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Database: PDB
Entry: 1JDP
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Original site: 1JDP 
HEADER    SIGNALING PROTEIN                       14-JUN-01   1JDP              
TITLE     CRYSTAL STRUCTURE OF HORMONE/RECEPTOR COMPLEX                         
CAVEAT     1JDP    NAG A 501 HAS WRONG CHIRALITY AT ATOM C1 NAG A 502 HAS WRONG 
CAVEAT   2 1JDP    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATRIAL NATRIURETIC PEPTIDE CLEARANCE RECEPTOR;             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NPR-C;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: C-TYPE NATRIURETIC PEPTIDE;                                
COMPND   8 CHAIN: H;                                                            
COMPND   9 SYNONYM: CNP;                                                        
COMPND  10 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: DROSOPHILA;                                       
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: S2;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRMHA3;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7215                                        
KEYWDS    HORMONE-RECEPTOR COMPLEX, NATRIURETIC PEPTIDE RECEPTOR, ALLOSTERIC    
KEYWDS   2 ACTIVATION, SIGNALING PROTEIN                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.-L.HE,D.-C.CHOW,M.M.MARTICK,K.C.GARCIA                              
REVDAT   5   29-JUL-20 1JDP    1       CAVEAT COMPND REMARK HET                 
REVDAT   5 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   13-JUL-11 1JDP    1       VERSN                                    
REVDAT   3   24-FEB-09 1JDP    1       VERSN                                    
REVDAT   2   01-APR-03 1JDP    1       JRNL                                     
REVDAT   1   05-SEP-01 1JDP    0                                                
JRNL        AUTH   X.L.HE,D.C.CHOW,M.M.MARTICK,K.C.GARCIA                       
JRNL        TITL   ALLOSTERIC ACTIVATION OF A SPRING-LOADED NATRIURETIC PEPTIDE 
JRNL        TITL 2 RECEPTOR DIMER BY HORMONE.                                   
JRNL        REF    SCIENCE                       V. 293  1657 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11533490                                                     
JRNL        DOI    10.1126/SCIENCE.1062246                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 70832                          
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 SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3609                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300                       
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 352                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6375                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 470                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 16.00000                                             
REMARK   3    B22 (A**2) : -10.23000                                            
REMARK   3    B33 (A**2) : -5.77000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.29                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JDP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013658.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-APR-01                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70832                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DP4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, PH 7.5, VAPOR            
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       28.40000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.79550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.22750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.79550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.40000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.22750            
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 300 REMARK: (CHAIN A + CHAIN B + CHAIN HA) OR (CHAIN A + CHAIN B +       
REMARK 300 CHAIN HB) FOR A SINGLE NPR-C MONOMER IN THE ASYMMETRIC UNIT, THE     
REMARK 300 CHAIN IDENTIFIER IS A OR B; FOR A CNP PEPTIDE THE CHAIN IDENTIFIER   
REMARK 300 IS HA OR HB ( EACH 0.5 OCCUPANCY ); FOR A BIOLOGICAL ASSEMBLY        
REMARK 300 CHOOSE EITHER A+B+HA OR A+B+HB.                                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     ASN A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     THR A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     ARG A    45                                                      
REMARK 465     ASN A   402                                                      
REMARK 465     VAL A   403                                                      
REMARK 465     LYS A   404                                                      
REMARK 465     TYR A   405                                                      
REMARK 465     PRO A   406                                                      
REMARK 465     TRP A   407                                                      
REMARK 465     GLY A   408                                                      
REMARK 465     PRO A   409                                                      
REMARK 465     LEU A   410                                                      
REMARK 465     LYS A   411                                                      
REMARK 465     LEU A   412                                                      
REMARK 465     ARG A   413                                                      
REMARK 465     ILE A   414                                                      
REMARK 465     ASP A   415                                                      
REMARK 465     GLU A   416                                                      
REMARK 465     ASN A   417                                                      
REMARK 465     ARG A   418                                                      
REMARK 465     ILE A   419                                                      
REMARK 465     VAL A   420                                                      
REMARK 465     GLU A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     THR A   423                                                      
REMARK 465     ASN A   424                                                      
REMARK 465     SER A   425                                                      
REMARK 465     SER A   426                                                      
REMARK 465     PRO A   427                                                      
REMARK 465     CYS A   428                                                      
REMARK 465     LYS A   429                                                      
REMARK 465     SER A   430                                                      
REMARK 465     CYS A   431                                                      
REMARK 465     GLY A   432                                                      
REMARK 465     LEU A   433                                                      
REMARK 465     GLU A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     SER A   436                                                      
REMARK 465     ALA A   437                                                      
REMARK 465     VAL A   438                                                      
REMARK 465     THR A   439                                                      
REMARK 465     GLU B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ASN B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     THR B    43                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     ARG B    45                                                      
REMARK 465     ASN B   402                                                      
REMARK 465     VAL B   403                                                      
REMARK 465     LYS B   404                                                      
REMARK 465     TYR B   405                                                      
REMARK 465     PRO B   406                                                      
REMARK 465     TRP B   407                                                      
REMARK 465     GLY B   408                                                      
REMARK 465     PRO B   409                                                      
REMARK 465     LEU B   410                                                      
REMARK 465     LYS B   411                                                      
REMARK 465     LEU B   412                                                      
REMARK 465     ARG B   413                                                      
REMARK 465     ILE B   414                                                      
REMARK 465     ASP B   415                                                      
REMARK 465     GLU B   416                                                      
REMARK 465     ASN B   417                                                      
REMARK 465     ARG B   418                                                      
REMARK 465     ILE B   419                                                      
REMARK 465     VAL B   420                                                      
REMARK 465     GLU B   421                                                      
REMARK 465     HIS B   422                                                      
REMARK 465     THR B   423                                                      
REMARK 465     ASN B   424                                                      
REMARK 465     SER B   425                                                      
REMARK 465     SER B   426                                                      
REMARK 465     PRO B   427                                                      
REMARK 465     CYS B   428                                                      
REMARK 465     LYS B   429                                                      
REMARK 465     SER B   430                                                      
REMARK 465     CYS B   431                                                      
REMARK 465     GLY B   432                                                      
REMARK 465     LEU B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     SER B   436                                                      
REMARK 465     ALA B   437                                                      
REMARK 465     VAL B   438                                                      
REMARK 465     THR B   439                                                      
REMARK 465     GLY H     1                                                      
REMARK 465     LEU H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     LYS H     4                                                      
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 B 166   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 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    ALA A   2      125.76    -15.45                                   
REMARK 500    SER A 124      -70.31   -146.33                                   
REMARK 500    HIS A 128       -1.71     79.61                                   
REMARK 500    LEU A 164      -93.49   -119.43                                   
REMARK 500    ASP A 198       79.13   -104.40                                   
REMARK 500    SER A 209      -65.66   -106.73                                   
REMARK 500    ALA A 217     -179.56   -172.59                                   
REMARK 500    TYR A 252      177.03    -59.62                                   
REMARK 500    ARG A 259       12.29   -145.62                                   
REMARK 500    MET A 305      149.41   -172.56                                   
REMARK 500    VAL A 309      136.73    -30.21                                   
REMARK 500    ASP B  62       18.87     58.96                                   
REMARK 500    SER B 124      -87.37   -129.39                                   
REMARK 500    LEU B 164      -90.80   -114.05                                   
REMARK 500    ASP B 198       67.59   -107.78                                   
REMARK 500    SER B 209      -72.97   -105.51                                   
REMARK 500    GLN B 301       34.32    -99.93                                   
REMARK 500    GLU B 306       50.48   -107.04                                   
REMARK 500    ASP B 307     -120.21     51.69                                   
REMARK 500    HIS B 328      -71.09    -64.70                                   
REMARK 500    ALA B 333       -2.07    -58.73                                   
REMARK 500    CYS H   6       -0.12    -57.17                                   
REMARK 500    CYS H   6       -0.07    -57.29                                   
REMARK 500    PHE H   7     -164.46   -108.14                                   
REMARK 500    PHE H   7     -164.40   -108.25                                   
REMARK 500    LEU H   9       72.13     34.02                                   
REMARK 500    LEU H   9       72.25     34.07                                   
REMARK 500    LYS H  10     -157.99   -165.17                                   
REMARK 500    LYS H  10     -157.59   -165.07                                   
REMARK 500    ARG H  13       13.65    -55.85                                   
REMARK 500    ARG H  13       13.70    -55.93                                   
REMARK 500    ILE H  14       87.32    -65.07                                   
REMARK 500    ILE H  14       87.31    -65.11                                   
REMARK 500    MET H  17      172.15    137.53                                   
REMARK 500    MET H  17      172.20    137.80                                   
REMARK 500    SER H  18      -35.80   -159.50                                   
REMARK 500    SER H  18      -35.78   -159.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JDN   RELATED DB: PDB                                   
REMARK 900 1JDN THE UNLIGANDED RECEPTOR.                                        
DBREF  1JDP A   -1   439  UNP    P17342   ANPC_HUMAN      44    484             
DBREF  1JDP B   -1   439  UNP    P17342   ANPC_HUMAN      44    484             
DBREF  1JDP H    1    22  UNP    P23582   ANFC_HUMAN     105    126             
SEQRES   1 A  441  GLU ARG GLU ALA LEU PRO PRO GLN LYS ILE GLU VAL LEU          
SEQRES   2 A  441  VAL LEU LEU PRO GLN ASP ASP SER TYR LEU PHE SER LEU          
SEQRES   3 A  441  THR ARG VAL ARG PRO ALA ILE GLU TYR ALA LEU ARG SER          
SEQRES   4 A  441  VAL GLU GLY ASN GLY THR GLY ARG ARG LEU LEU PRO PRO          
SEQRES   5 A  441  GLY THR ARG PHE GLN VAL ALA TYR GLU ASP SER ASP CYS          
SEQRES   6 A  441  GLY ASN ARG ALA LEU PHE SER LEU VAL ASP ARG VAL ALA          
SEQRES   7 A  441  ALA ALA ARG GLY ALA LYS PRO ASP LEU ILE LEU GLY PRO          
SEQRES   8 A  441  VAL CYS GLU TYR ALA ALA ALA PRO VAL ALA ARG LEU ALA          
SEQRES   9 A  441  SER HIS TRP ASP LEU PRO MET LEU SER ALA GLY ALA LEU          
SEQRES  10 A  441  ALA ALA GLY PHE GLN HIS LYS ASP SER GLU TYR SER HIS          
SEQRES  11 A  441  LEU THR ARG VAL ALA PRO ALA TYR ALA LYS MET GLY GLU          
SEQRES  12 A  441  MET MET LEU ALA LEU PHE ARG HIS HIS HIS TRP SER ARG          
SEQRES  13 A  441  ALA ALA LEU VAL TYR SER ASP ASP LYS LEU GLU ARG ASN          
SEQRES  14 A  441  CYS TYR PHE THR LEU GLU GLY VAL HIS GLU VAL PHE GLN          
SEQRES  15 A  441  GLU GLU GLY LEU HIS THR SER ILE TYR SER PHE ASP GLU          
SEQRES  16 A  441  THR LYS ASP LEU ASP LEU GLU ASP ILE VAL ARG ASN ILE          
SEQRES  17 A  441  GLN ALA SER GLU ARG VAL VAL ILE MET CYS ALA SER SER          
SEQRES  18 A  441  ASP THR ILE ARG SER ILE MET LEU VAL ALA HIS ARG HIS          
SEQRES  19 A  441  GLY MET THR SER GLY ASP TYR ALA PHE PHE ASN ILE GLU          
SEQRES  20 A  441  LEU PHE ASN SER SER SER TYR GLY ASP GLY SER TRP LYS          
SEQRES  21 A  441  ARG GLY ASP LYS HIS ASP PHE GLU ALA LYS GLN ALA TYR          
SEQRES  22 A  441  SER SER LEU GLN THR VAL THR LEU LEU ARG THR VAL LYS          
SEQRES  23 A  441  PRO GLU PHE GLU LYS PHE SER MET GLU VAL LYS SER SER          
SEQRES  24 A  441  VAL GLU LYS GLN GLY LEU ASN MET GLU ASP TYR VAL ASN          
SEQRES  25 A  441  MET PHE VAL GLU GLY PHE HIS ASP ALA ILE LEU LEU TYR          
SEQRES  26 A  441  VAL LEU ALA LEU HIS GLU VAL LEU ARG ALA GLY TYR SER          
SEQRES  27 A  441  LYS LYS ASP GLY GLY LYS ILE ILE GLN GLN THR TRP ASN          
SEQRES  28 A  441  ARG THR PHE GLU GLY ILE ALA GLY GLN VAL SER ILE ASP          
SEQRES  29 A  441  ALA ASN GLY ASP ARG TYR GLY ASP PHE SER VAL ILE ALA          
SEQRES  30 A  441  MET THR ASP VAL GLU ALA GLY THR GLN GLU VAL ILE GLY          
SEQRES  31 A  441  ASP TYR PHE GLY LYS GLU GLY ARG PHE GLU MET ARG PRO          
SEQRES  32 A  441  ASN VAL LYS TYR PRO TRP GLY PRO LEU LYS LEU ARG ILE          
SEQRES  33 A  441  ASP GLU ASN ARG ILE VAL GLU HIS THR ASN SER SER PRO          
SEQRES  34 A  441  CYS LYS SER CYS GLY LEU GLU GLU SER ALA VAL THR              
SEQRES   1 B  441  GLU ARG GLU ALA LEU PRO PRO GLN LYS ILE GLU VAL LEU          
SEQRES   2 B  441  VAL LEU LEU PRO GLN ASP ASP SER TYR LEU PHE SER LEU          
SEQRES   3 B  441  THR ARG VAL ARG PRO ALA ILE GLU TYR ALA LEU ARG SER          
SEQRES   4 B  441  VAL GLU GLY ASN GLY THR GLY ARG ARG LEU LEU PRO PRO          
SEQRES   5 B  441  GLY THR ARG PHE GLN VAL ALA TYR GLU ASP SER ASP CYS          
SEQRES   6 B  441  GLY ASN ARG ALA LEU PHE SER LEU VAL ASP ARG VAL ALA          
SEQRES   7 B  441  ALA ALA ARG GLY ALA LYS PRO ASP LEU ILE LEU GLY PRO          
SEQRES   8 B  441  VAL CYS GLU TYR ALA ALA ALA PRO VAL ALA ARG LEU ALA          
SEQRES   9 B  441  SER HIS TRP ASP LEU PRO MET LEU SER ALA GLY ALA LEU          
SEQRES  10 B  441  ALA ALA GLY PHE GLN HIS LYS ASP SER GLU TYR SER HIS          
SEQRES  11 B  441  LEU THR ARG VAL ALA PRO ALA TYR ALA LYS MET GLY GLU          
SEQRES  12 B  441  MET MET LEU ALA LEU PHE ARG HIS HIS HIS TRP SER ARG          
SEQRES  13 B  441  ALA ALA LEU VAL TYR SER ASP ASP LYS LEU GLU ARG ASN          
SEQRES  14 B  441  CYS TYR PHE THR LEU GLU GLY VAL HIS GLU VAL PHE GLN          
SEQRES  15 B  441  GLU GLU GLY LEU HIS THR SER ILE TYR SER PHE ASP GLU          
SEQRES  16 B  441  THR LYS ASP LEU ASP LEU GLU ASP ILE VAL ARG ASN ILE          
SEQRES  17 B  441  GLN ALA SER GLU ARG VAL VAL ILE MET CYS ALA SER SER          
SEQRES  18 B  441  ASP THR ILE ARG SER ILE MET LEU VAL ALA HIS ARG HIS          
SEQRES  19 B  441  GLY MET THR SER GLY ASP TYR ALA PHE PHE ASN ILE GLU          
SEQRES  20 B  441  LEU PHE ASN SER SER SER TYR GLY ASP GLY SER TRP LYS          
SEQRES  21 B  441  ARG GLY ASP LYS HIS ASP PHE GLU ALA LYS GLN ALA TYR          
SEQRES  22 B  441  SER SER LEU GLN THR VAL THR LEU LEU ARG THR VAL LYS          
SEQRES  23 B  441  PRO GLU PHE GLU LYS PHE SER MET GLU VAL LYS SER SER          
SEQRES  24 B  441  VAL GLU LYS GLN GLY LEU ASN MET GLU ASP TYR VAL ASN          
SEQRES  25 B  441  MET PHE VAL GLU GLY PHE HIS ASP ALA ILE LEU LEU TYR          
SEQRES  26 B  441  VAL LEU ALA LEU HIS GLU VAL LEU ARG ALA GLY TYR SER          
SEQRES  27 B  441  LYS LYS ASP GLY GLY LYS ILE ILE GLN GLN THR TRP ASN          
SEQRES  28 B  441  ARG THR PHE GLU GLY ILE ALA GLY GLN VAL SER ILE ASP          
SEQRES  29 B  441  ALA ASN GLY ASP ARG TYR GLY ASP PHE SER VAL ILE ALA          
SEQRES  30 B  441  MET THR ASP VAL GLU ALA GLY THR GLN GLU VAL ILE GLY          
SEQRES  31 B  441  ASP TYR PHE GLY LYS GLU GLY ARG PHE GLU MET ARG PRO          
SEQRES  32 B  441  ASN VAL LYS TYR PRO TRP GLY PRO LEU LYS LEU ARG ILE          
SEQRES  33 B  441  ASP GLU ASN ARG ILE VAL GLU HIS THR ASN SER SER PRO          
SEQRES  34 B  441  CYS LYS SER CYS GLY LEU GLU GLU SER ALA VAL THR              
SEQRES   1 H   22  GLY LEU SER LYS GLY CYS PHE GLY LEU LYS LEU ASP ARG          
SEQRES   2 H   22  ILE GLY SER MET SER GLY LEU GLY CYS                          
MODRES 1JDP ASN A  248  ASN  GLYCOSYLATION SITE                                 
MODRES 1JDP ASN A  349  ASN  GLYCOSYLATION SITE                                 
MODRES 1JDP ASN B  248  ASN  GLYCOSYLATION SITE                                 
MODRES 1JDP ASN B  349  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET     CL  A 503       1                                                       
HET    NAG  B 503      14                                                       
HET     CL  B 504       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4  NAG    5(C8 H15 N O6)                                               
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL  10  HOH   *470(H2 O)                                                    
HELIX    1   1 SER A   23  GLU A   39  1                                  17    
HELIX    2   2 ASN A   65  ALA A   78  1                                  14    
HELIX    3   3 CYS A   91  ASP A  106  1                                  16    
HELIX    4   4 ALA A  116  HIS A  121  5                                   6    
HELIX    5   5 ALA A  135  HIS A  151  1                                  17    
HELIX    6   6 ARG A  166  GLY A  183  1                                  18    
HELIX    7   7 ASP A  198  GLU A  210  1                                  13    
HELIX    8   8 SER A  218  HIS A  232  1                                  15    
HELIX    9   9 HIS A  263  TYR A  271  1                                   9    
HELIX   10  10 LYS A  284  LYS A  300  1                                  17    
HELIX   11  11 ASN A  310  ALA A  333  1                                  24    
HELIX   12  12 ASP A  339  TRP A  348  1                                  10    
HELIX   13  13 SER B   23  GLU B   39  1                                  17    
HELIX   14  14 ASN B   65  ALA B   76  1                                  12    
HELIX   15  15 CYS B   91  TRP B  105  1                                  15    
HELIX   16  16 ALA B  116  HIS B  121  5                                   6    
HELIX   17  17 ALA B  135  HIS B  151  1                                  17    
HELIX   18  18 ARG B  166  GLY B  183  1                                  18    
HELIX   19  19 ASP B  198  ALA B  208  1                                  11    
HELIX   20  20 SER B  218  HIS B  232  1                                  15    
HELIX   21  21 ASN B  248  GLY B  253  1                                   6    
HELIX   22  22 HIS B  263  TYR B  271  1                                   9    
HELIX   23  23 LYS B  284  GLN B  301  1                                  18    
HELIX   24  24 ASN B  310  ALA B  333  1                                  24    
HELIX   25  25 ASP B  339  TRP B  348  1                                  10    
SHEET    1   A 5 ARG A  53  ASP A  60  0                                        
SHEET    2   A 5 LYS A   7  LEU A  14  1  O  ILE A   8   N  GLN A  55           
SHEET    3   A 5 LEU A  85  LEU A  87  1  O  LEU A  85   N  LEU A  11           
SHEET    4   A 5 MET A 109  SER A 111  1  N  LEU A 110   O  ILE A  86           
SHEET    5   A 5 LEU A 129  ARG A 131  1  N  THR A 130   O  MET A 109           
SHEET    1   B 8 HIS A 185  PHE A 191  0                                        
SHEET    2   B 8 ARG A 154  SER A 160  1  O  ALA A 155   N  SER A 187           
SHEET    3   B 8 VAL A 212  CYS A 216  1  O  VAL A 212   N  ALA A 156           
SHEET    4   B 8 ALA A 240  ILE A 244  1  O  ALA A 240   N  VAL A 213           
SHEET    5   B 8 LEU A 274  LEU A 279  1  N  GLN A 275   O  PHE A 241           
SHEET    6   B 8 ASP A 370  ASP A 378 -1  N  SER A 372   O  THR A 278           
SHEET    7   B 8 THR A 383  PHE A 391 -1  O  THR A 383   N  THR A 377           
SHEET    8   B 8 ARG A 396  MET A 399 -1  O  ARG A 396   N  PHE A 391           
SHEET    1   C 2 ARG A 350  GLY A 354  0                                        
SHEET    2   C 2 GLY A 357  ILE A 361 -1  O  GLY A 357   N  GLY A 354           
SHEET    1   D 5 ARG B  53  ASP B  60  0                                        
SHEET    2   D 5 LYS B   7  LEU B  14  1  O  ILE B   8   N  GLN B  55           
SHEET    3   D 5 LEU B  85  LEU B  87  1  O  LEU B  85   N  LEU B  11           
SHEET    4   D 5 MET B 109  SER B 111  1  N  LEU B 110   O  ILE B  86           
SHEET    5   D 5 LEU B 129  ARG B 131  1  N  THR B 130   O  MET B 109           
SHEET    1   E 8 HIS B 185  PHE B 191  0                                        
SHEET    2   E 8 ARG B 154  SER B 160  1  O  ALA B 155   N  SER B 187           
SHEET    3   E 8 VAL B 212  CYS B 216  1  O  VAL B 212   N  ALA B 156           
SHEET    4   E 8 ALA B 240  ILE B 244  1  O  ALA B 240   N  VAL B 213           
SHEET    5   E 8 LEU B 274  LEU B 279  1  N  GLN B 275   O  PHE B 241           
SHEET    6   E 8 ASP B 370  ASP B 378 -1  N  SER B 372   O  THR B 278           
SHEET    7   E 8 THR B 383  PHE B 391 -1  O  THR B 383   N  THR B 377           
SHEET    8   E 8 ARG B 396  MET B 399 -1  O  ARG B 396   N  PHE B 391           
SHEET    1   F 2 ARG B 350  GLY B 354  0                                        
SHEET    2   F 2 GLY B 357  ILE B 361 -1  O  GLY B 357   N  GLY B 354           
SSBOND   1 CYS A   63    CYS A   91                          1555   1555  2.06  
SSBOND   2 CYS A  168    CYS A  216                          1555   1555  2.05  
SSBOND   3 CYS B   63    CYS B   91                          1555   1555  2.03  
SSBOND   4 CYS B  168    CYS B  216                          1555   1555  2.06  
SSBOND   5 CYS H    6    CYS H   22                          1555   1555  2.03  
LINK         ND2 ASN A 248                 C1  NAG A 501     1555   1555  1.46  
LINK         ND2 ASN A 349                 C1  NAG A 502     1555   1555  1.45  
LINK         ND2 ASN B 248                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN B 349                 C1  NAG B 503     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.39  
CISPEP   1 GLY A   88    PRO A   89          0        -0.73                     
CISPEP   2 GLY B   88    PRO B   89          0         0.06                     
CRYST1   56.800  136.455  137.591  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017606  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007328  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007268        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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