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Database: PDB
Entry: 6AYW
LinkDB: 6AYW
Original site: 6AYW 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       08-SEP-17   6AYW              
TITLE     THE STRUCTURE OF HUMAN CAMKII WITH BOUND INHIBITOR                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II SUBUNIT
COMPND   3 DELTA;                                                               
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 3-301;                                        
COMPND   6 SYNONYM: CAMK-II SUBUNIT DELTA;                                      
COMPND   7 EC: 2.7.11.17;                                                       
COMPND   8 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: CAMK2D, CAMKD;                                                 
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    KINASE, CAMKII, INHIBITOR, TRANSFERASE, TRANSFERASE-TRANSFERASE       
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.SOMOZA,A.G.VILLASENOR                                             
REVDAT   1   15-NOV-17 6AYW    0                                                
JRNL        AUTH   J.R.SOMOZA,A.G.VILLASENOR                                    
JRNL        TITL   THE STRUCTURE OF HUMAN CAMKII WITH BOUND INHIBITOR           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.12_2829)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.337                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36326                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.520                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2008                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.2400 -  4.9400    0.92     2467   139  0.1669 0.2242        
REMARK   3     2  4.9400 -  3.9200    0.92     2425   146  0.1546 0.2223        
REMARK   3     3  3.9200 -  3.4300    0.95     2482   139  0.1788 0.2348        
REMARK   3     4  3.4300 -  3.1100    0.97     2515   150  0.2057 0.2576        
REMARK   3     5  3.1100 -  2.8900    0.98     2598   147  0.2170 0.3098        
REMARK   3     6  2.8900 -  2.7200    0.99     2556   156  0.2226 0.2815        
REMARK   3     7  2.7200 -  2.5800    0.99     2595   147  0.2257 0.2896        
REMARK   3     8  2.5800 -  2.4700    0.99     2576   154  0.2272 0.3312        
REMARK   3     9  2.4700 -  2.3800    0.99     2579   150  0.2316 0.2917        
REMARK   3    10  2.3800 -  2.2900    0.99     2574   155  0.2263 0.3295        
REMARK   3    11  2.2900 -  2.2200    0.98     2546   141  0.2408 0.3085        
REMARK   3    12  2.2200 -  2.1600    0.94     2463   139  0.2458 0.2883        
REMARK   3    13  2.1600 -  2.1000    0.87     2255   139  0.2572 0.3513        
REMARK   3    14  2.1000 -  2.0500    0.65     1687   106  0.2874 0.3917        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.271            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           4902                                  
REMARK   3   ANGLE     :  0.868           6629                                  
REMARK   3   CHIRALITY :  0.051            707                                  
REMARK   3   PLANARITY :  0.006            850                                  
REMARK   3   DIHEDRAL  : 12.310           2947                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6AYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229999.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36488                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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   (%): 47.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CAMKII S3-K301, IN 20MM IMIDAZOLE PH     
REMARK 280  8.5, 0.3M SODIUM CHLORIDE, 5MM TCEP, WAS CONCENTRATED TO 36 MG/     
REMARK 280  ML AND FLASH FROZEN IN LIQUID NITROGEN FOR LONG TERM STORAGE AT -   
REMARK 280  80 C IN 10 MICROL ALIQUOTS. THE PROTEIN WAS THAWED AND DILUTED      
REMARK 280  DOWN TO 12 MG/ML IN THE SAME BUFFER JUST PRIOR TO                   
REMARK 280  CRYSTALLIZATION EXPERIMENTS. SITTING DROP VAPOR DIFFUSION           
REMARK 280  DROPLETS WERE ASSEMBLED WITH 250 NL OF 12 MG/ML CAMKII, 0.6 MM      
REMARK 280  INHIBITOR AND 250 NL OF RESERVOIR SOLUTION 24% PEG 3350, 0.2 M      
REMARK 280  AMMONIUM TARTRATE, 0.1 M ARGININE. FLAT CRYSTAL PLATES              
REMARK 280  (TYPICALLY 0.03 MM X 0.2 MM X 0.4 MM IN SIZE) GREW IN 4-7 DAYS      
REMARK 280  AT 20 C. A CRYSTAL SEED SUSPENSION WAS PREPARED WITH TEN CRUSHED    
REMARK 280  CRYSTALS COMBINED INTO 100 UL OF RESERVOIR SOLUTION AND STORED      
REMARK 280  AT -80 C. A THIRTY FOLD SEED DILUTION WAS PREPARED IN THE SAME      
REMARK 280  SOLUTION FOR ADDITION TO PROTEIN DROPLETS IN A 1 TO 1 VOLUME        
REMARK 280  RATIO TO ENHANCE CRYSTALLIZATION OF DIFFICULT TO CRYSTALLIZE        
REMARK 280  INHIBITORS., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.05500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     LYS B   301                                                      
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   NE2  GLN B   169     O    HOH B   501              1.67            
REMARK 500   OE1  GLU B    97     O    HOH B   502              2.10            
REMARK 500   OE2  GLU A   122     O    HOH A   501              2.11            
REMARK 500   OG   SER B   235     OD2  ASP B   239              2.12            
REMARK 500   O    HOH A   538     O    HOH A   625              2.13            
REMARK 500   N    THR A     8     O    HOH A   502              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   505     O    HOH B   551     2556     2.15            
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    PHE A  17     -143.22   -119.72                                   
REMARK 500    ARG A 135       -3.66     76.44                                   
REMARK 500    ASP A 136       50.45   -147.56                                   
REMARK 500    ASP A 157       94.93     66.98                                   
REMARK 500    PHE A 172       32.75    -86.93                                   
REMARK 500    PHE A 233       70.48   -119.79                                   
REMARK 500    LEU A 253       41.17   -101.49                                   
REMARK 500    PHE B  17     -141.30   -115.25                                   
REMARK 500    GLU B  18      159.30    -47.95                                   
REMARK 500    ARG B 135       -6.98     76.86                                   
REMARK 500    ASP B 157       89.59     60.28                                   
REMARK 500    LEU B 253       45.67    -91.81                                   
REMARK 500    ARG B 284       79.46   -114.84                                   
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 C2V A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue C2V B 402                 
DBREF  6AYW A    3   301  UNP    Q13557   KCC2D_HUMAN      3    301             
DBREF  6AYW B    3   301  UNP    Q13557   KCC2D_HUMAN      3    301             
SEQADV 6AYW GLY A    0  UNP  Q13557              EXPRESSION TAG                 
SEQADV 6AYW HIS A    1  UNP  Q13557              EXPRESSION TAG                 
SEQADV 6AYW MET A    2  UNP  Q13557              EXPRESSION TAG                 
SEQADV 6AYW GLY B    0  UNP  Q13557              EXPRESSION TAG                 
SEQADV 6AYW HIS B    1  UNP  Q13557              EXPRESSION TAG                 
SEQADV 6AYW MET B    2  UNP  Q13557              EXPRESSION TAG                 
SEQRES   1 A  302  GLY HIS MET SER THR THR THR CYS THR ARG PHE THR ASP          
SEQRES   2 A  302  GLU TYR GLN LEU PHE GLU GLU LEU GLY LYS GLY ALA PHE          
SEQRES   3 A  302  SER VAL VAL ARG ARG CYS MET LYS ILE PRO THR GLY GLN          
SEQRES   4 A  302  GLU TYR ALA ALA LYS ILE ILE ASN THR LYS LYS LEU SER          
SEQRES   5 A  302  ALA ARG ASP HIS GLN LYS LEU GLU ARG GLU ALA ARG ILE          
SEQRES   6 A  302  CYS ARG LEU LEU LYS HIS PRO ASN ILE VAL ARG LEU HIS          
SEQRES   7 A  302  ASP SER ILE SER GLU GLU GLY PHE HIS TYR LEU VAL PHE          
SEQRES   8 A  302  ASP LEU VAL THR GLY GLY GLU LEU PHE GLU ASP ILE VAL          
SEQRES   9 A  302  ALA ARG GLU TYR TYR SER GLU ALA ASP ALA SER HIS CYS          
SEQRES  10 A  302  ILE GLN GLN ILE LEU GLU SER VAL ASN HIS CYS HIS LEU          
SEQRES  11 A  302  ASN GLY ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN LEU          
SEQRES  12 A  302  LEU LEU ALA SER LYS SER LYS GLY ALA ALA VAL LYS LEU          
SEQRES  13 A  302  ALA ASP PHE GLY LEU ALA ILE GLU VAL GLN GLY ASP GLN          
SEQRES  14 A  302  GLN ALA TRP PHE GLY PHE ALA GLY THR PRO GLY TYR LEU          
SEQRES  15 A  302  SER PRO GLU VAL LEU ARG LYS ASP PRO TYR GLY LYS PRO          
SEQRES  16 A  302  VAL ASP MET TRP ALA CYS GLY VAL ILE LEU TYR ILE LEU          
SEQRES  17 A  302  LEU VAL GLY TYR PRO PRO PHE TRP ASP GLU ASP GLN HIS          
SEQRES  18 A  302  ARG LEU TYR GLN GLN ILE LYS ALA GLY ALA TYR ASP PHE          
SEQRES  19 A  302  PRO SER PRO GLU TRP ASP THR VAL THR PRO GLU ALA LYS          
SEQRES  20 A  302  ASP LEU ILE ASN LYS MET LEU THR ILE ASN PRO ALA LYS          
SEQRES  21 A  302  ARG ILE THR ALA SER GLU ALA LEU LYS HIS PRO TRP ILE          
SEQRES  22 A  302  CYS GLN ARG SER THR VAL ALA SER MET MET HIS ARG GLN          
SEQRES  23 A  302  GLU THR VAL ASP CYS LEU LYS LYS PHE ASN ALA ARG ARG          
SEQRES  24 A  302  LYS LEU LYS                                                  
SEQRES   1 B  302  GLY HIS MET SER THR THR THR CYS THR ARG PHE THR ASP          
SEQRES   2 B  302  GLU TYR GLN LEU PHE GLU GLU LEU GLY LYS GLY ALA PHE          
SEQRES   3 B  302  SER VAL VAL ARG ARG CYS MET LYS ILE PRO THR GLY GLN          
SEQRES   4 B  302  GLU TYR ALA ALA LYS ILE ILE ASN THR LYS LYS LEU SER          
SEQRES   5 B  302  ALA ARG ASP HIS GLN LYS LEU GLU ARG GLU ALA ARG ILE          
SEQRES   6 B  302  CYS ARG LEU LEU LYS HIS PRO ASN ILE VAL ARG LEU HIS          
SEQRES   7 B  302  ASP SER ILE SER GLU GLU GLY PHE HIS TYR LEU VAL PHE          
SEQRES   8 B  302  ASP LEU VAL THR GLY GLY GLU LEU PHE GLU ASP ILE VAL          
SEQRES   9 B  302  ALA ARG GLU TYR TYR SER GLU ALA ASP ALA SER HIS CYS          
SEQRES  10 B  302  ILE GLN GLN ILE LEU GLU SER VAL ASN HIS CYS HIS LEU          
SEQRES  11 B  302  ASN GLY ILE VAL HIS ARG ASP LEU LYS PRO GLU ASN LEU          
SEQRES  12 B  302  LEU LEU ALA SER LYS SER LYS GLY ALA ALA VAL LYS LEU          
SEQRES  13 B  302  ALA ASP PHE GLY LEU ALA ILE GLU VAL GLN GLY ASP GLN          
SEQRES  14 B  302  GLN ALA TRP PHE GLY PHE ALA GLY THR PRO GLY TYR LEU          
SEQRES  15 B  302  SER PRO GLU VAL LEU ARG LYS ASP PRO TYR GLY LYS PRO          
SEQRES  16 B  302  VAL ASP MET TRP ALA CYS GLY VAL ILE LEU TYR ILE LEU          
SEQRES  17 B  302  LEU VAL GLY TYR PRO PRO PHE TRP ASP GLU ASP GLN HIS          
SEQRES  18 B  302  ARG LEU TYR GLN GLN ILE LYS ALA GLY ALA TYR ASP PHE          
SEQRES  19 B  302  PRO SER PRO GLU TRP ASP THR VAL THR PRO GLU ALA LYS          
SEQRES  20 B  302  ASP LEU ILE ASN LYS MET LEU THR ILE ASN PRO ALA LYS          
SEQRES  21 B  302  ARG ILE THR ALA SER GLU ALA LEU LYS HIS PRO TRP ILE          
SEQRES  22 B  302  CYS GLN ARG SER THR VAL ALA SER MET MET HIS ARG GLN          
SEQRES  23 B  302  GLU THR VAL ASP CYS LEU LYS LYS PHE ASN ALA ARG ARG          
SEQRES  24 B  302  LYS LEU LYS                                                  
HET    C2V  A 401      28                                                       
HET    DTT  A 402       8                                                       
HET    DTT  B 401       8                                                       
HET    C2V  B 402      28                                                       
HETNAM     C2V N-[2-(DIMETHYLAMINO)ETHYL]-3-[6-(THIOPHEN-2-YL)                  
HETNAM   2 C2V  IMIDAZO[1,2-B]PYRIDAZIN-3-YL]BENZAMIDE                          
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   3  C2V    2(C21 H21 N5 O S)                                            
FORMUL   4  DTT    2(C4 H10 O2 S2)                                              
FORMUL   7  HOH   *259(H2 O)                                                    
HELIX    1 AA1 THR A    8  GLU A   13  1                                   6    
HELIX    2 AA2 SER A   51  LEU A   68  1                                  18    
HELIX    3 AA3 GLU A   97  VAL A  103  1                                   7    
HELIX    4 AA4 SER A  109  ASN A  130  1                                  22    
HELIX    5 AA5 LYS A  138  GLU A  140  5                                   3    
HELIX    6 AA6 SER A  146  GLY A  150  5                                   5    
HELIX    7 AA7 THR A  177  LEU A  181  5                                   5    
HELIX    8 AA8 SER A  182  ARG A  187  1                                   6    
HELIX    9 AA9 LYS A  193  GLY A  210  1                                  18    
HELIX   10 AB1 ASP A  218  GLY A  229  1                                  12    
HELIX   11 AB2 PRO A  236  VAL A  241  5                                   6    
HELIX   12 AB3 THR A  242  LEU A  253  1                                  12    
HELIX   13 AB4 THR A  262  LEU A  267  1                                   6    
HELIX   14 AB5 HIS A  269  GLN A  274  1                                   6    
HELIX   15 AB6 GLN A  274  ALA A  279  1                                   6    
HELIX   16 AB7 ARG A  284  LEU A  300  1                                  17    
HELIX   17 AB8 THR B    8  GLU B   13  1                                   6    
HELIX   18 AB9 LYS B   48  LEU B   50  5                                   3    
HELIX   19 AC1 SER B   51  LEU B   68  1                                  18    
HELIX   20 AC2 GLU B   97  VAL B  103  1                                   7    
HELIX   21 AC3 SER B  109  ASN B  130  1                                  22    
HELIX   22 AC4 LYS B  138  GLU B  140  5                                   3    
HELIX   23 AC5 THR B  177  LEU B  181  5                                   5    
HELIX   24 AC6 SER B  182  ARG B  187  1                                   6    
HELIX   25 AC7 LYS B  193  GLY B  210  1                                  18    
HELIX   26 AC8 ASP B  218  ALA B  228  1                                  11    
HELIX   27 AC9 PRO B  236  VAL B  241  5                                   6    
HELIX   28 AD1 THR B  242  LEU B  253  1                                  12    
HELIX   29 AD2 THR B  262  LEU B  267  1                                   6    
HELIX   30 AD3 HIS B  269  GLN B  274  1                                   6    
HELIX   31 AD4 GLN B  274  ALA B  279  1                                   6    
HELIX   32 AD5 ARG B  284  LYS B  299  1                                  16    
SHEET    1 AA1 5 TYR A  14  LYS A  22  0                                        
SHEET    2 AA1 5 VAL A  27  LYS A  33 -1  O  ARG A  30   N  PHE A  17           
SHEET    3 AA1 5 GLU A  39  ASN A  46 -1  O  ILE A  44   N  VAL A  27           
SHEET    4 AA1 5 PHE A  85  ASP A  91 -1  O  LEU A  88   N  LYS A  43           
SHEET    5 AA1 5 LEU A  76  GLU A  82 -1  N  HIS A  77   O  VAL A  89           
SHEET    1 AA2 2 ILE A 132  VAL A 133  0                                        
SHEET    2 AA2 2 ILE A 162  GLU A 163 -1  O  ILE A 162   N  VAL A 133           
SHEET    1 AA3 2 LEU A 142  LEU A 144  0                                        
SHEET    2 AA3 2 VAL A 153  LEU A 155 -1  O  LYS A 154   N  LEU A 143           
SHEET    1 AA4 5 TYR B  14  LYS B  22  0                                        
SHEET    2 AA4 5 VAL B  27  LYS B  33 -1  O  ARG B  30   N  PHE B  17           
SHEET    3 AA4 5 GLU B  39  ASN B  46 -1  O  ILE B  44   N  VAL B  27           
SHEET    4 AA4 5 PHE B  85  ASP B  91 -1  O  PHE B  90   N  ALA B  41           
SHEET    5 AA4 5 LEU B  76  SER B  81 -1  N  HIS B  77   O  VAL B  89           
SHEET    1 AA5 2 ILE B 132  VAL B 133  0                                        
SHEET    2 AA5 2 ILE B 162  GLU B 163 -1  O  ILE B 162   N  VAL B 133           
SHEET    1 AA6 2 LEU B 142  LEU B 144  0                                        
SHEET    2 AA6 2 VAL B 153  LEU B 155 -1  O  LYS B 154   N  LEU B 143           
CISPEP   1 SER A  235    PRO A  236          0         2.82                     
CISPEP   2 SER B  235    PRO B  236          0         4.17                     
SITE     1 AC1 11 LEU A  20  VAL A  28  ALA A  41  VAL A  74                    
SITE     2 AC1 11 PHE A  90  ASP A  91  VAL A  93  GLU A 140                    
SITE     3 AC1 11 ASN A 141  LEU A 143  ASP A 157                               
SITE     1 AC2  7 GLN A 118  ILE A 272  CYS A 273  GLN A 274                    
SITE     2 AC2  7 ARG A 275  SER A 276  HOH A 623                               
SITE     1 AC3  6 GLN B 118  ILE B 272  CYS B 273  GLN B 274                    
SITE     2 AC3  6 ARG B 275  SER B 276                                          
SITE     1 AC4 13 LEU B  20  GLY B  21  VAL B  28  ALA B  41                    
SITE     2 AC4 13 PHE B  90  ASP B  91  LEU B  92  VAL B  93                    
SITE     3 AC4 13 GLU B 140  ASN B 141  LEU B 143  ASP B 157                    
SITE     4 AC4 13 HOH B 508                                                     
CRYST1   54.149   68.110   84.825  90.00  94.56  90.00 P 1 21 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      0.018468  0.000000  0.001472        0.00000                         
SCALE2      0.000000  0.014682  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011826        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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