GenomeNet

Database: PDB
Entry: 6CNO
LinkDB: 6CNO
Original site: 6CNO 
HEADER    MEMBRANE PROTEIN                        08-MAR-18   6CNO              
TITLE     CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX IN THE  
TITLE    2 CA2+ BOUND STATE II                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERMEDIATE CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM       
COMPND   3 CHANNEL PROTEIN 4;                                                   
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 SYNONYM: SK4 CHANNEL, SKCA4, IKCA1, IK1, KCA3.1, KCA4, PUTATIVE      
COMPND   6 GARDOS CHANNEL;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CALMODULIN-1;                                              
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 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: KCNN4, IK1, IKCA1, KCA4, SK4;                                  
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CALM1, CALM, CAM, CAM1;                                        
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    ION CHANNEL, NEUROSCIENCE, CALMODULIN, MEMBRANE PROTEIN               
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    C.H.LEE,R.MACKINNON                                                   
REVDAT   4   13-MAR-24 6CNO    1       REMARK                                   
REVDAT   3   20-NOV-19 6CNO    1       REMARK                                   
REVDAT   2   23-MAY-18 6CNO    1       JRNL                                     
REVDAT   1   02-MAY-18 6CNO    0                                                
JRNL        AUTH   C.H.LEE,R.MACKINNON                                          
JRNL        TITL   ACTIVATION MECHANISM OF A HUMAN SK-CALMODULIN CHANNEL        
JRNL        TITL 2 COMPLEX ELUCIDATED BY CRYO-EM STRUCTURES.                    
JRNL        REF    SCIENCE                       V. 360   508 2018              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   29724949                                                     
JRNL        DOI    10.1126/SCIENCE.AAS9466                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.700                          
REMARK   3   NUMBER OF PARTICLES               : 52056                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6CNO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233106.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : HUMAN SK4/CALMODULIN CHANNEL      
REMARK 245                                    COMPLEX                           
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 7500.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLY A   124                                                      
REMARK 465     PRO A   125                                                      
REMARK 465     PRO A   126                                                      
REMARK 465     CYS A   127                                                      
REMARK 465     VAL A   128                                                      
REMARK 465     GLN A   129                                                      
REMARK 465     ASP A   130                                                      
REMARK 465     LEU A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     ALA A   133                                                      
REMARK 465     PRO A   134                                                      
REMARK 465     LEU A   135                                                      
REMARK 465     THR A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     PRO A   138                                                      
REMARK 465     GLN A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     TRP A   141                                                      
REMARK 465     SER A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     ARG A   390                                                      
REMARK 465     ALA A   391                                                      
REMARK 465     LEU A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     LYS A   394                                                      
REMARK 465     GLN A   395                                                      
REMARK 465     ILE A   396                                                      
REMARK 465     ASP A   397                                                      
REMARK 465     THR A   398                                                      
REMARK 465     LEU A   399                                                      
REMARK 465     ALA A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     LEU A   403                                                      
REMARK 465     ASP A   404                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     LEU A   406                                                      
REMARK 465     THR A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     LEU A   409                                                      
REMARK 465     LEU A   410                                                      
REMARK 465     SER A   411                                                      
REMARK 465     THR A   412                                                      
REMARK 465     ALA A   413                                                      
REMARK 465     LEU A   414                                                      
REMARK 465     GLY A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     ARG A   417                                                      
REMARK 465     GLN A   418                                                      
REMARK 465     LEU A   419                                                      
REMARK 465     PRO A   420                                                      
REMARK 465     GLU A   421                                                      
REMARK 465     PRO A   422                                                      
REMARK 465     SER A   423                                                      
REMARK 465     GLN A   424                                                      
REMARK 465     GLN A   425                                                      
REMARK 465     SER A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLY B   124                                                      
REMARK 465     PRO B   125                                                      
REMARK 465     PRO B   126                                                      
REMARK 465     CYS B   127                                                      
REMARK 465     VAL B   128                                                      
REMARK 465     GLN B   129                                                      
REMARK 465     ASP B   130                                                      
REMARK 465     LEU B   131                                                      
REMARK 465     GLY B   132                                                      
REMARK 465     ALA B   133                                                      
REMARK 465     PRO B   134                                                      
REMARK 465     LEU B   135                                                      
REMARK 465     THR B   136                                                      
REMARK 465     SER B   137                                                      
REMARK 465     PRO B   138                                                      
REMARK 465     GLN B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     TRP B   141                                                      
REMARK 465     SER B   387                                                      
REMARK 465     SER B   388                                                      
REMARK 465     HIS B   389                                                      
REMARK 465     ARG B   390                                                      
REMARK 465     ALA B   391                                                      
REMARK 465     LEU B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     LYS B   394                                                      
REMARK 465     GLN B   395                                                      
REMARK 465     ILE B   396                                                      
REMARK 465     ASP B   397                                                      
REMARK 465     THR B   398                                                      
REMARK 465     LEU B   399                                                      
REMARK 465     ALA B   400                                                      
REMARK 465     GLY B   401                                                      
REMARK 465     LYS B   402                                                      
REMARK 465     LEU B   403                                                      
REMARK 465     ASP B   404                                                      
REMARK 465     ALA B   405                                                      
REMARK 465     LEU B   406                                                      
REMARK 465     THR B   407                                                      
REMARK 465     GLU B   408                                                      
REMARK 465     LEU B   409                                                      
REMARK 465     LEU B   410                                                      
REMARK 465     SER B   411                                                      
REMARK 465     THR B   412                                                      
REMARK 465     ALA B   413                                                      
REMARK 465     LEU B   414                                                      
REMARK 465     GLY B   415                                                      
REMARK 465     PRO B   416                                                      
REMARK 465     ARG B   417                                                      
REMARK 465     GLN B   418                                                      
REMARK 465     LEU B   419                                                      
REMARK 465     PRO B   420                                                      
REMARK 465     GLU B   421                                                      
REMARK 465     PRO B   422                                                      
REMARK 465     SER B   423                                                      
REMARK 465     GLN B   424                                                      
REMARK 465     GLN B   425                                                      
REMARK 465     SER B   426                                                      
REMARK 465     LYS B   427                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     GLY C   124                                                      
REMARK 465     PRO C   125                                                      
REMARK 465     PRO C   126                                                      
REMARK 465     CYS C   127                                                      
REMARK 465     VAL C   128                                                      
REMARK 465     GLN C   129                                                      
REMARK 465     ASP C   130                                                      
REMARK 465     LEU C   131                                                      
REMARK 465     GLY C   132                                                      
REMARK 465     ALA C   133                                                      
REMARK 465     PRO C   134                                                      
REMARK 465     LEU C   135                                                      
REMARK 465     THR C   136                                                      
REMARK 465     SER C   137                                                      
REMARK 465     PRO C   138                                                      
REMARK 465     GLN C   139                                                      
REMARK 465     PRO C   140                                                      
REMARK 465     TRP C   141                                                      
REMARK 465     SER C   387                                                      
REMARK 465     SER C   388                                                      
REMARK 465     HIS C   389                                                      
REMARK 465     ARG C   390                                                      
REMARK 465     ALA C   391                                                      
REMARK 465     LEU C   392                                                      
REMARK 465     GLU C   393                                                      
REMARK 465     LYS C   394                                                      
REMARK 465     GLN C   395                                                      
REMARK 465     ILE C   396                                                      
REMARK 465     ASP C   397                                                      
REMARK 465     THR C   398                                                      
REMARK 465     LEU C   399                                                      
REMARK 465     ALA C   400                                                      
REMARK 465     GLY C   401                                                      
REMARK 465     LYS C   402                                                      
REMARK 465     LEU C   403                                                      
REMARK 465     ASP C   404                                                      
REMARK 465     ALA C   405                                                      
REMARK 465     LEU C   406                                                      
REMARK 465     THR C   407                                                      
REMARK 465     GLU C   408                                                      
REMARK 465     LEU C   409                                                      
REMARK 465     LEU C   410                                                      
REMARK 465     SER C   411                                                      
REMARK 465     THR C   412                                                      
REMARK 465     ALA C   413                                                      
REMARK 465     LEU C   414                                                      
REMARK 465     GLY C   415                                                      
REMARK 465     PRO C   416                                                      
REMARK 465     ARG C   417                                                      
REMARK 465     GLN C   418                                                      
REMARK 465     LEU C   419                                                      
REMARK 465     PRO C   420                                                      
REMARK 465     GLU C   421                                                      
REMARK 465     PRO C   422                                                      
REMARK 465     SER C   423                                                      
REMARK 465     GLN C   424                                                      
REMARK 465     GLN C   425                                                      
REMARK 465     SER C   426                                                      
REMARK 465     LYS C   427                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     LEU D     5                                                      
REMARK 465     VAL D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     GLY D   124                                                      
REMARK 465     PRO D   125                                                      
REMARK 465     PRO D   126                                                      
REMARK 465     CYS D   127                                                      
REMARK 465     VAL D   128                                                      
REMARK 465     GLN D   129                                                      
REMARK 465     ASP D   130                                                      
REMARK 465     LEU D   131                                                      
REMARK 465     GLY D   132                                                      
REMARK 465     ALA D   133                                                      
REMARK 465     PRO D   134                                                      
REMARK 465     LEU D   135                                                      
REMARK 465     THR D   136                                                      
REMARK 465     SER D   137                                                      
REMARK 465     PRO D   138                                                      
REMARK 465     GLN D   139                                                      
REMARK 465     PRO D   140                                                      
REMARK 465     TRP D   141                                                      
REMARK 465     SER D   387                                                      
REMARK 465     SER D   388                                                      
REMARK 465     HIS D   389                                                      
REMARK 465     ARG D   390                                                      
REMARK 465     ALA D   391                                                      
REMARK 465     LEU D   392                                                      
REMARK 465     GLU D   393                                                      
REMARK 465     LYS D   394                                                      
REMARK 465     GLN D   395                                                      
REMARK 465     ILE D   396                                                      
REMARK 465     ASP D   397                                                      
REMARK 465     THR D   398                                                      
REMARK 465     LEU D   399                                                      
REMARK 465     ALA D   400                                                      
REMARK 465     GLY D   401                                                      
REMARK 465     LYS D   402                                                      
REMARK 465     LEU D   403                                                      
REMARK 465     ASP D   404                                                      
REMARK 465     ALA D   405                                                      
REMARK 465     LEU D   406                                                      
REMARK 465     THR D   407                                                      
REMARK 465     GLU D   408                                                      
REMARK 465     LEU D   409                                                      
REMARK 465     LEU D   410                                                      
REMARK 465     SER D   411                                                      
REMARK 465     THR D   412                                                      
REMARK 465     ALA D   413                                                      
REMARK 465     LEU D   414                                                      
REMARK 465     GLY D   415                                                      
REMARK 465     PRO D   416                                                      
REMARK 465     ARG D   417                                                      
REMARK 465     GLN D   418                                                      
REMARK 465     LEU D   419                                                      
REMARK 465     PRO D   420                                                      
REMARK 465     GLU D   421                                                      
REMARK 465     PRO D   422                                                      
REMARK 465     SER D   423                                                      
REMARK 465     GLN D   424                                                      
REMARK 465     GLN D   425                                                      
REMARK 465     SER D   426                                                      
REMARK 465     LYS D   427                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     LYS E   148                                                      
REMARK 465     MET F     0                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     LYS F   148                                                      
REMARK 465     MET G     0                                                      
REMARK 465     ALA G     1                                                      
REMARK 465     LYS G   148                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     LYS H   148                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     CYS A  52    SG                                                  
REMARK 470     ASP A  95    CG   OD1  OD2                                       
REMARK 470     THR A 101    OG1  CG2                                            
REMARK 470     VAL A 122    CG1  CG2                                            
REMARK 470     ARG A 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 231    CG1  CG2                                            
REMARK 470     ASN A 232    CG   OD1  ND2                                       
REMARK 470     THR A 234    OG1  CG2                                            
REMARK 470     GLU A 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 332    CG   CD   CE   NZ                                   
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 363    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 366    CG   OD1  ND2                                       
REMARK 470     MET A 368    CG   SD   CE                                        
REMARK 470     ASP A 370    CG   OD1  OD2                                       
REMARK 470     SER A 372    OG                                                  
REMARK 470     MET A 376    CG   SD   CE                                        
REMARK 470     TYR A 379    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 380    CG   OD1  OD2                                       
REMARK 470     LEU A 381    CG   CD1  CD2                                       
REMARK 470     GLN A 382    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 383    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 384    CG   OD1  ND2                                       
REMARK 470     LEU A 385    CG   CD1  CD2                                       
REMARK 470     SER A 386    OG                                                  
REMARK 470     CYS B  52    SG                                                  
REMARK 470     ASP B  95    CG   OD1  OD2                                       
REMARK 470     THR B 101    OG1  CG2                                            
REMARK 470     VAL B 122    CG1  CG2                                            
REMARK 470     ARG B 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 231    CG1  CG2                                            
REMARK 470     ASN B 232    CG   OD1  ND2                                       
REMARK 470     THR B 234    OG1  CG2                                            
REMARK 470     GLU B 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 332    CG   CD   CE   NZ                                   
REMARK 470     GLU B 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 363    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 366    CG   OD1  ND2                                       
REMARK 470     MET B 368    CG   SD   CE                                        
REMARK 470     ASP B 370    CG   OD1  OD2                                       
REMARK 470     SER B 372    OG                                                  
REMARK 470     MET B 376    CG   SD   CE                                        
REMARK 470     TYR B 379    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 380    CG   OD1  OD2                                       
REMARK 470     LEU B 381    CG   CD1  CD2                                       
REMARK 470     GLN B 382    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 383    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 384    CG   OD1  ND2                                       
REMARK 470     LEU B 385    CG   CD1  CD2                                       
REMARK 470     SER B 386    OG                                                  
REMARK 470     CYS C  52    SG                                                  
REMARK 470     ASP C  95    CG   OD1  OD2                                       
REMARK 470     THR C 101    OG1  CG2                                            
REMARK 470     VAL C 122    CG1  CG2                                            
REMARK 470     ARG C 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 231    CG1  CG2                                            
REMARK 470     ASN C 232    CG   OD1  ND2                                       
REMARK 470     THR C 234    OG1  CG2                                            
REMARK 470     GLU C 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 332    CG   CD   CE   NZ                                   
REMARK 470     GLU C 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 363    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 366    CG   OD1  ND2                                       
REMARK 470     MET C 368    CG   SD   CE                                        
REMARK 470     ASP C 370    CG   OD1  OD2                                       
REMARK 470     SER C 372    OG                                                  
REMARK 470     MET C 376    CG   SD   CE                                        
REMARK 470     TYR C 379    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP C 380    CG   OD1  OD2                                       
REMARK 470     LEU C 381    CG   CD1  CD2                                       
REMARK 470     GLN C 382    CG   CD   OE1  NE2                                  
REMARK 470     GLN C 383    CG   CD   OE1  NE2                                  
REMARK 470     ASN C 384    CG   OD1  ND2                                       
REMARK 470     LEU C 385    CG   CD1  CD2                                       
REMARK 470     SER C 386    OG                                                  
REMARK 470     CYS D  52    SG                                                  
REMARK 470     ASP D  95    CG   OD1  OD2                                       
REMARK 470     THR D 101    OG1  CG2                                            
REMARK 470     VAL D 122    CG1  CG2                                            
REMARK 470     ARG D 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D 231    CG1  CG2                                            
REMARK 470     ASN D 232    CG   OD1  ND2                                       
REMARK 470     THR D 234    OG1  CG2                                            
REMARK 470     GLU D 290    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 332    CG   CD   CE   NZ                                   
REMARK 470     GLU D 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 363    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 366    CG   OD1  ND2                                       
REMARK 470     MET D 368    CG   SD   CE                                        
REMARK 470     ASP D 370    CG   OD1  OD2                                       
REMARK 470     SER D 372    OG                                                  
REMARK 470     MET D 376    CG   SD   CE                                        
REMARK 470     TYR D 379    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP D 380    CG   OD1  OD2                                       
REMARK 470     LEU D 381    CG   CD1  CD2                                       
REMARK 470     GLN D 382    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 383    CG   CD   OE1  NE2                                  
REMARK 470     ASN D 384    CG   OD1  ND2                                       
REMARK 470     LEU D 385    CG   CD1  CD2                                       
REMARK 470     SER D 386    OG                                                  
REMARK 470     ASP E   2    CG   OD1  OD2                                       
REMARK 470     GLN E   3    CG   CD   OE1  NE2                                  
REMARK 470     ASP E  80    CG   OD1  OD2                                       
REMARK 470     LYS E  94    CG   CD   CE   NZ                                   
REMARK 470     ARG E 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP E 118    CG   OD1  OD2                                       
REMARK 470     GLU E 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 120    CG   CD   OE1  OE2                                  
REMARK 470     VAL E 121    CG1  CG2                                            
REMARK 470     ASP E 122    CG   OD1  OD2                                       
REMARK 470     GLU E 123    CG   CD   OE1  OE2                                  
REMARK 470     MET E 124    CG   SD   CE                                        
REMARK 470     ILE E 125    CG1  CG2  CD1                                       
REMARK 470     ARG E 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 127    CG   CD   OE1  OE2                                  
REMARK 470     ASP E 129    CG   OD1  OD2                                       
REMARK 470     ILE E 130    CG1  CG2  CD1                                       
REMARK 470     ASP E 131    CG   OD1  OD2                                       
REMARK 470     ASP E 133    CG   OD1  OD2                                       
REMARK 470     GLU E 139    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 140    CG   CD   OE1  OE2                                  
REMARK 470     VAL E 142    CG1  CG2                                            
REMARK 470     ASP F   2    CG   OD1  OD2                                       
REMARK 470     GLN F   3    CG   CD   OE1  NE2                                  
REMARK 470     ASP F  80    CG   OD1  OD2                                       
REMARK 470     LYS F  94    CG   CD   CE   NZ                                   
REMARK 470     ARG F 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP F 118    CG   OD1  OD2                                       
REMARK 470     GLU F 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 120    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 121    CG1  CG2                                            
REMARK 470     ASP F 122    CG   OD1  OD2                                       
REMARK 470     GLU F 123    CG   CD   OE1  OE2                                  
REMARK 470     MET F 124    CG   SD   CE                                        
REMARK 470     ILE F 125    CG1  CG2  CD1                                       
REMARK 470     ARG F 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F 127    CG   CD   OE1  OE2                                  
REMARK 470     ASP F 129    CG   OD1  OD2                                       
REMARK 470     ILE F 130    CG1  CG2  CD1                                       
REMARK 470     ASP F 131    CG   OD1  OD2                                       
REMARK 470     ASP F 133    CG   OD1  OD2                                       
REMARK 470     GLU F 139    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 140    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 142    CG1  CG2                                            
REMARK 470     ASP G   2    CG   OD1  OD2                                       
REMARK 470     GLN G   3    CG   CD   OE1  NE2                                  
REMARK 470     ASP G  80    CG   OD1  OD2                                       
REMARK 470     LYS G  94    CG   CD   CE   NZ                                   
REMARK 470     ARG G 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP G 118    CG   OD1  OD2                                       
REMARK 470     GLU G 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 120    CG   CD   OE1  OE2                                  
REMARK 470     VAL G 121    CG1  CG2                                            
REMARK 470     ASP G 122    CG   OD1  OD2                                       
REMARK 470     GLU G 123    CG   CD   OE1  OE2                                  
REMARK 470     MET G 124    CG   SD   CE                                        
REMARK 470     ILE G 125    CG1  CG2  CD1                                       
REMARK 470     ARG G 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU G 127    CG   CD   OE1  OE2                                  
REMARK 470     ASP G 129    CG   OD1  OD2                                       
REMARK 470     ILE G 130    CG1  CG2  CD1                                       
REMARK 470     ASP G 131    CG   OD1  OD2                                       
REMARK 470     ASP G 133    CG   OD1  OD2                                       
REMARK 470     GLU G 139    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 140    CG   CD   OE1  OE2                                  
REMARK 470     VAL G 142    CG1  CG2                                            
REMARK 470     ASP H   2    CG   OD1  OD2                                       
REMARK 470     GLN H   3    CG   CD   OE1  NE2                                  
REMARK 470     ASP H  80    CG   OD1  OD2                                       
REMARK 470     LYS H  94    CG   CD   CE   NZ                                   
REMARK 470     ARG H 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP H 118    CG   OD1  OD2                                       
REMARK 470     GLU H 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 120    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 121    CG1  CG2                                            
REMARK 470     ASP H 122    CG   OD1  OD2                                       
REMARK 470     GLU H 123    CG   CD   OE1  OE2                                  
REMARK 470     MET H 124    CG   SD   CE                                        
REMARK 470     ILE H 125    CG1  CG2  CD1                                       
REMARK 470     ARG H 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 127    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 129    CG   OD1  OD2                                       
REMARK 470     ILE H 130    CG1  CG2  CD1                                       
REMARK 470     ASP H 131    CG   OD1  OD2                                       
REMARK 470     ASP H 133    CG   OD1  OD2                                       
REMARK 470     GLU H 139    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 140    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 142    CG1  CG2                                            
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   OD1  ASP E    93     OD1  ASN E    97              1.94            
REMARK 500   OD1  ASP H    93     OD1  ASN H    97              1.94            
REMARK 500   OD1  ASP G    93     OD1  ASN G    97              1.94            
REMARK 500   OD1  ASP F    93     OD1  ASN F    97              1.94            
REMARK 500   OD1  ASP E    24     O    THR E    26              2.00            
REMARK 500   OD1  ASP G    24     O    THR G    26              2.00            
REMARK 500   OD1  ASP F    24     O    THR F    26              2.00            
REMARK 500   OD1  ASP H    24     O    THR H    26              2.00            
REMARK 500   OD1  ASP F    20     OD1  ASP F    22              2.07            
REMARK 500   OD1  ASP H    20     OD1  ASP H    22              2.07            
REMARK 500   OD1  ASP E    20     OD1  ASP E    22              2.07            
REMARK 500   OD1  ASP G    20     OD1  ASP G    22              2.07            
REMARK 500   OD1  ASN H    60     O    THR H    62              2.11            
REMARK 500   OD1  ASN F    60     O    THR F    62              2.11            
REMARK 500   OD1  ASN E    60     O    THR E    62              2.11            
REMARK 500   OD1  ASN G    60     O    THR G    62              2.11            
REMARK 500   OD1  ASP E    22     OE2  GLU E    31              2.16            
REMARK 500   OD1  ASP F    22     OE2  GLU F    31              2.16            
REMARK 500   OD1  ASP H    22     OE2  GLU H    31              2.16            
REMARK 500   OD1  ASP G    22     OE2  GLU G    31              2.16            
REMARK 500   OD1  ASP F    20     OD1  ASP F    24              2.19            
REMARK 500   OD1  ASP G    20     OD1  ASP G    24              2.19            
REMARK 500   OD1  ASP E    20     OD1  ASP E    24              2.19            
REMARK 500   OD1  ASP H    20     OD1  ASP H    24              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  94      -32.44   -131.70                                   
REMARK 500    ARG A 189       77.00     59.83                                   
REMARK 500    ARG B  94      -32.44   -131.79                                   
REMARK 500    ARG B 189       77.03     59.77                                   
REMARK 500    ARG C  94      -32.50   -131.75                                   
REMARK 500    ARG C 189       76.98     59.77                                   
REMARK 500    ARG D  94      -32.47   -131.73                                   
REMARK 500    ARG D 189       77.02     59.81                                   
REMARK 500    THR E 146       31.52    -98.42                                   
REMARK 500    THR F 146       31.53    -98.39                                   
REMARK 500    THR G 146       31.52    -98.44                                   
REMARK 500    THR H 146       31.55    -98.36                                   
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 E 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  20   OD1                                                    
REMARK 620 2 ASP E  22   OD1  51.8                                              
REMARK 620 3 ASP E  24   OD1  59.0  88.5                                        
REMARK 620 4 ASP E  24   OD2 119.5 108.7  64.8                                  
REMARK 620 5 THR E  26   O    82.9 132.5  51.6  79.2                            
REMARK 620 6 GLU E  31   OE1 109.2 107.3 147.9 130.6  99.8                      
REMARK 620 7 GLU E  31   OE2  91.3  54.8 143.2 125.5 153.3  57.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  56   OD1                                                    
REMARK 620 2 ASP E  58   OD1  74.6                                              
REMARK 620 3 ASP E  58   OD2 128.3  54.8                                        
REMARK 620 4 ASN E  60   OD1  69.3  83.6  93.4                                  
REMARK 620 5 THR E  62   O    94.6 136.0 113.5  53.2                            
REMARK 620 6 GLU E  67   OE1 101.9 128.7 116.7 144.3  95.1                      
REMARK 620 7 GLU E  67   OE2 110.4  78.0  71.5 160.8 143.4  54.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  93   OD1                                                    
REMARK 620 2 ASP E  95   OD1  56.2                                              
REMARK 620 3 ASN E  97   OD1  49.7  77.7                                        
REMARK 620 4 TYR E  99   O    85.4 139.7  67.0                                  
REMARK 620 5 GLU E 104   OE1 124.6 118.7 157.6  91.8                            
REMARK 620 6 GLU E 104   OE2 112.4  68.0 144.6 148.2  56.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  20   OD1                                                    
REMARK 620 2 ASP F  22   OD1  51.6                                              
REMARK 620 3 ASP F  24   OD1  58.5  88.5                                        
REMARK 620 4 ASP F  24   OD2 119.8 110.0  65.3                                  
REMARK 620 5 THR F  26   O    82.0 131.7  51.3  79.4                            
REMARK 620 6 GLU F  31   OE1 107.7 106.8 146.2 131.4  98.7                      
REMARK 620 7 GLU F  31   OE2  90.6  54.9 143.1 127.3 151.5  57.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  56   OD1                                                    
REMARK 620 2 ASP F  58   OD1  74.5                                              
REMARK 620 3 ASP F  58   OD2 128.3  54.9                                        
REMARK 620 4 ASN F  60   OD1  69.0  83.4  93.2                                  
REMARK 620 5 THR F  62   O    94.2 135.5 113.3  52.9                            
REMARK 620 6 GLU F  67   OE1 101.9 129.2 117.2 144.0  95.0                      
REMARK 620 7 GLU F  67   OE2 110.6  78.4  71.8 160.9 143.6  55.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  93   OD1                                                    
REMARK 620 2 ASP F  95   OD1  55.9                                              
REMARK 620 3 ASN F  97   OD1  49.5  77.2                                        
REMARK 620 4 TYR F  99   O    85.5 139.4  67.1                                  
REMARK 620 5 GLU F 104   OE1 124.7 118.5 158.3  92.5                            
REMARK 620 6 GLU F 104   OE2 112.0  67.7 143.7 148.9  56.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  20   OD1                                                    
REMARK 620 2 ASP G  22   OD1  51.7                                              
REMARK 620 3 ASP G  24   OD1  59.0  88.6                                        
REMARK 620 4 ASP G  24   OD2 119.8 109.1  65.1                                  
REMARK 620 5 THR G  26   O    82.8 132.4  51.6  79.5                            
REMARK 620 6 GLU G  31   OE1 108.7 107.0 147.6 130.8  99.5                      
REMARK 620 7 GLU G  31   OE2  91.0  54.8 143.2 125.8 152.8  57.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  56   OD1                                                    
REMARK 620 2 ASP G  58   OD1  74.8                                              
REMARK 620 3 ASP G  58   OD2 128.9  55.2                                        
REMARK 620 4 ASN G  60   OD1  69.2  83.8  93.6                                  
REMARK 620 5 THR G  62   O    94.2 136.0 113.5  52.9                            
REMARK 620 6 GLU G  67   OE1 101.7 129.2 117.0 143.5  94.6                      
REMARK 620 7 GLU G  67   OE2 110.7  78.6  71.9 161.6 143.0  54.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  93   OD1                                                    
REMARK 620 2 ASP G  95   OD1  56.0                                              
REMARK 620 3 ASN G  97   OD1  49.6  77.5                                        
REMARK 620 4 TYR G  99   O    85.4 139.5  67.1                                  
REMARK 620 5 GLU G 104   OE1 124.3 118.4 157.8  92.1                            
REMARK 620 6 GLU G 104   OE2 112.0  67.8 144.2 148.4  56.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  20   OD1                                                    
REMARK 620 2 ASP H  22   OD1  52.2                                              
REMARK 620 3 ASP H  24   OD1  60.3  89.5                                        
REMARK 620 4 ASP H  24   OD2 121.2 108.4  65.6                                  
REMARK 620 5 THR H  26   O    84.7 134.7  52.7  80.3                            
REMARK 620 6 GLU H  31   OE1 109.7 106.4 150.0 128.8 100.3                      
REMARK 620 7 GLU H  31   OE2  91.3  54.3 143.8 123.1 153.7  56.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  56   OD1                                                    
REMARK 620 2 ASP H  58   OD1  76.0                                              
REMARK 620 3 ASP H  58   OD2 130.3  55.7                                        
REMARK 620 4 ASN H  60   OD1  69.0  84.0  93.1                                  
REMARK 620 5 THR H  62   O    93.2 134.9 111.8  51.8                            
REMARK 620 6 GLU H  67   OE1 102.3 131.8 117.5 141.5  93.2                      
REMARK 620 7 GLU H  67   OE2 112.8  80.4  72.8 163.1 141.8  55.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 203  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  93   OD1                                                    
REMARK 620 2 ASP H  95   OD1  56.1                                              
REMARK 620 3 ASN H  97   OD1  50.5  78.1                                        
REMARK 620 4 TYR H  99   O    87.4 141.9  69.2                                  
REMARK 620 5 GLU H 104   OE1 123.8 115.8 160.1  92.4                            
REMARK 620 6 GLU H 104   OE2 110.5  66.2 143.2 147.4  55.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 203                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-7539   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX IN     
REMARK 900 THE CA2+ BOUND STATE II                                              
REMARK 900 RELATED ID: EMD-7537   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX        
REMARK 900 RELATED ID: EMD-7538   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX IN     
REMARK 900 THE CA2+ BOUND STATE I                                               
DBREF  6CNO A    1   427  UNP    O15554   KCNN4_HUMAN      1    427             
DBREF  6CNO B    1   427  UNP    O15554   KCNN4_HUMAN      1    427             
DBREF  6CNO C    1   427  UNP    O15554   KCNN4_HUMAN      1    427             
DBREF  6CNO D    1   427  UNP    O15554   KCNN4_HUMAN      1    427             
DBREF  6CNO E    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6CNO F    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6CNO G    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
DBREF  6CNO H    0   148  UNP    P0DP23   CALM1_HUMAN      1    149             
SEQRES   1 A  427  MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG          
SEQRES   2 A  427  ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA          
SEQRES   3 A  427  GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU          
SEQRES   4 A  427  MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS          
SEQRES   5 A  427  SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE          
SEQRES   6 A  427  SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA          
SEQRES   7 A  427  PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN          
SEQRES   8 A  427  GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN          
SEQRES   9 A  427  ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU          
SEQRES  10 A  427  HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP          
SEQRES  11 A  427  LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY          
SEQRES  12 A  427  PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET          
SEQRES  13 A  427  LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU          
SEQRES  14 A  427  ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE          
SEQRES  15 A  427  GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL          
SEQRES  16 A  427  ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU          
SEQRES  17 A  427  LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP          
SEQRES  18 A  427  VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR          
SEQRES  19 A  427  GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR          
SEQRES  20 A  427  PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR          
SEQRES  21 A  427  MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET          
SEQRES  22 A  427  GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA          
SEQRES  23 A  427  ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS          
SEQRES  24 A  427  ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS          
SEQRES  25 A  427  GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE          
SEQRES  26 A  427  TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG          
SEQRES  27 A  427  ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE          
SEQRES  28 A  427  ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN          
SEQRES  29 A  427  VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE          
SEQRES  30 A  427  LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG          
SEQRES  31 A  427  ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU          
SEQRES  32 A  427  ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO          
SEQRES  33 A  427  ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS                  
SEQRES   1 B  427  MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG          
SEQRES   2 B  427  ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA          
SEQRES   3 B  427  GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU          
SEQRES   4 B  427  MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS          
SEQRES   5 B  427  SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE          
SEQRES   6 B  427  SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA          
SEQRES   7 B  427  PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN          
SEQRES   8 B  427  GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN          
SEQRES   9 B  427  ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU          
SEQRES  10 B  427  HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP          
SEQRES  11 B  427  LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY          
SEQRES  12 B  427  PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET          
SEQRES  13 B  427  LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU          
SEQRES  14 B  427  ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE          
SEQRES  15 B  427  GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL          
SEQRES  16 B  427  ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU          
SEQRES  17 B  427  LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP          
SEQRES  18 B  427  VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR          
SEQRES  19 B  427  GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR          
SEQRES  20 B  427  PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR          
SEQRES  21 B  427  MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET          
SEQRES  22 B  427  GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA          
SEQRES  23 B  427  ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS          
SEQRES  24 B  427  ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS          
SEQRES  25 B  427  GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE          
SEQRES  26 B  427  TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG          
SEQRES  27 B  427  ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE          
SEQRES  28 B  427  ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN          
SEQRES  29 B  427  VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE          
SEQRES  30 B  427  LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG          
SEQRES  31 B  427  ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU          
SEQRES  32 B  427  ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO          
SEQRES  33 B  427  ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS                  
SEQRES   1 C  427  MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG          
SEQRES   2 C  427  ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA          
SEQRES   3 C  427  GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU          
SEQRES   4 C  427  MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS          
SEQRES   5 C  427  SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE          
SEQRES   6 C  427  SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA          
SEQRES   7 C  427  PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN          
SEQRES   8 C  427  GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN          
SEQRES   9 C  427  ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU          
SEQRES  10 C  427  HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP          
SEQRES  11 C  427  LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY          
SEQRES  12 C  427  PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET          
SEQRES  13 C  427  LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU          
SEQRES  14 C  427  ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE          
SEQRES  15 C  427  GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL          
SEQRES  16 C  427  ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU          
SEQRES  17 C  427  LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP          
SEQRES  18 C  427  VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR          
SEQRES  19 C  427  GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR          
SEQRES  20 C  427  PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR          
SEQRES  21 C  427  MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET          
SEQRES  22 C  427  GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA          
SEQRES  23 C  427  ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS          
SEQRES  24 C  427  ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS          
SEQRES  25 C  427  GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE          
SEQRES  26 C  427  TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG          
SEQRES  27 C  427  ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE          
SEQRES  28 C  427  ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN          
SEQRES  29 C  427  VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE          
SEQRES  30 C  427  LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG          
SEQRES  31 C  427  ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU          
SEQRES  32 C  427  ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO          
SEQRES  33 C  427  ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS                  
SEQRES   1 D  427  MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG          
SEQRES   2 D  427  ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA          
SEQRES   3 D  427  GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU          
SEQRES   4 D  427  MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS          
SEQRES   5 D  427  SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE          
SEQRES   6 D  427  SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA          
SEQRES   7 D  427  PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN          
SEQRES   8 D  427  GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN          
SEQRES   9 D  427  ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU          
SEQRES  10 D  427  HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP          
SEQRES  11 D  427  LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY          
SEQRES  12 D  427  PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET          
SEQRES  13 D  427  LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU          
SEQRES  14 D  427  ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE          
SEQRES  15 D  427  GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL          
SEQRES  16 D  427  ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU          
SEQRES  17 D  427  LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP          
SEQRES  18 D  427  VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR          
SEQRES  19 D  427  GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR          
SEQRES  20 D  427  PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR          
SEQRES  21 D  427  MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET          
SEQRES  22 D  427  GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA          
SEQRES  23 D  427  ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS          
SEQRES  24 D  427  ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS          
SEQRES  25 D  427  GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE          
SEQRES  26 D  427  TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG          
SEQRES  27 D  427  ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE          
SEQRES  28 D  427  ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN          
SEQRES  29 D  427  VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE          
SEQRES  30 D  427  LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG          
SEQRES  31 D  427  ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU          
SEQRES  32 D  427  ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO          
SEQRES  33 D  427  ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS                  
SEQRES   1 E  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 E  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 E  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 E  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 E  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 E  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 E  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 E  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 E  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 E  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 E  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 E  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 F  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 F  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 F  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 F  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 F  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 F  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 F  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 F  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 F  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 F  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 F  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 F  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 G  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 G  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 G  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 G  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 G  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 G  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 G  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 G  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 G  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 G  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 G  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 G  149  GLN MET MET THR ALA LYS                                      
SEQRES   1 H  149  MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE          
SEQRES   2 H  149  LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY          
SEQRES   3 H  149  THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER          
SEQRES   4 H  149  LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET          
SEQRES   5 H  149  ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP          
SEQRES   6 H  149  PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS          
SEQRES   7 H  149  ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG          
SEQRES   8 H  149  VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA          
SEQRES   9 H  149  GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU          
SEQRES  10 H  149  THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP          
SEQRES  11 H  149  ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL          
SEQRES  12 H  149  GLN MET MET THR ALA LYS                                      
HET     CA  E 201       1                                                       
HET     CA  E 202       1                                                       
HET     CA  E 203       1                                                       
HET     CA  F 201       1                                                       
HET     CA  F 202       1                                                       
HET     CA  F 203       1                                                       
HET     CA  G 201       1                                                       
HET     CA  G 202       1                                                       
HET     CA  G 203       1                                                       
HET     CA  H 201       1                                                       
HET     CA  H 202       1                                                       
HET     CA  H 203       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   9   CA    12(CA 2+)                                                    
HELIX    1   1 LEU A    9  PHE A   49  1                                  41    
HELIX    2   2 ALA A   55  ASN A   91  1                                  37    
HELIX    3   3 GLY A  102  CYS A  115  1                                  14    
HELIX    4   4 GLN A  147  ALA A  155  1                                   9    
HELIX    5   5 MET A  156  LEU A  162  5                                   7    
HELIX    6   6 VAL A  163  ARG A  170  1                                   8    
HELIX    7   7 ALA A  177  ASN A  186  1                                  10    
HELIX    8   8 HIS A  192  THR A  202  1                                  11    
HELIX    9   9 GLY A  205  GLU A  227  1                                  23    
HELIX   10  10 LEU A  237  LEU A  249  1                                  13    
HELIX   11  11 MET A  261  LEU A  289  1                                  29    
HELIX   12  12 LYS A  293  ARG A  331  1                                  39    
HELIX   13  13 SER A  334  SER A  367  1                                  34    
HELIX   14  14 ASP A  370  SER A  386  1                                  17    
HELIX   15  15 LEU B    9  PHE B   49  1                                  41    
HELIX   16  16 ALA B   55  ASN B   91  1                                  37    
HELIX   17  17 GLY B  102  CYS B  115  1                                  14    
HELIX   18  18 GLN B  147  ALA B  155  1                                   9    
HELIX   19  19 MET B  156  LEU B  162  5                                   7    
HELIX   20  20 VAL B  163  ARG B  170  1                                   8    
HELIX   21  21 ALA B  177  ASN B  186  1                                  10    
HELIX   22  22 HIS B  192  THR B  202  1                                  11    
HELIX   23  23 GLY B  205  GLU B  227  1                                  23    
HELIX   24  24 LEU B  237  LEU B  249  1                                  13    
HELIX   25  25 MET B  261  LEU B  289  1                                  29    
HELIX   26  26 LYS B  293  ARG B  331  1                                  39    
HELIX   27  27 SER B  334  SER B  367  1                                  34    
HELIX   28  28 ASP B  370  SER B  386  1                                  17    
HELIX   29  29 LEU C    9  PHE C   49  1                                  41    
HELIX   30  30 ALA C   55  ASN C   91  1                                  37    
HELIX   31  31 GLY C  102  CYS C  115  1                                  14    
HELIX   32  32 GLN C  147  ALA C  155  1                                   9    
HELIX   33  33 MET C  156  LEU C  162  5                                   7    
HELIX   34  34 VAL C  163  ARG C  170  1                                   8    
HELIX   35  35 ALA C  177  ASN C  186  1                                  10    
HELIX   36  36 HIS C  192  THR C  202  1                                  11    
HELIX   37  37 GLY C  205  GLU C  227  1                                  23    
HELIX   38  38 LEU C  237  LEU C  249  1                                  13    
HELIX   39  39 MET C  261  LEU C  289  1                                  29    
HELIX   40  40 LYS C  293  ARG C  331  1                                  39    
HELIX   41  41 SER C  334  SER C  367  1                                  34    
HELIX   42  42 ASP C  370  SER C  386  1                                  17    
HELIX   43  43 LEU D    9  PHE D   49  1                                  41    
HELIX   44  44 ALA D   55  ASN D   91  1                                  37    
HELIX   45  45 GLY D  102  CYS D  115  1                                  14    
HELIX   46  46 GLN D  147  ALA D  155  1                                   9    
HELIX   47  47 MET D  156  LEU D  162  5                                   7    
HELIX   48  48 VAL D  163  ARG D  170  1                                   8    
HELIX   49  49 ALA D  177  ASN D  186  1                                  10    
HELIX   50  50 HIS D  192  THR D  202  1                                  11    
HELIX   51  51 GLY D  205  GLU D  227  1                                  23    
HELIX   52  52 LEU D  237  LEU D  249  1                                  13    
HELIX   53  53 MET D  261  LEU D  289  1                                  29    
HELIX   54  54 LYS D  293  ARG D  331  1                                  39    
HELIX   55  55 SER D  334  SER D  367  1                                  34    
HELIX   56  56 ASP D  370  SER D  386  1                                  17    
HELIX   57  57 GLU E    6  ASP E   20  1                                  15    
HELIX   58  58 THR E   29  LEU E   39  1                                  11    
HELIX   59  59 THR E   44  VAL E   55  1                                  12    
HELIX   60  60 PHE E   65  ARG E   74  1                                  10    
HELIX   61  61 SER E   81  PHE E   92  1                                  12    
HELIX   62  62 ALA E  102  THR E  110  1                                   9    
HELIX   63  63 THR E  117  ASP E  129  1                                  13    
HELIX   64  64 TYR E  138  ALA E  147  1                                  10    
HELIX   65  65 GLU F    6  ASP F   20  1                                  15    
HELIX   66  66 THR F   29  LEU F   39  1                                  11    
HELIX   67  67 THR F   44  VAL F   55  1                                  12    
HELIX   68  68 PHE F   65  ARG F   74  1                                  10    
HELIX   69  69 SER F   81  PHE F   92  1                                  12    
HELIX   70  70 ALA F  102  THR F  110  1                                   9    
HELIX   71  71 THR F  117  ASP F  129  1                                  13    
HELIX   72  72 TYR F  138  ALA F  147  1                                  10    
HELIX   73  73 GLU G    6  ASP G   20  1                                  15    
HELIX   74  74 THR G   29  LEU G   39  1                                  11    
HELIX   75  75 THR G   44  VAL G   55  1                                  12    
HELIX   76  76 PHE G   65  ARG G   74  1                                  10    
HELIX   77  77 SER G   81  PHE G   92  1                                  12    
HELIX   78  78 ALA G  102  THR G  110  1                                   9    
HELIX   79  79 THR G  117  ASP G  129  1                                  13    
HELIX   80  80 TYR G  138  ALA G  147  1                                  10    
HELIX   81  81 GLU H    6  ASP H   20  1                                  15    
HELIX   82  82 THR H   29  LEU H   39  1                                  11    
HELIX   83  83 THR H   44  VAL H   55  1                                  12    
HELIX   84  84 PHE H   65  ARG H   74  1                                  10    
HELIX   85  85 SER H   81  PHE H   92  1                                  12    
HELIX   86  86 ALA H  102  THR H  110  1                                   9    
HELIX   87  87 THR H  117  ASP H  129  1                                  13    
HELIX   88  88 TYR H  138  ALA H  147  1                                  10    
SHEET    1   A 2 THR E  26  ILE E  27  0                                        
SHEET    2   A 2 ILE E  63  ASP E  64 -1  O  ILE E  63   N  ILE E  27           
SHEET    1   B 2 TYR E  99  SER E 101  0                                        
SHEET    2   B 2 GLN E 135  ASN E 137 -1  O  VAL E 136   N  ILE E 100           
SHEET    1   C 2 THR F  26  ILE F  27  0                                        
SHEET    2   C 2 ILE F  63  ASP F  64 -1  O  ILE F  63   N  ILE F  27           
SHEET    1   D 2 TYR F  99  SER F 101  0                                        
SHEET    2   D 2 GLN F 135  ASN F 137 -1  O  VAL F 136   N  ILE F 100           
SHEET    1   E 2 THR G  26  ILE G  27  0                                        
SHEET    2   E 2 ILE G  63  ASP G  64 -1  O  ILE G  63   N  ILE G  27           
SHEET    1   F 2 TYR G  99  SER G 101  0                                        
SHEET    2   F 2 GLN G 135  ASN G 137 -1  O  VAL G 136   N  ILE G 100           
SHEET    1   G 2 THR H  26  ILE H  27  0                                        
SHEET    2   G 2 ILE H  63  ASP H  64 -1  O  ILE H  63   N  ILE H  27           
SHEET    1   H 2 TYR H  99  SER H 101  0                                        
SHEET    2   H 2 GLN H 135  ASN H 137 -1  O  VAL H 136   N  ILE H 100           
LINK         OD1 ASP E  20                CA    CA E 201     1555   1555  2.31  
LINK         OD1 ASP E  22                CA    CA E 201     1555   1555  2.43  
LINK         OD1 ASP E  24                CA    CA E 201     1555   1555  2.12  
LINK         OD2 ASP E  24                CA    CA E 201     1555   1555  1.97  
LINK         O   THR E  26                CA    CA E 201     1555   1555  2.43  
LINK         OE1 GLU E  31                CA    CA E 201     1555   1555  2.31  
LINK         OE2 GLU E  31                CA    CA E 201     1555   1555  2.25  
LINK         OD1 ASP E  56                CA    CA E 202     1555   1555  2.45  
LINK         OD1 ASP E  58                CA    CA E 202     1555   1555  2.10  
LINK         OD2 ASP E  58                CA    CA E 202     1555   1555  2.53  
LINK         OD1 ASN E  60                CA    CA E 202     1555   1555  2.29  
LINK         O   THR E  62                CA    CA E 202     1555   1555  2.43  
LINK         OE1 GLU E  67                CA    CA E 202     1555   1555  2.41  
LINK         OE2 GLU E  67                CA    CA E 202     1555   1555  2.36  
LINK         OD1 ASP E  93                CA    CA E 203     1555   1555  2.38  
LINK         OD1 ASP E  95                CA    CA E 203     1555   1555  2.31  
LINK         OD1 ASN E  97                CA    CA E 203     1555   1555  2.21  
LINK         O   TYR E  99                CA    CA E 203     1555   1555  2.16  
LINK         OE1 GLU E 104                CA    CA E 203     1555   1555  2.36  
LINK         OE2 GLU E 104                CA    CA E 203     1555   1555  2.27  
LINK         OD1 ASP F  20                CA    CA F 201     1555   1555  2.33  
LINK         OD1 ASP F  22                CA    CA F 201     1555   1555  2.43  
LINK         OD1 ASP F  24                CA    CA F 201     1555   1555  2.12  
LINK         OD2 ASP F  24                CA    CA F 201     1555   1555  1.94  
LINK         O   THR F  26                CA    CA F 201     1555   1555  2.45  
LINK         OE1 GLU F  31                CA    CA F 201     1555   1555  2.33  
LINK         OE2 GLU F  31                CA    CA F 201     1555   1555  2.25  
LINK         OD1 ASP F  56                CA    CA F 202     1555   1555  2.45  
LINK         OD1 ASP F  58                CA    CA F 202     1555   1555  2.10  
LINK         OD2 ASP F  58                CA    CA F 202     1555   1555  2.53  
LINK         OD1 ASN F  60                CA    CA F 202     1555   1555  2.30  
LINK         O   THR F  62                CA    CA F 202     1555   1555  2.44  
LINK         OE1 GLU F  67                CA    CA F 202     1555   1555  2.40  
LINK         OE2 GLU F  67                CA    CA F 202     1555   1555  2.35  
LINK         OD1 ASP F  93                CA    CA F 203     1555   1555  2.39  
LINK         OD1 ASP F  95                CA    CA F 203     1555   1555  2.32  
LINK         OD1 ASN F  97                CA    CA F 203     1555   1555  2.22  
LINK         O   TYR F  99                CA    CA F 203     1555   1555  2.15  
LINK         OE1 GLU F 104                CA    CA F 203     1555   1555  2.35  
LINK         OE2 GLU F 104                CA    CA F 203     1555   1555  2.27  
LINK         OD1 ASP G  20                CA    CA G 201     1555   1555  2.31  
LINK         OD1 ASP G  22                CA    CA G 201     1555   1555  2.44  
LINK         OD1 ASP G  24                CA    CA G 201     1555   1555  2.12  
LINK         OD2 ASP G  24                CA    CA G 201     1555   1555  1.96  
LINK         O   THR G  26                CA    CA G 201     1555   1555  2.43  
LINK         OE1 GLU G  31                CA    CA G 201     1555   1555  2.31  
LINK         OE2 GLU G  31                CA    CA G 201     1555   1555  2.25  
LINK         OD1 ASP G  56                CA    CA G 202     1555   1555  2.45  
LINK         OD1 ASP G  58                CA    CA G 202     1555   1555  2.08  
LINK         OD2 ASP G  58                CA    CA G 202     1555   1555  2.52  
LINK         OD1 ASN G  60                CA    CA G 202     1555   1555  2.29  
LINK         O   THR G  62                CA    CA G 202     1555   1555  2.45  
LINK         OE1 GLU G  67                CA    CA G 202     1555   1555  2.41  
LINK         OE2 GLU G  67                CA    CA G 202     1555   1555  2.35  
LINK         OD1 ASP G  93                CA    CA G 203     1555   1555  2.39  
LINK         OD1 ASP G  95                CA    CA G 203     1555   1555  2.32  
LINK         OD1 ASN G  97                CA    CA G 203     1555   1555  2.21  
LINK         O   TYR G  99                CA    CA G 203     1555   1555  2.15  
LINK         OE1 GLU G 104                CA    CA G 203     1555   1555  2.36  
LINK         OE2 GLU G 104                CA    CA G 203     1555   1555  2.27  
LINK         OD1 ASP H  20                CA    CA H 201     1555   1555  2.27  
LINK         OD1 ASP H  22                CA    CA H 201     1555   1555  2.44  
LINK         OD1 ASP H  24                CA    CA H 201     1555   1555  2.08  
LINK         OD2 ASP H  24                CA    CA H 201     1555   1555  1.98  
LINK         O   THR H  26                CA    CA H 201     1555   1555  2.38  
LINK         OE1 GLU H  31                CA    CA H 201     1555   1555  2.33  
LINK         OE2 GLU H  31                CA    CA H 201     1555   1555  2.29  
LINK         OD1 ASP H  56                CA    CA H 202     1555   1555  2.43  
LINK         OD1 ASP H  58                CA    CA H 202     1555   1555  2.04  
LINK         OD2 ASP H  58                CA    CA H 202     1555   1555  2.51  
LINK         OD1 ASN H  60                CA    CA H 202     1555   1555  2.32  
LINK         O   THR H  62                CA    CA H 202     1555   1555  2.50  
LINK         OE1 GLU H  67                CA    CA H 202     1555   1555  2.41  
LINK         OE2 GLU H  67                CA    CA H 202     1555   1555  2.31  
LINK         OD1 ASP H  93                CA    CA H 203     1555   1555  2.36  
LINK         OD1 ASP H  95                CA    CA H 203     1555   1555  2.34  
LINK         OD1 ASN H  97                CA    CA H 203     1555   1555  2.15  
LINK         O   TYR H  99                CA    CA H 203     1555   1555  2.09  
LINK         OE1 GLU H 104                CA    CA H 203     1555   1555  2.40  
LINK         OE2 GLU H 104                CA    CA H 203     1555   1555  2.34  
SITE     1 AC1  5 ASP E  20  ASP E  22  ASP E  24  THR E  26                    
SITE     2 AC1  5 GLU E  31                                                     
SITE     1 AC2  5 ASP E  56  ASP E  58  ASN E  60  THR E  62                    
SITE     2 AC2  5 GLU E  67                                                     
SITE     1 AC3  5 ASP E  93  ASP E  95  ASN E  97  TYR E  99                    
SITE     2 AC3  5 GLU E 104                                                     
SITE     1 AC4  5 ASP F  20  ASP F  22  ASP F  24  THR F  26                    
SITE     2 AC4  5 GLU F  31                                                     
SITE     1 AC5  5 ASP F  56  ASP F  58  ASN F  60  THR F  62                    
SITE     2 AC5  5 GLU F  67                                                     
SITE     1 AC6  5 ASP F  93  ASP F  95  ASN F  97  TYR F  99                    
SITE     2 AC6  5 GLU F 104                                                     
SITE     1 AC7  5 ASP G  20  ASP G  22  ASP G  24  THR G  26                    
SITE     2 AC7  5 GLU G  31                                                     
SITE     1 AC8  5 ASP G  56  ASP G  58  ASN G  60  THR G  62                    
SITE     2 AC8  5 GLU G  67                                                     
SITE     1 AC9  5 ASP G  93  ASP G  95  ASN G  97  TYR G  99                    
SITE     2 AC9  5 GLU G 104                                                     
SITE     1 AD1  5 ASP H  20  ASP H  22  ASP H  24  THR H  26                    
SITE     2 AD1  5 GLU H  31                                                     
SITE     1 AD2  5 ASP H  56  ASP H  58  ASN H  60  THR H  62                    
SITE     2 AD2  5 GLU H  67                                                     
SITE     1 AD3  5 ASP H  93  ASP H  95  ASN H  97  TYR H  99                    
SITE     2 AD3  5 GLU H 104                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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