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Database: PDB
Entry: 3D48
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Original site: 3D48 
HEADER    HORMONE/HORMONE RECEPTOR                14-MAY-08   3D48              
TITLE     CRYSTAL STRUCTURE OF A PROLACTIN RECEPTOR ANTAGONIST BOUND TO THE     
TITLE    2 EXTRACELLULAR DOMAIN OF THE PROLACTIN RECEPTOR                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLACTIN;                                                 
COMPND   3 CHAIN: P;                                                            
COMPND   4 FRAGMENT: RESIDUES 12-199;                                           
COMPND   5 SYNONYM: PRL;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROLACTIN RECEPTOR;                                        
COMPND  10 CHAIN: R;                                                            
COMPND  11 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  12 SYNONYM: PRL-R;                                                      
COMPND  13 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: PRL;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32-A(+);                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: PRLR;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET39-B(+)                                
KEYWDS    CYTOKINE-CYTOKINE RECEPTOR COMPLEX, FOUR-HELIX BUNDLE, GLYCOPROTEIN,  
KEYWDS   2 HORMONE, LACTATION, SECRETED, ALTERNATIVE SPLICING, MEMBRANE,        
KEYWDS   3 RECEPTOR, TRANSMEMBRANE, HORMONE-HORMONE RECEPTOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.A.SVENSSON,J.BREINHOLT                                              
REVDAT   4   23-MAY-18 3D48    1       REMARK                                   
REVDAT   3   24-FEB-09 3D48    1       VERSN                                    
REVDAT   2   28-OCT-08 3D48    1       JRNL                                     
REVDAT   1   03-JUN-08 3D48    0                                                
JRNL        AUTH   L.A.SVENSSON,K.BONDENSGAARD,L.NORSKOV-LAURITSEN,             
JRNL        AUTH 2 L.CHRISTENSEN,P.BECKER,M.D.ANDERSEN,M.J.MALTESEN,K.D.RAND,   
JRNL        AUTH 3 J.BREINHOLT                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF A PROLACTIN RECEPTOR ANTAGONIST BOUND   
JRNL        TITL 2 TO THE EXTRACELLULAR DOMAIN OF THE PROLACTIN RECEPTOR        
JRNL        REF    J.BIOL.CHEM.                  V. 283 19085 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18467331                                                     
JRNL        DOI    10.1074/JBC.M801202200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.4.0066                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 20629                          
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1088                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1501                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2945                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.48000                                             
REMARK   3    B22 (A**2) : -2.48000                                             
REMARK   3    B33 (A**2) : 3.73000                                              
REMARK   3    B12 (A**2) : -1.24000                                             
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): 0.335         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.289         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.222         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.770         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.863                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3040 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4121 ; 2.013 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   353 ; 8.690 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   139 ;35.912 ;23.885       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   522 ;22.244 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;20.394 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   446 ; 0.133 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2281 ; 0.010 ; 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):  1813 ; 0.964 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2929 ; 1.782 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1227 ; 2.465 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1192 ; 4.035 ; 4.500       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 3D48 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047571.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21797                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.50100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
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: FOR THE R CHAIN, PDB ENTRY 1BP3. FOR THE P CHAIN,    
REMARK 200  A CORE OF A MODELER HOMOLOGY MODEL BASED ON PDB ENTRIES 1BP3,       
REMARK 200  1F6F, 1RW5 AND 1N9D.                                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM CHLORIDE, 0.1M HEPES, PH     
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 297K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       46.54667            
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       23.27333            
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       34.91000            
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       11.63667            
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       58.18333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, 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     SER P    12                                                      
REMARK 465     ARG P    43                                                      
REMARK 465     TYR P    44                                                      
REMARK 465     THR P    45                                                      
REMARK 465     HIS P    46                                                      
REMARK 465     GLY P    47                                                      
REMARK 465     ARG P    48                                                      
REMARK 465     GLY P   104                                                      
REMARK 465     MET P   105                                                      
REMARK 465     GLN P   106                                                      
REMARK 465     GLU P   107                                                      
REMARK 465     ALA P   108                                                      
REMARK 465     PRO P   109                                                      
REMARK 465     GLU P   110                                                      
REMARK 465     HIS P   138                                                      
REMARK 465     PRO P   139                                                      
REMARK 465     GLU P   140                                                      
REMARK 465     THR P   141                                                      
REMARK 465     LYS P   142                                                      
REMARK 465     GLU P   143                                                      
REMARK 465     ASN P   144                                                      
REMARK 465     GLU P   145                                                      
REMARK 465     CYS P   199                                                      
REMARK 465     SER R     0                                                      
REMARK 465     GLN R     1                                                      
REMARK 465     GLN R   115                                                      
REMARK 465     PRO R   116                                                      
REMARK 465     GLU R   117                                                      
REMARK 465     ASP R   118                                                      
REMARK 465     ARG R   119                                                      
REMARK 465     LYS R   120                                                      
REMARK 465     LEU R   172                                                      
REMARK 465     HIS R   173                                                      
REMARK 465     ASP R   205                                                      
REMARK 465     PHE R   206                                                      
REMARK 465     THR R   207                                                      
REMARK 465     MET R   208                                                      
REMARK 465     ASN R   209                                                      
REMARK 465     ASP R   210                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG P    16     N    LEU P    18              1.89            
REMARK 500   O    LEU R     2     ND2  ASN R    83              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    CYS R 184   CB    CYS R 184   SG     -0.113                       
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 R 179   CA  -  CB  -  CG  ANGL. DEV. =  14.2 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    ARG P  16     -118.27    -64.80                                   
REMARK 500    ASP P  17      -43.33     12.77                                   
REMARK 500    ASP P  41       93.74    -66.85                                   
REMARK 500    SER P  90      -19.46    -48.07                                   
REMARK 500    GLU P  93      -73.77    -57.04                                   
REMARK 500    ASN P 197       60.97     62.55                                   
REMARK 500    ASN R  16       22.09   -158.28                                   
REMARK 500    LYS R  17       14.55     53.05                                   
REMARK 500    THR R  28      125.36    -37.41                                   
REMARK 500    ASP R  29      128.14    -28.45                                   
REMARK 500    GLU R  45      136.58    158.45                                   
REMARK 500    CYS R  51      124.37    -33.19                                   
REMARK 500    ASP R  53      102.41   -166.11                                   
REMARK 500    PRO R  59      132.21    -36.84                                   
REMARK 500    ASP R 104      172.46    -54.41                                   
REMARK 500    LEU R 109      107.24    -56.63                                   
REMARK 500    PRO R 203     -168.93    -60.05                                   
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 PRO R    4     GLY R    5                   45.06                    
REMARK 500 GLY R  175     GLN R  176                 -146.15                    
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 CO3 P 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 R 211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 R 212                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 R 213                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BP3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1F6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1RW5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1N9D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2Q98   RELATED DB: PDB                                   
DBREF  3D48 P   12   199  UNP    P01236   PRL_HUMAN       40    227             
DBREF  3D48 R    1   210  UNP    P16471   PRLR_HUMAN      25    234             
SEQADV 3D48 SER P   12  UNP  P01236    GLN    40 ENGINEERED                     
SEQADV 3D48 ARG P  129  UNP  P01236    GLY   157 ENGINEERED                     
SEQADV 3D48 SER R    0  UNP  P16471              EXPRESSION TAG                 
SEQRES   1 P  188  SER VAL THR LEU ARG ASP LEU PHE ASP ARG ALA VAL VAL          
SEQRES   2 P  188  LEU SER HIS TYR ILE HIS ASN LEU SER SER GLU MET PHE          
SEQRES   3 P  188  SER GLU PHE ASP LYS ARG TYR THR HIS GLY ARG GLY PHE          
SEQRES   4 P  188  ILE THR LYS ALA ILE ASN SER CYS HIS THR SER SER LEU          
SEQRES   5 P  188  ALA THR PRO GLU ASP LYS GLU GLN ALA GLN GLN MET ASN          
SEQRES   6 P  188  GLN LYS ASP PHE LEU SER LEU ILE VAL SER ILE LEU ARG          
SEQRES   7 P  188  SER TRP ASN GLU PRO LEU TYR HIS LEU VAL THR GLU VAL          
SEQRES   8 P  188  ARG GLY MET GLN GLU ALA PRO GLU ALA ILE LEU SER LYS          
SEQRES   9 P  188  ALA VAL GLU ILE GLU GLU GLN THR LYS ARG LEU LEU GLU          
SEQRES  10 P  188  ARG MET GLU LEU ILE VAL SER GLN VAL HIS PRO GLU THR          
SEQRES  11 P  188  LYS GLU ASN GLU ILE TYR PRO VAL TRP SER GLY LEU PRO          
SEQRES  12 P  188  SER LEU GLN MET ALA ASP GLU GLU SER ARG LEU SER ALA          
SEQRES  13 P  188  TYR TYR ASN LEU LEU HIS CYS LEU ARG ARG ASP SER HIS          
SEQRES  14 P  188  LYS ILE ASP ASN TYR LEU LYS LEU LEU LYS CYS ARG ILE          
SEQRES  15 P  188  ILE HIS ASN ASN ASN CYS                                      
SEQRES   1 R  211  SER GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS          
SEQRES   2 R  211  ARG SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG          
SEQRES   3 R  211  PRO GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU          
SEQRES   4 R  211  THR TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS          
SEQRES   5 R  211  PRO ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE          
SEQRES   6 R  211  GLY LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET          
SEQRES   7 R  211  MET VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER          
SEQRES   8 R  211  ASP GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO          
SEQRES   9 R  211  ASP PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO          
SEQRES  10 R  211  GLU ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO          
SEQRES  11 R  211  PRO THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU          
SEQRES  12 R  211  LEU TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU          
SEQRES  13 R  211  TRP GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS          
SEQRES  14 R  211  ILE LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN          
SEQRES  15 R  211  VAL ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP          
SEQRES  16 R  211  SER PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR          
SEQRES  17 R  211  MET ASN ASP                                                  
HET    CO3  P   1       4                                                       
HET    CO3  R 211       4                                                       
HET    CO3  R 212       4                                                       
HET    CO3  R 213       4                                                       
HETNAM     CO3 CARBONATE ION                                                    
FORMUL   3  CO3    4(C O3 2-)                                                   
FORMUL   7  HOH   *103(H2 O)                                                    
HELIX    1   1 THR P   14  ASP P   41  1                                  28    
HELIX    2   2 PHE P   50  ILE P   55  1                                   6    
HELIX    3   3 CYS P   58  LEU P   63  5                                   6    
HELIX    4   4 ASP P   68  GLN P   73  1                                   6    
HELIX    5   5 ASN P   76  ARG P  103  1                                  28    
HELIX    6   6 ALA P  111  VAL P  137  1                                  27    
HELIX    7   7 GLY P  152  GLN P  157  1                                   6    
HELIX    8   8 ASP P  160  ILE P  194  1                                  35    
HELIX    9   9 GLY R   65  THR R   69  5                                   5    
HELIX   10  10 THR R   98  ILE R  100  5                                   3    
SHEET    1   A 3 LYS R   6  ARG R  13  0                                        
SHEET    2   A 3 PHE R  20  THR R  28 -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 THR R  74  ASN R  83 -1  O  ASN R  80   N  SER R  37           
SHEET    4   B 4 GLY R  86  PHE R  89 -1  O  GLY R  86   N  ASN R  83           
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 THR R  74  ASN R  83 -1  O  ASN R  80   N  SER R  37           
SHEET    4   C 4 LEU R  93  ASP R  96 -1  O  VAL R  95   N  TYR R  75           
SHEET    1   D 3 LEU R 107  GLU R 112  0                                        
SHEET    2   D 3 LEU R 123  SER R 128 -1  O  LYS R 126   N  ALA R 110           
SHEET    3   D 3 GLU R 166  ILE R 169 -1  O  ILE R 169   N  LEU R 123           
SHEET    1   E 4 GLU R 157  GLY R 162  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  GLN R 181   N  ARG R 147           
SHEET    4   E 4 THR R 198  GLN R 201 -1  O  THR R 198   N  VAL R 180           
SSBOND   1 CYS P   58    CYS P  174                          1555   1555  2.05  
SSBOND   2 CYS R   12    CYS R   22                          1555   1555  2.08  
SSBOND   3 CYS R   51    CYS R   62                          1555   1555  2.12  
SITE     1 AC1  5 SER P  57  CYS P  58  HIS P  59  LEU P 171                    
SITE     2 AC1  5 CYS P 174                                                     
SITE     1 AC2  2 TYR R 190  TRP R 191                                          
SITE     1 AC3  3 CYS R  12  ARG R  13  GLN R 102                               
SITE     1 AC4  5 THR R  39  TYR R  40  HIS R  41  ILE R  76                    
SITE     2 AC4  5 MET R  78                                                     
CRYST1  125.350  125.350   69.820  90.00  90.00 120.00 P 65          6          
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      0.007980  0.004610  0.000000        0.00000                         
SCALE2      0.000000  0.009210  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014320        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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