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Database: PDB
Entry: 1BP3
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Original site: 1BP3 
HEADER    HORMONE/GROWTH FACTOR                   12-AUG-98   1BP3              
TITLE     THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR             
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (GROWTH HORMONE);                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROTEIN (PROLACTIN RECEPTOR);                              
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HORMONE, RECEPTOR, HORMONE/GROWTH FACTOR                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.SOMERS,M.ULTSCH,A.M.DE VOS,A.A.KOSSIAKOFF                           
REVDAT   4   24-FEB-09 1BP3    1       VERSN                                    
REVDAT   3   29-DEC-99 1BP3    4       HEADER COMPND REMARK JRNL                
REVDAT   3 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   2   23-SEP-98 1BP3    3       HET    REMARK TITLE  HETATM              
REVDAT   2 2                   3       DBREF  SEQADV SSBOND TER                 
REVDAT   2 3                   3       LINK   ATOM   SEQRES SITE                
REVDAT   2 4                   3       FORMUL SHEET  HELIX  HETSYN              
REVDAT   2 5                   3       CONECT HETNAM                            
REVDAT   1   19-AUG-98 1BP3    0                                                
JRNL        AUTH   W.SOMERS,M.ULTSCH,A.M.DE VOS,A.A.KOSSIAKOFF                  
JRNL        TITL   THE X-RAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN            
JRNL        TITL 2 RECEPTOR COMPLEX.                                            
JRNL        REF    NATURE                        V. 372   478 1994              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7984244                                                      
JRNL        DOI    10.1038/372478A0                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53033                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.019 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.046 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BP3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008017.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 300.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 9                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.908                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9883                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1A22                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       77.10000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       77.10000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN A   149                                                      
REMARK 465     SER A   150                                                      
REMARK 465     HIS A   151                                                      
REMARK 465     ASN A   152                                                      
REMARK 465     PHE A   191                                                      
REMARK 465     GLN B   201                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     LEU B   232                                                      
REMARK 465     PRO B   233                                                      
REMARK 465     GLN B   284                                                      
REMARK 465     MET B   285                                                      
REMARK 465     GLY B   286                                                      
REMARK 465     ASP B   405                                                      
REMARK 465     PHE B   406                                                      
REMARK 465     THR B   407                                                      
REMARK 465     MET B   408                                                      
REMARK 465     ASN B   409                                                      
REMARK 465     ASP B   410                                                      
REMARK 465     THR B   411                                                      
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     GLU A 119    CG   CD   OE1  OE2                                  
REMARK 470     SER A 132    OG                                                  
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 470     GLN A 141    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 202    CG   CD1  CD2                                       
REMARK 470     GLU B 308    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 377    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    GLY B 338   N     GLY B 338   CA     -0.116                       
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    ARG A   8   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A  16   CD  -  NE  -  CZ  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG A  16   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A  19   CD  -  NE  -  CZ  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ASP A  26   CB  -  CA  -  C   ANGL. DEV. =  12.6 DEGREES          
REMARK 500    ASP A  26   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    GLN A  29   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    GLU A  33   CA  -  CB  -  CG  ANGL. DEV. =  23.7 DEGREES          
REMARK 500    TYR A  35   CB  -  CG  -  CD2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    PRO A  37   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    GLU A  39   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    GLU A  39   CB  -  CG  -  CD  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    GLN A  46   CB  -  CG  -  CD  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    GLU A  56   CB  -  CG  -  CD  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ILE A  58   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ARG A  64   CG  -  CD  -  NE  ANGL. DEV. =  18.8 DEGREES          
REMARK 500    ARG A  64   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A  64   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    GLU A  88   OE1 -  CD  -  OE2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    SER A  95   CA  -  CB  -  OG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    VAL A 102   C   -  N   -  CA  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    TYR A 103   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    TYR A 103   CB  -  CG  -  CD1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 127   CG  -  CD  -  NE  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    ARG A 127   CD  -  NE  -  CZ  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ARG A 127   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A 127   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    GLY A 131   N   -  CA  -  C   ANGL. DEV. =  20.2 DEGREES          
REMARK 500    PHE A 139   CB  -  CA  -  C   ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ARG A 167   CD  -  NE  -  CZ  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    GLU A 174   CG  -  CD  -  OE2 ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ARG A 178   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    CYS A 182   CA  -  CB  -  SG  ANGL. DEV. = -15.5 DEGREES          
REMARK 500    ARG A 183   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 183   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 183   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    CYS A 189   CB  -  CA  -  C   ANGL. DEV. =   7.3 DEGREES          
REMARK 500    CYS A 189   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500    GLU B 208   CB  -  CG  -  CD  ANGL. DEV. =  17.7 DEGREES          
REMARK 500    SER B 214   N   -  CA  -  CB  ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    TRP B 224   N   -  CA  -  CB  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ARG B 225   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B 225   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    THR B 228   C   -  N   -  CA  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    ASP B 229   CB  -  CA  -  C   ANGL. DEV. =  16.7 DEGREES          
REMARK 500    ASP B 229   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TYR B 236   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    TYR B 236   CB  -  CG  -  CD1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      83 ANGLE DEVIATIONS.                             
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    THR A   3       94.43    -59.29                                   
REMARK 500    ILE A   4      130.48    -23.16                                   
REMARK 500    SER A   7      -71.75    -38.69                                   
REMARK 500    ILE A  36       48.74     70.39                                   
REMARK 500    LYS A  38      -93.80   -123.82                                   
REMARK 500    LYS A  41     -100.51     -0.52                                   
REMARK 500    GLN A  46      -67.59    -17.93                                   
REMARK 500    PRO A  48      -62.74    -16.27                                   
REMARK 500    GLN A  49      -84.39    -19.04                                   
REMARK 500    SER A  55       40.71    -86.10                                   
REMARK 500    ARG A  64      -77.67    -60.19                                   
REMARK 500    GLU A  65      -71.50    -24.04                                   
REMARK 500    VAL A  90       -1.76    -57.28                                   
REMARK 500    ALA A 105      -76.69    -37.31                                   
REMARK 500    VAL A 110      -39.29    -32.05                                   
REMARK 500    LEU A 128       44.61   -104.72                                   
REMARK 500    GLU A 129     -110.07   -115.26                                   
REMARK 500    ASP A 130        4.35     93.11                                   
REMARK 500    GLN A 137      -95.26   -108.94                                   
REMARK 500    GLN A 141       85.99    -55.39                                   
REMARK 500    THR A 142       72.82    -69.69                                   
REMARK 500    PHE A 146      -73.67    -87.56                                   
REMARK 500    GLU A 186       89.19    -59.34                                   
REMARK 500    SER A 188       66.01    -63.42                                   
REMARK 500    CYS A 189      -77.55   -151.39                                   
REMARK 500    PRO B 204     -104.32    -65.31                                   
REMARK 500    LYS B 206      -57.10   -120.66                                   
REMARK 500    LYS B 211      167.84    176.10                                   
REMARK 500    ASN B 216       26.05   -168.81                                   
REMARK 500    GLU B 218      -11.13   -154.80                                   
REMARK 500    ARG B 225      115.41   -162.98                                   
REMARK 500    PRO B 226       94.51    -66.67                                   
REMARK 500    ASP B 229       68.35   -101.24                                   
REMARK 500    ASN B 235       61.05   -102.40                                   
REMARK 500    GLU B 245       75.14    -35.93                                   
REMARK 500    THR B 246      -29.00     -6.22                                   
REMARK 500    ILE B 255      -73.45   -109.49                                   
REMARK 500    THR B 256       73.75    -60.21                                   
REMARK 500    ASN B 260       46.55     77.79                                   
REMARK 500    SER B 290     -177.68   -172.73                                   
REMARK 500    GLU B 308       68.30     62.92                                   
REMARK 500    GLU B 317      -80.68    -13.43                                   
REMARK 500    ARG B 319      179.75    -54.91                                   
REMARK 500    TRP B 324       93.67   -162.59                                   
REMARK 500    TRP B 327     -147.10   -149.38                                   
REMARK 500    SER B 328      142.95   -178.63                                   
REMARK 500    THR B 331      -70.33    -47.42                                   
REMARK 500    LEU B 332      -31.12    -37.79                                   
REMARK 500    THR B 337       56.18   -119.53                                   
REMARK 500    GLU B 351      -71.16    -20.37                                   
REMARK 500    ALA B 353      150.39    -24.72                                   
REMARK 500    ALA B 354      -96.53    -84.15                                   
REMARK 500    PRO B 374      -49.77    -27.53                                   
REMARK 500    ASP B 387      -56.15    -23.60                                   
REMARK 500    PRO B 403     -150.79    -70.71                                   
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                              ZN A 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   ND1                                                    
REMARK 620 2 GLU A 174   OE2  91.2                                              
REMARK 620 3 ASP B 387   OD2 117.5 101.7                                        
REMARK 620 4 HIS B 388   NE2 116.9 135.5  95.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ZNA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE BETWEEN HGH AND PROLACTIN        
REMARK 800  RECEPTOR.                                                           
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 500                  
DBREF  1BP3 A    1   191  UNP    P01241   SOMA_HUMAN      27    217             
DBREF  1BP3 B  201   411  UNP    P16471   PRLR_HUMAN      25    235             
SEQADV 1BP3 ARG A  120  UNP  P01241    GLY   146 ENGINEERED                     
SEQRES   1 A  191  PHE PRO THR ILE PRO LEU SER ARG LEU PHE ASP ASN ALA          
SEQRES   2 A  191  MET LEU ARG ALA HIS ARG LEU HIS GLN LEU ALA PHE ASP          
SEQRES   3 A  191  THR TYR GLN GLU PHE GLU GLU ALA TYR ILE PRO LYS GLU          
SEQRES   4 A  191  GLN LYS TYR SER PHE LEU GLN ASN PRO GLN THR SER LEU          
SEQRES   5 A  191  CYS PHE SER GLU SER ILE PRO THR PRO SER ASN ARG GLU          
SEQRES   6 A  191  GLU THR GLN GLN LYS SER ASN LEU GLU LEU LEU ARG ILE          
SEQRES   7 A  191  SER LEU LEU LEU ILE GLN SER TRP LEU GLU PRO VAL GLN          
SEQRES   8 A  191  PHE LEU ARG SER VAL PHE ALA ASN SER LEU VAL TYR GLY          
SEQRES   9 A  191  ALA SER ASP SER ASN VAL TYR ASP LEU LEU LYS ASP LEU          
SEQRES  10 A  191  GLU GLU ARG ILE GLN THR LEU MET GLY ARG LEU GLU ASP          
SEQRES  11 A  191  GLY SER PRO ARG THR GLY GLN ILE PHE LYS GLN THR TYR          
SEQRES  12 A  191  SER LYS PHE ASP THR ASN SER HIS ASN ASP ASP ALA LEU          
SEQRES  13 A  191  LEU LYS ASN TYR GLY LEU LEU TYR CYS PHE ARG LYS ASP          
SEQRES  14 A  191  MET ASP LYS VAL GLU THR PHE LEU ARG ILE VAL GLN CYS          
SEQRES  15 A  191  ARG SER VAL GLU GLY SER CYS GLY PHE                          
SEQRES   1 B  211  GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG          
SEQRES   2 B  211  SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO          
SEQRES   3 B  211  GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR          
SEQRES   4 B  211  TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO          
SEQRES   5 B  211  ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY          
SEQRES   6 B  211  LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET          
SEQRES   7 B  211  VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP          
SEQRES   8 B  211  GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP          
SEQRES   9 B  211  PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU          
SEQRES  10 B  211  ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO          
SEQRES  11 B  211  THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU          
SEQRES  12 B  211  TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP          
SEQRES  13 B  211  GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE          
SEQRES  14 B  211  LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL          
SEQRES  15 B  211  ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP SER          
SEQRES  16 B  211  PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET          
SEQRES  17 B  211  ASN ASP THR                                                  
HET     ZN  A 500       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    ZN 2+                                                        
HELIX    1   1 LEU A    6  ALA A   34  1                                  29    
HELIX    2   2 LYS A   41  SER A   43  5                                   3    
HELIX    3   3 PRO A   48  SER A   51  1                                   4    
HELIX    4   4 ARG A   64  THR A   67  1                                   4    
HELIX    5   5 ASN A   72  GLN A   91  1                                  20    
HELIX    6   6 ARG A   94  ALA A   98  1                                   5    
HELIX    7   7 VAL A  110  LEU A  128  1                                  19    
HELIX    8   8 ALA A  155  SER A  184  1                                  30    
HELIX    9   9 VAL B  297  TYR B  299  5                                   3    
SHEET    1   A 3 SER B 261  PHE B 264  0                                        
SHEET    2   A 3 PHE B 220  PRO B 226 -1  N  CYS B 222   O  CYS B 262           
SHEET    3   A 3 PRO B 207  ARG B 213 -1  N  ARG B 213   O  THR B 221           
SHEET    1   B 3 SER B 237  ARG B 242  0                                        
SHEET    2   B 3 THR B 274  ASN B 280 -1  N  ASN B 280   O  SER B 237           
SHEET    3   B 3 LEU B 293  ASP B 296 -1  N  VAL B 295   O  TYR B 275           
SHEET    1   C 3 TYR B 378  PRO B 386  0                                        
SHEET    2   C 3 LEU B 342  PRO B 350 -1  N  LYS B 349   O  LEU B 379           
SHEET    3   C 3 GLU B 357  GLY B 362 -1  N  GLY B 362   O  TYR B 344           
SSBOND   1 CYS A   53    CYS A  165                          1555   1555  1.96  
SSBOND   2 CYS A  182    CYS A  189                          1555   1555  1.90  
SSBOND   3 CYS B  251    CYS B  262                          1555   1555  2.05  
SSBOND   4 CYS B  212    CYS B  222                          1555   1555  2.07  
LINK         ND1 HIS A  18                ZN    ZN A 500     1555   1555  2.04  
LINK         OE2 GLU A 174                ZN    ZN A 500     1555   1555  2.06  
LINK         OD2 ASP B 387                ZN    ZN A 500     1555   1555  2.00  
LINK         NE2 HIS B 388                ZN    ZN A 500     1555   1555  2.09  
SITE     1 ZNA  4 HIS A  18  GLU A 174  ASP B 387  HIS B 388                    
SITE     1 AC1  4 HIS A  18  GLU A 174  ASP B 387  HIS B 388                    
CRYST1  154.200   69.800   43.300  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006485  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014327  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023095        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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