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Database: PDB
Entry: 5MTM
LinkDB: 5MTM
Original site: 5MTM 
HEADER    TRANSFERASE                             10-JAN-17   5MTM              
TITLE     MONOBODY MB(LCK_3) BOUND TO LCK-SH2 DOMAIN                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE LCK;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LEUKOCYTE C-TERMINAL SRC KINASE,LSK,LYMPHOCYTE CELL-SPECIFIC
COMPND   5 PROTEIN-TYROSINE KINASE,PROTEIN YT16,PROTO-ONCOGENE LCK,T CELL-      
COMPND   6 SPECIFIC PROTEIN-TYROSINE KINASE,P56-LCK;                            
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: MONOBODY MB(LCK_3);                                        
COMPND  11 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LCK;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  10 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  11 ORGANISM_TAXID: 10090                                                
KEYWDS    SRC HOMOLOGY DOMAIN, MONOBODIES, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.POJER,T.KUKENSHONER,S.KOIDE,O.HANTSCHEL                             
REVDAT   3   07-MAR-18 5MTM    1       COMPND SOURCE                            
REVDAT   2   03-MAY-17 5MTM    1       JRNL                                     
REVDAT   1   05-APR-17 5MTM    0                                                
JRNL        AUTH   T.KUKENSHONER,N.E.SCHMIT,E.BOUDA,F.SHA,F.POJER,A.KOIDE,      
JRNL        AUTH 2 M.SEELIGER,S.KOIDE,O.HANTSCHEL                               
JRNL        TITL   SELECTIVE TARGETING OF SH2 DOMAIN-PHOSPHOTYROSINE            
JRNL        TITL 2 INTERACTIONS OF SRC FAMILY TYROSINE KINASES WITH MONOBODIES. 
JRNL        REF    J. MOL. BIOL.                 V. 429  1364 2017              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   28347651                                                     
JRNL        DOI    10.1016/J.JMB.2017.03.023                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.260                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 14544                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1335                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.9229 -  5.1774    1.00     2521   139  0.1912 0.2417        
REMARK   3     2  5.1774 -  4.1107    1.00     2533   133  0.1639 0.2041        
REMARK   3     3  4.1107 -  3.5914    1.00     2541   133  0.2065 0.2683        
REMARK   3     4  3.5914 -  3.2632    1.00     2541   134  0.2177 0.2424        
REMARK   3     5  3.2632 -  3.0294    1.00     2540   132  0.2316 0.3653        
REMARK   3     6  3.0294 -  2.8508    1.00     2543   135  0.2302 0.2747        
REMARK   3     7  2.8508 -  2.7081    1.00     2523   135  0.2505 0.2842        
REMARK   3     8  2.7081 -  2.5902    1.00     2557   131  0.2620 0.3145        
REMARK   3     9  2.5902 -  2.4905    1.00     2529   133  0.2749 0.3190        
REMARK   3    10  2.4905 -  2.4046    0.99     2497   130  0.3080 0.3826        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.230           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           1598                                  
REMARK   3   ANGLE     :  1.159           2183                                  
REMARK   3   CHIRALITY :  0.062            242                                  
REMARK   3   PLANARITY :  0.008            283                                  
REMARK   3   DIHEDRAL  : 13.157            934                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MTM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200002984.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14544                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 37.9100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.5, 15 % PEG 20000, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       52.98050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.91700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.91700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.49025            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.91700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.91700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       79.47075            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.91700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.91700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       26.49025            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.91700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.91700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       79.47075            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       52.98050            
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: 1530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLN A   112                                                      
REMARK 465     LYS A   113                                                      
REMARK 465     PRO A   114                                                      
REMARK 465     GLN A   115                                                      
REMARK 465     LYS A   116                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   8    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  15    CG   CD   CE   NZ                                   
REMARK 470     ASN A  16    CG   OD1  ND2                                       
REMARK 470     LYS A  67    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASN A    70     O    HOH A   201              2.11            
REMARK 500   OH   TYR A    94     O    HOH A   202              2.14            
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    LYS A  15     -114.93    -47.89                                   
REMARK 500    ASN A  16       94.04     -2.29                                   
REMARK 500    ASP A  99       50.75     39.99                                   
REMARK 500    PRO B   7     -169.57    -72.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A   15     ASN A   16                 -147.85                    
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                              ZN B 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  11   OE1                                                    
REMARK 620 2 GLU B  11   OE2  53.0                                              
REMARK 620 3 ASP A  56   OD1  20.4  33.2                                        
REMARK 620 4 ASP A  56   OD2  20.0  34.2   1.9                                  
REMARK 620 5 GLU A  61   OE1  22.7  30.6   2.8   4.4                            
REMARK 620 6 GLU A  61   OE2  22.9  31.1   2.5   3.2   2.2                      
REMARK 620 7 HOH A 205   O    79.1  83.2  75.4  73.6  76.7  74.5                
REMARK 620 8 HOH A 206   O    73.2 125.3  92.1  91.0  94.8  94.2  77.6          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  40   OE1                                                    
REMARK 620 2 ASP B  43   OD2 102.8                                              
REMARK 620 3 GLU A  10   OE1 136.2  56.5                                        
REMARK 620 4 GLU A  10   OE2 133.2  56.5   3.1                                  
REMARK 620 5 HOH A 210   O    76.5  84.3 130.4 132.5                            
REMARK 620 6 HOH A 208   O    78.2 115.9  78.7  76.4 150.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 102                  
DBREF  5MTM A    3   116  UNP    P06239   LCK_HUMAN      118    231             
DBREF  5MTM B    1    95  PDB    5MTM     5MTM             1     95             
SEQADV 5MTM GLY A    1  UNP  P06239              EXPRESSION TAG                 
SEQADV 5MTM SER A    2  UNP  P06239              EXPRESSION TAG                 
SEQRES   1 A  116  GLY SER LYS ALA ASN SER LEU GLU PRO GLU PRO TRP PHE          
SEQRES   2 A  116  PHE LYS ASN LEU SER ARG LYS ASP ALA GLU ARG GLN LEU          
SEQRES   3 A  116  LEU ALA PRO GLY ASN THR HIS GLY SER PHE LEU ILE ARG          
SEQRES   4 A  116  GLU SER GLU SER THR ALA GLY SER PHE SER LEU SER VAL          
SEQRES   5 A  116  ARG ASP PHE ASP GLN ASN GLN GLY GLU VAL VAL LYS HIS          
SEQRES   6 A  116  TYR LYS ILE ARG ASN LEU ASP ASN GLY GLY PHE TYR ILE          
SEQRES   7 A  116  SER PRO ARG ILE THR PHE PRO GLY LEU HIS GLU LEU VAL          
SEQRES   8 A  116  ARG HIS TYR THR ASN ALA SER ASP GLY LEU CYS THR ARG          
SEQRES   9 A  116  LEU SER ARG PRO CYS GLN THR GLN LYS PRO GLN LYS              
SEQRES   1 B   95  GLY SER VAL SER SER VAL PRO THR LYS LEU GLU VAL VAL          
SEQRES   2 B   95  ALA ALA THR PRO THR SER LEU LEU ILE SER TRP ASP ALA          
SEQRES   3 B   95  PRO ALA VAL THR VAL LEU TYR TYR LEU ILE THR TYR GLY          
SEQRES   4 B   95  GLU THR GLY ASP HIS TRP SER GLY HIS GLN ALA PHE GLU          
SEQRES   5 B   95  VAL PRO GLY SER LYS SER THR ALA THR ILE SER GLY LEU          
SEQRES   6 B   95  LYS PRO GLY VAL ASP TYR THR ILE THR VAL TYR ALA HIS          
SEQRES   7 B   95  ALA GLU SER TYR GLY GLU SER TYR SER PRO ILE SER ILE          
SEQRES   8 B   95  ASN TYR ARG THR                                              
HET     ZN  B 101       1                                                       
HET     ZN  B 102       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   5  HOH   *32(H2 O)                                                     
HELIX    1 AA1 SER A   18  ALA A   28  1                                  11    
HELIX    2 AA2 GLY A   86  ALA A   97  1                                  12    
HELIX    3 AA3 HIS B   44  HIS B   48  5                                   5    
SHEET    1 AA1 4 PHE A  13  PHE A  14  0                                        
SHEET    2 AA1 4 SER A  35  GLU A  40  1  O  ILE A  38   N  PHE A  14           
SHEET    3 AA1 4 PHE A  48  ARG A  53 -1  O  ARG A  53   N  SER A  35           
SHEET    4 AA1 4 VAL A  63  LYS A  67 -1  O  LYS A  64   N  VAL A  52           
SHEET    1 AA2 3 PHE A  13  PHE A  14  0                                        
SHEET    2 AA2 3 SER A  35  GLU A  40  1  O  ILE A  38   N  PHE A  14           
SHEET    3 AA2 3 ARG A 107  PRO A 108  1  O  ARG A 107   N  PHE A  36           
SHEET    1 AA3 2 ARG A  69  ASN A  70  0                                        
SHEET    2 AA3 2 PHE A  76  TYR A  77 -1  O  TYR A  77   N  ARG A  69           
SHEET    1 AA4 2 ILE A  82  THR A  83  0                                        
SHEET    2 AA4 2 GLY B  83  GLU B  84 -1  O  GLY B  83   N  THR A  83           
SHEET    1 AA5 3 THR B   8  ALA B  15  0                                        
SHEET    2 AA5 3 LEU B  20  ASP B  25 -1  O  LEU B  21   N  VAL B  13           
SHEET    3 AA5 3 THR B  59  ILE B  62 -1  O  ALA B  60   N  ILE B  22           
SHEET    1 AA6 4 GLN B  49  PRO B  54  0                                        
SHEET    2 AA6 4 TYR B  33  GLU B  40 -1  N  TYR B  34   O  VAL B  53           
SHEET    3 AA6 4 ASP B  70  HIS B  78 -1  O  THR B  72   N  GLY B  39           
SHEET    4 AA6 4 ILE B  89  ARG B  94 -1  O  ILE B  89   N  VAL B  75           
LINK         OE1 GLU B  11                ZN    ZN B 102     1555   1555  2.66  
LINK         OE2 GLU B  11                ZN    ZN B 102     1555   1555  2.26  
LINK         OE1 GLU B  40                ZN    ZN B 101     1555   1555  2.14  
LINK         OD2 ASP B  43                ZN    ZN B 101     1555   1555  2.45  
LINK         OE1 GLU A  10                ZN    ZN B 101     1555   3555  2.44  
LINK         OE2 GLU A  10                ZN    ZN B 101     1555   3555  2.12  
LINK         OD1 ASP A  56                ZN    ZN B 102     1555   6554  2.43  
LINK         OD2 ASP A  56                ZN    ZN B 102     1555   6554  2.29  
LINK         OE1 GLU A  61                ZN    ZN B 102     1555   6554  2.40  
LINK         OE2 GLU A  61                ZN    ZN B 102     1555   6554  2.42  
LINK        ZN    ZN B 101                 O   HOH A 210     1555   4454  2.50  
LINK        ZN    ZN B 101                 O   HOH A 208     1555   4454  2.30  
LINK        ZN    ZN B 102                 O   HOH A 205     1555   6454  2.59  
LINK        ZN    ZN B 102                 O   HOH A 206     1555   6454  2.17  
CISPEP   1 VAL B    6    PRO B    7          0        -5.22                     
SITE     1 AC1  5 GLU A  10  HOH A 208  HOH A 210  GLU B  40                    
SITE     2 AC1  5 ASP B  43                                                     
SITE     1 AC2  5 ASP A  56  GLU A  61  HOH A 205  HOH A 206                    
SITE     2 AC2  5 GLU B  11                                                     
CRYST1   81.834   81.834  105.961  90.00  90.00  90.00 P 41 21 2     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      0.012220  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009437        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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