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Database: PDB
Entry: 4LCW
LinkDB: 4LCW
Original site: 4LCW 
HEADER    MEMBRANE PROTEIN/IMMUNE SYSTEM          24-JUN-13   4LCW              
TITLE     THE STRUCTURE OF HUMAN MAIT TCR IN COMPLEX WITH MR1-K43A-RL-6-ME-7OH  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX CLASS I-RELATED GENE      
COMPND   3 PROTEIN;                                                             
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 23-292;                     
COMPND   6 SYNONYM: MHC CLASS I-RELATED GENE PROTEIN, CLASS I HISTOCOMPATIBILITY
COMPND   7 ANTIGEN-LIKE PROTEIN;                                                
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND  12 CHAIN: B, F;                                                         
COMPND  13 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;                           
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: MAIT T CELL RECEPTOR ALPHA CHAIN;                          
COMPND  17 CHAIN: D, G;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: MAIT T CELL RECEPTOR BETA CHAIN;                           
COMPND  21 CHAIN: E, H;                                                         
COMPND  22 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: MR1;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: B2M;                                                           
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: TCR ALPHA;                                                     
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PET30;                                    
SOURCE  28 MOL_ID: 4;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  30 ORGANISM_COMMON: HUMAN;                                              
SOURCE  31 ORGANISM_TAXID: 9606;                                                
SOURCE  32 GENE: TCR BETA;                                                      
SOURCE  33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  34 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  35 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    MHC CLASS I-RELATED PROTEIN, MAIT T CELL RECEPTOR, VITAMIN B2         
KEYWDS   2 METABOLITES, MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.PATEL,J.ROSSJOHN                                                    
REVDAT   3   20-SEP-23 4LCW    1       REMARK SEQADV                            
REVDAT   2   20-NOV-13 4LCW    1       JRNL                                     
REVDAT   1   02-OCT-13 4LCW    0                                                
JRNL        AUTH   R.REANTRAGOON,A.J.CORBETT,I.G.SAKALA,N.A.GHERARDIN,          
JRNL        AUTH 2 J.B.FURNESS,Z.CHEN,S.B.ECKLE,A.P.ULDRICH,R.W.BIRKINSHAW,     
JRNL        AUTH 3 O.PATEL,L.KOSTENKO,B.MEEHAN,K.KEDZIERSKA,L.LIU,D.P.FAIRLIE,  
JRNL        AUTH 4 T.H.HANSEN,D.I.GODFREY,J.ROSSJOHN,J.MCCLUSKEY,L.KJER-NIELSEN 
JRNL        TITL   ANTIGEN-LOADED MR1 TETRAMERS DEFINE T CELL RECEPTOR          
JRNL        TITL 2 HETEROGENEITY IN MUCOSAL-ASSOCIATED INVARIANT T CELLS.       
JRNL        REF    J.EXP.MED.                    V. 210  2305 2013              
JRNL        REFN                   ISSN 0022-1007                               
JRNL        PMID   24101382                                                     
JRNL        DOI    10.1084/JEM.20130958                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 80339                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : COPIED FROM 4L4T               
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.181                          
REMARK   3   R VALUE            (WORKING SET)  : 0.179                          
REMARK   3   FREE R VALUE                      : 0.227                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 4021                           
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) : 2.40                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.46                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.81                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 5912                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2142                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 5613                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2121                   
REMARK   3   BIN FREE R VALUE                        : 0.2510                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.06                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 299                      
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            : 12397                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 334                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.82590                                              
REMARK   3    B22 (A**2) : -9.25240                                             
REMARK   3    B33 (A**2) : 1.42650                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.48900                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.271               
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) : 0.284               
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      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 12824  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 17487  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5659   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 295    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1880   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 12824  ; 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   : 1654   ; 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   : 13953  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.11                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.50                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.94                     
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 4LCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080471.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95453                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80366                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4L4V                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M BIS-TRIS       
REMARK 280  -PROPANE PH 6.5 AND 20% PEG 3350, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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      107.95750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.68050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      107.95750            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.68050            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H                            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F                            
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     ASP A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     GLN A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     SER A   251                                                      
REMARK 465     ASN A   252                                                      
REMARK 465     PRO A   270                                                      
REMARK 465     ARG B    97                                                      
REMARK 465     ASP B    98                                                      
REMARK 465     MET B    99                                                      
REMARK 465     GLU C   190                                                      
REMARK 465     THR C   191                                                      
REMARK 465     PHE C   192                                                      
REMARK 465     PRO C   193                                                      
REMARK 465     GLY C   194                                                      
REMARK 465     VAL C   195                                                      
REMARK 465     GLU C   220                                                      
REMARK 465     ILE C   221                                                      
REMARK 465     VAL C   222                                                      
REMARK 465     GLN C   223                                                      
REMARK 465     ASP C   247                                                      
REMARK 465     PRO C   248                                                      
REMARK 465     GLN C   249                                                      
REMARK 465     SER C   250                                                      
REMARK 465     PRO C   270                                                      
REMARK 465     GLU D   201                                                      
REMARK 465     SER D   202                                                      
REMARK 465     SER D   203                                                      
REMARK 465     ASN E     1                                                      
REMARK 465     ASP E   245                                                      
REMARK 465     ARG F    97                                                      
REMARK 465     ASP F    98                                                      
REMARK 465     MET F    99                                                      
REMARK 465     ASP G   123                                                      
REMARK 465     SER G   124                                                      
REMARK 465     LYS G   125                                                      
REMARK 465     SER G   126                                                      
REMARK 465     SER G   127                                                      
REMARK 465     ASP G   128                                                      
REMARK 465     LYS G   129                                                      
REMARK 465     LYS G   177                                                      
REMARK 465     SER G   178                                                      
REMARK 465     ASP G   179                                                      
REMARK 465     SER G   199                                                      
REMARK 465     PRO G   200                                                      
REMARK 465     GLU G   201                                                      
REMARK 465     SER G   202                                                      
REMARK 465     SER G   203                                                      
REMARK 465     ASN H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     ARG H   243                                                      
REMARK 465     ALA H   244                                                      
REMARK 465     ASP H   245                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  17    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 190    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 216    CG   CD   CE   NZ                                   
REMARK 470     GLU A 219    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 220    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 223    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 224    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 253    CG   CD1  CD2                                       
REMARK 470     GLU B  16    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  36    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  44    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  48    CG   CD   CE   NZ                                   
REMARK 470     LYS B  58    CG   CD   CE   NZ                                   
REMARK 470     GLU B  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  75    CG   CD   CE   NZ                                   
REMARK 470     HIS C  17    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU C  52    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 102    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 147    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 189    CG   CD   CE   NZ                                   
REMARK 470     TYR C 211    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 216    CG   CD   CE   NZ                                   
REMARK 470     GLU C 219    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 224    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 245    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 252    CG   OD1  ND2                                       
REMARK 470     LEU C 253    CG   CD1  CD2                                       
REMARK 470     GLN C 268    CG   CD   OE1  NE2                                  
REMARK 470     GLN D   2    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  55    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  56    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  57    CG   CD   CE   NZ                                   
REMARK 470     LYS D  76    CG   CD   CE   NZ                                   
REMARK 470     LYS D 125    CG   CD   CE   NZ                                   
REMARK 470     LYS D 147    CG   CD   CE   NZ                                   
REMARK 470     ASP D 148    CG   OD1  OD2                                       
REMARK 470     ASN D 184    CG   OD1  ND2                                       
REMARK 470     ASP D 194    CG   OD1  OD2                                       
REMARK 470     LYS E   9    CG   CD   CE   NZ                                   
REMARK 470     LYS E  57    CG   CD   CE   NZ                                   
REMARK 470     GLU E 116    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 133    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 165    CG   CD   CE   NZ                                   
REMARK 470     ASN E 185    CG   OD1  ND2                                       
REMARK 470     GLU E 220    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 223    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 243    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  16    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  19    CG   CD   CE   NZ                                   
REMARK 470     GLU F  44    CG   CD   OE1  OE2                                  
REMARK 470     ARG F  45    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  48    CG   CD   CE   NZ                                   
REMARK 470     GLU F  74    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  75    CG   CD   CE   NZ                                   
REMARK 470     GLU F  77    CG   CD   OE1  OE2                                  
REMARK 470     GLN F  89    CG   CD   OE1  NE2                                  
REMARK 470     LYS F  94    CG   CD   CE   NZ                                   
REMARK 470     ASP G 110    CG   OD1  OD2                                       
REMARK 470     GLN G 112    CG   CD   OE1  NE2                                  
REMARK 470     ARG G 122    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP G 138    CG   OD1  OD2                                       
REMARK 470     GLN G 140    CG   CD   OE1  NE2                                  
REMARK 470     GLN G 145    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 147    CG   CD   CE   NZ                                   
REMARK 470     ASP G 148    CG   OD1  OD2                                       
REMARK 470     ASP G 150    CG   OD1  OD2                                       
REMARK 470     ARG G 162    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP G 165    CG   OD1  OD2                                       
REMARK 470     ASN G 176    CG   OD1  ND2                                       
REMARK 470     ASN G 184    CG   OD1  ND2                                       
REMARK 470     ASN G 187    CG   OD1  ND2                                       
REMARK 470     ASN G 188    CG   OD1  ND2                                       
REMARK 470     GLU G 193    CG   CD   OE1  OE2                                  
REMARK 470     ASP G 194    CG   OD1  OD2                                       
REMARK 470     LYS H   9    CG   CD   CE   NZ                                   
REMARK 470     LYS H  14    CG   CD   CE   NZ                                   
REMARK 470     LYS H  57    CG   CD   CE   NZ                                   
REMARK 470     ARG H  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H  79    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 116    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 119    CG   CD   CE   NZ                                   
REMARK 470     GLU H 125    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 133    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 140    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 165    CG   CD   CE   NZ                                   
REMARK 470     GLN H 176    CG   CD   OE1  NE2                                  
REMARK 470     ARG H 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 220    CG   CD   OE1  OE2                                  
REMARK 470     ASN H 221    CG   OD1  ND2                                       
REMARK 470     GLU H 223    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 226    CG   CD   OE1  NE2                                  
REMARK 470     ASP H 227    CG   OD1  OD2                                       
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  29     -125.75     62.58                                   
REMARK 500    PHE A 119      -58.43   -123.47                                   
REMARK 500    THR A 191     -117.15    -89.76                                   
REMARK 500    PRO A 193      120.75    -29.99                                   
REMARK 500    ASP C  29     -123.11     56.24                                   
REMARK 500    PHE C 119      -56.78   -127.60                                   
REMARK 500    ASN C 217       48.65     39.87                                   
REMARK 500    VAL D  50      -31.41   -133.13                                   
REMARK 500    LYS D  57       82.87   -160.90                                   
REMARK 500    ASN E  70     -169.36   -165.01                                   
REMARK 500    TRP F  60       -2.70     75.84                                   
REMARK 500    VAL G  50      -32.83   -131.89                                   
REMARK 500    LYS G  57       66.18   -117.07                                   
REMARK 500    ASP G 150       32.52    -95.88                                   
REMARK 500    ASP H  26       51.11   -115.44                                   
REMARK 500    ASN H  28       35.53     71.62                                   
REMARK 500    ASN H  70     -168.72   -164.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VY A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1VY C 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L4V   RELATED DB: PDB                                   
DBREF  4LCW A    1   270  UNP    Q95460   HMR1_HUMAN      23    292             
DBREF  4LCW B    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  4LCW C    1   270  UNP    Q95460   HMR1_HUMAN      23    292             
DBREF  4LCW F    1    99  UNP    P61769   B2MG_HUMAN      21    119             
DBREF  4LCW D    1   203  PDB    4LCW     4LCW             1    203             
DBREF  4LCW G    1   203  PDB    4LCW     4LCW             1    203             
DBREF  4LCW E    1   245  PDB    4LCW     4LCW             1    245             
DBREF  4LCW H    1   245  PDB    4LCW     4LCW             1    245             
SEQADV 4LCW MET A    0  UNP  Q95460              EXPRESSION TAG                 
SEQADV 4LCW ALA A   43  UNP  Q95460    LYS    65 ENGINEERED MUTATION            
SEQADV 4LCW SER A  261  UNP  Q95460    CYS   283 ENGINEERED MUTATION            
SEQADV 4LCW MET C    0  UNP  Q95460              EXPRESSION TAG                 
SEQADV 4LCW ALA C   43  UNP  Q95460    LYS    65 ENGINEERED MUTATION            
SEQADV 4LCW SER C  261  UNP  Q95460    CYS   283 ENGINEERED MUTATION            
SEQRES   1 A  271  MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL          
SEQRES   2 A  271  SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL          
SEQRES   3 A  271  GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER          
SEQRES   4 A  271  VAL THR ARG GLN ALA GLU PRO ARG ALA PRO TRP MET ALA          
SEQRES   5 A  271  GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN          
SEQRES   6 A  271  LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU          
SEQRES   7 A  271  LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS          
SEQRES   8 A  271  THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP          
SEQRES   9 A  271  GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY          
SEQRES  10 A  271  GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP          
SEQRES  11 A  271  LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA          
SEQRES  12 A  271  TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN          
SEQRES  13 A  271  TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE          
SEQRES  14 A  271  LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO          
SEQRES  15 A  271  PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY          
SEQRES  16 A  271  VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO          
SEQRES  17 A  271  PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU          
SEQRES  18 A  271  ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER          
SEQRES  19 A  271  GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU          
SEQRES  20 A  271  ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU          
SEQRES  21 A  271  HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO                  
SEQRES   1 B   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 B   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 B   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 B   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 B   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 C  271  MET ARG THR HIS SER LEU ARG TYR PHE ARG LEU GLY VAL          
SEQRES   2 C  271  SER ASP PRO ILE HIS GLY VAL PRO GLU PHE ILE SER VAL          
SEQRES   3 C  271  GLY TYR VAL ASP SER HIS PRO ILE THR THR TYR ASP SER          
SEQRES   4 C  271  VAL THR ARG GLN ALA GLU PRO ARG ALA PRO TRP MET ALA          
SEQRES   5 C  271  GLU ASN LEU ALA PRO ASP HIS TRP GLU ARG TYR THR GLN          
SEQRES   6 C  271  LEU LEU ARG GLY TRP GLN GLN MET PHE LYS VAL GLU LEU          
SEQRES   7 C  271  LYS ARG LEU GLN ARG HIS TYR ASN HIS SER GLY SER HIS          
SEQRES   8 C  271  THR TYR GLN ARG MET ILE GLY CYS GLU LEU LEU GLU ASP          
SEQRES   9 C  271  GLY SER THR THR GLY PHE LEU GLN TYR ALA TYR ASP GLY          
SEQRES  10 C  271  GLN ASP PHE LEU ILE PHE ASN LYS ASP THR LEU SER TRP          
SEQRES  11 C  271  LEU ALA VAL ASP ASN VAL ALA HIS THR ILE LYS GLN ALA          
SEQRES  12 C  271  TRP GLU ALA ASN GLN HIS GLU LEU LEU TYR GLN LYS ASN          
SEQRES  13 C  271  TRP LEU GLU GLU GLU CYS ILE ALA TRP LEU LYS ARG PHE          
SEQRES  14 C  271  LEU GLU TYR GLY LYS ASP THR LEU GLN ARG THR GLU PRO          
SEQRES  15 C  271  PRO LEU VAL ARG VAL ASN ARG LYS GLU THR PHE PRO GLY          
SEQRES  16 C  271  VAL THR ALA LEU PHE CYS LYS ALA HIS GLY PHE TYR PRO          
SEQRES  17 C  271  PRO GLU ILE TYR MET THR TRP MET LYS ASN GLY GLU GLU          
SEQRES  18 C  271  ILE VAL GLN GLU ILE ASP TYR GLY ASP ILE LEU PRO SER          
SEQRES  19 C  271  GLY ASP GLY THR TYR GLN ALA TRP ALA SER ILE GLU LEU          
SEQRES  20 C  271  ASP PRO GLN SER SER ASN LEU TYR SER CYS HIS VAL GLU          
SEQRES  21 C  271  HIS SER GLY VAL HIS MET VAL LEU GLN VAL PRO                  
SEQRES   1 D  203  GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR          
SEQRES   2 D  203  GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR          
SEQRES   3 D  203  SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA          
SEQRES   4 D  203  GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP          
SEQRES   5 D  203  GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER          
SEQRES   6 D  203  ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU          
SEQRES   7 D  203  GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS          
SEQRES   8 D  203  ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS          
SEQRES   9 D  203  LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA          
SEQRES  10 D  203  VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER          
SEQRES  11 D  203  VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL          
SEQRES  12 D  203  SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS          
SEQRES  13 D  203  CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN          
SEQRES  14 D  203  SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS          
SEQRES  15 D  203  ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR          
SEQRES  16 D  203  PHE PHE PRO SER PRO GLU SER SER                              
SEQRES   1 E  245  ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU          
SEQRES   2 E  245  LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP          
SEQRES   3 E  245  MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO          
SEQRES   4 E  245  GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU          
SEQRES   5 E  245  GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN          
SEQRES   6 E  245  VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU          
SEQRES   7 E  245  GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS          
SEQRES   8 E  245  ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU          
SEQRES   9 E  245  PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP          
SEQRES  10 E  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU          
SEQRES  11 E  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR          
SEQRES  12 E  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL          
SEQRES  13 E  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER          
SEQRES  14 E  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO          
SEQRES  15 E  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU          
SEQRES  16 E  245  ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS          
SEQRES  17 E  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN          
SEQRES  18 E  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN          
SEQRES  19 E  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP                  
SEQRES   1 F   99  ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 F   99  PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS TYR          
SEQRES   3 F   99  VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP LEU          
SEQRES   4 F   99  LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS SER          
SEQRES   5 F   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU LEU          
SEQRES   6 F   99  TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU TYR          
SEQRES   7 F   99  ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO LYS          
SEQRES   8 F   99  ILE VAL LYS TRP ASP ARG ASP MET                              
SEQRES   1 G  203  GLY GLN ASN ILE ASP GLN PRO THR GLU MET THR ALA THR          
SEQRES   2 G  203  GLU GLY ALA ILE VAL GLN ILE ASN CYS THR TYR GLN THR          
SEQRES   3 G  203  SER GLY PHE ASN GLY LEU PHE TRP TYR GLN GLN HIS ALA          
SEQRES   4 G  203  GLY GLU ALA PRO THR PHE LEU SER TYR ASN VAL LEU ASP          
SEQRES   5 G  203  GLY LEU GLU GLU LYS GLY ARG PHE SER SER PHE LEU SER          
SEQRES   6 G  203  ARG SER LYS GLY TYR SER TYR LEU LEU LEU LYS GLU LEU          
SEQRES   7 G  203  GLN MET LYS ASP SER ALA SER TYR LEU CYS ALA VAL LYS          
SEQRES   8 G  203  ASP SER ASN TYR GLN LEU ILE TRP GLY ALA GLY THR LYS          
SEQRES   9 G  203  LEU ILE ILE LYS PRO ASP ILE GLN ASN PRO ASP PRO ALA          
SEQRES  10 G  203  VAL TYR GLN LEU ARG ASP SER LYS SER SER ASP LYS SER          
SEQRES  11 G  203  VAL CYS LEU PHE THR ASP PHE ASP SER GLN THR ASN VAL          
SEQRES  12 G  203  SER GLN SER LYS ASP SER ASP VAL TYR ILE THR ASP LYS          
SEQRES  13 G  203  CYS VAL LEU ASP MET ARG SER MET ASP PHE LYS SER ASN          
SEQRES  14 G  203  SER ALA VAL ALA TRP SER ASN LYS SER ASP PHE ALA CYS          
SEQRES  15 G  203  ALA ASN ALA PHE ASN ASN SER ILE ILE PRO GLU ASP THR          
SEQRES  16 G  203  PHE PHE PRO SER PRO GLU SER SER                              
SEQRES   1 H  245  ASN ALA GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU          
SEQRES   2 H  245  LYS THR GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP          
SEQRES   3 H  245  MET ASN HIS ASN SER MET TYR TRP TYR ARG GLN ASP PRO          
SEQRES   4 H  245  GLY MET GLY LEU ARG LEU ILE TYR TYR SER ALA SER GLU          
SEQRES   5 H  245  GLY THR THR ASP LYS GLY GLU VAL PRO ASN GLY TYR ASN          
SEQRES   6 H  245  VAL SER ARG LEU ASN LYS ARG GLU PHE SER LEU ARG LEU          
SEQRES   7 H  245  GLU SER ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS          
SEQRES   8 H  245  ALA SER SER VAL TRP THR GLY GLU GLY SER GLY GLU LEU          
SEQRES   9 H  245  PHE PHE GLY GLU GLY SER ARG LEU THR VAL LEU GLU ASP          
SEQRES  10 H  245  LEU LYS ASN VAL PHE PRO PRO GLU VAL ALA VAL PHE GLU          
SEQRES  11 H  245  PRO SER GLU ALA GLU ILE SER HIS THR GLN LYS ALA THR          
SEQRES  12 H  245  LEU VAL CYS LEU ALA THR GLY PHE TYR PRO ASP HIS VAL          
SEQRES  13 H  245  GLU LEU SER TRP TRP VAL ASN GLY LYS GLU VAL HIS SER          
SEQRES  14 H  245  GLY VAL CYS THR ASP PRO GLN PRO LEU LYS GLU GLN PRO          
SEQRES  15 H  245  ALA LEU ASN ASP SER ARG TYR ALA LEU SER SER ARG LEU          
SEQRES  16 H  245  ARG VAL SER ALA THR PHE TRP GLN ASN PRO ARG ASN HIS          
SEQRES  17 H  245  PHE ARG CYS GLN VAL GLN PHE TYR GLY LEU SER GLU ASN          
SEQRES  18 H  245  ASP GLU TRP THR GLN ASP ARG ALA LYS PRO VAL THR GLN          
SEQRES  19 H  245  ILE VAL SER ALA GLU ALA TRP GLY ARG ALA ASP                  
HET    GOL  A 301       6                                                       
HET    1VY  A 302      23                                                       
HET    1VY  C 301      23                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     1VY 1-DEOXY-1-(7-HYDROXY-6-METHYL-2,4-DIOXO-3,4-                     
HETNAM   2 1VY  DIHYDROPTERIDIN-8(2H)-YL)-D-RIBITOL                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  GOL    C3 H8 O3                                                     
FORMUL  10  1VY    2(C12 H16 N4 O7)                                             
FORMUL  12  HOH   *334(H2 O)                                                    
HELIX    1   1 ALA A   47  LEU A   54  1                                   8    
HELIX    2   2 ALA A   55  ASN A   85  1                                  31    
HELIX    3   3 ASP A  133  GLU A  144  1                                  12    
HELIX    4   4 ASN A  146  GLU A  159  1                                  14    
HELIX    5   5 GLU A  159  GLY A  172  1                                  14    
HELIX    6   6 GLY A  172  GLN A  177  1                                   6    
HELIX    7   7 ALA C   47  LEU C   54  1                                   8    
HELIX    8   8 ALA C   55  ASN C   85  1                                  31    
HELIX    9   9 ASP C  133  ALA C  145  1                                  13    
HELIX   10  10 ASN C  146  GLU C  159  1                                  14    
HELIX   11  11 GLU C  159  GLY C  172  1                                  14    
HELIX   12  12 GLY C  172  GLN C  177  1                                   6    
HELIX   13  13 GLN D   79  SER D   83  5                                   5    
HELIX   14  14 ALA D  181  PHE D  186  1                                   6    
HELIX   15  15 ALA E   82  THR E   86  5                                   5    
HELIX   16  16 ASP E  117  VAL E  121  5                                   5    
HELIX   17  17 SER E  132  GLN E  140  1                                   9    
HELIX   18  18 ALA E  199  GLN E  203  1                                   5    
HELIX   19  19 GLN G   79  SER G   83  5                                   5    
HELIX   20  20 ARG G  162  ASP G  165  5                                   4    
HELIX   21  21 ALA H   82  THR H   86  5                                   5    
HELIX   22  22 SER H  132  GLN H  140  1                                   9    
HELIX   23  23 ALA H  199  ASN H  204  1                                   6    
SHEET    1   A 8 GLU A  44  PRO A  45  0                                        
SHEET    2   A 8 HIS A  31  ASP A  37 -1  N  THR A  35   O  GLU A  44           
SHEET    3   A 8 PHE A  22  VAL A  28 -1  N  GLY A  26   O  ILE A  33           
SHEET    4   A 8 HIS A   3  VAL A  12 -1  N  LEU A  10   O  ILE A  23           
SHEET    5   A 8 THR A  91  LEU A 100 -1  O  ILE A  96   N  TYR A   7           
SHEET    6   A 8 THR A 106  TYR A 114 -1  O  ALA A 113   N  GLN A  93           
SHEET    7   A 8 GLN A 117  ASN A 123 -1  O  LEU A 120   N  TYR A 112           
SHEET    8   A 8 SER A 128  ALA A 131 -1  O  SER A 128   N  ASN A 123           
SHEET    1   B 4 LEU A 183  GLU A 190  0                                        
SHEET    2   B 4 THR A 196  PHE A 205 -1  O  ALA A 197   N  LYS A 189           
SHEET    3   B 4 TYR A 238  GLU A 245 -1  O  ALA A 240   N  ALA A 202           
SHEET    4   B 4 ASP A 226  TYR A 227 -1  N  ASP A 226   O  SER A 243           
SHEET    1   C 4 LEU A 183  GLU A 190  0                                        
SHEET    2   C 4 THR A 196  PHE A 205 -1  O  ALA A 197   N  LYS A 189           
SHEET    3   C 4 TYR A 238  GLU A 245 -1  O  ALA A 240   N  ALA A 202           
SHEET    4   C 4 LEU A 231  PRO A 232 -1  N  LEU A 231   O  GLN A 239           
SHEET    1   D 4 GLU A 219  GLU A 220  0                                        
SHEET    2   D 4 ILE A 210  LYS A 216 -1  N  LYS A 216   O  GLU A 219           
SHEET    3   D 4 TYR A 254  HIS A 260 -1  O  HIS A 257   N  THR A 213           
SHEET    4   D 4 VAL A 263  GLN A 268 -1  O  MET A 265   N  VAL A 258           
SHEET    1   E 4 LYS B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4   E 4 GLU B  50  HIS B  51 -1  N  GLU B  50   O  TYR B  67           
SHEET    1   F 4 LYS B   6  SER B  11  0                                        
SHEET    2   F 4 ASN B  21  PHE B  30 -1  O  SER B  28   N  LYS B   6           
SHEET    3   F 4 PHE B  62  PHE B  70 -1  O  PHE B  70   N  ASN B  21           
SHEET    4   F 4 SER B  55  PHE B  56 -1  N  SER B  55   O  TYR B  63           
SHEET    1   G 4 GLU B  44  ARG B  45  0                                        
SHEET    2   G 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  GLU B  44           
SHEET    3   G 4 TYR B  78  HIS B  84 -1  O  ARG B  81   N  ASP B  38           
SHEET    4   G 4 LYS B  91  LYS B  94 -1  O  VAL B  93   N  CYS B  80           
SHEET    1   H 8 GLU C  44  PRO C  45  0                                        
SHEET    2   H 8 HIS C  31  ASP C  37 -1  N  THR C  35   O  GLU C  44           
SHEET    3   H 8 PHE C  22  VAL C  28 -1  N  SER C  24   O  TYR C  36           
SHEET    4   H 8 HIS C   3  VAL C  12 -1  N  LEU C  10   O  ILE C  23           
SHEET    5   H 8 THR C  91  LEU C 100 -1  O  TYR C  92   N  GLY C  11           
SHEET    6   H 8 THR C 106  TYR C 114 -1  O  GLN C 111   N  MET C  95           
SHEET    7   H 8 GLN C 117  ASN C 123 -1  O  LEU C 120   N  TYR C 112           
SHEET    8   H 8 SER C 128  ALA C 131 -1  O  LEU C 130   N  ILE C 121           
SHEET    1   I 4 LEU C 183  ARG C 188  0                                        
SHEET    2   I 4 ALA C 197  PHE C 205 -1  O  HIS C 203   N  LEU C 183           
SHEET    3   I 4 TYR C 238  GLU C 245 -1  O  ALA C 242   N  CYS C 200           
SHEET    4   I 4 ASP C 226  TYR C 227 -1  N  ASP C 226   O  SER C 243           
SHEET    1   J 4 LEU C 183  ARG C 188  0                                        
SHEET    2   J 4 ALA C 197  PHE C 205 -1  O  HIS C 203   N  LEU C 183           
SHEET    3   J 4 TYR C 238  GLU C 245 -1  O  ALA C 242   N  CYS C 200           
SHEET    4   J 4 LEU C 231  PRO C 232 -1  N  LEU C 231   O  GLN C 239           
SHEET    1   K 3 TYR C 211  LYS C 216  0                                        
SHEET    2   K 3 TYR C 254  HIS C 260 -1  O  HIS C 257   N  THR C 213           
SHEET    3   K 3 VAL C 263  GLN C 268 -1  O  MET C 265   N  VAL C 258           
SHEET    1   L 5 ASN D   3  ASP D   5  0                                        
SHEET    2   L 5 VAL D  18  GLN D  25 -1  O  GLN D  25   N  ASN D   3           
SHEET    3   L 5 TYR D  70  LEU D  75 -1  O  LEU D  73   N  ILE D  20           
SHEET    4   L 5 PHE D  60  SER D  65 -1  N  SER D  65   O  TYR D  70           
SHEET    5   L 5 GLY D  53  LYS D  57 -1  N  GLU D  55   O  SER D  62           
SHEET    1   M 5 GLU D   9  THR D  13  0                                        
SHEET    2   M 5 THR D 103  LYS D 108  1  O  LYS D 108   N  ALA D  12           
SHEET    3   M 5 ALA D  84  LYS D  91 -1  N  ALA D  84   O  LEU D 105           
SHEET    4   M 5 LEU D  32  GLN D  37 -1  N  PHE D  33   O  ALA D  89           
SHEET    5   M 5 THR D  44  ASN D  49 -1  O  LEU D  46   N  TRP D  34           
SHEET    1   N 4 GLU D   9  THR D  13  0                                        
SHEET    2   N 4 THR D 103  LYS D 108  1  O  LYS D 108   N  ALA D  12           
SHEET    3   N 4 ALA D  84  LYS D  91 -1  N  ALA D  84   O  LEU D 105           
SHEET    4   N 4 LEU D  97  TRP D  99 -1  O  ILE D  98   N  VAL D  90           
SHEET    1   O 4 ALA D 117  GLN D 120  0                                        
SHEET    2   O 4 SER D 130  THR D 135 -1  O  LEU D 133   N  TYR D 119           
SHEET    3   O 4 PHE D 166  SER D 175 -1  O  ALA D 173   N  CYS D 132           
SHEET    4   O 4 TYR D 152  ILE D 153 -1  N  TYR D 152   O  TRP D 174           
SHEET    1   P 4 ALA D 117  GLN D 120  0                                        
SHEET    2   P 4 SER D 130  THR D 135 -1  O  LEU D 133   N  TYR D 119           
SHEET    3   P 4 PHE D 166  SER D 175 -1  O  ALA D 173   N  CYS D 132           
SHEET    4   P 4 CYS D 157  MET D 161 -1  N  MET D 161   O  PHE D 166           
SHEET    1   Q 4 VAL E   4  THR E   7  0                                        
SHEET    2   Q 4 MET E  19  GLN E  25 -1  O  ALA E  24   N  THR E   5           
SHEET    3   Q 4 SER E  75  LEU E  78 -1  O  LEU E  76   N  LEU E  21           
SHEET    4   Q 4 TYR E  64  SER E  67 -1  N  ASN E  65   O  ARG E  77           
SHEET    1   R 6 PHE E  10  LYS E  14  0                                        
SHEET    2   R 6 SER E 110  LEU E 115  1  O  LEU E 115   N  LEU E  13           
SHEET    3   R 6 SER E  87  SER E  94 -1  N  SER E  87   O  LEU E 112           
SHEET    4   R 6 SER E  31  GLN E  37 -1  N  TYR E  35   O  PHE E  90           
SHEET    5   R 6 ARG E  44  SER E  49 -1  O  ILE E  46   N  TRP E  34           
SHEET    6   R 6 ASP E  56  LYS E  57 -1  O  ASP E  56   N  TYR E  48           
SHEET    1   S 4 PHE E  10  LYS E  14  0                                        
SHEET    2   S 4 SER E 110  LEU E 115  1  O  LEU E 115   N  LEU E  13           
SHEET    3   S 4 SER E  87  SER E  94 -1  N  SER E  87   O  LEU E 112           
SHEET    4   S 4 PHE E 105  PHE E 106 -1  O  PHE E 105   N  SER E  93           
SHEET    1   T 4 GLU E 125  PHE E 129  0                                        
SHEET    2   T 4 LYS E 141  PHE E 151 -1  O  THR E 149   N  GLU E 125           
SHEET    3   T 4 TYR E 189  SER E 198 -1  O  TYR E 189   N  PHE E 151           
SHEET    4   T 4 VAL E 171  THR E 173 -1  N  CYS E 172   O  ARG E 194           
SHEET    1   U 4 GLU E 125  PHE E 129  0                                        
SHEET    2   U 4 LYS E 141  PHE E 151 -1  O  THR E 149   N  GLU E 125           
SHEET    3   U 4 TYR E 189  SER E 198 -1  O  TYR E 189   N  PHE E 151           
SHEET    4   U 4 LEU E 178  LYS E 179 -1  N  LEU E 178   O  ALA E 190           
SHEET    1   V 4 LYS E 165  VAL E 167  0                                        
SHEET    2   V 4 VAL E 156  VAL E 162 -1  N  VAL E 162   O  LYS E 165           
SHEET    3   V 4 HIS E 208  PHE E 215 -1  O  GLN E 214   N  GLU E 157           
SHEET    4   V 4 GLN E 234  TRP E 241 -1  O  ALA E 240   N  PHE E 209           
SHEET    1   W 4 LYS F   6  SER F  11  0                                        
SHEET    2   W 4 ASN F  21  PHE F  30 -1  O  ASN F  24   N  TYR F  10           
SHEET    3   W 4 PHE F  62  PHE F  70 -1  O  TYR F  66   N  CYS F  25           
SHEET    4   W 4 GLU F  50  HIS F  51 -1  N  GLU F  50   O  TYR F  67           
SHEET    1   X 4 LYS F   6  SER F  11  0                                        
SHEET    2   X 4 ASN F  21  PHE F  30 -1  O  ASN F  24   N  TYR F  10           
SHEET    3   X 4 PHE F  62  PHE F  70 -1  O  TYR F  66   N  CYS F  25           
SHEET    4   X 4 SER F  55  PHE F  56 -1  N  SER F  55   O  TYR F  63           
SHEET    1   Y 4 GLU F  44  ARG F  45  0                                        
SHEET    2   Y 4 GLU F  36  LYS F  41 -1  N  LYS F  41   O  GLU F  44           
SHEET    3   Y 4 TYR F  78  ASN F  83 -1  O  ALA F  79   N  LEU F  40           
SHEET    4   Y 4 LYS F  91  LYS F  94 -1  O  LYS F  91   N  VAL F  82           
SHEET    1   Z 5 ASN G   3  ASP G   5  0                                        
SHEET    2   Z 5 VAL G  18  GLN G  25 -1  O  GLN G  25   N  ASN G   3           
SHEET    3   Z 5 TYR G  70  LEU G  75 -1  O  LEU G  73   N  ILE G  20           
SHEET    4   Z 5 PHE G  60  SER G  65 -1  N  SER G  61   O  LEU G  74           
SHEET    5   Z 5 GLY G  53  LYS G  57 -1  N  GLU G  55   O  SER G  62           
SHEET    1  AA 5 GLU G   9  THR G  13  0                                        
SHEET    2  AA 5 THR G 103  LYS G 108  1  O  ILE G 106   N  MET G  10           
SHEET    3  AA 5 ALA G  84  LYS G  91 -1  N  ALA G  84   O  LEU G 105           
SHEET    4  AA 5 LEU G  32  GLN G  37 -1  N  PHE G  33   O  ALA G  89           
SHEET    5  AA 5 THR G  44  ASN G  49 -1  O  ASN G  49   N  LEU G  32           
SHEET    1  AB 4 GLU G   9  THR G  13  0                                        
SHEET    2  AB 4 THR G 103  LYS G 108  1  O  ILE G 106   N  MET G  10           
SHEET    3  AB 4 ALA G  84  LYS G  91 -1  N  ALA G  84   O  LEU G 105           
SHEET    4  AB 4 LEU G  97  TRP G  99 -1  O  ILE G  98   N  VAL G  90           
SHEET    1  AC 4 ALA G 117  LEU G 121  0                                        
SHEET    2  AC 4 VAL G 131  THR G 135 -1  O  LEU G 133   N  TYR G 119           
SHEET    3  AC 4 PHE G 166  SER G 175 -1  O  ALA G 171   N  PHE G 134           
SHEET    4  AC 4 VAL G 151  ILE G 153 -1  N  TYR G 152   O  TRP G 174           
SHEET    1  AD 4 ALA G 117  LEU G 121  0                                        
SHEET    2  AD 4 VAL G 131  THR G 135 -1  O  LEU G 133   N  TYR G 119           
SHEET    3  AD 4 PHE G 166  SER G 175 -1  O  ALA G 171   N  PHE G 134           
SHEET    4  AD 4 CYS G 157  MET G 161 -1  N  MET G 161   O  PHE G 166           
SHEET    1  AE 4 VAL H   4  THR H   7  0                                        
SHEET    2  AE 4 MET H  19  GLN H  25 -1  O  ALA H  24   N  THR H   5           
SHEET    3  AE 4 PHE H  74  LEU H  78 -1  O  LEU H  76   N  LEU H  21           
SHEET    4  AE 4 TYR H  64  ARG H  68 -1  N  ASN H  65   O  ARG H  77           
SHEET    1  AF 6 PHE H  10  LYS H  14  0                                        
SHEET    2  AF 6 SER H 110  LEU H 115  1  O  THR H 113   N  LEU H  13           
SHEET    3  AF 6 SER H  87  SER H  94 -1  N  SER H  87   O  LEU H 112           
SHEET    4  AF 6 SER H  31  GLN H  37 -1  N  TYR H  35   O  PHE H  90           
SHEET    5  AF 6 ARG H  44  SER H  49 -1  O  SER H  49   N  MET H  32           
SHEET    6  AF 6 ASP H  56  LYS H  57 -1  O  ASP H  56   N  TYR H  48           
SHEET    1  AG 4 PHE H  10  LYS H  14  0                                        
SHEET    2  AG 4 SER H 110  LEU H 115  1  O  THR H 113   N  LEU H  13           
SHEET    3  AG 4 SER H  87  SER H  94 -1  N  SER H  87   O  LEU H 112           
SHEET    4  AG 4 PHE H 105  PHE H 106 -1  O  PHE H 105   N  SER H  93           
SHEET    1  AH 4 GLU H 125  PHE H 129  0                                        
SHEET    2  AH 4 LYS H 141  PHE H 151 -1  O  LEU H 147   N  ALA H 127           
SHEET    3  AH 4 TYR H 189  SER H 198 -1  O  LEU H 191   N  ALA H 148           
SHEET    4  AH 4 VAL H 171  THR H 173 -1  N  CYS H 172   O  ARG H 194           
SHEET    1  AI 4 GLU H 125  PHE H 129  0                                        
SHEET    2  AI 4 LYS H 141  PHE H 151 -1  O  LEU H 147   N  ALA H 127           
SHEET    3  AI 4 TYR H 189  SER H 198 -1  O  LEU H 191   N  ALA H 148           
SHEET    4  AI 4 LEU H 178  LYS H 179 -1  N  LEU H 178   O  ALA H 190           
SHEET    1  AJ 4 LYS H 165  VAL H 167  0                                        
SHEET    2  AJ 4 VAL H 156  VAL H 162 -1  N  VAL H 162   O  LYS H 165           
SHEET    3  AJ 4 HIS H 208  PHE H 215 -1  O  GLN H 212   N  SER H 159           
SHEET    4  AJ 4 GLN H 234  TRP H 241 -1  O  ALA H 238   N  CYS H 211           
SSBOND   1 CYS A   98    CYS A  161                          1555   1555  2.06  
SSBOND   2 CYS A  200    CYS A  256                          1555   1555  2.04  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.03  
SSBOND   4 CYS C   98    CYS C  161                          1555   1555  2.07  
SSBOND   5 CYS C  200    CYS C  256                          1555   1555  2.02  
SSBOND   6 CYS D   22    CYS D   88                          1555   1555  2.04  
SSBOND   7 CYS D  132    CYS D  182                          1555   1555  2.05  
SSBOND   8 CYS D  157    CYS E  172                          1555   1555  2.06  
SSBOND   9 CYS E   23    CYS E   91                          1555   1555  2.03  
SSBOND  10 CYS E  146    CYS E  211                          1555   1555  2.03  
SSBOND  11 CYS F   25    CYS F   80                          1555   1555  2.04  
SSBOND  12 CYS G   22    CYS G   88                          1555   1555  2.03  
SSBOND  13 CYS G  132    CYS G  182                          1555   1555  2.06  
SSBOND  14 CYS G  157    CYS H  172                          1555   1555  2.05  
SSBOND  15 CYS H   23    CYS H   91                          1555   1555  2.04  
SSBOND  16 CYS H  146    CYS H  211                          1555   1555  2.03  
CISPEP   1 TYR A  206    PRO A  207          0         5.66                     
CISPEP   2 HIS B   31    PRO B   32          0         5.17                     
CISPEP   3 TYR C  206    PRO C  207          0         3.64                     
CISPEP   4 THR E    7    PRO E    8          0        -7.04                     
CISPEP   5 TYR E  152    PRO E  153          0        -1.76                     
CISPEP   6 HIS F   31    PRO F   32          0         4.68                     
CISPEP   7 THR H    7    PRO H    8          0        -3.58                     
CISPEP   8 TYR H  152    PRO H  153          0        -0.07                     
SITE     1 AC1  4 GLU A 180  PRO A 181  GLY A 204  GLN D  19                    
SITE     1 AC2 14 TYR A   7  ARG A   9  SER A  24  THR A  34                    
SITE     2 AC2 14 TYR A  62  TRP A  69  ARG A  94  ILE A  96                    
SITE     3 AC2 14 TYR A 152  TRP A 156  HOH A 402  HOH A 407                    
SITE     4 AC2 14 HOH A 408  TYR G  95                                          
SITE     1 AC3 16 TYR C   7  ARG C   9  SER C  24  TYR C  62                    
SITE     2 AC3 16 LEU C  66  TRP C  69  ARG C  94  ILE C  96                    
SITE     3 AC3 16 TYR C 152  GLN C 153  TRP C 156  HOH C 401                    
SITE     4 AC3 16 HOH C 407  HOH C 408  TYR D  95  HOH D 401                    
CRYST1  215.915   69.361  142.829  90.00 104.30  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004631  0.000000  0.001181        0.00000                         
SCALE2      0.000000  0.014417  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007225        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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