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Database: PDB
Entry: 5IH4
LinkDB: 5IH4
Original site: 5IH4 
HEADER    TRANSFERASE                             29-FEB-16   5IH4              
TITLE     HUMAN CASEIN KINASE 1 ISOFORM DELTA APO (KINASE DOMAIN)               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CASEIN KINASE I ISOFORM DELTA;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CKID,TAU-PROTEIN KINASE CSNK1D;                             
COMPND   5 EC: 2.7.11.1,2.7.11.26;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: N-TERMINAL CLONING ARTIFACT: GP                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CSNK1D, HCKID;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: RIL (K+);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET19                                     
KEYWDS    KINASE DOMAIN, STEM CELL REPROGRAMMING, TRANSFERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.URSU,D.J.ILLICH,Y.TAKEMOTO,A.T.PORFETYE,M.ZHANG,A.BROCKMEYER,       
AUTHOR   2 P.JANNING,N.WATANABE,H.OSADA,I.R.VETTER,S.ZIEGLER,H.R.SCHOELER,      
AUTHOR   3 H.WALDMANN                                                           
REVDAT   3   04-MAY-16 5IH4    1       JRNL                                     
REVDAT   2   20-APR-16 5IH4    1       JRNL                                     
REVDAT   1   13-APR-16 5IH4    0                                                
JRNL        AUTH   A.URSU,D.J.ILLICH,Y.TAKEMOTO,A.T.PORFETYE,M.ZHANG,           
JRNL        AUTH 2 A.BROCKMEYER,P.JANNING,N.WATANABE,H.OSADA,I.R.VETTER,        
JRNL        AUTH 3 S.ZIEGLER,H.R.SCHOLER,H.WALDMANN                             
JRNL        TITL   EPIBLASTIN A INDUCES REPROGRAMMING OF EPIBLAST STEM CELLS    
JRNL        TITL 2 INTO EMBRYONIC STEM CELLS BY INHIBITION OF CASEIN KINASE 1.  
JRNL        REF    CELL CHEM BIOL                V.  23   494 2016              
JRNL        REFN                   ESSN 2451-9456                               
JRNL        PMID   27049670                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2016.02.015                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27925                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1456                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1394                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.6140                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 72                           
REMARK   3   BIN FREE R VALUE                    : 0.6220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2350                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 257                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89000                                              
REMARK   3    B22 (A**2) : 0.89000                                              
REMARK   3    B33 (A**2) : -2.88000                                             
REMARK   3    B12 (A**2) : 0.44000                                              
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): 0.146         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.825         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2439 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2328 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3282 ; 2.061 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5351 ; 1.140 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   291 ; 6.688 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   119 ;36.439 ;22.941       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   448 ;16.324 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;15.571 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   343 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2726 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   602 ; 0.002 ; 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):  1152 ; 3.413 ; 3.436       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1151 ; 3.408 ; 3.431       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1438 ; 5.104 ; 5.129       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5IH4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218051.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.916                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29688                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 16.70                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.1600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.140                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3UYS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ELLIPSOID                                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LI2SO4, 0.7 - 0.8 M NA-K           
REMARK 280  TARTRATE, 0.1 M CHES (PH 9.5), VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 277.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.96033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      101.92067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      101.92067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       50.96033            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 690 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 14650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 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     LYS A   217                                                      
REMARK 465     ALA A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     THR A   220                                                      
REMARK 465     LYS A   221                                                      
REMARK 465     ARG A   222                                                      
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   NH1  ARG A     8     OD2  ASP A    28              1.58            
REMARK 500   OD1  ASN A   143     O    HOH A   401              2.07            
REMARK 500   O    HOH A   594     O    HOH A   638              2.08            
REMARK 500   O    HOH A   472     O    HOH A   624              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   595     O    HOH A   595     4465     1.06            
REMARK 500   O    HOH A   414     O    HOH A   414     4465     1.69            
REMARK 500   O    HOH A   632     O    HOH A   632     6555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  13   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 160   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 123       18.78     82.90                                   
REMARK 500    ARG A 127       -4.33     75.25                                   
REMARK 500    ASP A 149       92.89     74.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 656        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH A 657        DISTANCE =  7.08 ANGSTROMS                       
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                              ZN A 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  50   ND1                                                    
REMARK 620 2 CYS A  71   SG  116.2                                              
REMARK 620 3 SRT A 302   O11 102.1 123.8                                        
REMARK 620 4 HIS A 278   NE2  82.7  47.0 104.8                                  
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 ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SRT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
DBREF  5IH4 A    1   294  UNP    P48730   KC1D_HUMAN       1    294             
SEQRES   1 A  294  MET GLU LEU ARG VAL GLY ASN ARG TYR ARG LEU GLY ARG          
SEQRES   2 A  294  LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR LEU GLY          
SEQRES   3 A  294  THR ASP ILE ALA ALA GLY GLU GLU VAL ALA ILE LYS LEU          
SEQRES   4 A  294  GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS ILE GLU          
SEQRES   5 A  294  SER LYS ILE TYR LYS MET MET GLN GLY GLY VAL GLY ILE          
SEQRES   6 A  294  PRO THR ILE ARG TRP CYS GLY ALA GLU GLY ASP TYR ASN          
SEQRES   7 A  294  VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU GLU ASP          
SEQRES   8 A  294  LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU LYS THR          
SEQRES   9 A  294  VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG ILE GLU          
SEQRES  10 A  294  TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP VAL LYS          
SEQRES  11 A  294  PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS GLY ASN          
SEQRES  12 A  294  LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS LYS TYR          
SEQRES  13 A  294  ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR ARG GLU          
SEQRES  14 A  294  ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA SER ILE          
SEQRES  15 A  294  ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG ASP ASP          
SEQRES  16 A  294  LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE ASN LEU          
SEQRES  17 A  294  GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA THR LYS          
SEQRES  18 A  294  ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS MET SER          
SEQRES  19 A  294  THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO SER GLU          
SEQRES  20 A  294  PHE ALA THR TYR LEU ASN PHE CYS ARG SER LEU ARG PHE          
SEQRES  21 A  294  ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN LEU PHE          
SEQRES  22 A  294  ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR ASP TYR          
SEQRES  23 A  294  VAL PHE ASP TRP ASN MET LEU LYS                              
HET     ZN  A 301       1                                                       
HET    SRT  A 302      10                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SRT S,R MESO-TARTARIC ACID                                           
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  SRT    C4 H6 O6                                                     
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   6  HOH   *257(H2 O)                                                    
HELIX    1 AA1 GLN A   48  MET A   59  1                                  12    
HELIX    2 AA2 SER A   88  CYS A   96  1                                   9    
HELIX    3 AA3 SER A  101  LYS A  122  1                                  22    
HELIX    4 AA4 LYS A  130  ASP A  132  5                                   3    
HELIX    5 AA5 LEU A  138  GLY A  142  5                                   5    
HELIX    6 AA6 THR A  176  ALA A  180  5                                   5    
HELIX    7 AA7 SER A  181  LEU A  186  1                                   6    
HELIX    8 AA8 SER A  191  GLY A  209  1                                  19    
HELIX    9 AA9 LYS A  224  THR A  235  1                                  12    
HELIX   10 AB1 PRO A  236  LYS A  242  1                                   7    
HELIX   11 AB2 SER A  246  LEU A  258  1                                  13    
HELIX   12 AB3 ASP A  265  GLY A  281  1                                  17    
SHEET    1 AA1 6 ARG A   4  VAL A   5  0                                        
SHEET    2 AA1 6 TYR A   9  SER A  17 -1  O  TYR A   9   N  VAL A   5           
SHEET    3 AA1 6 ASP A  22  ASP A  28 -1  O  ILE A  23   N  ILE A  15           
SHEET    4 AA1 6 GLU A  33  CYS A  41 -1  O  ILE A  37   N  TYR A  24           
SHEET    5 AA1 6 TYR A  77  MET A  82 -1  O  ASN A  78   N  GLU A  40           
SHEET    6 AA1 6 ILE A  68  GLU A  74 -1  N  GLU A  74   O  TYR A  77           
SHEET    1 AA2 2 PHE A 124  ILE A 125  0                                        
SHEET    2 AA2 2 LYS A 154  LYS A 155 -1  O  LYS A 154   N  ILE A 125           
SHEET    1 AA3 2 PHE A 134  MET A 136  0                                        
SHEET    2 AA3 2 VAL A 145  ILE A 147 -1  O  TYR A 146   N  LEU A 135           
LINK         ND1 HIS A  50                ZN    ZN A 301     1555   1555  2.11  
LINK         SG  CYS A  71                ZN    ZN A 301     1555   1555  2.19  
LINK        ZN    ZN A 301                 O11 SRT A 302     1555   1555  2.20  
LINK         NE2 HIS A 278                ZN    ZN A 301     1555   2565  2.14  
SITE     1 AC1  4 HIS A  50  CYS A  71  HIS A 278  SRT A 302                    
SITE     1 AC2 12 HIS A  50  LYS A  57  CYS A  71  ARG A 259                    
SITE     2 AC2 12 HIS A 278  ARG A 279   ZN A 301  HOH A 475                    
SITE     3 AC2 12 HOH A 508  HOH A 524  HOH A 547  HOH A 552                    
SITE     1 AC3  4 ARG A 127  LYS A 154  LYS A 171  GLU A 189                    
SITE     1 AC4  6 ARG A 178  GLN A 214  GLY A 215  LYS A 224                    
SITE     2 AC4  6 HOH A 421  HOH A 541                                          
CRYST1   64.999   64.999  152.881  90.00  90.00 120.00 P 31 2 1      6          
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      0.015385  0.008882  0.000000        0.00000                         
SCALE2      0.000000  0.017765  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006541        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system