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Database: PDB
Entry: 4I18
LinkDB: 4I18
Original site: 4I18 
HEADER    CYTOKINE, SIGNALING PROTEIN             20-NOV-12   4I18              
TITLE     CRYSTAL STRUCTURE OF HUMAN PROLACTIN RECEPTOR COMPLEXED WITH FAB      
TITLE    2 FRAGMENT                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTIBODY LIGHT CHAIN;                                      
COMPND   3 CHAIN: L, B;                                                         
COMPND   4 FRAGMENT: FAB;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ANTIBODY HEAVY CHAIN;                                      
COMPND   8 CHAIN: H, A;                                                         
COMPND   9 FRAGMENT: FAB;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PROLACTIN RECEPTOR;                                        
COMPND  13 CHAIN: R, C;                                                         
COMPND  14 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 25-235);                
COMPND  15 SYNONYM: PRL-R;                                                      
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: 55244;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PHAGEMID;                             
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: 55244;                                     
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PHAGEMID;                             
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: PRLR;                                                          
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    IMMUNOGLOBULIN FOLD, PROLACTIN BINDING, RECEPTOR SIGNALING, CYTOKINE, 
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.M.DUGUID,S.MUKHERJEE,J.L.KOUADIO                                    
REVDAT   3   15-NOV-17 4I18    1       REMARK                                   
REVDAT   2   28-JAN-15 4I18    1       JRNL                                     
REVDAT   1   20-NOV-13 4I18    0                                                
JRNL        AUTH   S.S.RIZK,J.L.KOUADIO,A.SZYMBORSKA,E.M.DUGUID,S.MUKHERJEE,    
JRNL        AUTH 2 J.ZHENG,C.V.CLEVENGER,A.A.KOSSIAKOFF                         
JRNL        TITL   ENGINEERING SYNTHETIC ANTIBODY BINDERS FOR ALLOSTERIC        
JRNL        TITL 2 INHIBITION OF PROLACTIN RECEPTOR SIGNALING.                  
JRNL        REF    CELL COMMUN SIGNAL            V.  13     1 2015              
JRNL        REFN                                                                
JRNL        PMID   25589173                                                     
JRNL        DOI    10.1186/S12964-014-0080-8                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 46730                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2365                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3031                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 158                          
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9873                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.69000                                              
REMARK   3    B22 (A**2) : 1.69000                                              
REMARK   3    B33 (A**2) : -2.54000                                             
REMARK   3    B12 (A**2) : 0.85000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.912         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.384         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.262         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.491        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.881                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10191 ; 0.016 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13885 ; 2.138 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1259 ; 9.484 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   418 ;34.222 ;23.923       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1562 ;22.205 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;22.118 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1502 ; 0.134 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7764 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : L B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    L    (A):    750 ; 0.090 ; 0.500           
REMARK   3   TIGHT THERMAL      1    L (A**2):    804 ; 8.840 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    L (A**2):    750 ; 8.940 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : H A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    H    (A):    689 ; 0.130 ; 0.500           
REMARK   3   TIGHT THERMAL      2    H (A**2):    801 ; 6.070 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    H (A**2):    689 ; 6.590 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L   216                          
REMARK   3    ORIGIN FOR THE GROUP (A):-157.3303 -16.0977 -17.7393              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1602 T22:   0.0899                                     
REMARK   3      T33:   0.1801 T12:  -0.0342                                     
REMARK   3      T13:  -0.0851 T23:   0.0629                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1416 L22:   2.8450                                     
REMARK   3      L33:   0.7302 L12:  -0.0618                                     
REMARK   3      L13:  -0.1372 L23:  -0.2759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0739 S12:   0.0430 S13:   0.0603                       
REMARK   3      S21:  -0.0785 S22:   0.2289 S23:   0.3964                       
REMARK   3      S31:  -0.0275 S32:  -0.2175 S33:  -0.1550                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     4        H   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):-144.8502 -24.7234  -8.2044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1378 T22:   0.0403                                     
REMARK   3      T33:   0.1116 T12:  -0.0242                                     
REMARK   3      T13:   0.0065 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2340 L22:   1.5711                                     
REMARK   3      L33:   1.2706 L12:   0.2609                                     
REMARK   3      L13:   0.1128 L23:  -0.1097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0850 S12:   0.0127 S13:   0.0431                       
REMARK   3      S21:  -0.2314 S22:   0.1475 S23:   0.1699                       
REMARK   3      S31:  -0.0452 S32:  -0.1300 S33:  -0.0625                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   215                          
REMARK   3    ORIGIN FOR THE GROUP (A):-101.7038 -19.9678   6.7179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0859 T22:   0.2372                                     
REMARK   3      T33:   0.4226 T12:  -0.0875                                     
REMARK   3      T13:  -0.0985 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2046 L22:   2.2002                                     
REMARK   3      L33:   2.5486 L12:  -0.0257                                     
REMARK   3      L13:   0.2116 L23:  -1.2434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1654 S12:  -0.0370 S13:   0.3790                       
REMARK   3      S21:   0.2429 S22:  -0.1530 S23:  -0.7311                       
REMARK   3      S31:  -0.3744 S32:   0.7111 S33:   0.3184                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   228                          
REMARK   3    ORIGIN FOR THE GROUP (A):-117.6431 -27.6810   1.1387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1491 T22:   0.0611                                     
REMARK   3      T33:   0.0713 T12:   0.0019                                     
REMARK   3      T13:   0.0553 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5371 L22:   0.9683                                     
REMARK   3      L33:   1.0856 L12:  -0.0087                                     
REMARK   3      L13:   0.1674 L23:  -0.6685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0590 S12:   0.1144 S13:   0.0624                       
REMARK   3      S21:   0.0289 S22:  -0.0174 S23:  -0.1012                       
REMARK   3      S31:   0.0531 S32:   0.1774 S33:   0.0764                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R     3        R   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):-115.7048 -59.8864  23.5513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2878 T22:   0.0887                                     
REMARK   3      T33:   0.1164 T12:   0.1367                                     
REMARK   3      T13:  -0.0075 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1676 L22:   1.1604                                     
REMARK   3      L33:   6.6959 L12:  -0.3751                                     
REMARK   3      L13:  -2.4678 L23:   0.6288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0341 S12:  -0.0514 S13:  -0.0590                       
REMARK   3      S21:  -0.0393 S22:  -0.1073 S23:  -0.1616                       
REMARK   3      S31:   0.4737 S32:   0.3427 S33:   0.0731                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   201                          
REMARK   3    ORIGIN FOR THE GROUP (A):-157.0219 -60.1505 -17.1508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2851 T22:   0.1235                                     
REMARK   3      T33:   0.1437 T12:  -0.1370                                     
REMARK   3      T13:  -0.0241 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8439 L22:   1.4690                                     
REMARK   3      L33:   5.5143 L12:   0.8674                                     
REMARK   3      L13:  -1.1158 L23:   0.3908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1673 S12:   0.1286 S13:  -0.1406                       
REMARK   3      S21:   0.0616 S22:   0.2257 S23:  -0.1069                       
REMARK   3      S31:   0.4605 S32:   0.0632 S33:  -0.0584                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT, ANISOU RECORDS REMOVED BY AUTHOR REQUEST                 
REMARK   4                                                                      
REMARK   4 4I18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000076176.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1271                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47509                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.238                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 250.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.20700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2R8S AND 3D48                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 160 MM CALCIUM ACETATE, 80 MM SODIUM     
REMARK 280  CACODYLATE, PH 6.2, 11% PEG8000, 20% GLYCEROL, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       20.74933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       41.49867            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.12400            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       51.87333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       10.37467            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, C                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, R                               
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     CYS L   217                                                      
REMARK 465     GLU H     1                                                      
REMARK 465     ILE H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     CYS H   231                                                      
REMARK 465     ASP H   232                                                      
REMARK 465     LYS H   233                                                      
REMARK 465     THR H   234                                                      
REMARK 465     HIS H   235                                                      
REMARK 465     THR H   236                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     CYS B   217                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LYS A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     THR A   146                                                      
REMARK 465     SER A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     LYS A   229                                                      
REMARK 465     SER A   230                                                      
REMARK 465     CYS A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     LYS A   233                                                      
REMARK 465     THR A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     THR A   236                                                      
REMARK 465     GLN R     1                                                      
REMARK 465     LEU R     2                                                      
REMARK 465     LEU R    32                                                      
REMARK 465     PRO R    33                                                      
REMARK 465     ASP R   134                                                      
REMARK 465     LEU R   135                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     GLN C   115                                                      
REMARK 465     PRO C   116                                                      
REMARK 465     GLU C   117                                                      
REMARK 465     ASP C   118                                                      
REMARK 465     ARG C   119                                                      
REMARK 465     LYS C   120                                                      
REMARK 465     LEU C   172                                                      
REMARK 465     HIS C   173                                                      
REMARK 465     PRO C   174                                                      
REMARK 465     GLY C   175                                                      
REMARK 465     GLN C   176                                                      
REMARK 465     ILE C   202                                                      
REMARK 465     PRO C   203                                                      
REMARK 465     SER C   204                                                      
REMARK 465     ASP C   205                                                      
REMARK 465     PHE C   206                                                      
REMARK 465     THR C   207                                                      
REMARK 465     MET C   208                                                      
REMARK 465     ASN C   209                                                      
REMARK 465     ASP C   210                                                      
REMARK 465     THR C   211                                                      
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     LYS H 144    CG   CD   CE   NZ                                   
REMARK 470     SER H 145    OG                                                  
REMARK 470     THR H 146    OG1  CG2                                            
REMARK 470     SER A 143    CA   C    O    CB   OG                              
REMARK 470     LYS R  11    NZ                                                  
REMARK 470     LYS R 136    CG   CD   CE   NZ                                   
REMARK 470     LYS C  11    NZ                                                  
REMARK 470     MET C  85    CG   SD   CE                                        
REMARK 470     LYS C 136    CG   CD   CE   NZ                                   
REMARK 470     LYS C 177    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP R 191   CE2   TRP R 191   CD2     0.072                       
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    LEU H 156   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES          
REMARK 500    VAL H 157   C   -  N   -  CA  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    LEU A  21   CB  -  CG  -  CD1 ANGL. DEV. = -12.3 DEGREES          
REMARK 500    VAL A 157   C   -  N   -  CA  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    PRO R   4   C   -  N   -  CD  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ASP R 104   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP R 104   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    LEU R 132   CA  -  CB  -  CG  ANGL. DEV. =  17.0 DEGREES          
REMARK 500    LEU R 143   CA  -  CB  -  CG  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    VAL R 182   CB  -  CA  -  C   ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ASP R 210   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    LEU C  38   CA  -  CB  -  CG  ANGL. DEV. =  15.6 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    VAL L  30       16.25   -148.52                                   
REMARK 500    SER L  31     -109.88     33.70                                   
REMARK 500    ALA L  52      -32.81     76.23                                   
REMARK 500    SER L  53        3.20   -157.93                                   
REMARK 500    ALA L  85     -173.58   -173.09                                   
REMARK 500    ASN L 155      -12.72     90.49                                   
REMARK 500    ASN L 161       14.12   -143.68                                   
REMARK 500    LYS L 193      -60.83    -98.95                                   
REMARK 500    SER H  66       -3.05    -55.77                                   
REMARK 500    VAL H 106      123.23    -39.13                                   
REMARK 500    TYR H 107        8.72     81.81                                   
REMARK 500    TRP H 108       58.19   -150.36                                   
REMARK 500    SER H 142     -154.77   -167.18                                   
REMARK 500    LYS H 144       71.27     55.83                                   
REMARK 500    SER H 145       74.57    -46.82                                   
REMARK 500    THR H 146      110.23    178.80                                   
REMARK 500    VAL H 157       66.69     77.47                                   
REMARK 500    ASP H 159       73.83     61.46                                   
REMARK 500    ASN H 170       74.18     36.71                                   
REMARK 500    SER H 171       39.22     32.96                                   
REMARK 500    THR H 175      -32.40   -139.00                                   
REMARK 500    PRO B   9      173.66    -55.00                                   
REMARK 500    VAL B  30       23.64   -143.43                                   
REMARK 500    SER B  31     -112.24     23.89                                   
REMARK 500    ALA B  52      -35.92     81.57                                   
REMARK 500    SER B  53        5.06   -154.87                                   
REMARK 500    ALA B  85     -179.98   -177.48                                   
REMARK 500    ASN B 155      -12.42     87.28                                   
REMARK 500    ASN B 161       13.19   -149.31                                   
REMARK 500    LYS B 193      -60.86    -97.50                                   
REMARK 500    ARG B 214      173.82    -41.93                                   
REMARK 500    SER A  66        5.48    -62.41                                   
REMARK 500    VAL A  67      -17.48   -143.21                                   
REMARK 500    TYR A 107        9.01     83.79                                   
REMARK 500    TRP A 108       56.89   -141.98                                   
REMARK 500    SER A 113       65.32   -100.15                                   
REMARK 500    SER A 142     -160.09   -170.35                                   
REMARK 500    VAL A 157       63.58     76.94                                   
REMARK 500    ASP A 159       78.17     62.60                                   
REMARK 500    ASN A 170       76.41     39.09                                   
REMARK 500    SER A 171       44.01     27.97                                   
REMARK 500    THR A 175      -30.57   -134.05                                   
REMARK 500    HIS A 215       77.23   -116.44                                   
REMARK 500    GLU R   8      120.98   -174.62                                   
REMARK 500    ASN R  16       25.33   -150.80                                   
REMARK 500    LYS R  17       -4.60     76.50                                   
REMARK 500    THR R  28      137.64     82.71                                   
REMARK 500    ASP R  29      -86.97   -179.29                                   
REMARK 500    GLU R  43       97.88    -28.24                                   
REMARK 500    GLU R  45      113.50    138.27                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      97 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY H  154     CYS H  155                  147.50                    
REMARK 500 GLY A  154     CYS A  155                   95.03                    
REMARK 500 CYS A  155     LEU A  156                  146.89                    
REMARK 500 PRO R  103     ASP R  104                  124.96                    
REMARK 500 ASN C   35     TYR C   36                   31.45                    
REMARK 500 PRO C  103     ASP C  104                  136.85                    
REMARK 500 LYS C  136     THR C  137                 -132.86                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA H 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER H  78   OG                                                     
REMARK 620 2 SER A  78   OG  133.8                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT R 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301                 
DBREF  4I18 R    1   211  UNP    P16471   PRLR_HUMAN      25    235             
DBREF  4I18 C    1   211  UNP    P16471   PRLR_HUMAN      25    235             
DBREF  4I18 L    1   217  PDB    4I18     4I18             1    217             
DBREF  4I18 B    1   217  PDB    4I18     4I18             1    217             
DBREF  4I18 H    1   236  PDB    4I18     4I18             1    236             
DBREF  4I18 A    1   236  PDB    4I18     4I18             1    236             
SEQRES   1 L  217  SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER          
SEQRES   2 L  217  ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA          
SEQRES   3 L  217  SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN          
SEQRES   4 L  217  LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA          
SEQRES   5 L  217  SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY          
SEQRES   6 L  217  SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER          
SEQRES   7 L  217  LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN          
SEQRES   8 L  217  TYR TYR SER TYR TYR TYR PRO PHE THR PHE GLY GLN GLY          
SEQRES   9 L  217  THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER          
SEQRES  10 L  217  VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER          
SEQRES  11 L  217  GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR          
SEQRES  12 L  217  PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA          
SEQRES  13 L  217  LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN          
SEQRES  14 L  217  ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU          
SEQRES  15 L  217  THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR          
SEQRES  16 L  217  ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL          
SEQRES  17 L  217  THR LYS SER PHE ASN ARG GLY GLU CYS                          
SEQRES   1 H  236  GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY          
SEQRES   2 H  236  LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA          
SEQRES   3 H  236  ALA SER GLY PHE ASN PHE SER SER SER SER MET HIS TRP          
SEQRES   4 H  236  VAL ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP VAL ALA          
SEQRES   5 H  236  TYR ILE SER PRO TYR TYR GLY SER THR SER TYR ALA ASP          
SEQRES   6 H  236  SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER          
SEQRES   7 H  236  LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA          
SEQRES   8 H  236  GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER TYR GLY          
SEQRES   9 H  236  TYR VAL TYR TRP ASN ALA TYR SER SER GLY MET ASP TYR          
SEQRES  10 H  236  TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER          
SEQRES  11 H  236  THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER          
SEQRES  12 H  236  LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU          
SEQRES  13 H  236  VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP          
SEQRES  14 H  236  ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO          
SEQRES  15 H  236  ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER          
SEQRES  16 H  236  VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR          
SEQRES  17 H  236  TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS          
SEQRES  18 H  236  VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR          
SEQRES  19 H  236  HIS THR                                                      
SEQRES   1 B  217  SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER          
SEQRES   2 B  217  ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA          
SEQRES   3 B  217  SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN          
SEQRES   4 B  217  LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA          
SEQRES   5 B  217  SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY          
SEQRES   6 B  217  SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER          
SEQRES   7 B  217  LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN          
SEQRES   8 B  217  TYR TYR SER TYR TYR TYR PRO PHE THR PHE GLY GLN GLY          
SEQRES   9 B  217  THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER          
SEQRES  10 B  217  VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER          
SEQRES  11 B  217  GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR          
SEQRES  12 B  217  PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA          
SEQRES  13 B  217  LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN          
SEQRES  14 B  217  ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU          
SEQRES  15 B  217  THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR          
SEQRES  16 B  217  ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL          
SEQRES  17 B  217  THR LYS SER PHE ASN ARG GLY GLU CYS                          
SEQRES   1 A  236  GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY          
SEQRES   2 A  236  LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA          
SEQRES   3 A  236  ALA SER GLY PHE ASN PHE SER SER SER SER MET HIS TRP          
SEQRES   4 A  236  VAL ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP VAL ALA          
SEQRES   5 A  236  TYR ILE SER PRO TYR TYR GLY SER THR SER TYR ALA ASP          
SEQRES   6 A  236  SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER          
SEQRES   7 A  236  LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA          
SEQRES   8 A  236  GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER TYR GLY          
SEQRES   9 A  236  TYR VAL TYR TRP ASN ALA TYR SER SER GLY MET ASP TYR          
SEQRES  10 A  236  TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER          
SEQRES  11 A  236  THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER          
SEQRES  12 A  236  LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU          
SEQRES  13 A  236  VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP          
SEQRES  14 A  236  ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO          
SEQRES  15 A  236  ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER          
SEQRES  16 A  236  VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR          
SEQRES  17 A  236  TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS          
SEQRES  18 A  236  VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR          
SEQRES  19 A  236  HIS THR                                                      
SEQRES   1 R  211  GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG          
SEQRES   2 R  211  SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO          
SEQRES   3 R  211  GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR          
SEQRES   4 R  211  TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO          
SEQRES   5 R  211  ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY          
SEQRES   6 R  211  LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET          
SEQRES   7 R  211  VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP          
SEQRES   8 R  211  GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP          
SEQRES   9 R  211  PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU          
SEQRES  10 R  211  ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO          
SEQRES  11 R  211  THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU          
SEQRES  12 R  211  TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP          
SEQRES  13 R  211  GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE          
SEQRES  14 R  211  LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL          
SEQRES  15 R  211  ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP SER          
SEQRES  16 R  211  PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET          
SEQRES  17 R  211  ASN ASP THR                                                  
SEQRES   1 C  211  GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG          
SEQRES   2 C  211  SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO          
SEQRES   3 C  211  GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR          
SEQRES   4 C  211  TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO          
SEQRES   5 C  211  ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY          
SEQRES   6 C  211  LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET          
SEQRES   7 C  211  VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP          
SEQRES   8 C  211  GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP          
SEQRES   9 C  211  PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU          
SEQRES  10 C  211  ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO          
SEQRES  11 C  211  THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU          
SEQRES  12 C  211  TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP          
SEQRES  13 C  211  GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE          
SEQRES  14 C  211  LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL          
SEQRES  15 C  211  ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP SER          
SEQRES  16 C  211  PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET          
SEQRES  17 C  211  ASN ASP THR                                                  
HET    GOL  L 301       6                                                       
HET     CA  H 301       1                                                       
HET    GOL  H 302       6                                                       
HET     CA  B 301       1                                                       
HET    GOL  A 301       6                                                       
HET    ACT  R 301       4                                                       
HET    GOL  C 301       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL  12  ACT    C2 H3 O2 1-                                                  
HELIX    1   6 GLN L   80  PHE L   84  5                                   5    
HELIX    2   7 SER L  124  GLY L  131  1                                   8    
HELIX    3   8 LYS L  186  LYS L  191  1                                   6    
HELIX    4  12 ASN H   31  SER H   33  5                                   3    
HELIX    5  13 ASP H   65  LYS H   68  5                                   4    
HELIX    6  14 SER H  202  LEU H  204  5                                   3    
HELIX    7  15 LYS H  216  ASN H  219  5                                   4    
HELIX    8   9 GLN B   80  PHE B   84  5                                   5    
HELIX    9  10 SER B  124  SER B  130  1                                   7    
HELIX   10  11 LYS B  186  LYS B  191  1                                   6    
HELIX   11  16 ASN A   31  SER A   33  5                                   3    
HELIX   12  17 ARG A   90  THR A   94  5                                   5    
HELIX   13  18 SER A  202  LEU A  204  5                                   3    
HELIX   14  19 LYS A  216  ASN A  219  5                                   4    
HELIX   15   1 GLY R   65  THR R   69  5                                   5    
HELIX   16   2 VAL R   97  VAL R  101  5                                   5    
HELIX   17   3 ASP R  205  ASN R  209  5                                   5    
HELIX   18   4 GLY C   65  SER C   70  1                                   6    
HELIX   19   5 THR C   98  VAL C  101  5                                   4    
SHEET    1   A 3 GLU R   8  ARG R  13  0                                        
SHEET    2   A 3 PHE R  20  ARG R  25 -1  O  THR R  21   N  ARG R  13           
SHEET    3   A 3 SER R  61  PHE R  64 -1  O  PHE R  64   N  PHE R  20           
SHEET    1   B 4 HIS R  49  GLU R  50  0                                        
SHEET    2   B 4 ASN R  35  ARG R  42 -1  N  TYR R  40   O  HIS R  49           
SHEET    3   B 4 TYR R  75  THR R  82 -1  O  ASN R  80   N  SER R  37           
SHEET    4   B 4 SER R  87  SER R  88 -1  O  SER R  88   N  ALA R  81           
SHEET    1   C 4 HIS R  49  GLU R  50  0                                        
SHEET    2   C 4 ASN R  35  ARG R  42 -1  N  TYR R  40   O  HIS R  49           
SHEET    3   C 4 TYR R  75  THR R  82 -1  O  ASN R  80   N  SER R  37           
SHEET    4   C 4 GLU R  92  VAL R  95 -1  O  VAL R  95   N  TYR R  75           
SHEET    1   D 3 LEU R 107  LYS R 114  0                                        
SHEET    2   D 3 TYR R 122  SER R 128 -1  O  TYR R 122   N  LYS R 114           
SHEET    3   D 3 GLU R 166  ILE R 169 -1  O  PHE R 167   N  ILE R 125           
SHEET    1   E 4 GLU R 157  PHE R 160  0                                        
SHEET    2   E 4 LEU R 142  PRO R 150 -1  N  ILE R 146   O  HIS R 159           
SHEET    3   E 4 LYS R 177  PRO R 186 -1  O  LYS R 185   N  LEU R 143           
SHEET    4   E 4 THR R 198  GLN R 201 -1  O  ILE R 200   N  TYR R 178           
SHEET    1   F 3 GLU C   8  ARG C  13  0                                        
SHEET    2   F 3 PHE C  20  ARG C  25 -1  O  TRP C  23   N  LYS C  11           
SHEET    3   F 3 SER C  61  PHE C  64 -1  O  PHE C  64   N  PHE C  20           
SHEET    1   G 4 HIS C  49  GLU C  50  0                                        
SHEET    2   G 4 LEU C  38  HIS C  41 -1  N  TYR C  40   O  HIS C  49           
SHEET    3   G 4 THR C  74  THR C  82 -1  O  ILE C  76   N  HIS C  41           
SHEET    4   G 4 SER C  87  PHE C  89 -1  O  SER C  88   N  ALA C  81           
SHEET    1   H 4 HIS C  49  GLU C  50  0                                        
SHEET    2   H 4 LEU C  38  HIS C  41 -1  N  TYR C  40   O  HIS C  49           
SHEET    3   H 4 THR C  74  THR C  82 -1  O  ILE C  76   N  HIS C  41           
SHEET    4   H 4 LEU C  93  ASP C  96 -1  O  VAL C  95   N  TYR C  75           
SHEET    1   I 3 LEU C 107  VAL C 113  0                                        
SHEET    2   I 3 LEU C 123  SER C 128 -1  O  TRP C 124   N  GLU C 112           
SHEET    3   I 3 GLU C 166  ILE C 169 -1  O  PHE C 167   N  ILE C 125           
SHEET    1   J 4 GLU C 157  PHE C 160  0                                        
SHEET    2   J 4 LEU C 143  LEU C 148 -1  N  LEU C 148   O  GLU C 157           
SHEET    3   J 4 TYR C 178  LYS C 185 -1  O  GLN C 181   N  ARG C 147           
SHEET    4   J 4 THR C 198  ILE C 200 -1  O  ILE C 200   N  TYR C 178           
SHEET    1   K 4 MET L   5  SER L   8  0                                        
SHEET    2   K 4 VAL L  20  ALA L  26 -1  O  ARG L  25   N  THR L   6           
SHEET    3   K 4 ASP L  71  ILE L  76 -1  O  PHE L  72   N  CYS L  24           
SHEET    4   K 4 PHE L  63  SER L  68 -1  N  SER L  68   O  ASP L  71           
SHEET    1   L 6 SER L  11  SER L  15  0                                        
SHEET    2   L 6 THR L 105  LYS L 110  1  O  GLU L 108   N  LEU L  12           
SHEET    3   L 6 ALA L  85  GLN L  91 -1  N  ALA L  85   O  VAL L 107           
SHEET    4   L 6 VAL L  34  GLN L  39 -1  N  TYR L  37   O  TYR L  88           
SHEET    5   L 6 LYS L  46  TYR L  50 -1  O  LEU L  48   N  TRP L  36           
SHEET    6   L 6 SER L  54  LEU L  55 -1  O  SER L  54   N  TYR L  50           
SHEET    1   M 4 SER L  11  SER L  15  0                                        
SHEET    2   M 4 THR L 105  LYS L 110  1  O  GLU L 108   N  LEU L  12           
SHEET    3   M 4 ALA L  85  GLN L  91 -1  N  ALA L  85   O  VAL L 107           
SHEET    4   M 4 THR L 100  PHE L 101 -1  O  THR L 100   N  GLN L  91           
SHEET    1   N 4 SER L 117  PHE L 121  0                                        
SHEET    2   N 4 THR L 132  PHE L 142 -1  O  VAL L 136   N  PHE L 121           
SHEET    3   N 4 TYR L 176  SER L 185 -1  O  TYR L 176   N  PHE L 142           
SHEET    4   N 4 SER L 162  VAL L 166 -1  N  SER L 165   O  SER L 179           
SHEET    1   O 4 ALA L 156  LEU L 157  0                                        
SHEET    2   O 4 LYS L 148  VAL L 153 -1  N  VAL L 153   O  ALA L 156           
SHEET    3   O 4 VAL L 194  THR L 200 -1  O  ALA L 196   N  LYS L 152           
SHEET    4   O 4 VAL L 208  ASN L 213 -1  O  VAL L 208   N  VAL L 199           
SHEET    1   P 4 MET B   5  SER B   8  0                                        
SHEET    2   P 4 VAL B  20  ALA B  26 -1  O  ARG B  25   N  THR B   6           
SHEET    3   P 4 ASP B  71  ILE B  76 -1  O  PHE B  72   N  CYS B  24           
SHEET    4   P 4 PHE B  63  SER B  68 -1  N  SER B  68   O  ASP B  71           
SHEET    1   Q 6 SER B  11  SER B  15  0                                        
SHEET    2   Q 6 THR B 105  LYS B 110  1  O  GLU B 108   N  LEU B  12           
SHEET    3   Q 6 ALA B  85  GLN B  91 -1  N  ALA B  85   O  VAL B 107           
SHEET    4   Q 6 VAL B  34  GLN B  39 -1  N  TYR B  37   O  TYR B  88           
SHEET    5   Q 6 LYS B  46  TYR B  50 -1  O  LEU B  48   N  TRP B  36           
SHEET    6   Q 6 SER B  54  LEU B  55 -1  O  SER B  54   N  TYR B  50           
SHEET    1   R 4 SER B 117  PHE B 121  0                                        
SHEET    2   R 4 THR B 132  PHE B 142 -1  O  VAL B 136   N  PHE B 121           
SHEET    3   R 4 TYR B 176  SER B 185 -1  O  LEU B 184   N  ALA B 133           
SHEET    4   R 4 SER B 162  VAL B 166 -1  N  GLN B 163   O  THR B 181           
SHEET    1   S 4 ALA B 156  LEU B 157  0                                        
SHEET    2   S 4 LYS B 148  VAL B 153 -1  N  VAL B 153   O  ALA B 156           
SHEET    3   S 4 VAL B 194  THR B 200 -1  O  ALA B 196   N  LYS B 152           
SHEET    4   S 4 VAL B 208  ASN B 213 -1  O  VAL B 208   N  VAL B 199           
SHEET    1   T 4 GLN H   6  SER H  10  0                                        
SHEET    2   T 4 LEU H  21  SER H  28 -1  O  SER H  24   N  SER H  10           
SHEET    3   T 4 THR H  81  MET H  86 -1  O  MET H  86   N  LEU H  21           
SHEET    4   T 4 PHE H  71  ASP H  76 -1  N  SER H  74   O  TYR H  83           
SHEET    1   U 6 GLY H  13  VAL H  15  0                                        
SHEET    2   U 6 THR H 122  VAL H 126  1  O  THR H 125   N  GLY H  13           
SHEET    3   U 6 ALA H  95  TYR H 103 -1  N  TYR H  97   O  THR H 122           
SHEET    4   U 6 SER H  35  GLN H  42 -1  N  HIS H  38   O  ALA H 100           
SHEET    5   U 6 LEU H  48  ILE H  54 -1  O  GLU H  49   N  ARG H  41           
SHEET    6   U 6 THR H  61  TYR H  63 -1  O  SER H  62   N  TYR H  53           
SHEET    1   V 4 GLY H  13  VAL H  15  0                                        
SHEET    2   V 4 THR H 122  VAL H 126  1  O  THR H 125   N  GLY H  13           
SHEET    3   V 4 ALA H  95  TYR H 103 -1  N  TYR H  97   O  THR H 122           
SHEET    4   V 4 TYR H 117  TRP H 118 -1  O  TYR H 117   N  ARG H 101           
SHEET    1   W 4 SER H 135  LEU H 139  0                                        
SHEET    2   W 4 THR H 150  TYR H 160 -1  O  GLY H 154   N  LEU H 139           
SHEET    3   W 4 TYR H 191  PRO H 200 -1  O  TYR H 191   N  TYR H 160           
SHEET    4   W 4 VAL H 178  THR H 180 -1  N  HIS H 179   O  VAL H 196           
SHEET    1   X 4 SER H 135  LEU H 139  0                                        
SHEET    2   X 4 THR H 150  TYR H 160 -1  O  GLY H 154   N  LEU H 139           
SHEET    3   X 4 TYR H 191  PRO H 200 -1  O  TYR H 191   N  TYR H 160           
SHEET    4   X 4 VAL H 184  LEU H 185 -1  N  VAL H 184   O  SER H 192           
SHEET    1   Y 3 THR H 166  TRP H 169  0                                        
SHEET    2   Y 3 ILE H 210  HIS H 215 -1  O  ASN H 212   N  SER H 168           
SHEET    3   Y 3 THR H 220  LYS H 225 -1  O  VAL H 222   N  VAL H 213           
SHEET    1   Z 4 GLN A   6  SER A  10  0                                        
SHEET    2   Z 4 LEU A  21  SER A  28 -1  O  ALA A  26   N  VAL A   8           
SHEET    3   Z 4 THR A  81  MET A  86 -1  O  MET A  86   N  LEU A  21           
SHEET    4   Z 4 PHE A  71  ASP A  76 -1  N  SER A  74   O  TYR A  83           
SHEET    1  AA 6 GLY A  13  VAL A  15  0                                        
SHEET    2  AA 6 THR A 122  VAL A 126  1  O  THR A 125   N  VAL A  15           
SHEET    3  AA 6 ALA A  95  TYR A 103 -1  N  TYR A  97   O  THR A 122           
SHEET    4  AA 6 SER A  35  GLN A  42 -1  N  HIS A  38   O  ALA A 100           
SHEET    5  AA 6 LEU A  48  ILE A  54 -1  O  ALA A  52   N  TRP A  39           
SHEET    6  AA 6 THR A  61  TYR A  63 -1  O  SER A  62   N  TYR A  53           
SHEET    1  AB 4 GLY A  13  VAL A  15  0                                        
SHEET    2  AB 4 THR A 122  VAL A 126  1  O  THR A 125   N  VAL A  15           
SHEET    3  AB 4 ALA A  95  TYR A 103 -1  N  TYR A  97   O  THR A 122           
SHEET    4  AB 4 TYR A 117  TRP A 118 -1  O  TYR A 117   N  ARG A 101           
SHEET    1  AC 4 SER A 135  LEU A 139  0                                        
SHEET    2  AC 4 THR A 150  TYR A 160 -1  O  LYS A 158   N  SER A 135           
SHEET    3  AC 4 TYR A 191  PRO A 200 -1  O  TYR A 191   N  TYR A 160           
SHEET    4  AC 4 VAL A 178  THR A 180 -1  N  HIS A 179   O  VAL A 196           
SHEET    1  AD 4 SER A 135  LEU A 139  0                                        
SHEET    2  AD 4 THR A 150  TYR A 160 -1  O  LYS A 158   N  SER A 135           
SHEET    3  AD 4 TYR A 191  PRO A 200 -1  O  TYR A 191   N  TYR A 160           
SHEET    4  AD 4 VAL A 184  LEU A 185 -1  N  VAL A 184   O  SER A 192           
SHEET    1  AE 3 THR A 166  TRP A 169  0                                        
SHEET    2  AE 3 ILE A 210  HIS A 215 -1  O  ASN A 212   N  SER A 168           
SHEET    3  AE 3 THR A 220  LYS A 225 -1  O  THR A 220   N  HIS A 215           
SSBOND   1 CYS L   24    CYS L   89                          1555   1555  2.09  
SSBOND   2 CYS L  137    CYS L  197                          1555   1555  2.06  
SSBOND   3 CYS H   25    CYS H   99                          1555   1555  2.08  
SSBOND   4 CYS H  155    CYS H  211                          1555   1555  2.03  
SSBOND   5 CYS B   24    CYS B   89                          1555   1555  2.09  
SSBOND   6 CYS B  137    CYS B  197                          1555   1555  2.05  
SSBOND   7 CYS A   25    CYS A   99                          1555   1555  2.11  
SSBOND   8 CYS A  155    CYS A  211                          1555   1555  2.01  
SSBOND   9 CYS R   12    CYS R   22                          1555   1555  2.14  
SSBOND  10 CYS R   51    CYS R   62                          1555   1555  2.08  
SSBOND  11 CYS C   12    CYS C   22                          1555   1555  2.12  
SSBOND  12 CYS C   51    CYS C   62                          1555   1555  2.07  
LINK         OG  SER H  78                CA    CA H 301     1555   1555  1.85  
LINK         OG  SER A  78                CA    CA H 301     1555   1555  2.50  
CISPEP   1 SER L    8    PRO L    9          0        -6.57                     
CISPEP   2 TYR L  143    PRO L  144          0         5.31                     
CISPEP   3 LYS H  144    SER H  145          0        20.49                     
CISPEP   4 LEU H  156    VAL H  157          0        20.39                     
CISPEP   5 PHE H  161    PRO H  162          0        -5.77                     
CISPEP   6 GLU H  163    PRO H  164          0        -4.02                     
CISPEP   7 SER B    8    PRO B    9          0       -13.70                     
CISPEP   8 TYR B  143    PRO B  144          0         6.29                     
CISPEP   9 LEU A  156    VAL A  157          0        18.92                     
CISPEP  10 PHE A  161    PRO A  162          0        -5.70                     
CISPEP  11 GLU A  163    PRO A  164          0        -7.20                     
CISPEP  12 GLY R   27    THR R   28          0       -22.02                     
CISPEP  13 THR R  137    GLY R  138          0        27.90                     
CISPEP  14 LEU R  172    HIS R  173          0        12.32                     
CISPEP  15 PRO C    4    GLY C    5          0         7.03                     
CISPEP  16 PRO C   26    GLY C   27          0        15.90                     
CISPEP  17 GLY C   30    GLY C   31          0        -4.25                     
CISPEP  18 THR C  137    GLY C  138          0        15.60                     
CISPEP  19 ASP C  187    HIS C  188          0        12.20                     
SITE     1 AC1  3 TYR A 111  LYS R  11  TRP R  23                               
SITE     1 AC2  4 LYS C  11  TRP C  23  TYR L  50  SER L  51                    
SITE     1 AC3  5 VAL L 149  GLN L 150  TRP L 151  GLN L 158                    
SITE     2 AC3  5 SER L 159                                                     
SITE     1 AC4  2 ASP B   2  TYR B  95                                          
SITE     1 AC5  4 SER A  78  ASP H  76  SER H  78  MET R 208                    
SITE     1 AC6  8 GLN C 102  PRO C 103  PRO C 105  ALA C 193                    
SITE     2 AC6  8 TYR H 107  TRP H 108  ASN H 109  ALA H 110                    
SITE     1 AC7  9 TYR A 107  TRP A 108  ASN A 109  ALA A 110                    
SITE     2 AC7  9 GLN R 102  PRO R 103  ASP R 104  PRO R 105                    
SITE     3 AC7  9 ALA R 193                                                     
CRYST1  285.826  285.826   62.248  90.00  90.00 120.00 P 61         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.003499  0.002020  0.000000        0.00000                         
SCALE2      0.000000  0.004040  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016065        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system