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Database: PDB
Entry: 3VRO
LinkDB: 3VRO
Original site: 3VRO 
HEADER    PROTEIN BINDING/TRANSFERASE             13-APR-12   3VRO              
TITLE     CRYSTAL STRUCTURE OF THE TYROSINE KINASE BINDING DOMAIN OF CBL-C IN   
TITLE    2 COMPLEX WITH PHOSPHO-SRC PEPTIDE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGNAL TRANSDUCTION PROTEIN CBL-C;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TYROSINE KINASE BINDING DOMAIN;                            
COMPND   5 SYNONYM: RING FINGER PROTEIN 57, SH3-BINDING PROTEIN CBL-3, SH3-     
COMPND   6 BINDING PROTEIN CBL-C;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC;                
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: PHOSPHO-SRC PEPTIDE, RESIDUES 412-424;                     
COMPND  12 SYNONYM: PROTO-ONCOGENE C-SRC, PP60C-SRC, P60-SRC;                   
COMPND  13 EC: 2.7.10.2;                                                        
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CBLC;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5A;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    PTB DOMAIN, TKB (TYROSINE KINASE BINDING) DOMAIN, FOUR-HELIX BUNDLE   
KEYWDS   2 (4H), CALCIUM-BINDING EF HAND, DIVERGENT SH2 DOMAIN, REGULATOR OF    
KEYWDS   3 EGFR MEDIATED SIGNAL TRANSDUCTION, UBIQUITOUSLY EXPRESSED, PROTEIN   
KEYWDS   4 BINDING-TRANSFERASE COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAKESHITA,T.TEZUKA,Y.ISOZAKI,E.YAMASHITA,M.SUZUKI,Y.YAMANASHI,      
AUTHOR   2 T.YAMAMOTO,A.NAKAGAWA                                                
REVDAT   2   22-NOV-17 3VRO    1       REMARK                                   
REVDAT   1   06-MAR-13 3VRO    0                                                
JRNL        AUTH   K.TAKESHITA,T.TEZUKA,Y.ISOZAKI,E.YAMASHITA,M.SUZUKI,M.KIM,   
JRNL        AUTH 2 Y.YAMANASHI,T.YAMAMOTO,A.NAKAGAWA                            
JRNL        TITL   STRUCTURAL FLEXIBILITY REGULATES PHOSPHOPEPTIDE-BINDING      
JRNL        TITL 2 ACTIVITY OF THE TYROSINE KINASE BINDING DOMAIN OF CBL-C.     
JRNL        REF    J.BIOCHEM.                    V. 152   487 2012              
JRNL        REFN                   ISSN 0021-924X                               
JRNL        PMID   22888118                                                     
JRNL        DOI    10.1093/JB/MVS085                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26211                          
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) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1332                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.84                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1746                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 84                           
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2274                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.123         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.448         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2347 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3186 ; 1.895 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   288 ; 5.293 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   104 ;34.230 ;22.404       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   381 ;15.372 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;18.081 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   347 ; 0.134 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1791 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1448 ; 1.352 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2320 ; 2.500 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   899 ; 3.896 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   866 ; 6.217 ; 4.500       
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   : 1.40                                          
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 3VRO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000095416.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900                              
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRUKER DIP-6040                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26228                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6090                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.53800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.283                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 0.1M AMMONIUM FORMATE,      
REMARK 280  0.1M NDSB-201, PH 7.0, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.38050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       27.38050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       46.64100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.24650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       46.64100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.24650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       27.38050            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       46.64100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       54.24650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       27.38050            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       46.64100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       54.24650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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     GLY A    -7                                                      
REMARK 465     PRO A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     TRP A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     TRP A    12                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     GLY A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     PRO A    99                                                      
REMARK 465     PRO A   100                                                      
REMARK 465     ARG A   101                                                      
REMARK 465     GLY A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     ALA A   106                                                      
REMARK 465     ASN A   107                                                      
REMARK 465     ASP A   108                                                      
REMARK 465     GLU A   109                                                      
REMARK 465     LEU A   110                                                      
REMARK 465     PHE A   111                                                      
REMARK 465     ARG A   112                                                      
REMARK 465     ALA A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     GLU A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     GLY A   323                                                      
REMARK 465     ARG B   412                                                      
REMARK 465     LEU B   413                                                      
REMARK 465     ILE B   414                                                      
REMARK 465     GLU B   415                                                      
REMARK 465     ASP B   416                                                      
REMARK 465     ARG B   422                                                      
REMARK 465     GLN B   423                                                      
REMARK 465     GLY B   424                                                      
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 291       76.07    -66.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 199   OD1                                                    
REMARK 620 2 GLU A 210   OE2  91.0                                              
REMARK 620 3 HIS A 205   O    95.9 117.0                                        
REMARK 620 4 THR A 201   OG1  96.4  83.1 156.2                                  
REMARK 620 5 SER A 203   OG   95.0 162.6  78.6  80.0                            
REMARK 620 6 GLU A 210   OE1 117.6  49.1  73.2 118.1 138.4                      
REMARK 620 7 HOH A 502   O   175.7  89.6  80.1  87.9  85.6  60.0                
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 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VRN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VRP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VRQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VRR   RELATED DB: PDB                                   
DBREF  3VRO A    1   323  UNP    Q9ULV8   CBLC_HUMAN       1    323             
DBREF  3VRO B  412   424  UNP    P12931   SRC_HUMAN      412    424             
SEQADV 3VRO GLY A   -7  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO PRO A   -6  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO LEU A   -5  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO GLY A   -4  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO SER A   -3  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO PRO A   -2  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO GLU A   -1  UNP  Q9ULV8              EXPRESSION TAG                 
SEQADV 3VRO PHE A    0  UNP  Q9ULV8              EXPRESSION TAG                 
SEQRES   1 A  331  GLY PRO LEU GLY SER PRO GLU PHE MET ALA LEU ALA VAL          
SEQRES   2 A  331  ALA PRO TRP GLY ARG GLN TRP GLU GLU ALA ARG ALA LEU          
SEQRES   3 A  331  GLY ARG ALA VAL ARG MET LEU GLN ARG LEU GLU GLU GLN          
SEQRES   4 A  331  CYS VAL ASP PRO ARG LEU SER VAL SER PRO PRO SER LEU          
SEQRES   5 A  331  ARG ASP LEU LEU PRO ARG THR ALA GLN LEU LEU ARG GLU          
SEQRES   6 A  331  VAL ALA HIS SER ARG ARG ALA ALA GLY GLY GLY GLY PRO          
SEQRES   7 A  331  GLY GLY PRO GLY GLY SER GLY ASP PHE LEU LEU ILE TYR          
SEQRES   8 A  331  LEU ALA ASN LEU GLU ALA LYS SER ARG GLN VAL ALA ALA          
SEQRES   9 A  331  LEU LEU PRO PRO ARG GLY ARG ARG SER ALA ASN ASP GLU          
SEQRES  10 A  331  LEU PHE ARG ALA GLY SER ARG LEU ARG ARG GLN LEU ALA          
SEQRES  11 A  331  LYS LEU ALA ILE ILE PHE SER HIS MET HIS ALA GLU LEU          
SEQRES  12 A  331  HIS ALA LEU PHE PRO GLY GLY LYS TYR CYS GLY HIS MET          
SEQRES  13 A  331  TYR GLN LEU THR LYS ALA PRO ALA HIS THR PHE TRP ARG          
SEQRES  14 A  331  GLU SER CYS GLY ALA ARG CYS VAL LEU PRO TRP ALA GLU          
SEQRES  15 A  331  PHE GLU SER LEU LEU GLY THR CYS HIS PRO VAL GLU PRO          
SEQRES  16 A  331  GLY CYS THR ALA LEU ALA LEU ARG THR THR ILE ASP LEU          
SEQRES  17 A  331  THR CYS SER GLY HIS VAL SER ILE PHE GLU PHE ASP VAL          
SEQRES  18 A  331  PHE THR ARG LEU PHE GLN PRO TRP PRO THR LEU LEU LYS          
SEQRES  19 A  331  ASN TRP GLN LEU LEU ALA VAL ASN HIS PRO GLY TYR MET          
SEQRES  20 A  331  ALA PHE LEU THR TYR ASP GLU VAL GLN GLU ARG LEU GLN          
SEQRES  21 A  331  ALA CYS ARG ASP LYS PRO GLY SER TYR ILE PHE ARG PRO          
SEQRES  22 A  331  SER CYS THR ARG LEU GLY GLN TRP ALA ILE GLY TYR VAL          
SEQRES  23 A  331  SER SER ASP GLY SER ILE LEU GLN THR ILE PRO ALA ASN          
SEQRES  24 A  331  LYS PRO LEU SER GLN VAL LEU LEU GLU GLY GLN LYS ASP          
SEQRES  25 A  331  GLY PHE TYR LEU TYR PRO ASP GLY LYS THR HIS ASN PRO          
SEQRES  26 A  331  ASP LEU THR GLU LEU GLY                                      
SEQRES   1 B   13  ARG LEU ILE GLU ASP ASN GLU PTR THR ALA ARG GLN GLY          
MODRES 3VRO PTR B  419  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  B 419      16                                                       
HET     CA  A 401       1                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM      CA CALCIUM ION                                                      
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   2  PTR    C9 H12 N O6 P                                                
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *204(H2 O)                                                    
HELIX    1   1 GLU A   13  CYS A   32  1                                  20    
HELIX    2   2 SER A   43  ARG A   63  1                                  21    
HELIX    3   3 GLY A   75  LEU A   98  1                                  24    
HELIX    4   4 ARG A  116  PHE A  139  1                                  24    
HELIX    5   5 PRO A  140  LYS A  143  5                                   4    
HELIX    6   6 LYS A  153  GLY A  165  1                                  13    
HELIX    7   7 TRP A  172  THR A  181  1                                  10    
HELIX    8   8 GLY A  188  ASP A  199  1                                  12    
HELIX    9   9 ILE A  208  PHE A  218  1                                  11    
HELIX   10  10 PRO A  220  PRO A  222  5                                   3    
HELIX   11  11 THR A  223  VAL A  233  1                                  11    
HELIX   12  12 THR A  243  GLN A  252  1                                  10    
HELIX   13  13 ALA A  253  ARG A  255  5                                   3    
HELIX   14  14 PRO A  293  ASP A  304  1                                  12    
SHEET    1   A 2 VAL A 169  PRO A 171  0                                        
SHEET    2   A 2 HIS A 205  SER A 207 -1  O  VAL A 206   N  LEU A 170           
SHEET    1   B 4 ILE A 284  THR A 287  0                                        
SHEET    2   B 4 TRP A 273  VAL A 278 -1  N  ILE A 275   O  THR A 287           
SHEET    3   B 4 SER A 260  PRO A 265 -1  N  ARG A 264   O  ALA A 274           
SHEET    4   B 4 TYR A 309  PRO A 310  1  O  TYR A 309   N  TYR A 261           
LINK         C   GLU B 418                 N   PTR B 419     1555   1555  1.33  
LINK         C   PTR B 419                 N   THR B 420     1555   1555  1.31  
LINK         OD1 ASP A 199                CA    CA A 401     1555   1555  2.34  
LINK         OE2 GLU A 210                CA    CA A 401     1555   1555  2.36  
LINK         O   HIS A 205                CA    CA A 401     1555   1555  2.46  
LINK         OG1 THR A 201                CA    CA A 401     1555   1555  2.48  
LINK         OG  SER A 203                CA    CA A 401     1555   1555  2.51  
LINK         OE1 GLU A 210                CA    CA A 401     1555   1555  2.84  
LINK        CA    CA A 401                 O   HOH A 502     1555   1555  2.53  
CISPEP   1 PRO A   41    PRO A   42          0        -4.46                     
CISPEP   2 GLN A  219    PRO A  220          0         5.62                     
SITE     1 AC1  6 ASP A 199  THR A 201  SER A 203  HIS A 205                    
SITE     2 AC1  6 GLU A 210  HOH A 502                                          
CRYST1   93.282  108.493   54.761  90.00  90.00  90.00 C 2 2 21      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      0.010720  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018261        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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