  64 -1  O  ILE A  63   N  ILE A  27           
SHEET    1   B 2 TYR A  99  ILE A 100  0                                        
SHEET    2   B 2 VAL A 136  ASN A 137 -1  O  VAL A 136   N  ILE A 100           
SSBOND   1 CYS A   41    CYS A   75                          1555   1555  2.05  
LINK         C   VAL A  35                 N   MSE A  36     1555   1555  1.32  
LINK         C   MSE A  36                 N   ARG A  37     1555   1555  1.34  
LINK         C   ASP A  50                 N   MSE A  51     1555   1555  1.33  
LINK         C   MSE A  51                 N   ILE A  52     1555   1555  1.33  
LINK         C   THR A  70                 N   MSE A  71     1555   1555  1.33  
LINK         C   MSE A  71                 N   MSE A  72     1555   1555  1.33  
LINK         C   MSE A  72                 N   ALA A  73     1555   1555  1.33  
LINK         C   CYS A  75                 N   MSE A  76     1555   1555  1.33  
LINK         C   MSE A  76                 N   LYS A  77     1555   1555  1.33  
LINK         C   VAL A 108                 N   MSE A 109     1555   1555  1.33  
LINK         C   MSE A 109                 N   THR A 110     1555   1555  1.33  
LINK         C   GLU A 123                 N   MSE A 124     1555   1555  1.33  
LINK         C   MSE A 124                 N   ILE A 125     1555   1555  1.33  
LINK         C   GLN A 143                 N   MSE A 144     1555   1555  1.33  
LINK         C   MSE A 144                 N   MSE A 145     1555   1555  1.33  
LINK         C   MSE A 145                 N   THR A 146     1555   1555  1.33  
LINK         OD1 ASP A  20                CA    CA A 149     1555   1555  2.35  
LINK         OD1 ASP A  22                CA    CA A 149     1555   1555  2.43  
LINK         OD2 ASP A  22                CA    CA A 149     1555   1555  2.98  
LINK         OD2 ASP A  24                CA    CA A 149     1555   1555  2.43  
LINK         O   THR A  26                CA    CA A 149     1555   1555  2.32  
LINK         OD1 ASP A  56                CA    CA A 150     1555   1555  2.57  
LINK         OD2 ASP A  56                CA    CA A 150     1555   1555  2.25  
LINK         OD1 ASP A  58                CA    CA A 150     1555   1555  2.69  
LINK         OD2 ASP A  58                CA    CA A 150     1555   1555  2.46  
LINK         OD1 ASN A  60                CA    CA A 150     1555   1555  2.37  
LINK         O   THR A  62                CA    CA A 150     1555   1555  2.49  
LINK         OD1 ASP A  93                CA    CA A 151     1555   1555  2.32  
LINK         OD2 ASP A  95                CA    CA A 151     1555   1555  2.32  
LINK         OD1 ASN A  97                CA    CA A 151     1555   1555  2.38  
LINK         O   TYR A  99                CA    CA A 151     1555   1555  2.27  
LINK         OE1 GLU A 104                CA    CA A 151     1555   1555  2.62  
LINK         OE2 GLU A 104                CA    CA A 151     1555   1555  2.46  
LINK         OD1 ASP A 129                CA    CA A 152     1555   1555  2.48  
LINK         OD1 ASP A 131                CA    CA A 152     1555   1555  2.15  
LINK         OD1 ASP A 133                CA    CA A 152     1555   1555  2.53  
LINK         O   GLN A 135                CA    CA A 152     1555   1555  2.36  
LINK         OE1 GLU A 140                CA    CA A 152     1555   1555  2.58  
LINK         OE2 GLU A 140                CA    CA A 152     1555   1555  2.70  
LINK        CA    CA A 149                 O   HOH A 602     1555   1555  2.56  
LINK        CA    CA A 149                 O   HOH A 606     1555   1555  2.78  
LINK        CA    CA A 150                 O2  MPD A 400     1555   1555  2.51  
LINK        CA    CA A 150                 O4  MPD A 400     1555   1555  2.36  
LINK        CA    CA A 151                 O   HOH A 611     1555   1555  2.72  
LINK        CA    CA A 152                 O   HOH A 604     1555   1555  2.46  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 HOH A 602  HOH A 606                                          
SITE     1 AC2  5 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  5 MPD A 400                                                     
SITE     1 AC3  6 ASP A  93  ASP A  95  ASN A  97  TYR A  99                    
SITE     2 AC3  6 GLU A 104  HOH A 611                                          
SITE     1 AC4  6 ASP A 129  ASP A 131  ASP A 133  GLN A 135                    
SITE     2 AC4  6 GLU A 140  HOH A 604                                          
SITE     1 AC5 10 THR A  26  ARG A  37  SER A  38  ASP A  56                    
SITE     2 AC5 10 ASP A  58  ASN A  60  THR A  62  ASN A  64                    
SITE     3 AC5 10 GLU A  67   CA A 150                                          
SITE     1 AC6  2 LEU A 105  MSE A 144                                          
CRYST1  109.875  109.875   42.640  90.00  90.00  90.00 P 43 21 2     8          
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      0.009101  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009101  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023452        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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