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Database: PDB
Entry: 2CT9
LinkDB: 2CT9
Original site: 2CT9 
HEADER    METAL BINDING PROTEIN                   23-MAY-05   2CT9              
TITLE     THE CRYSTAL STRUCTURE OF CALCINEURIN B HOMOLOGOUS PROEIN 1 (CHP1)     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM-BINDING PROTEIN P22;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CALCINEURIN B HOMOLOGOUS PROTEIN 1, CALCIUM-BINDING PROTEIN 
COMPND   5 CHP, CALCINEURIN HOMOLOGOUS PROTEIN;                                 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    EF-HAND, CALCIUM BINDING PROTEIN, METAL BINDING PROTEIN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NAOE,K.ARITA,H.HASHIMOTO,H.KANAZAWA,M.SATO,T.SHIMIZU                
REVDAT   4   13-JUL-11 2CT9    1       VERSN                                    
REVDAT   3   24-FEB-09 2CT9    1       VERSN                                    
REVDAT   2   24-JAN-06 2CT9    1       JRNL                                     
REVDAT   1   05-JUL-05 2CT9    0                                                
JRNL        AUTH   Y.NAOE,K.ARITA,H.HASHIMOTO,H.KANAZAWA,M.SATO,T.SHIMIZU       
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF CALCINEURIN B HOMOLOGOUS      
JRNL        TITL 2 PROTEIN 1                                                    
JRNL        REF    J.BIOL.CHEM.                  V. 280 32372 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15987692                                                     
JRNL        DOI    10.1074/JBC.M503390200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 19499                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1004                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1371                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3106                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 34.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.57000                                              
REMARK   3    B22 (A**2) : 2.06000                                              
REMARK   3    B33 (A**2) : -2.63000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.17000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.376         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.253         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.275        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3153 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2871 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4232 ; 1.369 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6675 ; 0.835 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   379 ; 5.622 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;36.172 ;24.205       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   595 ;16.651 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;17.592 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   464 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3519 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   660 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   844 ; 0.223 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3068 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1602 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1839 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   153 ; 0.178 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    19 ; 0.122 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    17 ; 0.110 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    56 ; 0.223 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.244 ; 0.200       
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):  1971 ; 0.858 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   780 ; 0.158 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3063 ; 1.417 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1296 ; 1.969 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1169 ; 3.158 ; 4.500       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   305        B   305                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7461  25.5775  65.5817              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0567 T22:  -0.0789                                     
REMARK   3      T33:  -0.0304 T12:  -0.0157                                     
REMARK   3      T13:   0.0022 T23:  -0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3739 L22:   0.2162                                     
REMARK   3      L33:   0.4572 L12:  -0.1474                                     
REMARK   3      L13:   0.0626 L23:  -0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0163 S12:   0.0290 S13:   0.0538                       
REMARK   3      S21:   0.0155 S22:   0.0028 S23:  -0.0002                       
REMARK   3      S31:  -0.0188 S32:   0.0492 S33:   0.0135                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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 2CT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024598.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.34045, 1.34095, 1.32312,         
REMARK 200                                   1.37000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19708                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.22100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, LITHIUM CHLORIDE, CALCIUM       
REMARK 280  CHLORIDE, CAPSO, PH 9.0, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       19.26500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ASP A    95                                                      
REMARK 465     ASN A    96                                                      
REMARK 465     GLU A    97                                                      
REMARK 465     LYS A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     LYS A   100                                                      
REMARK 465     ASP A   101                                                      
REMARK 465     VAL A   102                                                      
REMARK 465     ASN A   103                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     PRO A   105                                                      
REMARK 465     HIS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LYS B    98                                                      
REMARK 465     SER B    99                                                      
REMARK 465     LYS B   100                                                      
REMARK 465     HIS B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     HIS B   208                                                      
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   OE1  GLU B   162     O    HOH B   316              1.93            
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    ASP B    76     O    HOH A   367     1565     2.10            
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    GLU A  73      126.45    -39.14                                   
REMARK 500    SER B  72      172.40    -54.33                                   
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 337        DISTANCE =  9.69 ANGSTROMS                       
REMARK 525    HOH A 365        DISTANCE =  9.15 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                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 123   OD1                                                    
REMARK 620 2 ASP A 125   OD2  84.4                                              
REMARK 620 3 ASP A 127   OD2  85.1  74.6                                        
REMARK 620 4 LYS A 129   O    84.6 150.2  76.9                                  
REMARK 620 5 GLU A 134   OE1  95.6  78.9 153.3 129.8                            
REMARK 620 6 HOH A 325   O   157.1  84.8  72.6  95.1 102.0                      
REMARK 620 7 GLU A 134   OE2 108.1 131.5 150.5  78.3  53.9  94.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 164   OD2                                                    
REMARK 620 2 ASP A 166   OD1  79.9                                              
REMARK 620 3 ASP A 168   OD2  82.1  82.8                                        
REMARK 620 4 ALA A 170   O    92.9 155.5  73.0                                  
REMARK 620 5 GLU A 175   OE1 115.6 120.7 151.5  83.6                            
REMARK 620 6 HOH A 343   O   156.4  89.3  75.7  88.2  87.9                      
REMARK 620 7 GLU A 175   OE2  91.4  72.6 155.3 131.4  51.5 105.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 303  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 123   OD1                                                    
REMARK 620 2 ASP B 125   OD2  78.0                                              
REMARK 620 3 ASP B 127   OD2  80.5  73.3                                        
REMARK 620 4 LYS B 129   O    79.9 148.0  80.5                                  
REMARK 620 5 GLU B 134   OE2 101.1  76.7 148.9 130.5                            
REMARK 620 6 GLU B 134   OE1 106.4 130.2 156.1  78.3  53.6                      
REMARK 620 7 HOH B 375   O   165.4 102.1  85.5  93.7  93.1  84.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 304  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 164   OD1                                                    
REMARK 620 2 ASP B 166   OD2  76.0                                              
REMARK 620 3 ASP B 168   OD2  75.3  76.9                                        
REMARK 620 4 ALA B 170   O    83.4 148.1  74.4                                  
REMARK 620 5 GLU B 175   OE1 112.7 132.6 150.1  77.9                            
REMARK 620 6 GLU B 175   OE2  94.6  80.4 156.8 125.9  53.1                      
REMARK 620 7 HOH B 344   O   154.2  96.3  79.0  91.7  90.8 108.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 304                  
DBREF  2CT9 A    1   195  UNP    P61023   CHP1_RAT         0    194             
DBREF  2CT9 B    1   195  UNP    P61023   CHP1_RAT         0    194             
SEQADV 2CT9 LYS A  196  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 LEU A  197  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 ALA A  198  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 ALA A  199  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 ALA A  200  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 LEU A  201  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 GLU A  202  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS A  203  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS A  204  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS A  205  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS A  206  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS A  207  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS A  208  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 LYS B  196  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 LEU B  197  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 ALA B  198  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 ALA B  199  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 ALA B  200  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 LEU B  201  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 GLU B  202  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS B  203  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS B  204  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS B  205  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS B  206  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS B  207  UNP  P61023              EXPRESSION TAG                 
SEQADV 2CT9 HIS B  208  UNP  P61023              EXPRESSION TAG                 
SEQRES   1 A  208  MET GLY SER ARG ALA SER THR LEU LEU ARG ASP GLU GLU          
SEQRES   2 A  208  LEU GLU GLU ILE LYS LYS GLU THR GLY PHE SER HIS SER          
SEQRES   3 A  208  GLN ILE THR ARG LEU TYR SER ARG PHE THR SER LEU ASP          
SEQRES   4 A  208  LYS GLY GLU ASN GLY THR LEU SER ARG GLU ASP PHE GLN          
SEQRES   5 A  208  ARG ILE PRO GLU LEU ALA ILE ASN PRO LEU GLY ASP ARG          
SEQRES   6 A  208  ILE ILE ASN ALA PHE PHE SER GLU GLY GLU ASP GLN VAL          
SEQRES   7 A  208  ASN PHE ARG GLY PHE MET ARG THR LEU ALA HIS PHE ARG          
SEQRES   8 A  208  PRO ILE GLU ASP ASN GLU LYS SER LYS ASP VAL ASN GLY          
SEQRES   9 A  208  PRO GLU PRO LEU ASN SER ARG SER ASN LYS LEU HIS PHE          
SEQRES  10 A  208  ALA PHE ARG LEU TYR ASP LEU ASP LYS ASP ASP LYS ILE          
SEQRES  11 A  208  SER ARG ASP GLU LEU LEU GLN VAL LEU ARG MET MET VAL          
SEQRES  12 A  208  GLY VAL ASN ILE SER ASP GLU GLN LEU GLY SER ILE ALA          
SEQRES  13 A  208  ASP ARG THR ILE GLN GLU ALA ASP GLN ASP GLY ASP SER          
SEQRES  14 A  208  ALA ILE SER PHE THR GLU PHE VAL LYS VAL LEU GLU LYS          
SEQRES  15 A  208  VAL ASP VAL GLU GLN LYS MET SER ILE ARG PHE LEU HIS          
SEQRES  16 A  208  LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  208  MET GLY SER ARG ALA SER THR LEU LEU ARG ASP GLU GLU          
SEQRES   2 B  208  LEU GLU GLU ILE LYS LYS GLU THR GLY PHE SER HIS SER          
SEQRES   3 B  208  GLN ILE THR ARG LEU TYR SER ARG PHE THR SER LEU ASP          
SEQRES   4 B  208  LYS GLY GLU ASN GLY THR LEU SER ARG GLU ASP PHE GLN          
SEQRES   5 B  208  ARG ILE PRO GLU LEU ALA ILE ASN PRO LEU GLY ASP ARG          
SEQRES   6 B  208  ILE ILE ASN ALA PHE PHE SER GLU GLY GLU ASP GLN VAL          
SEQRES   7 B  208  ASN PHE ARG GLY PHE MET ARG THR LEU ALA HIS PHE ARG          
SEQRES   8 B  208  PRO ILE GLU ASP ASN GLU LYS SER LYS ASP VAL ASN GLY          
SEQRES   9 B  208  PRO GLU PRO LEU ASN SER ARG SER ASN LYS LEU HIS PHE          
SEQRES  10 B  208  ALA PHE ARG LEU TYR ASP LEU ASP LYS ASP ASP LYS ILE          
SEQRES  11 B  208  SER ARG ASP GLU LEU LEU GLN VAL LEU ARG MET MET VAL          
SEQRES  12 B  208  GLY VAL ASN ILE SER ASP GLU GLN LEU GLY SER ILE ALA          
SEQRES  13 B  208  ASP ARG THR ILE GLN GLU ALA ASP GLN ASP GLY ASP SER          
SEQRES  14 B  208  ALA ILE SER PHE THR GLU PHE VAL LYS VAL LEU GLU LYS          
SEQRES  15 B  208  VAL ASP VAL GLU GLN LYS MET SER ILE ARG PHE LEU HIS          
SEQRES  16 B  208  LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS          
HET     CA  A 301       1                                                       
HET     CA  A 302       1                                                       
HET     CA  B 303       1                                                       
HET     CA  B 304       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   7  HOH   *153(H2 O)                                                    
HELIX    1   1 ARG A   10  GLY A   22  1                                  13    
HELIX    2   2 SER A   24  ASP A   39  1                                  16    
HELIX    3   3 ARG A   48  ARG A   53  5                                   6    
HELIX    4   4 ILE A   54  ILE A   59  1                                   6    
HELIX    5   5 LEU A   62  ALA A   69  1                                   8    
HELIX    6   6 PHE A   80  HIS A   89  1                                  10    
HELIX    7   7 SER A  110  ASP A  123  1                                  14    
HELIX    8   8 SER A  131  VAL A  143  1                                  13    
HELIX    9   9 SER A  148  ASP A  164  1                                  17    
HELIX   10  10 PHE A  173  VAL A  179  1                                   7    
HELIX   11  11 ASP A  184  GLN A  187  5                                   4    
HELIX   12  12 LYS A  188  HIS A  203  1                                  16    
HELIX   13  13 SER B    3  GLY B   22  1                                  20    
HELIX   14  14 SER B   24  ASP B   39  1                                  16    
HELIX   15  15 ARG B   48  ARG B   53  1                                   6    
HELIX   16  16 ILE B   54  ILE B   59  1                                   6    
HELIX   17  17 LEU B   62  PHE B   70  1                                   9    
HELIX   18  18 ASN B   79  HIS B   89  1                                  11    
HELIX   19  19 PHE B   90  ARG B   91  5                                   2    
HELIX   20  20 PRO B   92  ASN B   96  5                                   5    
HELIX   21  21 SER B  110  ASP B  123  1                                  14    
HELIX   22  22 SER B  131  VAL B  143  1                                  13    
HELIX   23  23 SER B  148  ASP B  164  1                                  17    
HELIX   24  24 PHE B  173  LEU B  180  1                                   8    
HELIX   25  25 ASP B  184  GLN B  187  5                                   4    
HELIX   26  26 LYS B  188  HIS B  203  1                                  16    
SHEET    1   A 2 THR A  45  LEU A  46  0                                        
SHEET    2   A 2 VAL A  78  ASN A  79 -1  O  VAL A  78   N  LEU A  46           
SHEET    1   B 2 LYS A 129  ILE A 130  0                                        
SHEET    2   B 2 ILE A 171  SER A 172 -1  O  ILE A 171   N  ILE A 130           
SHEET    1   C 2 LEU B  46  SER B  47  0                                        
SHEET    2   C 2 GLN B  77  VAL B  78 -1  O  VAL B  78   N  LEU B  46           
SHEET    1   D 2 LYS B 129  ILE B 130  0                                        
SHEET    2   D 2 ILE B 171  SER B 172 -1  O  ILE B 171   N  ILE B 130           
LINK        CA    CA A 301                 OD1 ASP A 123     1555   1555  2.21  
LINK        CA    CA A 301                 OD2 ASP A 125     1555   1555  2.43  
LINK        CA    CA A 301                 OD2 ASP A 127     1555   1555  2.40  
LINK        CA    CA A 301                 O   LYS A 129     1555   1555  2.29  
LINK        CA    CA A 301                 OE1 GLU A 134     1555   1555  2.35  
LINK        CA    CA A 302                 OD2 ASP A 164     1555   1555  2.14  
LINK        CA    CA A 302                 OD1 ASP A 166     1555   1555  2.33  
LINK        CA    CA A 302                 OD2 ASP A 168     1555   1555  2.45  
LINK        CA    CA A 302                 O   ALA A 170     1555   1555  2.42  
LINK        CA    CA A 302                 OE1 GLU A 175     1555   1555  2.32  
LINK        CA    CA B 303                 OD1 ASP B 123     1555   1555  2.19  
LINK        CA    CA B 303                 OD2 ASP B 125     1555   1555  2.49  
LINK        CA    CA B 303                 OD2 ASP B 127     1555   1555  2.27  
LINK        CA    CA B 303                 O   LYS B 129     1555   1555  2.38  
LINK        CA    CA B 303                 OE2 GLU B 134     1555   1555  2.41  
LINK        CA    CA B 304                 OD1 ASP B 164     1555   1555  2.45  
LINK        CA    CA B 304                 OD2 ASP B 166     1555   1555  2.58  
LINK        CA    CA B 304                 OD2 ASP B 168     1555   1555  2.52  
LINK        CA    CA B 304                 O   ALA B 170     1555   1555  2.38  
LINK        CA    CA B 304                 OE1 GLU B 175     1555   1555  2.37  
LINK        CA    CA A 301                 O   HOH A 325     1555   1555  2.37  
LINK        CA    CA A 301                 OE2 GLU A 134     1555   1555  2.40  
LINK        CA    CA A 302                 O   HOH A 343     1555   1555  2.34  
LINK        CA    CA A 302                 OE2 GLU A 175     1555   1555  2.62  
LINK        CA    CA B 303                 OE1 GLU B 134     1555   1555  2.44  
LINK        CA    CA B 303                 O   HOH B 375     1555   1555  2.41  
LINK        CA    CA B 304                 OE2 GLU B 175     1555   1555  2.48  
LINK        CA    CA B 304                 O   HOH B 344     1555   1555  2.25  
SITE     1 AC1  6 ASP A 123  ASP A 125  ASP A 127  LYS A 129                    
SITE     2 AC1  6 GLU A 134  HOH A 325                                          
SITE     1 AC2  6 ASP A 164  ASP A 166  ASP A 168  ALA A 170                    
SITE     2 AC2  6 GLU A 175  HOH A 343                                          
SITE     1 AC3  6 ASP B 123  ASP B 125  ASP B 127  LYS B 129                    
SITE     2 AC3  6 GLU B 134  HOH B 375                                          
SITE     1 AC4  6 ASP B 164  ASP B 166  ASP B 168  ALA B 170                    
SITE     2 AC4  6 GLU B 175  HOH B 344                                          
CRYST1   55.550   38.530   89.950  90.00  90.69  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018003  0.000000  0.000217        0.00000                         
SCALE2      0.000000  0.025957  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011118        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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