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Database: PDB
Entry: 3IMD
LinkDB: 3IMD
Original site: 3IMD 
HEADER    SIGNALING PROTEIN/PEPTIDE               10-AUG-09   3IMD              
TITLE     CRYSTAL STRUCTURE OF THE GRB2 SH2 DOMAIN IN COMPLEX WITH A FLEXIBLE   
TITLE    2 AC-PY-Q-N-NH2 TRIPEPTIDE MIMIC                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GROWTH FACTOR RECEPTOR-BOUND PROTEIN 2;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: SH2 DOMAIN;                                                
COMPND   5 SYNONYM: ADAPTER PROTEIN GRB2, SH2/SH3 ADAPTER GRB2, PROTEIN ASH;    
COMPND   6 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: GRB2, ASH;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SG13009;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE-60                                    
KEYWDS    LIGAND PREORGANIZATION, PEPTIDE MIMICS, GOLGI APPARATUS, HOST-VIRUS   
KEYWDS   2 INTERACTION, PHOSPHOPROTEIN, SH2 DOMAIN, SIGNALING PROTEIN,          
KEYWDS   3 SIGNALING PROTEIN-PSEUDOPEPTIDE LIGAND COMPLEX, SIGNALING PROTEIN-   
KEYWDS   4 PEPTIDE COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.CLEMENTS                                                          
REVDAT   4   01-NOV-17 3IMD    1       REMARK                                   
REVDAT   3   13-JUL-11 3IMD    1       VERSN                                    
REVDAT   2   01-DEC-09 3IMD    1       JRNL                                     
REVDAT   1   17-NOV-09 3IMD    0                                                
JRNL        AUTH   J.E.DELORBE,J.H.CLEMENTS,M.G.TERESK,A.P.BENFIELD,H.R.PLAKE,  
JRNL        AUTH 2 L.E.MILLSPAUGH,S.F.MARTIN                                    
JRNL        TITL   THERMODYNAMIC AND STRUCTURAL EFFECTS OF CONFORMATIONAL       
JRNL        TITL 2 CONSTRAINTS IN PROTEIN-LIGAND INTERACTIONS. ENTROPIC         
JRNL        TITL 3 PARADOXY ASSOCIATED WITH LIGAND PREORGANIZATION.             
JRNL        REF    J.AM.CHEM.SOC.                V. 131 16758 2009              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   19886660                                                     
JRNL        DOI    10.1021/JA904698Q                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.P.BENFIELD,M.G.TERESK,H.R.PLAKE,J.E.DELORBE,               
REMARK   1  AUTH 2 L.E.MILLSPAUGH,S.F.MARTIN                                    
REMARK   1  TITL   LIGAND PREORGANIZATION MAY BE ACCOMPANIED BY ENTROPIC        
REMARK   1  TITL 2 PENALTIES IN PROTEIN-LIGAND INTERACTIONS                     
REMARK   1  REF    ANGEW.CHEM.INT.ED.ENGL.       V.  45  6830 2006              
REMARK   1  REFN                   ISSN 1433-7851                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 12970                          
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 SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 641                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1664                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00500                                              
REMARK   3    B22 (A**2) : 0.04900                                              
REMARK   3    B33 (A**2) : -0.05500                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.114 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.663 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.776 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.528 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 11.41                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : FPYQN.PARAM                                    
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : CNS_TOPPAR:PROTEIN.TOP                         
REMARK   3  TOPOLOGY FILE  2   : CNS_TOPPAR:DNA-RNA.TOP                         
REMARK   3  TOPOLOGY FILE  3   : CNS_TOPPAR:WATER.TOP                           
REMARK   3  TOPOLOGY FILE  4   : CNS_TOPPAR:ION.TOP                             
REMARK   3  TOPOLOGY FILE  5   : FPYQN.TOP                                      
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054591.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : BLUE MAX-FLUX CONFOCAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18279                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.790                              
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     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 50.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: PDB ENTRY 3C7I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LIGAND IN LYPHILIZED POWDER FORM WAS     
REMARK 280  DISSOLVED IN A 9.1 MG/ML SOLUTION OF GRB2 SH2 IN WATER SUCH TO      
REMARK 280  GIVE A PROTEIN/LIGAND MOLAR RATIO OF 2:1. 3 UL OF THIS SOLUTION     
REMARK 280  WAS MIXED WITH 4 UL OF 0.2 M MGCL2 X 6H2O, 30% W/V PEG MW4000,      
REMARK 280  0.1 M TRIS, PH 8.5 TO CREATE THE HANGING DROP, WHICH YIELDED        
REMARK 280  CRYSTALS OF THE PROTEIN-LIGAND COMPLEX IN THE PRESENCE OF THE       
REMARK 280  ABOVE-MENTIONED SOLUTION AFTER FOUR WEEKS AT ROOM TEMPERATURE.,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       21.11950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.19200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.12150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.19200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.11950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       21.12150            
REMARK 290   SMTRY3   4  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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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     ILE A    53                                                      
REMARK 465     GLU A    54                                                      
REMARK 465     GLN A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     PRO A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     TYR A   160                                                      
REMARK 465     VAL A   161                                                      
REMARK 465     GLN A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     HIS A   167                                                      
REMARK 465     HIS A   168                                                      
REMARK 465     HIS A   169                                                      
REMARK 465     ILE B    53                                                      
REMARK 465     GLU B    54                                                      
REMARK 465     GLN B   156                                                      
REMARK 465     GLN B   157                                                      
REMARK 465     PRO B   158                                                      
REMARK 465     THR B   159                                                      
REMARK 465     TYR B   160                                                      
REMARK 465     VAL B   161                                                      
REMARK 465     GLN B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     HIS B   165                                                      
REMARK 465     HIS B   166                                                      
REMARK 465     HIS B   167                                                      
REMARK 465     HIS B   168                                                      
REMARK 465     HIS B   169                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG B 112   CZ    ARG B 112   NH1    -0.207                       
REMARK 500    ARG B 112   CZ    ARG B 112   NH2    -0.165                       
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 B 112   NH1 -  CZ  -  NH2 ANGL. DEV. = -15.3 DEGREES          
REMARK 500    ARG B 112   NE  -  CZ  -  NH1 ANGL. DEV. =  16.9 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    TRP A 121      -79.72   -127.29                                   
REMARK 500    TRP A 121      -79.45   -127.29                                   
REMARK 500    VAL A 122      -52.79   -120.93                                   
REMARK 500    TRP B 121      -75.82   -125.80                                   
REMARK 500    VAL B 122      -53.99   -124.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG B 112         0.25    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
REMARK 630 MOLECULE NAME: N~2~-{(2R)-4-(METHYLAMINO)-4-OXO-2-[4-(PHOSPHONOOXY)  
REMARK 630 BENZYL]BUTANOYL}-L-GLUTAMINYL-L-ASPARTAMIDE                          
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     FYQ A     1                                                      
REMARK 630     FYQ B     1                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    FY0 GLN ASN NH2                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FYQ A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FYQ B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 170                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C7I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HUW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IMJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IN7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IN8   RELATED DB: PDB                                   
DBREF  3IMD A   53   163  UNP    P62993   GRB2_HUMAN      53    163             
DBREF  3IMD B   53   163  UNP    P62993   GRB2_HUMAN      53    163             
SEQADV 3IMD HIS A  164  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS A  165  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS A  166  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS A  167  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS A  168  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS A  169  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS B  164  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS B  165  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS B  166  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS B  167  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS B  168  UNP  P62993              EXPRESSION TAG                 
SEQADV 3IMD HIS B  169  UNP  P62993              EXPRESSION TAG                 
SEQRES   1 A  117  ILE GLU MET LYS PRO HIS PRO TRP PHE PHE GLY LYS ILE          
SEQRES   2 A  117  PRO ARG ALA LYS ALA GLU GLU MET LEU SER LYS GLN ARG          
SEQRES   3 A  117  HIS ASP GLY ALA PHE LEU ILE ARG GLU SER GLU SER ALA          
SEQRES   4 A  117  PRO GLY ASP PHE SER LEU SER VAL LYS PHE GLY ASN ASP          
SEQRES   5 A  117  VAL GLN HIS PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS          
SEQRES   6 A  117  TYR PHE LEU TRP VAL VAL LYS PHE ASN SER LEU ASN GLU          
SEQRES   7 A  117  LEU VAL ASP TYR HIS ARG SER THR SER VAL SER ARG ASN          
SEQRES   8 A  117  GLN GLN ILE PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN          
SEQRES   9 A  117  GLN PRO THR TYR VAL GLN ALA HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  117  ILE GLU MET LYS PRO HIS PRO TRP PHE PHE GLY LYS ILE          
SEQRES   2 B  117  PRO ARG ALA LYS ALA GLU GLU MET LEU SER LYS GLN ARG          
SEQRES   3 B  117  HIS ASP GLY ALA PHE LEU ILE ARG GLU SER GLU SER ALA          
SEQRES   4 B  117  PRO GLY ASP PHE SER LEU SER VAL LYS PHE GLY ASN ASP          
SEQRES   5 B  117  VAL GLN HIS PHE LYS VAL LEU ARG ASP GLY ALA GLY LYS          
SEQRES   6 B  117  TYR PHE LEU TRP VAL VAL LYS PHE ASN SER LEU ASN GLU          
SEQRES   7 B  117  LEU VAL ASP TYR HIS ARG SER THR SER VAL SER ARG ASN          
SEQRES   8 B  117  GLN GLN ILE PHE LEU ARG ASP ILE GLU GLN VAL PRO GLN          
SEQRES   9 B  117  GLN PRO THR TYR VAL GLN ALA HIS HIS HIS HIS HIS HIS          
HET    FYQ  A   1      38                                                       
HET     CL  A   2       1                                                       
HET     MG  A   4       1                                                       
HET     CL  A   5       1                                                       
HET     CL  A   6       1                                                       
HET    FYQ  B   1      38                                                       
HET     CL  B 170       1                                                       
HETNAM     FYQ N~2~-{(2R)-4-(METHYLAMINO)-4-OXO-2-[4-(PHOSPHONOOXY)             
HETNAM   2 FYQ  BENZYL]BUTANOYL}-L-GLUTAMINYL-L-ASPARTAMIDE                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  FYQ    2(C21 H31 N6 O10 P)                                          
FORMUL   4   CL    4(CL 1-)                                                     
FORMUL   5   MG    MG 2+                                                        
FORMUL  10  HOH   *191(H2 O)                                                    
HELIX    1   1 PRO A   66  SER A   75  1                                  10    
HELIX    2   2 SER A  127  HIS A  135  1                                   9    
HELIX    3   3 PRO B   66  SER B   75  1                                  10    
HELIX    4   4 SER B  127  HIS B  135  1                                   9    
SHEET    1   A 5 PHE A  61  GLY A  63  0                                        
SHEET    2   A 5 PHE A  83  GLU A  87  1  O  GLU A  87   N  GLY A  63           
SHEET    3   A 5 PHE A  95  PHE A 101 -1  O  SER A  96   N  ARG A  86           
SHEET    4   A 5 ASP A 104  ARG A 112 -1  O  GLN A 106   N  VAL A  99           
SHEET    5   A 5 TYR A 118  PHE A 119 -1  O  PHE A 119   N  LEU A 111           
SHEET    1   B 4 PHE B  83  GLU B  87  0                                        
SHEET    2   B 4 PHE B  95  PHE B 101 -1  O  SER B  96   N  ARG B  86           
SHEET    3   B 4 ASP B 104  ARG B 112 -1  O  PHE B 108   N  LEU B  97           
SHEET    4   B 4 TYR B 118  PHE B 119 -1  O  PHE B 119   N  LEU B 111           
SITE     1 AC1 19 ARG A  67  ARG A  86  SER A  88  SER A  90                    
SITE     2 AC1 19 SER A  96  HIS A 107  PHE A 108  LYS A 109                    
SITE     3 AC1 19 LEU A 120  TRP A 121  HOH A 171  HOH A 177                    
SITE     4 AC1 19 HOH A 178  HOH A 186  HOH A 187  ARG B  78                    
SITE     5 AC1 19 VAL B 154  PRO B 155  HOH B 207                               
SITE     1 AC2  3 SER A 139  GLN A 145  HOH A 195                               
SITE     1 AC3  3 HIS A  58  ASN A 129  ASP A 133                               
SITE     1 AC4  3 ARG A  78  GLU A 152  LYS B 109                               
SITE     1 AC5  3 LYS A 109  ARG B  78  GLU B 152                               
SITE     1 AC6 21 ARG A  78  GLU A 152  VAL A 154  PRO A 155                    
SITE     2 AC6 21 HOH B   5  HOH B   7  HOH B   8  HOH B  13                    
SITE     3 AC6 21 HOH B  27  ARG B  67  ARG B  86  SER B  88                    
SITE     4 AC6 21 SER B  90  SER B  96  HIS B 107  PHE B 108                    
SITE     5 AC6 21 LYS B 109  LEU B 120  TRP B 121  HOH B 196                    
SITE     6 AC6 21 HOH B 206                                                     
SITE     1 AC7  2 SER B 139  GLN B 145                                          
CRYST1   42.239   42.243  110.384  90.00  90.00  90.00 P 21 21 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      0.023675  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.023673  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009059        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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