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Database: PDB
Entry: 5TX4
LinkDB: 5TX4
Original site: 5TX4 
HEADER    TRANSFERASE/CYTOKINE                    15-NOV-16   5TX4              
TITLE     DERIVATIVE OF MOUSE TGF-BETA2, WITH A DELETION OF RESIDUES 52-71 AND  
TITLE    2 K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V SINGLE     
TITLE    3 AMINO ACID SUBSTITUTIONS, BOUND TO HUMAN TGF-BETA TYPE II RECEPTOR   
TITLE    4 ECTODOMAIN RESIDUES 15-130                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE-2;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 38-153;                                       
COMPND   5 SYNONYM: TGFR-2,TGF-BETA TYPE II RECEPTOR,TRANSFORMING GROWTH FACTOR-
COMPND   6 BETA RECEPTOR TYPE II,TBETAR-II;                                     
COMPND   7 EC: 2.7.11.30;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: TRANSFORMING GROWTH FACTOR BETA-2;                         
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 303-414;                                      
COMPND  13 SYNONYM: TGF-BETA-2,BSC-1 CELL GROWTH INHIBITOR,CETERMIN,            
COMPND  14 GLIOBLASTOMA-DERIVED T-CELL SUPPRESSOR FACTOR,G-TSF,POLYERGIN;       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TGFBR2;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: TGFB2;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TGF-BETA, TGF-BETA TYPE II RECEPTOR, TRANSFERASE-CYTOKINE COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.P.HINCK,S.KIM                                                       
REVDAT   5   04-DEC-19 5TX4    1       REMARK                                   
REVDAT   4   27-SEP-17 5TX4    1       REMARK                                   
REVDAT   3   10-MAY-17 5TX4    1       JRNL                                     
REVDAT   2   08-MAR-17 5TX4    1       JRNL                                     
REVDAT   1   01-MAR-17 5TX4    0                                                
JRNL        AUTH   S.K.KIM,L.BARRON,C.S.HINCK,E.M.PETRUNAK,K.E.CANO,            
JRNL        AUTH 2 A.THANGIRALA,B.ISKRA,M.BROTHERS,M.VONBERG,B.LEAL,B.RICHTER,  
JRNL        AUTH 3 R.KODALI,A.B.TAYLOR,S.DU,C.O.BARNES,T.SULEA,G.CALERO,        
JRNL        AUTH 4 P.J.HART,M.J.HART,B.DEMELER,A.P.HINCK                        
JRNL        TITL   AN ENGINEERED TRANSFORMING GROWTH FACTOR BETA (TGF-BETA )    
JRNL        TITL 2 MONOMER THAT FUNCTIONS AS A DOMINANT NEGATIVE TO BLOCK       
JRNL        TITL 3 TGF-BETA SIGNALING.                                          
JRNL        REF    J. BIOL. CHEM.                V. 292  7173 2017              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   28228478                                                     
JRNL        DOI    10.1074/JBC.M116.768754                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.88 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17714                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 883                             
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 35.3923 -  3.4082    0.99     2975   170  0.1885 0.2052        
REMARK   3     2  3.4082 -  2.7055    1.00     2874   154  0.1986 0.2193        
REMARK   3     3  2.7055 -  2.3636    1.00     2851   148  0.1869 0.2579        
REMARK   3     4  2.3636 -  2.1475    1.00     2823   126  0.1895 0.2294        
REMARK   3     5  2.1475 -  1.9936    1.00     2836   146  0.2051 0.2635        
REMARK   3     6  1.9936 -  1.8761    0.89     2472   139  0.2300 0.2739        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.970           
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      :  0.011           1621                                  
REMARK   3   ANGLE     :  1.086           2195                                  
REMARK   3   CHIRALITY :  0.064            234                                  
REMARK   3   PLANARITY :  0.007            281                                  
REMARK   3   DIHEDRAL  : 13.387           1026                                  
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 5TX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000224948.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17715                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.876                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.1700                            
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: 1M9Z,5TX2                                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 60 % V/V (+/-)-2    
REMARK 280  -METHYL-2,4-PENTANEDIOL, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  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       19.50950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.55800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.38600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.55800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.50950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.38600            
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                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     VAL A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     GLU A   128                                                      
REMARK 465     GLU A   129                                                      
REMARK 465     TYR A   130                                                      
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   NH2  ARG B     9     O    HOH B   101              1.93            
REMARK 500   NZ   LYS B    54     OXT  SER B    92              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ASP A    87     O    HOH B   101     1545     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  32     -146.91     60.60                                   
REMARK 500    ASN A  68     -167.28   -117.29                                   
REMARK 500    ASN B  42      171.75     66.58                                   
REMARK 500    ALA B  52     -108.84     57.18                                   
REMARK 500    GLN B  61      -82.60   -122.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TX2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TX6   RELATED DB: PDB                                   
DBREF  5TX4 A   15   130  UNP    P37173   TGFR2_HUMAN     38    153             
DBREF  5TX4 B    1    92  UNP    P61812   TGFB2_HUMAN    303    414             
SEQADV 5TX4 ARG B   25  UNP  P61812    LYS   327 ENGINEERED MUTATION            
SEQADV 5TX4 LYS B   26  UNP  P61812    ARG   328 ENGINEERED MUTATION            
SEQADV 5TX4     B       UNP  P61812    LEU   353 DELETION                       
SEQADV 5TX4     B       UNP  P61812    TRP   354 DELETION                       
SEQADV 5TX4     B       UNP  P61812    SER   355 DELETION                       
SEQADV 5TX4     B       UNP  P61812    SER   356 DELETION                       
SEQADV 5TX4     B       UNP  P61812    ASP   357 DELETION                       
SEQADV 5TX4     B       UNP  P61812    THR   358 DELETION                       
SEQADV 5TX4     B       UNP  P61812    GLN   359 DELETION                       
SEQADV 5TX4     B       UNP  P61812    HIS   360 DELETION                       
SEQADV 5TX4     B       UNP  P61812    SER   361 DELETION                       
SEQADV 5TX4     B       UNP  P61812    ARG   362 DELETION                       
SEQADV 5TX4     B       UNP  P61812    VAL   363 DELETION                       
SEQADV 5TX4     B       UNP  P61812    LEU   364 DELETION                       
SEQADV 5TX4     B       UNP  P61812    SER   365 DELETION                       
SEQADV 5TX4     B       UNP  P61812    LEU   366 DELETION                       
SEQADV 5TX4     B       UNP  P61812    TYR   367 DELETION                       
SEQADV 5TX4     B       UNP  P61812    ASN   368 DELETION                       
SEQADV 5TX4     B       UNP  P61812    THR   369 DELETION                       
SEQADV 5TX4     B       UNP  P61812    ILE   370 DELETION                       
SEQADV 5TX4     B       UNP  P61812    ASN   371 DELETION                       
SEQADV 5TX4     B       UNP  P61812    PRO   372 DELETION                       
SEQADV 5TX4 ARG B   51  UNP  P61812    GLU   373 ENGINEERED MUTATION            
SEQADV 5TX4 LYS B   54  UNP  P61812    ALA   376 ENGINEERED MUTATION            
SEQADV 5TX4 SER B   57  UNP  P61812    CYS   379 ENGINEERED MUTATION            
SEQADV 5TX4 VAL B   69  UNP  P61812    LEU   391 ENGINEERED MUTATION            
SEQADV 5TX4 VAL B   72  UNP  P61812    ILE   394 ENGINEERED MUTATION            
SEQADV 5TX4 ARG B   74  UNP  P61812    LYS   396 ENGINEERED MUTATION            
SEQADV 5TX4 LYS B   75  UNP  P61812    THR   397 ENGINEERED MUTATION            
SEQADV 5TX4 VAL B   78  UNP  P61812    ILE   400 ENGINEERED MUTATION            
SEQRES   1 A  116  VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU          
SEQRES   2 A  116  CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN          
SEQRES   3 A  116  GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE          
SEQRES   4 A  116  CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG          
SEQRES   5 A  116  LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS          
SEQRES   6 A  116  ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP          
SEQRES   7 A  116  ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS          
SEQRES   8 A  116  PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP          
SEQRES   9 A  116  GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR              
SEQRES   1 B   92  ALA LEU ASP ALA ALA TYR CYS PHE ARG ASN VAL GLN ASP          
SEQRES   2 B   92  ASN CYS CYS LEU ARG PRO LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 B   92  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 B   92  ASN ALA ASN PHE CYS ALA GLY ALA CYS PRO TYR ARG ALA          
SEQRES   5 B   92  SER LYS SER PRO SER CYS VAL SER GLN ASP LEU GLU PRO          
SEQRES   6 B   92  LEU THR ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL          
SEQRES   7 B   92  GLU GLN LEU SER ASN MET ILE VAL LYS SER CYS LYS CYS          
SEQRES   8 B   92  SER                                                          
FORMUL   3  HOH   *82(H2 O)                                                     
HELIX    1 AA1 GLU A  119  ASN A  121  5                                   3    
HELIX    2 AA2 ALA B    4  ASN B   10  1                                   7    
HELIX    3 AA3 PHE B   24  GLY B   29  1                                   6    
SHEET    1 AA1 4 LEU A  27  LYS A  29  0                                        
SHEET    2 AA1 4 THR A  51  ILE A  53 -1  O  SER A  52   N  CYS A  28           
SHEET    3 AA1 4 LEU B  63  VAL B  72  1  O  TYR B  71   N  ILE A  53           
SHEET    4 AA1 4 ILE B  33  GLU B  35 -1  N  GLU B  35   O  VAL B  69           
SHEET    1 AA2 4 LEU A  27  LYS A  29  0                                        
SHEET    2 AA2 4 THR A  51  ILE A  53 -1  O  SER A  52   N  CYS A  28           
SHEET    3 AA2 4 LEU B  63  VAL B  72  1  O  TYR B  71   N  ILE A  53           
SHEET    4 AA2 4 LYS B  75  VAL B  86 -1  O  GLU B  79   N  ILE B  68           
SHEET    1 AA3 5 ASP A  32  PHE A  35  0                                        
SHEET    2 AA3 5 ILE A  72  HIS A  79 -1  O  LEU A  74   N  ARG A  34           
SHEET    3 AA3 5 VAL A  60  LYS A  67 -1  N  VAL A  64   O  GLU A  75           
SHEET    4 AA3 5 GLU A 108  CYS A 115 -1  O  THR A 109   N  LYS A  67           
SHEET    5 AA3 5 LYS A 101  LYS A 105 -1  N  LYS A 103   O  PHE A 110           
SHEET    1 AA4 3 SER A  43  MET A  45  0                                        
SHEET    2 AA4 3 ASN A 123  ILE A 125 -1  O  ILE A 124   N  CYS A  44           
SHEET    3 AA4 3 CYS A  98  ILE A  99  1  N  CYS A  98   O  ILE A 125           
SHEET    1 AA5 3 LEU B   2  ASP B   3  0                                        
SHEET    2 AA5 3 SER B  88  SER B  92 -1  O  CYS B  89   N  LEU B   2           
SHEET    3 AA5 3 SER B  57  SER B  60 -1  N  VAL B  59   O  LYS B  90           
SHEET    1 AA6 2 CYS B  16  ARG B  18  0                                        
SHEET    2 AA6 2 PHE B  43  ALA B  45 -1  O  PHE B  43   N  ARG B  18           
SHEET    1 AA7 2 TYR B  21  ASP B  23  0                                        
SHEET    2 AA7 2 GLY B  38  ASN B  40 -1  O  TYR B  39   N  ILE B  22           
SSBOND   1 CYS A   28    CYS A   61                          1555   1555  2.04  
SSBOND   2 CYS A   31    CYS A   48                          1555   1555  2.05  
SSBOND   3 CYS A   38    CYS A   44                          1555   1555  2.01  
SSBOND   4 CYS A   54    CYS A   78                          1555   1555  2.08  
SSBOND   5 CYS A   98    CYS A  113                          1555   1555  1.97  
SSBOND   6 CYS A  115    CYS A  120                          1555   1555  2.03  
SSBOND   7 CYS B    7    CYS B   16                          1555   1555  2.04  
SSBOND   8 CYS B   15    CYS B   58                          1555   1555  2.02  
SSBOND   9 CYS B   44    CYS B   89                          1555   1555  2.04  
SSBOND  10 CYS B   48    CYS B   91                          1555   1555  2.06  
CISPEP   1 GLU B   35    PRO B   36          0        -5.51                     
CRYST1   39.019   70.772   77.116  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025629  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014130  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012967        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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