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Database: PDB
Entry: 5KUM
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HEADER    METAL TRANSPORT                         13-JUL-16   5KUM              
TITLE     CRYSTAL STRUCTURE OF INWARD RECTIFIER KIR2.2 K62W MUTANT IN COMPLEX   
TITLE    2 WITH PIP2                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 12;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 38-369;                                       
COMPND   5 SYNONYM: INWARD RECTIFIER K(+) CHANNEL KIR2.2,POTASSIUM CHANNEL,     
COMPND   6 INWARDLY RECTIFYING SUBFAMILY J MEMBER 12;                           
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 GENE: KCNJ12;                                                        
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    METAL TRANSPORT, KIR 2.2 K62W MUTANT STRUCTURE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-J.LEE,F.REN,S.HEYMAN,P.YUAN,C.G.NICHOLS                            
REVDAT   3   07-SEP-16 5KUM    1       JRNL                                     
REVDAT   2   31-AUG-16 5KUM    1       JRNL                                     
REVDAT   1   10-AUG-16 5KUM    0                                                
JRNL        AUTH   S.J.LEE,F.REN,E.M.ZANGERL-PLESSL,S.HEYMAN,                   
JRNL        AUTH 2 A.STARY-WEINZINGER,P.YUAN,C.G.NICHOLS                        
JRNL        TITL   STRUCTURAL BASIS OF CONTROL OF INWARD RECTIFIER KIR2 CHANNEL 
JRNL        TITL 2 GATING BY BULK ANIONIC PHOSPHOLIPIDS.                        
JRNL        REF    J.GEN.PHYSIOL.                V. 148   227 2016              
JRNL        REFN                   ESSN 1540-7748                               
JRNL        PMID   27527100                                                     
JRNL        DOI    10.1085/JGP.201611616                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 13843                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 713                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1029                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2612                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 38                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.37000                                              
REMARK   3    B22 (A**2) : 4.37000                                              
REMARK   3    B33 (A**2) : -8.74000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.535         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.326         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.306         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.573        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2725 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2582 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3703 ; 1.444 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5930 ; 0.758 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   325 ; 7.164 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;36.124 ;23.548       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   459 ;15.859 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;15.203 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   425 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2995 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   639 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1303 ; 4.309 ; 7.248       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1302 ; 4.298 ; 7.246       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1627 ; 6.696 ;10.866       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1628 ; 6.694 ;10.870       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1422 ; 4.292 ; 7.919       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1423 ; 4.292 ; 7.920       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2077 ; 7.035 ;11.722       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3167 ;10.196 ;58.802       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3162 ;10.147 ;58.829       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5KUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222772.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 6.3-6.8                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14556                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.670                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5KUK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, KCL, PEG 400, EVAPORATION,        
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       40.65150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.65150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       91.78600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       40.65150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.65150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       91.78600            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       40.65150            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       40.65150            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       91.78600            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       40.65150            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       40.65150            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       91.78600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 30410 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 54460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -166.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 K      K A 402  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 403  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 404  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 405  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 406  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 407  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 408  LIES ON A SPECIAL POSITION.                          
REMARK 375 K      K A 409  LIES ON A SPECIAL POSITION.                          
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    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     ARG A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     PHE A   367                                                      
REMARK 465     LEU A   368                                                      
REMARK 465     LEU A   369                                                      
REMARK 465     SER A   370                                                      
REMARK 465     ASN A   371                                                      
REMARK 465     SER A   372                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     GLU A   374                                                      
REMARK 465     VAL A   375                                                      
REMARK 465     LEU A   376                                                      
REMARK 465     PHE A   377                                                      
REMARK 465     GLN A   378                                                      
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     LYS A 335    CG   CD   CE   NZ                                   
REMARK 470     GLU A 364    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 366    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  53       52.63   -116.58                                   
REMARK 500    ASP A  69       53.41   -110.88                                   
REMARK 500    ASN A 113       77.24   -117.98                                   
REMARK 500    PHE A 120      118.52   -163.92                                   
REMARK 500    ALA A 203      171.04    178.31                                   
REMARK 500    VAL A 265      -79.47   -103.11                                   
REMARK 500    SER A 319       -3.20    -59.34                                   
REMARK 500    SER A 353       -6.07    -59.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A   58     MET A   59                  147.48                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PIO A  401                                                       
REMARK 610     DMU A  410                                                       
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                               K A 404   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 143   O                                                      
REMARK 620 2 ILE A 144   O    69.8                                              
REMARK 620 3 THR A 143   O     0.0  69.8                                        
REMARK 620 4 ILE A 144   O    69.8   0.0  69.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 405   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 143   O                                                      
REMARK 620 2 THR A 143   OG1  56.4                                              
REMARK 620 3 THR A 143   O     0.0  56.4                                        
REMARK 620 4 THR A 143   OG1  56.4   0.0  56.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 403   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE A 144   O                                                      
REMARK 620 2 GLY A 145   O    64.5                                              
REMARK 620 3 ILE A 144   O     0.0  64.5                                        
REMARK 620 4 GLY A 145   O    64.5   0.0  64.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 402   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 145   O                                                      
REMARK 620 2 TYR A 146   O    70.6                                              
REMARK 620 3 GLY A 145   O     0.0  70.6                                        
REMARK 620 4 TYR A 146   O    70.6   0.0  70.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PIO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 402                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 403                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 404                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 405                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMU A 410                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KUK   RELATED DB: PDB                                   
DBREF  5KUM A   38   369  UNP    F1NHE9   KCJ12_CHICK     38    369             
SEQADV 5KUM MET A   36  UNP  F1NHE9              INITIATING METHIONINE          
SEQADV 5KUM ALA A   37  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM TRP A   62  UNP  F1NHE9    LYS    62 ENGINEERED MUTATION            
SEQADV 5KUM SER A  370  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM ASN A  371  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM SER A  372  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM LEU A  373  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM GLU A  374  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM VAL A  375  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM LEU A  376  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM PHE A  377  UNP  F1NHE9              EXPRESSION TAG                 
SEQADV 5KUM GLN A  378  UNP  F1NHE9              EXPRESSION TAG                 
SEQRES   1 A  343  MET ALA ARG ARG LYS CYS ARG ASN ARG PHE VAL LYS LYS          
SEQRES   2 A  343  ASN GLY GLN CYS ASN VAL GLU PHE THR ASN MET ASP ASP          
SEQRES   3 A  343  TRP PRO GLN ARG TYR ILE ALA ASP MET PHE THR THR CYS          
SEQRES   4 A  343  VAL ASP ILE ARG TRP ARG TYR MET LEU LEU LEU PHE SER          
SEQRES   5 A  343  LEU ALA PHE LEU VAL SER TRP LEU LEU PHE GLY LEU ILE          
SEQRES   6 A  343  PHE TRP LEU ILE ALA LEU ILE HIS GLY ASP LEU GLU ASN          
SEQRES   7 A  343  PRO GLY GLY ASP ASP THR PHE LYS PRO CYS VAL LEU GLN          
SEQRES   8 A  343  VAL ASN GLY PHE VAL ALA ALA PHE LEU PHE SER ILE GLU          
SEQRES   9 A  343  THR GLN THR THR ILE GLY TYR GLY PHE ARG CYS VAL THR          
SEQRES  10 A  343  GLU GLU CYS PRO LEU ALA VAL PHE MET VAL VAL VAL GLN          
SEQRES  11 A  343  SER ILE VAL GLY CYS ILE ILE ASP SER PHE MET ILE GLY          
SEQRES  12 A  343  ALA ILE MET ALA LYS MET ALA ARG PRO LYS LYS ARG ALA          
SEQRES  13 A  343  GLN THR LEU LEU PHE SER HIS ASN ALA VAL VAL ALA MET          
SEQRES  14 A  343  ARG ASP GLY LYS LEU CYS LEU MET TRP ARG VAL GLY ASN          
SEQRES  15 A  343  LEU ARG LYS SER HIS ILE VAL GLU ALA HIS VAL ARG ALA          
SEQRES  16 A  343  GLN LEU ILE LYS PRO ARG ILE THR GLU GLU GLY GLU TYR          
SEQRES  17 A  343  ILE PRO LEU ASP GLN ILE ASP ILE ASP VAL GLY PHE ASP          
SEQRES  18 A  343  LYS GLY LEU ASP ARG ILE PHE LEU VAL SER PRO ILE THR          
SEQRES  19 A  343  ILE LEU HIS GLU ILE ASN GLU ASP SER PRO LEU PHE GLY          
SEQRES  20 A  343  ILE SER ARG GLN ASP LEU GLU THR ASP ASP PHE GLU ILE          
SEQRES  21 A  343  VAL VAL ILE LEU GLU GLY MET VAL GLU ALA THR ALA MET          
SEQRES  22 A  343  THR THR GLN ALA ARG SER SER TYR LEU ALA SER GLU ILE          
SEQRES  23 A  343  LEU TRP GLY HIS ARG PHE GLU PRO VAL LEU PHE GLU GLU          
SEQRES  24 A  343  LYS ASN GLN TYR LYS VAL ASP TYR SER HIS PHE HIS LYS          
SEQRES  25 A  343  THR TYR GLU VAL PRO SER THR PRO ARG CYS SER ALA LYS          
SEQRES  26 A  343  ASP LEU VAL GLU ASN LYS PHE LEU LEU SER ASN SER LEU          
SEQRES  27 A  343  GLU VAL LEU PHE GLN                                          
HET    PIO  A 401      26                                                       
HET      K  A 402       1                                                       
HET      K  A 403       1                                                       
HET      K  A 404       1                                                       
HET      K  A 405       1                                                       
HET      K  A 406       1                                                       
HET      K  A 407       1                                                       
HET      K  A 408       1                                                       
HET      K  A 409       1                                                       
HET    DMU  A 410      24                                                       
HETNAM     PIO [(2R)-2-OCTANOYLOXY-3-[OXIDANYL-[(1R,2R,3S,4R,5R,6S)-2,          
HETNAM   2 PIO  3,6-TRIS(OXIDANYL)-4,5-DIPHOSPHONOOXY-CYCLOHEXYL]OXY-           
HETNAM   3 PIO  PHOSPHORYL]OXY-PROPYL] OCTANOATE                                
HETNAM       K POTASSIUM ION                                                    
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE                                     
HETSYN     PIO DIOCTANOYL L-ALPHA-PHOSPHATIDYL-D-MYO-INOSITOL 4,5-              
HETSYN   2 PIO  DIPHOSPHATE                                                     
HETSYN     DMU DECYLMALTOSIDE                                                   
FORMUL   2  PIO    C25 H49 O19 P3                                               
FORMUL   3    K    8(K 1+)                                                      
FORMUL  11  DMU    C22 H42 O11                                                  
FORMUL  12  HOH   *38(H2 O)                                                     
HELIX    1 AA1 ASP A   61  ASP A   69  1                                   9    
HELIX    2 AA2 ASP A   69  ILE A   77  1                                   9    
HELIX    3 AA3 ARG A   78  GLY A  109  1                                  32    
HELIX    4 AA4 PHE A  130  THR A  142  1                                  13    
HELIX    5 AA5 CYS A  155  ARG A  186  1                                  32    
HELIX    6 AA6 PRO A  187  GLN A  192  5                                   6    
HELIX    7 AA7 GLY A  254  GLY A  258  5                                   5    
HELIX    8 AA8 SER A  284  ASP A  291  1                                   8    
HELIX    9 AA9 SER A  343  HIS A  346  5                                   4    
HELIX   10 AB1 SER A  358  LYS A  366  1                                   9    
SHEET    1 AA1 2 VAL A 124  LEU A 125  0                                        
SHEET    2 AA1 2 CYS A 150  VAL A 151 -1  O  CYS A 150   N  LEU A 125           
SHEET    1 AA2 3 LEU A 194  PHE A 196  0                                        
SHEET    2 AA2 3 LYS A 208  ASN A 217 -1  O  GLY A 216   N  LEU A 195           
SHEET    3 AA2 3 ILE A 268  GLU A 273 -1  O  ILE A 270   N  TRP A 213           
SHEET    1 AA3 4 LEU A 194  PHE A 196  0                                        
SHEET    2 AA3 4 LYS A 208  ASN A 217 -1  O  GLY A 216   N  LEU A 195           
SHEET    3 AA3 4 ALA A 200  ARG A 205 -1  N  ALA A 203   O  CYS A 210           
SHEET    4 AA3 4 ILE A 321  TRP A 323  1  O  LEU A 322   N  ALA A 200           
SHEET    1 AA4 4 TYR A 243  ASP A 250  0                                        
SHEET    2 AA4 4 ILE A 223  ILE A 237 -1  N  LEU A 232   O  ILE A 249           
SHEET    3 AA4 4 GLU A 294  VAL A 303 -1  O  GLU A 294   N  ILE A 233           
SHEET    4 AA4 4 MET A 308  LEU A 317 -1  O  THR A 310   N  GLY A 301           
SHEET    1 AA5 2 HIS A 325  PHE A 327  0                                        
SHEET    2 AA5 2 THR A 348  GLU A 350 -1  O  TYR A 349   N  ARG A 326           
SHEET    1 AA6 2 LEU A 331  GLU A 333  0                                        
SHEET    2 AA6 2 TYR A 338  VAL A 340 -1  O  LYS A 339   N  PHE A 332           
SSBOND   1 CYS A  123    CYS A  155                          1555   1555  2.04  
LINK         O   THR A 143                 K     K A 404     1555   1555  2.74  
LINK         O   THR A 143                 K     K A 405     1555   1555  2.75  
LINK         OG1 THR A 143                 K     K A 405     1555   1555  2.84  
LINK         O   ILE A 144                 K     K A 403     1555   1555  3.10  
LINK         O   ILE A 144                 K     K A 404     1555   1555  2.97  
LINK         O   GLY A 145                 K     K A 402     1555   1555  2.92  
LINK         O   GLY A 145                 K     K A 403     1555   1555  2.60  
LINK         O   TYR A 146                 K     K A 402     1555   1555  3.09  
LINK         O   THR A 143                 K     K A 404     1555   2555  2.74  
LINK         O   THR A 143                 K     K A 405     1555   2555  2.75  
LINK         OG1 THR A 143                 K     K A 405     1555   2555  2.84  
LINK         O   ILE A 144                 K     K A 403     1555   2555  3.10  
LINK         O   ILE A 144                 K     K A 404     1555   2555  2.97  
LINK         O   GLY A 145                 K     K A 402     1555   2555  2.92  
LINK         O   GLY A 145                 K     K A 403     1555   2555  2.60  
LINK         O   TYR A 146                 K     K A 402     1555   2555  3.09  
SITE     1 AC1  7 ARG A  78  TRP A  79  ARG A  80  LYS A 183                    
SITE     2 AC1  7 ARG A 186  LYS A 188  LYS A 189                               
SITE     1 AC2  3 GLY A 145  TYR A 146    K A 403                               
SITE     1 AC3  4 ILE A 144  GLY A 145    K A 402    K A 404                    
SITE     1 AC4  4 THR A 143  ILE A 144    K A 403    K A 405                    
SITE     1 AC5  2 THR A 143    K A 404                                          
SITE     1 AC6  6 PHE A  56  THR A  57  ASN A  58  MET A  59                    
SITE     2 AC6  6 TRP A  62  TYR A  66                                          
CRYST1   81.303   81.303  183.572  90.00  90.00  90.00 I 4           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012300  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005447        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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