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Database: PDB
Entry: 3MAZ
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Original site: 3MAZ 
HEADER    SIGNALING PROTEIN                       24-MAR-10   3MAZ              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN BRDG1/STAP-1 SH2 DOMAIN IN COMPLEX WITH
TITLE    2 THE NTAL PTYR136 PEPTIDE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIGNAL-TRANSDUCING ADAPTOR PROTEIN 1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 167-285, SH2 DOMAIN;                          
COMPND   5 SYNONYM: STAP-1, STEM CELL ADAPTOR PROTEIN 1, BCR DOWNSTREAM-        
COMPND   6 SIGNALING PROTEIN 1, DOCKING PROTEIN BRDG1;                          
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CHED FAMILY PROTEIN;                                       
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES;                                                       
COMPND  14 OTHER_DETAILS: PTYR136 PEPTIDE                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: STAP1, BRDG1;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.             
KEYWDS    MODULAR DOMAIN, PHOSPHOTYROSINE, SPECIFICITY, CYTOPLASM,              
KEYWDS   2 PHOSPHOPROTEIN, SH2 DOMAIN, SIGNALING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.KANEKO,H.HUANG,B.ZHAO,L.LI,H.LIU,C.K.VOSS,C.WU,M.R.SCHILLER,S.S.LI  
REVDAT   1   12-MAY-10 3MAZ    0                                                
JRNL        AUTH   T.KANEKO,H.HUANG,B.ZHAO,L.LI,H.LIU,C.K.VOSS,C.WU,            
JRNL        AUTH 2 M.R.SCHILLER,S.S.LI                                          
JRNL        TITL   LOOPS GOVERN SH2 DOMAIN SPECIFICITY BY CONTROLLING ACCESS    
JRNL        TITL 2 TO BINDING POCKETS.                                          
JRNL        REF    SCI.SIGNAL.                   V.   3  RA34 2010              
JRNL        REFN                   ESSN 1937-9145                               
JRNL        PMID   20442417                                                     
JRNL        DOI    10.1126/SCISIGNAL.2000796                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.21                                             
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1413652.720                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12583                          
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) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 606                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1935                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 103                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 885                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 83                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.33000                                             
REMARK   3    B22 (A**2) : -1.33000                                             
REMARK   3    B33 (A**2) : 2.67000                                              
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) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.88                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.670 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.780 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.150 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 46.20                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : T                                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : T                                              
REMARK   3  PARAMETER FILE  5  : T                                              
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3MAZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058327.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
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 RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1BMB 1H9O 1I3Z 1KC2                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M SODIUM MALONATE, PH 5.0, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.22667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       32.61333            
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  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       65.22667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       32.61333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       65.22667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       32.61333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       65.22667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       32.61333            
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: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6610 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A  83  LIES ON A SPECIAL POSITION.                          
REMARK 375 C2   MLI A1001  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     MET A   166                                                      
REMARK 465     ASP A   167                                                      
REMARK 465     TYR A   168                                                      
REMARK 465     VAL A   169                                                      
REMARK 465     ASP A   170                                                      
REMARK 465     SER A   270                                                      
REMARK 465     THR A   271                                                      
REMARK 465     ASP A   272                                                      
REMARK 465     GLU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     THR A   275                                                      
REMARK 465     GLY A   276                                                      
REMARK 465     GLN A   277                                                      
REMARK 465     GLU A   278                                                      
REMARK 465     PRO A   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     MET A   281                                                      
REMARK 465     GLU A   282                                                      
REMARK 465     GLY A   283                                                      
REMARK 465     ARG A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     ALA B   133                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A    69     O    HOH A    69    11455     2.16            
REMARK 500   O    HOH A    75     O    HOH A    75    11455     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 1001                
DBREF  3MAZ A  167   285  UNP    Q9ULZ2   STAP1_HUMAN    167    285             
DBREF  3MAZ B  133   143  UNP    Q9GZY6   NTAL_HUMAN     133    143             
SEQADV 3MAZ GLY A  161  UNP  Q9ULZ2              EXPRESSION TAG                 
SEQADV 3MAZ SER A  162  UNP  Q9ULZ2              EXPRESSION TAG                 
SEQADV 3MAZ GLY A  163  UNP  Q9ULZ2              EXPRESSION TAG                 
SEQADV 3MAZ ARG A  164  UNP  Q9ULZ2              EXPRESSION TAG                 
SEQADV 3MAZ ALA A  165  UNP  Q9ULZ2              EXPRESSION TAG                 
SEQADV 3MAZ MET A  166  UNP  Q9ULZ2              EXPRESSION TAG                 
SEQADV 3MAZ ALA A  269  UNP  Q9ULZ2    CYS   269 ENGINEERED                     
SEQADV 3MAZ ALA B  142  UNP  Q9GZY6    CYS   142 ENGINEERED                     
SEQADV 3MAZ NH2 B  144  UNP  Q9GZY6              AMIDATION                      
SEQRES   1 A  125  GLY SER GLY ARG ALA MET ASP TYR VAL ASP VAL LEU ASN          
SEQRES   2 A  125  PRO MET PRO ALA CYS PHE TYR THR VAL SER ARG LYS GLU          
SEQRES   3 A  125  ALA THR GLU MET LEU GLN LYS ASN PRO SER LEU GLY ASN          
SEQRES   4 A  125  MET ILE LEU ARG PRO GLY SER ASP SER ARG ASN TYR SER          
SEQRES   5 A  125  ILE THR ILE ARG GLN GLU ILE ASP ILE PRO ARG ILE LYS          
SEQRES   6 A  125  HIS TYR LYS VAL MET SER VAL GLY GLN ASN TYR THR ILE          
SEQRES   7 A  125  GLU LEU GLU LYS PRO VAL THR LEU PRO ASN LEU PHE SER          
SEQRES   8 A  125  VAL ILE ASP TYR PHE VAL LYS GLU THR ARG GLY ASN LEU          
SEQRES   9 A  125  ARG PRO PHE ILE ALA SER THR ASP GLU ASN THR GLY GLN          
SEQRES  10 A  125  GLU PRO SER MET GLU GLY ARG SER                              
SEQRES   1 B   12  ALA ASN SER PTR GLU ASN VAL LEU ILE ALA LYS NH2              
MODRES 3MAZ PTR B  136  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  B 136      16                                                       
HET    NH2  B 144       1                                                       
HET    MLI  A1001       7                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     NH2 AMINO GROUP                                                      
HETNAM     MLI MALONATE ION                                                     
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   2  PTR    C9 H12 N O6 P                                                
FORMUL   2  NH2    H2 N                                                         
FORMUL   3  MLI    C3 H2 O4 2-                                                  
FORMUL   4  HOH   *83(H2 O)                                                     
HELIX    1   1 SER A  183  ASN A  194  1                                  12    
HELIX    2   2 PRO A  195  GLY A  198  5                                   4    
HELIX    3   3 ASN A  248  THR A  260  1                                  13    
SHEET    1   A 5 MET A 200  PRO A 204  0                                        
SHEET    2   A 5 TYR A 211  GLN A 217 -1  O  SER A 212   N  ARG A 203           
SHEET    3   A 5 ARG A 223  VAL A 232 -1  O  LYS A 225   N  ILE A 215           
SHEET    4   A 5 ASN A 235  ILE A 238 -1  O  THR A 237   N  MET A 230           
SHEET    5   A 5 VAL A 244  LEU A 246 -1  O  VAL A 244   N  ILE A 238           
LINK         C   SER B 135                 N   PTR B 136     1555   1555  1.33  
LINK         C   PTR B 136                 N   GLU B 137     1555   1555  1.33  
SITE     1 AC1  3 HOH A   2  HOH A  83  PRO A 266                               
CRYST1   72.640   72.640   97.840  90.00  90.00 120.00 P 62 2 2     12          
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      0.013767  0.007948  0.000000        0.00000                         
SCALE2      0.000000  0.015896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010221        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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