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Database: PDB
Entry: 3NCC
LinkDB: 3NCC
Original site: 3NCC 
HEADER    HORMONE/HORMONE RECEPTOR                04-JUN-10   3NCC              
TITLE     A HUMAN PROLACTIN RECEPTOR ANTAGONIST IN COMPLEX WITH THE MUTANT      
TITLE    2 EXTRACELLULAR DOMAIN H188A OF THE HUMAN PROLACTIN RECEPTOR           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLACTIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: SEQUENCE DATABASE RESIDUES 43-227;                         
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: B;                                                            
COMPND  11 FRAGMENT: EXTRACELLULAR DOMAIN RESIDUES 26-234;                      
COMPND  12 SYNONYM: PRL-R;                                                      
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HPRL, PRL;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7L;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HPRLR, PRLR;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PH DEPENDENCE, HEMATOPOIETIC CYTOKINE, HORMONE-HORMONE RECEPTOR       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.V.KULKARNI,M.C.TETTAMANZI,J.W.MURPHY,C.KEELER,D.G.MYSZKA,           
AUTHOR   2 N.E.CHAYEN,E.J.LOLIS,M.E.HODSDON                                     
REVDAT   4   08-NOV-17 3NCC    1       REMARK                                   
REVDAT   3   15-DEC-10 3NCC    1       JRNL                                     
REVDAT   2   20-OCT-10 3NCC    1       JRNL                                     
REVDAT   1   29-SEP-10 3NCC    0                                                
JRNL        AUTH   M.V.KULKARNI,M.C.TETTAMANZI,J.W.MURPHY,C.KEELER,D.G.MYSZKA,  
JRNL        AUTH 2 N.E.CHAYEN,E.J.LOLIS,M.E.HODSDON                             
JRNL        TITL   TWO INDEPENDENT HISTIDINES, ONE IN HUMAN PROLACTIN AND ONE   
JRNL        TITL 2 IN ITS RECEPTOR, ARE CRITICAL FOR PH-DEPENDENT RECEPTOR      
JRNL        TITL 3 RECOGNITION AND ACTIVATION.                                  
JRNL        REF    J.BIOL.CHEM.                  V. 285 38524 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20889499                                                     
JRNL        DOI    10.1074/JBC.M110.172072                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 20987                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1114                            
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) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1544                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3204                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 229                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.71000                                             
REMARK   3    B22 (A**2) : -2.71000                                             
REMARK   3    B33 (A**2) : 4.07000                                              
REMARK   3    B12 (A**2) : -1.36000                                             
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): 0.315         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.249         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.166         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.314         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3333 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4538 ; 1.986 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   400 ; 7.270 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   159 ;34.235 ;24.025       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   578 ;19.704 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;22.566 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   482 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2555 ; 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):  1987 ; 1.206 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3233 ; 2.333 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1346 ; 3.355 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1298 ; 5.596 ; 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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3NCC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059651.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30305                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.81500                            
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 2.1.4                                          
REMARK 200 STARTING MODEL: 3MZG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.7M NACL, 0.1 M HEPES 7.5, 6% PEG       
REMARK 280  MONOMETHYLETHER 550, HANGING DROP, TEMPERATURE 291K, VAPOR          
REMARK 280  DIFFUSION, HANGING DROP, PH 7.5                                     
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       48.76533            
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       24.38267            
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       36.57400            
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       12.19133            
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       60.95667            
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: 3010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
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     THR B   207                                                      
REMARK 465     MET B   208                                                      
REMARK 465     ASN B   209                                                      
REMARK 465     ASP B   210                                                      
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     ASP B 118    CG   OD1  OD2                                       
REMARK 470     ARG B 119    CG   CD   NE   CZ   NH1  NH2                        
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   NH2  ARG B    42     O    HOH B   277              1.64            
REMARK 500   OH   TYR A    28     OE2  GLU A   118              2.07            
REMARK 500   OH   TYR B   178     O    HOH B   271              2.12            
REMARK 500   OH   TYR B    99     O    HOH B   287              2.17            
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 129   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B  13   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B  13   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 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    TYR A  44      -34.66   -158.83                                   
REMARK 500    ARG A  48      177.56    174.19                                   
REMARK 500    GLU A 140       71.17   -109.39                                   
REMARK 500    LYS A 142      127.24    -17.19                                   
REMARK 500    ILE A 146       49.23   -141.76                                   
REMARK 500    ASN A 197       35.15     70.78                                   
REMARK 500    ASN B  16       19.29   -153.36                                   
REMARK 500    LYS B  17       19.97     56.14                                   
REMARK 500    THR B  46      -49.42     76.00                                   
REMARK 500    CYS B  51      126.27    -32.28                                   
REMARK 500    ASP B  53      101.52   -167.46                                   
REMARK 500    ASP B 118       20.63     40.79                                   
REMARK 500    LYS B 120      135.45    -30.61                                   
REMARK 500    LEU B 132        8.42     81.84                                   
REMARK 500    LYS B 152       -6.67     78.07                                   
REMARK 500    ASP B 205       37.34    -76.65                                   
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 THR A  141     LYS A  142                  142.18                    
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                              NA B 212  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  69   O                                                      
REMARK 620 2 LYS B  66   O   109.3                                              
REMARK 620 3 HOH A 244   O   162.5  86.6                                        
REMARK 620 4 HOH B 331   O    94.1  98.4  90.7                                  
REMARK 620 5 HOH A 238   O    88.6  81.6  86.4 177.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 214  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  61   O                                                      
REMARK 620 2 TYR B  54   O    80.8                                              
REMARK 620 3 HOH B 309   O   166.2 102.6                                        
REMARK 620 4 HOH B 319   O   121.5 116.6  69.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 211  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  19   OG1                                                    
REMARK 620 2 THR B  21   OG1 141.4                                              
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 NA B 211                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 212                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 213                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 214                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 215                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MZG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N06   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3N0P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NCB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NCE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NCF   RELATED DB: PDB                                   
DBREF  3NCC A   15   199  UNP    P01236   PRL_HUMAN       43    227             
DBREF  3NCC B    2   210  UNP    P16471   PRLR_HUMAN      26    234             
SEQADV 3NCC MET A   14  UNP  P01236              INITIATING METHIONINE          
SEQADV 3NCC ARG A  129  UNP  P01236    GLY   157 ENGINEERED MUTATION            
SEQADV 3NCC MET B    1  UNP  P16471              INITIATING METHIONINE          
SEQADV 3NCC ALA B  188  UNP  P16471    HIS   212 ENGINEERED MUTATION            
SEQRES   1 A  186  MET LEU ARG ASP LEU PHE ASP ARG ALA VAL VAL LEU SER          
SEQRES   2 A  186  HIS TYR ILE HIS ASN LEU SER SER GLU MET PHE SER GLU          
SEQRES   3 A  186  PHE ASP LYS ARG TYR THR HIS GLY ARG GLY PHE ILE THR          
SEQRES   4 A  186  LYS ALA ILE ASN SER CYS HIS THR SER SER LEU ALA THR          
SEQRES   5 A  186  PRO GLU ASP LYS GLU GLN ALA GLN GLN MET ASN GLN LYS          
SEQRES   6 A  186  ASP PHE LEU SER LEU ILE VAL SER ILE LEU ARG SER TRP          
SEQRES   7 A  186  ASN GLU PRO LEU TYR HIS LEU VAL THR GLU VAL ARG GLY          
SEQRES   8 A  186  MET GLN GLU ALA PRO GLU ALA ILE LEU SER LYS ALA VAL          
SEQRES   9 A  186  GLU ILE GLU GLU GLN THR LYS ARG LEU LEU GLU ARG MET          
SEQRES  10 A  186  GLU LEU ILE VAL SER GLN VAL HIS PRO GLU THR LYS GLU          
SEQRES  11 A  186  ASN GLU ILE TYR PRO VAL TRP SER GLY LEU PRO SER LEU          
SEQRES  12 A  186  GLN MET ALA ASP GLU GLU SER ARG LEU SER ALA TYR TYR          
SEQRES  13 A  186  ASN LEU LEU HIS CYS LEU ARG ARG ASP SER HIS LYS ILE          
SEQRES  14 A  186  ASP ASN TYR LEU LYS LEU LEU LYS CYS ARG ILE ILE HIS          
SEQRES  15 A  186  ASN ASN ASN CYS                                              
SEQRES   1 B  210  MET LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG          
SEQRES   2 B  210  SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO          
SEQRES   3 B  210  GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR          
SEQRES   4 B  210  TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO          
SEQRES   5 B  210  ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY          
SEQRES   6 B  210  LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET          
SEQRES   7 B  210  VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP          
SEQRES   8 B  210  GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP          
SEQRES   9 B  210  PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU          
SEQRES  10 B  210  ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO          
SEQRES  11 B  210  THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU          
SEQRES  12 B  210  TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP          
SEQRES  13 B  210  GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE          
SEQRES  14 B  210  LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL          
SEQRES  15 B  210  ARG CYS LYS PRO ASP ALA GLY TYR TRP SER ALA TRP SER          
SEQRES  16 B  210  PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET          
SEQRES  17 B  210  ASN ASP                                                      
HET     NA  B 211       1                                                       
HET     NA  B 212       1                                                       
HET     CL  B 213       1                                                       
HET     NA  B 214       1                                                       
HET    CO3  B 215       4                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     CO3 CARBONATE ION                                                    
FORMUL   3   NA    3(NA 1+)                                                     
FORMUL   5   CL    CL 1-                                                        
FORMUL   7  CO3    C O3 2-                                                      
FORMUL   8  HOH   *229(H2 O)                                                    
HELIX    1   1 MET A   14  ARG A   43  1                                  30    
HELIX    2   2 GLY A   49  ALA A   54  1                                   6    
HELIX    3   3 ASP A   68  MET A   75  1                                   8    
HELIX    4   4 ASN A   76  GLY A  104  1                                  29    
HELIX    5   5 PRO A  109  HIS A  138  1                                  30    
HELIX    6   6 GLY A  152  MET A  158  1                                   7    
HELIX    7   7 ASP A  160  ASN A  196  1                                  37    
HELIX    8   8 GLY B   65  THR B   69  5                                   5    
HELIX    9   9 ASP B   96  ILE B  100  5                                   5    
SHEET    1   A 3 GLU B   8  ARG B  13  0                                        
SHEET    2   A 3 PHE B  20  ARG B  25 -1  O  TRP B  23   N  LYS B  11           
SHEET    3   A 3 SER B  61  PHE B  64 -1  O  PHE B  64   N  PHE B  20           
SHEET    1   B 4 HIS B  49  GLU B  50  0                                        
SHEET    2   B 4 ASN B  35  ARG B  42 -1  N  TYR B  40   O  HIS B  49           
SHEET    3   B 4 TYR B  75  ASN B  83 -1  O  ILE B  76   N  HIS B  41           
SHEET    4   B 4 GLY B  86  PHE B  89 -1  O  SER B  88   N  ALA B  81           
SHEET    1   C 4 HIS B  49  GLU B  50  0                                        
SHEET    2   C 4 ASN B  35  ARG B  42 -1  N  TYR B  40   O  HIS B  49           
SHEET    3   C 4 TYR B  75  ASN B  83 -1  O  ILE B  76   N  HIS B  41           
SHEET    4   C 4 LEU B  93  VAL B  95 -1  O  LEU B  93   N  MET B  77           
SHEET    1   D 3 LEU B 107  LYS B 114  0                                        
SHEET    2   D 3 TYR B 122  SER B 128 -1  O  TYR B 122   N  LYS B 114           
SHEET    3   D 3 GLU B 166  ILE B 169 -1  O  ILE B 169   N  LEU B 123           
SHEET    1   E 4 GLU B 157  PHE B 160  0                                        
SHEET    2   E 4 LEU B 142  LYS B 149 -1  N  LEU B 148   O  GLU B 157           
SHEET    3   E 4 LYS B 177  PRO B 186 -1  O  GLN B 181   N  ARG B 147           
SHEET    4   E 4 THR B 198  GLN B 201 -1  O  ILE B 200   N  TYR B 178           
SSBOND   1 CYS A   58    CYS A  174                          1555   1555  2.09  
SSBOND   2 CYS A  191    CYS A  199                          1555   1555  2.09  
SSBOND   3 CYS B   12    CYS B   22                          1555   1555  2.10  
SSBOND   4 CYS B   51    CYS B   62                          1555   1555  2.11  
LINK         O   THR B  69                NA    NA B 212     1555   1555  2.18  
LINK         O   LYS B  66                NA    NA B 212     1555   1555  2.30  
LINK         O   SER B  61                NA    NA B 214     1555   1555  2.78  
LINK         O   TYR B  54                NA    NA B 214     1555   1555  2.97  
LINK         OG1 THR B  19                NA    NA B 211     1555   1555  3.02  
LINK         OG1 THR B  21                NA    NA B 211     1555   1555  3.07  
LINK        NA    NA B 212                 O   HOH A 244     1555   1555  2.30  
LINK        NA    NA B 212                 O   HOH B 331     1555   1555  2.31  
LINK        NA    NA B 212                 O   HOH A 238     1555   1555  2.35  
LINK        NA    NA B 214                 O   HOH B 309     1555   1555  3.12  
LINK        NA    NA B 214                 O   HOH B 319     1555   1555  3.17  
SITE     1 AC1  5 PRO B  15  THR B  19  PHE B  20  THR B  21                    
SITE     2 AC1  5 HIS B  63                                                     
SITE     1 AC2  6 ASP A  68  HOH A 238  HOH A 244  LYS B  66                    
SITE     2 AC2  6 THR B  69  HOH B 331                                          
SITE     1 AC3  2 TYR B 190  TRP B 191                                          
SITE     1 AC4  4 TYR B  54  GLY B  58  ASN B  60  SER B  61                    
SITE     1 AC5  3 LYS B  11  TRP B  23  HOH B 337                               
CRYST1  123.411  123.411   73.148  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      0.008103  0.004678  0.000000        0.00000                         
SCALE2      0.000000  0.009357  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013671        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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