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Database: PDB
Entry: 4KXZ
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Original site: 4KXZ 
HEADER    IMMUNE SYSTEM                           28-MAY-13   4KXZ              
TITLE     CRYSTAL STRUCTURE OF TGFB2 IN COMPLEX WITH GC2008.                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA-2;                         
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 303-414;                                      
COMPND   5 SYNONYM: TGF-BETA-2, BSC-1 CELL GROWTH INHIBITOR, CETERMIN,          
COMPND   6 GLIOBLASTOMA-DERIVED T-CELL SUPPRESSOR FACTOR, G-TSF, POLYERGIN,     
COMPND   7 LATENCY-ASSOCIATED PEPTIDE, LAP;                                     
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: GC1008 HEAVY CHAIN;                                        
COMPND  11 CHAIN: H, J, N, Q;                                                   
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: GC1008 LIGHT CHAIN;                                        
COMPND  15 CHAIN: I, L, M, P;                                                   
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TGFB2;                                                         
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 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    CYSTEINE KNOT, FAB, VARIOUS GROWTH FUNCTIONS (TGF-BETA), TGF-BETA     
KEYWDS   2 ANTAGONIST (GC2008), TGF-BETA RECEPTORS, IMMUNE SYSTEM               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MATHIEU,A.G.MOULIN,R.WEI                                            
REVDAT   2   03-DEC-14 4KXZ    1       JRNL                                     
REVDAT   1   24-SEP-14 4KXZ    0                                                
JRNL        AUTH   A.MOULIN,M.MATHIEU,C.LAWRENCE,R.BIGELOW,M.LEVINE,C.HAMEL,    
JRNL        AUTH 2 J.P.MARQUETTE,J.LE PARC,C.LOUX,P.FERRARI,C.CAPDEVILA,        
JRNL        AUTH 3 J.DUMAS,B.DUMAS,A.RAK,J.BIRD,H.QIU,C.Q.PAN,T.EDMUNDS,R.R.WEI 
JRNL        TITL   STRUCTURES OF A PAN-SPECIFIC ANTAGONIST ANTIBODY COMPLEXED   
JRNL        TITL 2 TO DIFFERENT ISOFORMS OF TGF BETA REVEAL STRUCTURAL          
JRNL        TITL 3 PLASTICITY OF ANTIBODY-ANTIGEN INTERACTIONS.                 
JRNL        REF    PROTEIN SCI.                  V.  23  1698 2014              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   25209176                                                     
JRNL        DOI    10.1002/PRO.2548                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.1                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 74174                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : NULL                           
REMARK   3   R VALUE            (WORKING SET)  : 0.183                          
REMARK   3   FREE R VALUE                      : 0.222                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3709                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.83                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.90                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.87                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5319                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2313                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5053                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2272                   
REMARK   3   BIN FREE R VALUE                        : 0.3115                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 266                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16652                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 73                                      
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.63                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.55230                                              
REMARK   3    B22 (A**2) : -1.39330                                             
REMARK   3    B33 (A**2) : -1.15900                                             
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) : 0.334               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.841               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 17149  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 23361  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5667   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 354    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2489   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 17149  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 2271   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 18537  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.19                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.32                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 19.06                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4KXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079935.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98011                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74205                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.730                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12100                            
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) : 2.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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   (%): 61.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG400, 100MM MES, VAPOR             
REMARK 280  DIFFUSION, TEMPERATURE 296K, PH 6.0                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       65.60000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      179.84000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       65.60000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      179.84000            
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13870 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, J, I, L                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14310 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 47730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, N, Q, M, P                      
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     GLN H     1                                                      
REMARK 465     GLN J     1                                                      
REMARK 465     ARG J   136                                                      
REMARK 465     SER J   137                                                      
REMARK 465     THR J   138                                                      
REMARK 465     HIS J   222                                                      
REMARK 465     HIS J   223                                                      
REMARK 465     HIS J   224                                                      
REMARK 465     GLN N     1                                                      
REMARK 465     ARG Q   136                                                      
REMARK 465     SER Q   137                                                      
REMARK 465     THR Q   138                                                      
REMARK 465     SER Q   139                                                      
REMARK 465     HIS Q   222                                                      
REMARK 465     HIS Q   223                                                      
REMARK 465     HIS Q   224                                                      
REMARK 465     GLU I     1                                                      
REMARK 465     GLU I   214                                                      
REMARK 465     CYS I   215                                                      
REMARK 465     GLU L   214                                                      
REMARK 465     CYS L   215                                                      
REMARK 465     GLU M   214                                                      
REMARK 465     CYS M   215                                                      
REMARK 465     GLU P   214                                                      
REMARK 465     CYS P   215                                                      
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   ND1  HIS H   223     O    HOH H   328              2.14            
REMARK 500   OE1  GLU I    80     O    HOH I   307              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    HIS H 224   CB  -  CA  -  C   ANGL. DEV. =  12.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  42      167.52     66.81                                   
REMARK 500    CYS A  48       71.84   -116.59                                   
REMARK 500    GLN A  81      -76.78   -114.44                                   
REMARK 500    CYS B  15      115.22    -26.47                                   
REMARK 500    ASN B  42      170.24     65.72                                   
REMARK 500    CYS B  48       69.70   -114.18                                   
REMARK 500    GLN B  81      -74.62   -115.82                                   
REMARK 500    LEU D   2       59.70    -93.49                                   
REMARK 500    CYS D  15      119.78    -34.67                                   
REMARK 500    ASN D  42      176.41     65.83                                   
REMARK 500    CYS D  48       72.18   -115.44                                   
REMARK 500    GLN D  81      -73.96   -115.52                                   
REMARK 500    CYS E  15      117.57    -35.24                                   
REMARK 500    ASN E  42      175.92     64.49                                   
REMARK 500    CYS E  48       72.43   -116.18                                   
REMARK 500    GLN E  81      -74.24   -116.60                                   
REMARK 500    TYR H  27       61.23   -103.91                                   
REMARK 500    ILE H  54      -52.05     70.97                                   
REMARK 500    SER H 135      -15.95     75.77                                   
REMARK 500    THR H 138        6.88    -62.73                                   
REMARK 500    SER H 139       44.06    -64.63                                   
REMARK 500    HIS H 223      105.36     56.35                                   
REMARK 500    SER J  25       78.17    -68.44                                   
REMARK 500    ARG J  67      -13.87   -141.33                                   
REMARK 500    SER J  75      -84.69    -53.77                                   
REMARK 500    THR J  76       -4.97    -49.33                                   
REMARK 500    PRO J 133     -159.05    -82.83                                   
REMARK 500    CYS J 134      -39.40   -133.26                                   
REMARK 500    HIS J 219     -101.49    -98.60                                   
REMARK 500    SER N  31       44.55   -105.05                                   
REMARK 500    SER N 135      -49.32    164.12                                   
REMARK 500    GLU N 140     -166.88   -102.01                                   
REMARK 500    HIS N 223      102.85     60.08                                   
REMARK 500    SER Q  25       47.24    -67.15                                   
REMARK 500    TYR Q  27       -5.69     62.13                                   
REMARK 500    SER Q  75       -9.13    -54.08                                   
REMARK 500    CYS Q 134      -57.33   -120.31                                   
REMARK 500    LEU Q 196      -79.47    -50.17                                   
REMARK 500    HIS Q 219     -134.89    -92.14                                   
REMARK 500    ALA I  52      -32.07     60.59                                   
REMARK 500    ASN I 153       -8.50     66.70                                   
REMARK 500    LYS I 191      -63.90   -104.18                                   
REMARK 500    ARG I 212       32.12    -72.65                                   
REMARK 500    SER L  31       -3.75   -140.57                                   
REMARK 500    ALA L  52      -28.39     59.21                                   
REMARK 500    SER L  53       -6.48   -140.45                                   
REMARK 500    ALA L  85     -176.23    177.60                                   
REMARK 500    ASN L 153       -9.28     75.39                                   
REMARK 500    LYS L 191      -70.17   -104.52                                   
REMARK 500    GLN L 200      -36.84    -29.58                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A  24        24.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU A  51        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP H  56        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ASN J  32        24.7      L          L   OUTSIDE RANGE           
REMARK 500    GLN J  62        23.9      L          L   OUTSIDE RANGE           
REMARK 500    CYS N 134        24.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU N 140        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN Q  32        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE5 P  701                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES J 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES Q 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES M 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE5 P 701                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4KV5   RELATED DB: PDB                                   
REMARK 900 GC1009 IN COMPLEX WITH TGF-BETA1                                     
REMARK 900 RELATED ID: 3EO1   RELATED DB: PDB                                   
REMARK 900 GC1008 IN COMPLEX WITH TGF-BETA3                                     
REMARK 900 RELATED ID: 3EO0   RELATED DB: PDB                                   
REMARK 900 GC1008 FAB                                                           
DBREF  4KXZ A    1   112  UNP    P61812   TGFB2_HUMAN    303    414             
DBREF  4KXZ B    1   112  UNP    P61812   TGFB2_HUMAN    303    414             
DBREF  4KXZ D    1   112  UNP    P61812   TGFB2_HUMAN    303    414             
DBREF  4KXZ E    1   112  UNP    P61812   TGFB2_HUMAN    303    414             
DBREF  4KXZ H    1   224  PDB    4KXZ     4KXZ             1    224             
DBREF  4KXZ J    1   224  PDB    4KXZ     4KXZ             1    224             
DBREF  4KXZ N    1   224  PDB    4KXZ     4KXZ             1    224             
DBREF  4KXZ Q    1   224  PDB    4KXZ     4KXZ             1    224             
DBREF  4KXZ I    1   215  PDB    4KXZ     4KXZ             1    215             
DBREF  4KXZ L    1   215  PDB    4KXZ     4KXZ             1    215             
DBREF  4KXZ M    1   215  PDB    4KXZ     4KXZ             1    215             
DBREF  4KXZ P    1   215  PDB    4KXZ     4KXZ             1    215             
SEQRES   1 A  112  ALA LEU ASP ALA ALA TYR CYS PHE ARG ASN VAL GLN ASP          
SEQRES   2 A  112  ASN CYS CYS LEU ARG PRO LEU TYR ILE ASP PHE LYS ARG          
SEQRES   3 A  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 A  112  ASN ALA ASN PHE CYS ALA GLY ALA CYS PRO TYR LEU TRP          
SEQRES   5 A  112  SER SER ASP THR GLN HIS SER ARG VAL LEU SER LEU TYR          
SEQRES   6 A  112  ASN THR ILE ASN PRO GLU ALA SER ALA SER PRO CYS CYS          
SEQRES   7 A  112  VAL SER GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR          
SEQRES   8 A  112  ILE GLY LYS THR PRO LYS ILE GLU GLN LEU SER ASN MET          
SEQRES   9 A  112  ILE VAL LYS SER CYS LYS CYS SER                              
SEQRES   1 B  112  ALA LEU ASP ALA ALA TYR CYS PHE ARG ASN VAL GLN ASP          
SEQRES   2 B  112  ASN CYS CYS LEU ARG PRO LEU TYR ILE ASP PHE LYS ARG          
SEQRES   3 B  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 B  112  ASN ALA ASN PHE CYS ALA GLY ALA CYS PRO TYR LEU TRP          
SEQRES   5 B  112  SER SER ASP THR GLN HIS SER ARG VAL LEU SER LEU TYR          
SEQRES   6 B  112  ASN THR ILE ASN PRO GLU ALA SER ALA SER PRO CYS CYS          
SEQRES   7 B  112  VAL SER GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR          
SEQRES   8 B  112  ILE GLY LYS THR PRO LYS ILE GLU GLN LEU SER ASN MET          
SEQRES   9 B  112  ILE VAL LYS SER CYS LYS CYS SER                              
SEQRES   1 D  112  ALA LEU ASP ALA ALA TYR CYS PHE ARG ASN VAL GLN ASP          
SEQRES   2 D  112  ASN CYS CYS LEU ARG PRO LEU TYR ILE ASP PHE LYS ARG          
SEQRES   3 D  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 D  112  ASN ALA ASN PHE CYS ALA GLY ALA CYS PRO TYR LEU TRP          
SEQRES   5 D  112  SER SER ASP THR GLN HIS SER ARG VAL LEU SER LEU TYR          
SEQRES   6 D  112  ASN THR ILE ASN PRO GLU ALA SER ALA SER PRO CYS CYS          
SEQRES   7 D  112  VAL SER GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR          
SEQRES   8 D  112  ILE GLY LYS THR PRO LYS ILE GLU GLN LEU SER ASN MET          
SEQRES   9 D  112  ILE VAL LYS SER CYS LYS CYS SER                              
SEQRES   1 E  112  ALA LEU ASP ALA ALA TYR CYS PHE ARG ASN VAL GLN ASP          
SEQRES   2 E  112  ASN CYS CYS LEU ARG PRO LEU TYR ILE ASP PHE LYS ARG          
SEQRES   3 E  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 E  112  ASN ALA ASN PHE CYS ALA GLY ALA CYS PRO TYR LEU TRP          
SEQRES   5 E  112  SER SER ASP THR GLN HIS SER ARG VAL LEU SER LEU TYR          
SEQRES   6 E  112  ASN THR ILE ASN PRO GLU ALA SER ALA SER PRO CYS CYS          
SEQRES   7 E  112  VAL SER GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR          
SEQRES   8 E  112  ILE GLY LYS THR PRO LYS ILE GLU GLN LEU SER ASN MET          
SEQRES   9 E  112  ILE VAL LYS SER CYS LYS CYS SER                              
SEQRES   1 H  224  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  224  PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  224  TYR THR PHE SER SER ASN VAL ILE SER TRP VAL ARG GLN          
SEQRES   4 H  224  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY VAL ILE          
SEQRES   5 H  224  PRO ILE VAL ASP ILE ALA ASN TYR ALA GLN ARG PHE LYS          
SEQRES   6 H  224  GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR          
SEQRES   7 H  224  THR TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  224  ALA VAL TYR TYR CYS ALA SER THR LEU GLY LEU VAL LEU          
SEQRES   9 H  224  ASP ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 H  224  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 H  224  LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR ALA          
SEQRES  12 H  224  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 H  224  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 H  224  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 H  224  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 H  224  LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS          
SEQRES  17 H  224  PRO SER ASN THR LYS VAL ASP LYS ARG VAL HIS HIS HIS          
SEQRES  18 H  224  HIS HIS HIS                                                  
SEQRES   1 J  224  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 J  224  PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 J  224  TYR THR PHE SER SER ASN VAL ILE SER TRP VAL ARG GLN          
SEQRES   4 J  224  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY VAL ILE          
SEQRES   5 J  224  PRO ILE VAL ASP ILE ALA ASN TYR ALA GLN ARG PHE LYS          
SEQRES   6 J  224  GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR          
SEQRES   7 J  224  THR TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 J  224  ALA VAL TYR TYR CYS ALA SER THR LEU GLY LEU VAL LEU          
SEQRES   9 J  224  ASP ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 J  224  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 J  224  LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR ALA          
SEQRES  12 J  224  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 J  224  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 J  224  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 J  224  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 J  224  LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS          
SEQRES  17 J  224  PRO SER ASN THR LYS VAL ASP LYS ARG VAL HIS HIS HIS          
SEQRES  18 J  224  HIS HIS HIS                                                  
SEQRES   1 N  224  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 N  224  PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 N  224  TYR THR PHE SER SER ASN VAL ILE SER TRP VAL ARG GLN          
SEQRES   4 N  224  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY VAL ILE          
SEQRES   5 N  224  PRO ILE VAL ASP ILE ALA ASN TYR ALA GLN ARG PHE LYS          
SEQRES   6 N  224  GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR          
SEQRES   7 N  224  THR TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 N  224  ALA VAL TYR TYR CYS ALA SER THR LEU GLY LEU VAL LEU          
SEQRES   9 N  224  ASP ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 N  224  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 N  224  LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR ALA          
SEQRES  12 N  224  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 N  224  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 N  224  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 N  224  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 N  224  LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS          
SEQRES  17 N  224  PRO SER ASN THR LYS VAL ASP LYS ARG VAL HIS HIS HIS          
SEQRES  18 N  224  HIS HIS HIS                                                  
SEQRES   1 Q  224  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 Q  224  PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 Q  224  TYR THR PHE SER SER ASN VAL ILE SER TRP VAL ARG GLN          
SEQRES   4 Q  224  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY VAL ILE          
SEQRES   5 Q  224  PRO ILE VAL ASP ILE ALA ASN TYR ALA GLN ARG PHE LYS          
SEQRES   6 Q  224  GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR          
SEQRES   7 Q  224  THR TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 Q  224  ALA VAL TYR TYR CYS ALA SER THR LEU GLY LEU VAL LEU          
SEQRES   9 Q  224  ASP ALA MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR          
SEQRES  10 Q  224  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 Q  224  LEU ALA PRO CYS SER ARG SER THR SER GLU SER THR ALA          
SEQRES  12 Q  224  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 Q  224  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 Q  224  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 Q  224  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 Q  224  LEU GLY THR LYS THR TYR THR CYS ASN VAL ASP HIS LYS          
SEQRES  17 Q  224  PRO SER ASN THR LYS VAL ASP LYS ARG VAL HIS HIS HIS          
SEQRES  18 Q  224  HIS HIS HIS                                                  
SEQRES   1 I  215  GLU THR VAL LEU THR GLN SER PRO GLY THR LEU SER LEU          
SEQRES   2 I  215  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 I  215  GLN SER LEU GLY SER SER TYR LEU ALA TRP TYR GLN GLN          
SEQRES   4 I  215  LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA          
SEQRES   5 I  215  SER SER ARG ALA PRO GLY ILE PRO ASP ARG PHE SER GLY          
SEQRES   6 I  215  SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG          
SEQRES   7 I  215  LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN          
SEQRES   8 I  215  TYR ALA ASP SER PRO ILE THR PHE GLY GLN GLY THR ARG          
SEQRES   9 I  215  LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE          
SEQRES  10 I  215  ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR          
SEQRES  11 I  215  ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG          
SEQRES  12 I  215  GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN          
SEQRES  13 I  215  SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER          
SEQRES  14 I  215  LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU          
SEQRES  15 I  215  SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS          
SEQRES  16 I  215  GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS          
SEQRES  17 I  215  SER PHE ASN ARG GLY GLU CYS                                  
SEQRES   1 L  215  GLU THR VAL LEU THR GLN SER PRO GLY THR LEU SER LEU          
SEQRES   2 L  215  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 L  215  GLN SER LEU GLY SER SER TYR LEU ALA TRP TYR GLN GLN          
SEQRES   4 L  215  LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA          
SEQRES   5 L  215  SER SER ARG ALA PRO GLY ILE PRO ASP ARG PHE SER GLY          
SEQRES   6 L  215  SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG          
SEQRES   7 L  215  LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN          
SEQRES   8 L  215  TYR ALA ASP SER PRO ILE THR PHE GLY GLN GLY THR ARG          
SEQRES   9 L  215  LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE          
SEQRES  10 L  215  ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR          
SEQRES  11 L  215  ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG          
SEQRES  12 L  215  GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN          
SEQRES  13 L  215  SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER          
SEQRES  14 L  215  LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU          
SEQRES  15 L  215  SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS          
SEQRES  16 L  215  GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS          
SEQRES  17 L  215  SER PHE ASN ARG GLY GLU CYS                                  
SEQRES   1 M  215  GLU THR VAL LEU THR GLN SER PRO GLY THR LEU SER LEU          
SEQRES   2 M  215  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 M  215  GLN SER LEU GLY SER SER TYR LEU ALA TRP TYR GLN GLN          
SEQRES   4 M  215  LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA          
SEQRES   5 M  215  SER SER ARG ALA PRO GLY ILE PRO ASP ARG PHE SER GLY          
SEQRES   6 M  215  SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG          
SEQRES   7 M  215  LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN          
SEQRES   8 M  215  TYR ALA ASP SER PRO ILE THR PHE GLY GLN GLY THR ARG          
SEQRES   9 M  215  LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE          
SEQRES  10 M  215  ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR          
SEQRES  11 M  215  ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG          
SEQRES  12 M  215  GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN          
SEQRES  13 M  215  SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER          
SEQRES  14 M  215  LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU          
SEQRES  15 M  215  SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS          
SEQRES  16 M  215  GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS          
SEQRES  17 M  215  SER PHE ASN ARG GLY GLU CYS                                  
SEQRES   1 P  215  GLU THR VAL LEU THR GLN SER PRO GLY THR LEU SER LEU          
SEQRES   2 P  215  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 P  215  GLN SER LEU GLY SER SER TYR LEU ALA TRP TYR GLN GLN          
SEQRES   4 P  215  LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA          
SEQRES   5 P  215  SER SER ARG ALA PRO GLY ILE PRO ASP ARG PHE SER GLY          
SEQRES   6 P  215  SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG          
SEQRES   7 P  215  LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN          
SEQRES   8 P  215  TYR ALA ASP SER PRO ILE THR PHE GLY GLN GLY THR ARG          
SEQRES   9 P  215  LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE          
SEQRES  10 P  215  ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR          
SEQRES  11 P  215  ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG          
SEQRES  12 P  215  GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN          
SEQRES  13 P  215  SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER          
SEQRES  14 P  215  LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU          
SEQRES  15 P  215  SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS          
SEQRES  16 P  215  GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS          
SEQRES  17 P  215  SER PHE ASN ARG GLY GLU CYS                                  
HET    MES  A 201      12                                                       
HET    MES  E 201      12                                                       
HET    MES  J 301      12                                                       
HET    MES  Q 801      12                                                       
HET    MES  M 301      12                                                       
HET    PE5  P 701      13                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL                       
HETSYN     PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-           
HETSYN   2 PE5  ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL, POLYETHYLENE           
HETSYN   3 PE5  GLYCOL PEG400                                                   
FORMUL  13  MES    5(C6 H13 N O4 S)                                             
FORMUL  18  PE5    C18 H38 O9                                                   
FORMUL  19  HOH   *226(H2 O)                                                    
HELIX    1   1 ALA A    4  PHE A    8  1                                   5    
HELIX    2   2 PHE A   24  GLY A   29  1                                   6    
HELIX    3   3 THR A   56  ASN A   69  1                                  14    
HELIX    4   4 PRO A   70  SER A   73  5                                   4    
HELIX    5   5 ALA B    4  PHE B    8  1                                   5    
HELIX    6   6 PHE B   24  GLY B   29  1                                   6    
HELIX    7   7 THR B   56  ASN B   69  1                                  14    
HELIX    8   8 PRO B   70  SER B   73  5                                   4    
HELIX    9   9 ASP D    3  PHE D    8  1                                   6    
HELIX   10  10 PHE D   24  GLY D   29  1                                   6    
HELIX   11  11 THR D   56  ASN D   69  1                                  14    
HELIX   12  12 PRO D   70  SER D   73  5                                   4    
HELIX   13  13 ASP E    3  PHE E    8  1                                   6    
HELIX   14  14 PHE E   24  GLY E   29  1                                   6    
HELIX   15  15 THR E   56  ASN E   69  1                                  14    
HELIX   16  16 PRO E   70  SER E   73  5                                   4    
HELIX   17  17 GLN H   62  LYS H   65  5                                   4    
HELIX   18  18 ARG H   87  THR H   91  5                                   5    
HELIX   19  19 SER H  163  ALA H  165  5                                   3    
HELIX   20  20 SER H  194  LEU H  196  5                                   3    
HELIX   21  21 LYS H  208  ASN H  211  5                                   4    
HELIX   22  22 GLY J   26  PHE J   29  5                                   4    
HELIX   23  23 ARG J   87  THR J   91  5                                   5    
HELIX   24  24 SER J  163  ALA J  165  5                                   3    
HELIX   25  25 SER J  194  LEU J  196  5                                   3    
HELIX   26  26 LYS J  208  ASN J  211  5                                   4    
HELIX   27  27 GLN N   62  LYS N   65  5                                   4    
HELIX   28  28 ARG N   87  THR N   91  5                                   5    
HELIX   29  29 SER N  163  ALA N  165  5                                   3    
HELIX   30  30 SER N  194  LEU N  196  5                                   3    
HELIX   31  31 LYS N  208  ASN N  211  5                                   4    
HELIX   32  32 TYR Q   27  ASN Q   32  1                                   6    
HELIX   33  33 GLU Q   74  THR Q   76  5                                   3    
HELIX   34  34 ARG Q   87  THR Q   91  5                                   5    
HELIX   35  35 SER Q  163  ALA Q  165  5                                   3    
HELIX   36  36 SER Q  193  GLY Q  197  1                                   5    
HELIX   37  37 LYS Q  208  ASN Q  211  5                                   4    
HELIX   38  38 GLU I   80  PHE I   84  5                                   5    
HELIX   39  39 SER I  122  SER I  128  1                                   7    
HELIX   40  40 LYS I  184  LYS I  189  1                                   6    
HELIX   41  41 GLU L   80  PHE L   84  5                                   5    
HELIX   42  42 SER L  122  SER L  128  1                                   7    
HELIX   43  43 LYS L  184  LYS L  189  1                                   6    
HELIX   44  44 GLU M   80  PHE M   84  5                                   5    
HELIX   45  45 SER M  122  SER M  128  1                                   7    
HELIX   46  46 LYS M  184  LYS M  189  1                                   6    
HELIX   47  47 GLU P   80  PHE P   84  5                                   5    
HELIX   48  48 SER P  122  LYS P  127  1                                   6    
HELIX   49  49 LYS P  184  LYS P  189  1                                   6    
SHEET    1   A 3 LEU A   2  ASP A   3  0                                        
SHEET    2   A 3 SER A 108  SER A 112 -1  O  CYS A 109   N  LEU A   2           
SHEET    3   A 3 CYS A  77  SER A  80 -1  N  VAL A  79   O  LYS A 110           
SHEET    1   B 2 CYS A  16  ARG A  18  0                                        
SHEET    2   B 2 PHE A  43  ALA A  45 -1  O  PHE A  43   N  ARG A  18           
SHEET    1   C 2 ILE A  22  ASP A  23  0                                        
SHEET    2   C 2 GLY A  38  TYR A  39 -1  O  TYR A  39   N  ILE A  22           
SHEET    1   D 3 ILE A  33  GLU A  35  0                                        
SHEET    2   D 3 LEU A  83  ILE A  92 -1  O  LEU A  89   N  GLU A  35           
SHEET    3   D 3 THR A  95  VAL A 106 -1  O  LEU A 101   N  LEU A  86           
SHEET    1   E 3 LEU B   2  ASP B   3  0                                        
SHEET    2   E 3 SER B 108  SER B 112 -1  O  CYS B 109   N  LEU B   2           
SHEET    3   E 3 CYS B  77  SER B  80 -1  N  VAL B  79   O  LYS B 110           
SHEET    1   F 2 CYS B  16  ARG B  18  0                                        
SHEET    2   F 2 PHE B  43  ALA B  45 -1  O  PHE B  43   N  ARG B  18           
SHEET    1   G 2 TYR B  21  ASP B  23  0                                        
SHEET    2   G 2 GLY B  38  ASN B  40 -1  O  TYR B  39   N  ILE B  22           
SHEET    1   H 3 ILE B  33  GLU B  35  0                                        
SHEET    2   H 3 LEU B  83  ILE B  92 -1  O  LEU B  89   N  GLU B  35           
SHEET    3   H 3 THR B  95  VAL B 106 -1  O  GLU B  99   N  ILE B  88           
SHEET    1   I 2 CYS D  16  ARG D  18  0                                        
SHEET    2   I 2 PHE D  43  ALA D  45 -1  O  PHE D  43   N  ARG D  18           
SHEET    1   J 2 TYR D  21  ASP D  23  0                                        
SHEET    2   J 2 GLY D  38  ASN D  40 -1  O  TYR D  39   N  ILE D  22           
SHEET    1   K 3 ILE D  33  GLU D  35  0                                        
SHEET    2   K 3 LEU D  83  ILE D  92 -1  O  LEU D  89   N  GLU D  35           
SHEET    3   K 3 THR D  95  VAL D 106 -1  O  GLU D  99   N  ILE D  88           
SHEET    1   L 2 CYS D  77  SER D  80  0                                        
SHEET    2   L 2 CYS D 109  SER D 112 -1  O  SER D 112   N  CYS D  77           
SHEET    1   M 2 CYS E  16  ARG E  18  0                                        
SHEET    2   M 2 PHE E  43  ALA E  45 -1  O  PHE E  43   N  ARG E  18           
SHEET    1   N 2 TYR E  21  ASP E  23  0                                        
SHEET    2   N 2 GLY E  38  ASN E  40 -1  O  TYR E  39   N  ILE E  22           
SHEET    1   O 3 ILE E  33  GLU E  35  0                                        
SHEET    2   O 3 LEU E  83  ILE E  92 -1  O  LEU E  89   N  GLU E  35           
SHEET    3   O 3 THR E  95  VAL E 106 -1  O  GLU E  99   N  ILE E  88           
SHEET    1   P 2 CYS E  77  SER E  80  0                                        
SHEET    2   P 2 CYS E 109  SER E 112 -1  O  SER E 112   N  CYS E  77           
SHEET    1   Q 4 LEU H   4  GLN H   6  0                                        
SHEET    2   Q 4 VAL H  18  ALA H  24 -1  O  LYS H  23   N  VAL H   5           
SHEET    3   Q 4 THR H  78  LEU H  83 -1  O  MET H  81   N  VAL H  20           
SHEET    4   Q 4 VAL H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1   R 6 GLU H  10  LYS H  12  0                                        
SHEET    2   R 6 THR H 114  VAL H 118  1  O  THR H 117   N  LYS H  12           
SHEET    3   R 6 ALA H  92  THR H  99 -1  N  ALA H  92   O  VAL H 116           
SHEET    4   R 6 ILE H  34  ALA H  40 -1  N  VAL H  37   O  TYR H  95           
SHEET    5   R 6 GLY H  44  ILE H  52 -1  O  MET H  48   N  TRP H  36           
SHEET    6   R 6 ILE H  57  TYR H  60 -1  O  ILE H  57   N  ILE H  52           
SHEET    1   S 4 GLU H  10  LYS H  12  0                                        
SHEET    2   S 4 THR H 114  VAL H 118  1  O  THR H 117   N  LYS H  12           
SHEET    3   S 4 ALA H  92  THR H  99 -1  N  ALA H  92   O  VAL H 116           
SHEET    4   S 4 MET H 107  TRP H 110 -1  O  TYR H 109   N  SER H  98           
SHEET    1   T 4 SER H 127  LEU H 131  0                                        
SHEET    2   T 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3   T 4 TYR H 183  PRO H 192 -1  O  LEU H 185   N  VAL H 149           
SHEET    4   T 4 VAL H 170  THR H 172 -1  N  HIS H 171   O  VAL H 188           
SHEET    1   U 4 SER H 127  LEU H 131  0                                        
SHEET    2   U 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3   U 4 TYR H 183  PRO H 192 -1  O  LEU H 185   N  VAL H 149           
SHEET    4   U 4 VAL H 176  LEU H 177 -1  N  VAL H 176   O  SER H 184           
SHEET    1   V 3 THR H 158  TRP H 161  0                                        
SHEET    2   V 3 TYR H 201  HIS H 207 -1  O  ASN H 204   N  SER H 160           
SHEET    3   V 3 THR H 212  VAL H 218 -1  O  VAL H 214   N  VAL H 205           
SHEET    1   W 4 LEU J   4  GLN J   6  0                                        
SHEET    2   W 4 VAL J  18  ALA J  24 -1  O  LYS J  23   N  VAL J   5           
SHEET    3   W 4 THR J  78  LEU J  83 -1  O  MET J  81   N  VAL J  20           
SHEET    4   W 4 VAL J  68  ASP J  73 -1  N  ASP J  73   O  THR J  78           
SHEET    1   X 6 GLU J  10  LYS J  12  0                                        
SHEET    2   X 6 THR J 114  VAL J 118  1  O  THR J 117   N  GLU J  10           
SHEET    3   X 6 ALA J  92  THR J  99 -1  N  ALA J  92   O  VAL J 116           
SHEET    4   X 6 ILE J  34  GLN J  39 -1  N  VAL J  37   O  TYR J  95           
SHEET    5   X 6 LEU J  45  ILE J  52 -1  O  MET J  48   N  TRP J  36           
SHEET    6   X 6 ILE J  57  TYR J  60 -1  O  ASN J  59   N  GLY J  50           
SHEET    1   Y 4 GLU J  10  LYS J  12  0                                        
SHEET    2   Y 4 THR J 114  VAL J 118  1  O  THR J 117   N  GLU J  10           
SHEET    3   Y 4 ALA J  92  THR J  99 -1  N  ALA J  92   O  VAL J 116           
SHEET    4   Y 4 MET J 107  TRP J 110 -1  O  TYR J 109   N  SER J  98           
SHEET    1   Z 4 SER J 127  LEU J 131  0                                        
SHEET    2   Z 4 THR J 142  TYR J 152 -1  O  GLY J 146   N  LEU J 131           
SHEET    3   Z 4 TYR J 183  PRO J 192 -1  O  LEU J 185   N  VAL J 149           
SHEET    4   Z 4 VAL J 170  THR J 172 -1  N  HIS J 171   O  VAL J 188           
SHEET    1  AA 4 SER J 127  LEU J 131  0                                        
SHEET    2  AA 4 THR J 142  TYR J 152 -1  O  GLY J 146   N  LEU J 131           
SHEET    3  AA 4 TYR J 183  PRO J 192 -1  O  LEU J 185   N  VAL J 149           
SHEET    4  AA 4 VAL J 176  LEU J 177 -1  N  VAL J 176   O  SER J 184           
SHEET    1  AB 3 THR J 158  TRP J 161  0                                        
SHEET    2  AB 3 THR J 202  HIS J 207 -1  O  ASN J 204   N  SER J 160           
SHEET    3  AB 3 THR J 212  ARG J 217 -1  O  VAL J 214   N  VAL J 205           
SHEET    1  AC 4 LEU N   4  GLN N   6  0                                        
SHEET    2  AC 4 VAL N  18  ALA N  24 -1  O  LYS N  23   N  VAL N   5           
SHEET    3  AC 4 THR N  78  LEU N  83 -1  O  MET N  81   N  VAL N  20           
SHEET    4  AC 4 VAL N  68  ASP N  73 -1  N  ASP N  73   O  THR N  78           
SHEET    1  AD 6 GLU N  10  LYS N  12  0                                        
SHEET    2  AD 6 THR N 114  VAL N 118  1  O  THR N 117   N  LYS N  12           
SHEET    3  AD 6 ALA N  92  THR N  99 -1  N  ALA N  92   O  VAL N 116           
SHEET    4  AD 6 ILE N  34  GLN N  39 -1  N  SER N  35   O  ALA N  97           
SHEET    5  AD 6 LEU N  45  ILE N  52 -1  O  GLU N  46   N  ARG N  38           
SHEET    6  AD 6 ILE N  57  TYR N  60 -1  O  ASN N  59   N  GLY N  50           
SHEET    1  AE 4 GLU N  10  LYS N  12  0                                        
SHEET    2  AE 4 THR N 114  VAL N 118  1  O  THR N 117   N  LYS N  12           
SHEET    3  AE 4 ALA N  92  THR N  99 -1  N  ALA N  92   O  VAL N 116           
SHEET    4  AE 4 MET N 107  TRP N 110 -1  O  TYR N 109   N  SER N  98           
SHEET    1  AF 4 SER N 127  LEU N 131  0                                        
SHEET    2  AF 4 THR N 142  TYR N 152 -1  O  GLY N 146   N  LEU N 131           
SHEET    3  AF 4 TYR N 183  PRO N 192 -1  O  LEU N 185   N  VAL N 149           
SHEET    4  AF 4 VAL N 170  THR N 172 -1  N  HIS N 171   O  VAL N 188           
SHEET    1  AG 4 SER N 127  LEU N 131  0                                        
SHEET    2  AG 4 THR N 142  TYR N 152 -1  O  GLY N 146   N  LEU N 131           
SHEET    3  AG 4 TYR N 183  PRO N 192 -1  O  LEU N 185   N  VAL N 149           
SHEET    4  AG 4 VAL N 176  LEU N 177 -1  N  VAL N 176   O  SER N 184           
SHEET    1  AH 3 THR N 158  TRP N 161  0                                        
SHEET    2  AH 3 TYR N 201  HIS N 207 -1  O  ASN N 204   N  SER N 160           
SHEET    3  AH 3 THR N 212  VAL N 218 -1  O  VAL N 214   N  VAL N 205           
SHEET    1  AI 4 LEU Q   4  GLN Q   6  0                                        
SHEET    2  AI 4 VAL Q  18  ALA Q  24 -1  O  LYS Q  23   N  VAL Q   5           
SHEET    3  AI 4 THR Q  78  LEU Q  83 -1  O  MET Q  81   N  VAL Q  20           
SHEET    4  AI 4 VAL Q  68  ASP Q  73 -1  N  ASP Q  73   O  THR Q  78           
SHEET    1  AJ 6 GLU Q  10  LYS Q  12  0                                        
SHEET    2  AJ 6 THR Q 114  VAL Q 118  1  O  THR Q 117   N  LYS Q  12           
SHEET    3  AJ 6 ALA Q  92  THR Q  99 -1  N  ALA Q  92   O  VAL Q 116           
SHEET    4  AJ 6 ILE Q  34  GLN Q  39 -1  N  VAL Q  37   O  TYR Q  95           
SHEET    5  AJ 6 LEU Q  45  ILE Q  52 -1  O  MET Q  48   N  TRP Q  36           
SHEET    6  AJ 6 ILE Q  57  TYR Q  60 -1  O  ASN Q  59   N  GLY Q  50           
SHEET    1  AK 4 GLU Q  10  LYS Q  12  0                                        
SHEET    2  AK 4 THR Q 114  VAL Q 118  1  O  THR Q 117   N  LYS Q  12           
SHEET    3  AK 4 ALA Q  92  THR Q  99 -1  N  ALA Q  92   O  VAL Q 116           
SHEET    4  AK 4 MET Q 107  TRP Q 110 -1  O  TYR Q 109   N  SER Q  98           
SHEET    1  AL 4 SER Q 127  LEU Q 131  0                                        
SHEET    2  AL 4 THR Q 142  TYR Q 152 -1  O  LEU Q 148   N  PHE Q 129           
SHEET    3  AL 4 TYR Q 183  PRO Q 192 -1  O  LEU Q 185   N  VAL Q 149           
SHEET    4  AL 4 VAL Q 170  THR Q 172 -1  N  HIS Q 171   O  VAL Q 188           
SHEET    1  AM 4 SER Q 127  LEU Q 131  0                                        
SHEET    2  AM 4 THR Q 142  TYR Q 152 -1  O  LEU Q 148   N  PHE Q 129           
SHEET    3  AM 4 TYR Q 183  PRO Q 192 -1  O  LEU Q 185   N  VAL Q 149           
SHEET    4  AM 4 VAL Q 176  LEU Q 177 -1  N  VAL Q 176   O  SER Q 184           
SHEET    1  AN 3 THR Q 158  TRP Q 161  0                                        
SHEET    2  AN 3 THR Q 202  HIS Q 207 -1  O  ASN Q 204   N  SER Q 160           
SHEET    3  AN 3 THR Q 212  ARG Q 217 -1  O  VAL Q 214   N  VAL Q 205           
SHEET    1  AO 4 LEU I   4  SER I   7  0                                        
SHEET    2  AO 4 ALA I  19  ALA I  25 -1  O  ARG I  24   N  THR I   5           
SHEET    3  AO 4 ASP I  71  ILE I  76 -1  O  ILE I  76   N  ALA I  19           
SHEET    4  AO 4 PHE I  63  SER I  68 -1  N  SER I  64   O  THR I  75           
SHEET    1  AP 6 THR I  10  LEU I  13  0                                        
SHEET    2  AP 6 THR I 103  ILE I 107  1  O  ARG I 104   N  LEU I  11           
SHEET    3  AP 6 VAL I  86  GLN I  91 -1  N  TYR I  87   O  THR I 103           
SHEET    4  AP 6 LEU I  34  GLN I  39 -1  N  GLN I  39   O  VAL I  86           
SHEET    5  AP 6 ARG I  46  TYR I  50 -1  O  LEU I  48   N  TRP I  36           
SHEET    6  AP 6 SER I  54  ARG I  55 -1  O  SER I  54   N  TYR I  50           
SHEET    1  AQ 4 THR I  10  LEU I  13  0                                        
SHEET    2  AQ 4 THR I 103  ILE I 107  1  O  ARG I 104   N  LEU I  11           
SHEET    3  AQ 4 VAL I  86  GLN I  91 -1  N  TYR I  87   O  THR I 103           
SHEET    4  AQ 4 THR I  98  PHE I  99 -1  O  THR I  98   N  GLN I  91           
SHEET    1  AR 4 SER I 115  PHE I 119  0                                        
SHEET    2  AR 4 THR I 130  PHE I 140 -1  O  LEU I 136   N  PHE I 117           
SHEET    3  AR 4 TYR I 174  SER I 183 -1  O  LEU I 176   N  LEU I 137           
SHEET    4  AR 4 SER I 160  VAL I 164 -1  N  SER I 163   O  SER I 177           
SHEET    1  AS 4 ALA I 154  GLN I 156  0                                        
SHEET    2  AS 4 LYS I 146  VAL I 151 -1  N  TRP I 149   O  GLN I 156           
SHEET    3  AS 4 VAL I 192  THR I 198 -1  O  GLU I 196   N  GLN I 148           
SHEET    4  AS 4 VAL I 206  ASN I 211 -1  O  VAL I 206   N  VAL I 197           
SHEET    1  AT 4 LEU L   4  SER L   7  0                                        
SHEET    2  AT 4 ALA L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3  AT 4 ASP L  71  ILE L  76 -1  O  LEU L  74   N  LEU L  21           
SHEET    4  AT 4 PHE L  63  SER L  68 -1  N  SER L  64   O  THR L  75           
SHEET    1  AU 6 THR L  10  LEU L  13  0                                        
SHEET    2  AU 6 THR L 103  ILE L 107  1  O  GLU L 106   N  LEU L  11           
SHEET    3  AU 6 ALA L  85  GLN L  91 -1  N  ALA L  85   O  LEU L 105           
SHEET    4  AU 6 LEU L  34  GLN L  39 -1  N  GLN L  39   O  VAL L  86           
SHEET    5  AU 6 ARG L  46  TYR L  50 -1  O  LEU L  48   N  TRP L  36           
SHEET    6  AU 6 SER L  54  ARG L  55 -1  O  SER L  54   N  TYR L  50           
SHEET    1  AV 4 THR L  10  LEU L  13  0                                        
SHEET    2  AV 4 THR L 103  ILE L 107  1  O  GLU L 106   N  LEU L  11           
SHEET    3  AV 4 ALA L  85  GLN L  91 -1  N  ALA L  85   O  LEU L 105           
SHEET    4  AV 4 THR L  98  PHE L  99 -1  O  THR L  98   N  GLN L  91           
SHEET    1  AW 4 SER L 115  PHE L 119  0                                        
SHEET    2  AW 4 THR L 130  PHE L 140 -1  O  LEU L 136   N  PHE L 117           
SHEET    3  AW 4 TYR L 174  SER L 183 -1  O  LEU L 176   N  LEU L 137           
SHEET    4  AW 4 SER L 160  VAL L 164 -1  N  SER L 163   O  SER L 177           
SHEET    1  AX 4 ALA L 154  GLN L 156  0                                        
SHEET    2  AX 4 LYS L 146  VAL L 151 -1  N  TRP L 149   O  GLN L 156           
SHEET    3  AX 4 VAL L 192  THR L 198 -1  O  GLU L 196   N  GLN L 148           
SHEET    4  AX 4 VAL L 206  ASN L 211 -1  O  VAL L 206   N  VAL L 197           
SHEET    1  AY 4 LEU M   4  SER M   7  0                                        
SHEET    2  AY 4 ALA M  19  ALA M  25 -1  O  ARG M  24   N  THR M   5           
SHEET    3  AY 4 ASP M  71  ILE M  76 -1  O  PHE M  72   N  CYS M  23           
SHEET    4  AY 4 PHE M  63  SER M  68 -1  N  SER M  64   O  THR M  75           
SHEET    1  AZ 6 THR M  10  LEU M  13  0                                        
SHEET    2  AZ 6 THR M 103  ILE M 107  1  O  ARG M 104   N  LEU M  11           
SHEET    3  AZ 6 ALA M  85  GLN M  91 -1  N  ALA M  85   O  LEU M 105           
SHEET    4  AZ 6 LEU M  34  GLN M  39 -1  N  GLN M  39   O  VAL M  86           
SHEET    5  AZ 6 ARG M  46  TYR M  50 -1  O  LEU M  48   N  TRP M  36           
SHEET    6  AZ 6 SER M  54  ARG M  55 -1  O  SER M  54   N  TYR M  50           
SHEET    1  BA 4 THR M  10  LEU M  13  0                                        
SHEET    2  BA 4 THR M 103  ILE M 107  1  O  ARG M 104   N  LEU M  11           
SHEET    3  BA 4 ALA M  85  GLN M  91 -1  N  ALA M  85   O  LEU M 105           
SHEET    4  BA 4 THR M  98  PHE M  99 -1  O  THR M  98   N  GLN M  91           
SHEET    1  BB 4 SER M 115  PHE M 119  0                                        
SHEET    2  BB 4 THR M 130  PHE M 140 -1  O  LEU M 136   N  PHE M 117           
SHEET    3  BB 4 TYR M 174  SER M 183 -1  O  LEU M 176   N  LEU M 137           
SHEET    4  BB 4 SER M 160  VAL M 164 -1  N  SER M 163   O  SER M 177           
SHEET    1  BC 4 ALA M 154  GLN M 156  0                                        
SHEET    2  BC 4 LYS M 146  VAL M 151 -1  N  TRP M 149   O  GLN M 156           
SHEET    3  BC 4 VAL M 192  THR M 198 -1  O  GLU M 196   N  GLN M 148           
SHEET    4  BC 4 VAL M 206  ASN M 211 -1  O  VAL M 206   N  VAL M 197           
SHEET    1  BD 4 LEU P   4  SER P   7  0                                        
SHEET    2  BD 4 ALA P  19  ALA P  25 -1  O  ARG P  24   N  THR P   5           
SHEET    3  BD 4 ASP P  71  ILE P  76 -1  O  LEU P  74   N  LEU P  21           
SHEET    4  BD 4 PHE P  63  SER P  68 -1  N  SER P  64   O  THR P  75           
SHEET    1  BE 6 THR P  10  LEU P  13  0                                        
SHEET    2  BE 6 THR P 103  ILE P 107  1  O  ARG P 104   N  LEU P  11           
SHEET    3  BE 6 VAL P  86  GLN P  91 -1  N  TYR P  87   O  THR P 103           
SHEET    4  BE 6 LEU P  34  GLN P  39 -1  N  GLN P  39   O  VAL P  86           
SHEET    5  BE 6 ARG P  46  TYR P  50 -1  O  LEU P  48   N  TRP P  36           
SHEET    6  BE 6 SER P  54  ARG P  55 -1  O  SER P  54   N  TYR P  50           
SHEET    1  BF 4 THR P  10  LEU P  13  0                                        
SHEET    2  BF 4 THR P 103  ILE P 107  1  O  ARG P 104   N  LEU P  11           
SHEET    3  BF 4 VAL P  86  GLN P  91 -1  N  TYR P  87   O  THR P 103           
SHEET    4  BF 4 THR P  98  PHE P  99 -1  O  THR P  98   N  GLN P  91           
SHEET    1  BG 4 SER P 115  PHE P 119  0                                        
SHEET    2  BG 4 THR P 130  PHE P 140 -1  O  LEU P 136   N  PHE P 117           
SHEET    3  BG 4 TYR P 174  SER P 183 -1  O  LEU P 176   N  LEU P 137           
SHEET    4  BG 4 SER P 160  VAL P 164 -1  N  SER P 163   O  SER P 177           
SHEET    1  BH 4 ALA P 154  GLN P 156  0                                        
SHEET    2  BH 4 LYS P 146  VAL P 151 -1  N  TRP P 149   O  GLN P 156           
SHEET    3  BH 4 VAL P 192  THR P 198 -1  O  GLU P 196   N  GLN P 148           
SHEET    4  BH 4 VAL P 206  ASN P 211 -1  O  VAL P 206   N  VAL P 197           
SSBOND   1 CYS A    7    CYS A   16                          1555   1555  2.08  
SSBOND   2 CYS A   15    CYS A   78                          1555   1555  2.06  
SSBOND   3 CYS A   44    CYS A  109                          1555   1555  2.07  
SSBOND   4 CYS A   48    CYS A  111                          1555   1555  2.08  
SSBOND   5 CYS B    7    CYS B   16                          1555   1555  2.08  
SSBOND   6 CYS B   15    CYS B   78                          1555   1555  2.03  
SSBOND   7 CYS B   44    CYS B  109                          1555   1555  2.05  
SSBOND   8 CYS B   48    CYS B  111                          1555   1555  2.07  
SSBOND   9 CYS D    7    CYS D   16                          1555   1555  2.07  
SSBOND  10 CYS D   15    CYS D   78                          1555   1555  2.04  
SSBOND  11 CYS D   44    CYS D  109                          1555   1555  2.06  
SSBOND  12 CYS D   48    CYS D  111                          1555   1555  2.07  
SSBOND  13 CYS D   77    CYS E   77                          1555   1555  2.07  
SSBOND  14 CYS E    7    CYS E   16                          1555   1555  2.08  
SSBOND  15 CYS E   15    CYS E   78                          1555   1555  2.05  
SSBOND  16 CYS E   44    CYS E  109                          1555   1555  2.07  
SSBOND  17 CYS E   48    CYS E  111                          1555   1555  2.08  
SSBOND  18 CYS H   22    CYS H   96                          1555   1555  2.05  
SSBOND  19 CYS H  147    CYS H  203                          1555   1555  2.05  
SSBOND  20 CYS J   22    CYS J   96                          1555   1555  2.05  
SSBOND  21 CYS J  147    CYS J  203                          1555   1555  2.04  
SSBOND  22 CYS N   22    CYS N   96                          1555   1555  2.05  
SSBOND  23 CYS N  147    CYS N  203                          1555   1555  2.05  
SSBOND  24 CYS Q   22    CYS Q   96                          1555   1555  2.06  
SSBOND  25 CYS Q  147    CYS Q  203                          1555   1555  2.05  
SSBOND  26 CYS I   23    CYS I   89                          1555   1555  2.11  
SSBOND  27 CYS I  135    CYS I  195                          1555   1555  2.05  
SSBOND  28 CYS L   23    CYS L   89                          1555   1555  2.13  
SSBOND  29 CYS L  135    CYS L  195                          1555   1555  2.06  
SSBOND  30 CYS M   23    CYS M   89                          1555   1555  2.11  
SSBOND  31 CYS M  135    CYS M  195                          1555   1555  2.06  
SSBOND  32 CYS P   23    CYS P   89                          1555   1555  2.11  
SSBOND  33 CYS P  135    CYS P  195                          1555   1555  2.06  
CISPEP   1 GLU A   35    PRO A   36          0         1.09                     
CISPEP   2 GLU B   35    PRO B   36          0        -5.60                     
CISPEP   3 GLU D   35    PRO D   36          0        -3.25                     
CISPEP   4 GLU E   35    PRO E   36          0        -0.43                     
CISPEP   5 PHE H  153    PRO H  154          0        -3.62                     
CISPEP   6 GLU H  155    PRO H  156          0         6.91                     
CISPEP   7 PHE J  153    PRO J  154          0        -5.14                     
CISPEP   8 GLU J  155    PRO J  156          0         4.25                     
CISPEP   9 PHE N  153    PRO N  154          0        -0.25                     
CISPEP  10 GLU N  155    PRO N  156          0         6.57                     
CISPEP  11 PHE Q  153    PRO Q  154          0        -3.57                     
CISPEP  12 GLU Q  155    PRO Q  156          0         4.67                     
CISPEP  13 SER I    7    PRO I    8          0        -3.68                     
CISPEP  14 SER I   95    PRO I   96          0         2.24                     
CISPEP  15 TYR I  141    PRO I  142          0        -0.78                     
CISPEP  16 SER L    7    PRO L    8          0        -2.91                     
CISPEP  17 SER L   95    PRO L   96          0         0.31                     
CISPEP  18 TYR L  141    PRO L  142          0         0.09                     
CISPEP  19 SER M    7    PRO M    8          0        -3.30                     
CISPEP  20 SER M   95    PRO M   96          0         0.36                     
CISPEP  21 TYR M  141    PRO M  142          0         1.09                     
CISPEP  22 SER P    7    PRO P    8          0        -3.69                     
CISPEP  23 SER P   95    PRO P   96          0         0.88                     
CISPEP  24 TYR P  141    PRO P  142          0         1.53                     
SITE     1 AC1  6 ILE A  98  GLU A  99  GLN A 100  LYS N  13                    
SITE     2 AC1  6 PRO N  14  GLY N  15                                          
SITE     1 AC2  6 GLU E  99  GLN E 100  LYS H  13  PRO H  14                    
SITE     2 AC2  6 GLY H  15  SER H 120                                          
SITE     1 AC3  9 ASN J 162  SER J 163  THR J 202  ASN J 204                    
SITE     2 AC3  9 VAL P 151  GLN P 156  LEU P 182  ASP P 186                    
SITE     3 AC3  9 HIS P 190                                                     
SITE     1 AC4 10 VAL I 151  GLN I 156  LEU I 182  ASP I 186                    
SITE     2 AC4 10 HIS I 190  ASN Q 162  SER Q 163  THR Q 202                    
SITE     3 AC4 10 ASN Q 204  ASP Q 215                                          
SITE     1 AC5  8 GLY M   9  VAL M  86  GLY M 102  ARG M 104                    
SITE     2 AC5  8 THR M 198  HIS M 199  GLN M 200  HOH M 431                    
SITE     1 AC6  7 TYR D  91  GLY D  93  LYS D  94  SER P  28                    
SITE     2 AC6  7 LEU P  29  TYR P  33  ALA P  93                               
CRYST1  131.200  359.680   64.630  90.00  90.00  90.00 P 21 21 2    16          
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      0.007622  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002780  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015473        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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