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Database: PDB
Entry: 3AQF
LinkDB: 3AQF
Original site: 3AQF 
HEADER    TRANSPORT PROTEIN/MEMBRANE PROTEIN      29-OCT-10   3AQF              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN CRLR/RAMP2 EXTRACELLULAR COMPLEX       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 39-139;                 
COMPND   5 SYNONYM: CALCITONIN-RECEPTOR-LIKE RECEPTOR ACTIVITY-MODIFYING PROTEIN
COMPND   6 2, CRLR ACTIVITY-MODIFYING PROTEIN 2;                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CALCITONIN GENE-RELATED PEPTIDE TYPE 1 RECEPTOR;           
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: N-TERMINAL DOMAIN, UNP RESIDUES 23-136;                    
COMPND  12 SYNONYM: CGRP TYPE 1 RECEPTOR, CALCITONIN RECEPTOR-LIKE RECEPTOR;    
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAMP2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI CELL-FREE SYSTEM;                
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PX070809-03;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CALCRL, CGRPR;                                                 
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI CELL-FREE SYSTEM;                
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PX080331-02                               
KEYWDS    TRANSMEMBRANE, GPCR, ADRENOMEDULLIN, TRAFFICKING, CLR, CGRP,          
KEYWDS   2 ENDOPLASMIC RETICULUM, AM-RECEPTOR, DISEASE, NEOVASCULARIZATION, CO- 
KEYWDS   3 ACTIVATING RECEPTOR FOR ADRENOMEDULLIN, ADRENOMEDULLIN (AM),         
KEYWDS   4 ENDOPLASMIC RETICULUM (ER), TRANSPORT PROTEIN-MEMBRANE PROTEIN       
KEYWDS   5 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KUSANO,M.KUKIMONO-NIINO,M.SHIROUZU,T.SHINDO,S.YOKOYAMA              
REVDAT   2   25-JUL-12 3AQF    1       JRNL                                     
REVDAT   1   02-NOV-11 3AQF    0                                                
JRNL        AUTH   S.KUSANO,M.KUKIMOTO-NIINO,N.HINO,N.OHSAWA,K.OKUDA,           
JRNL        AUTH 2 K.SAKAMOTO,M.SHIROUZU,T.SHINDO,S.YOKOYAMA                    
JRNL        TITL   STRUCTURAL BASIS FOR EXTRACELLULAR INTERACTIONS BETWEEN      
JRNL        TITL 2 CALCITONIN RECEPTOR-LIKE RECEPTOR AND RECEPTOR               
JRNL        TITL 3 ACTIVITY-MODIFYING PROTEIN 2 FOR ADRENOMEDULLIN-SPECIFIC     
JRNL        TITL 4 BINDING                                                      
JRNL        REF    PROTEIN SCI.                  V.  21   199 2012              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   22102369                                                     
JRNL        DOI    10.1002/PRO.2003                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.62                          
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)   (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 6075                           
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) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.700                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 662                             
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           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 802                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2400                       
REMARK   3   BIN FREE R VALUE                    : 0.2770                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.30                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 102                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.027                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1462                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 30                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.67400                                             
REMARK   3    B22 (A**2) : -6.67400                                             
REMARK   3    B33 (A**2) : 13.34800                                             
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) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.050 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.309 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.482 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.960 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 38.88                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AQF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029566.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790, 0.9793, 0.9640             
REMARK 200  MONOCHROMATOR                  : SI DOUBLE CRYSTAL                  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6157                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 11.200                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 33.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, 30 % (V/V) PEG MME 550,   
REMARK 280  0.05M CALCIUM CHLORIDE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.69550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       27.71200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.71200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.84775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.71200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       27.71200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       89.54325            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.71200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       27.71200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       29.84775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       27.71200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.71200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       89.54325            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       59.69550            
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: 1860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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     GLY A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     GLN A   135                                                      
REMARK 465     PRO A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     PHE A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     SER B    27                                                      
REMARK 465     PRO B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     ILE B    32                                                      
REMARK 465     GLN B    33                                                      
REMARK 465     LEU B    34                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     LYS B   134                                                      
REMARK 465     VAL B   135                                                      
REMARK 465     LYS B   136                                                      
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   OD1  ASP B    96     OG   SER B    98              2.19            
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    ASP B  70   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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    ASN A  60     -179.21   -170.19                                   
REMARK 500    GLN B  59      -97.55     51.72                                   
REMARK 500    ALA B  60       71.52     32.74                                   
REMARK 500    ALA B  80      158.80    -42.13                                   
REMARK 500    GLN B 107       -9.85    -59.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AQE   RELATED DB: PDB                                   
REMARK 900 RECEPTOR ACTIVITY-MODIFYING PROTEIN 2 EXTRACELLULAR DOMAIN           
DBREF  3AQF A   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
DBREF  3AQF B   23   136  UNP    Q16602   CALRL_HUMAN     23    136             
SEQADV 3AQF GLY A   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF SER A   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF SER A   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF GLY A   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF SER A   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF SER A   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF GLY A   55  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQF GLY B   16  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3AQF SER B   17  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3AQF SER B   18  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3AQF GLY B   19  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3AQF SER B   20  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3AQF SER B   21  UNP  Q16602              EXPRESSION TAG                 
SEQADV 3AQF GLY B   22  UNP  Q16602              EXPRESSION TAG                 
SEQRES   1 A   91  GLY SER SER GLY SER SER GLY GLY THR VAL LYS ASN TYR          
SEQRES   2 A   91  GLU THR ALA VAL GLN PHE CYS TRP ASN HIS TYR LYS ASP          
SEQRES   3 A   91  GLN MSE ASP PRO ILE GLU LYS ASP TRP CYS ASP TRP ALA          
SEQRES   4 A   91  MSE ILE SER ARG PRO TYR SER THR LEU ARG ASP CYS LEU          
SEQRES   5 A   91  GLU HIS PHE ALA GLU LEU PHE ASP LEU GLY PHE PRO ASN          
SEQRES   6 A   91  PRO LEU ALA GLU ARG ILE ILE PHE GLU THR HIS GLN ILE          
SEQRES   7 A   91  HIS PHE ALA ASN CYS SER LEU VAL GLN PRO THR PHE SER          
SEQRES   1 B  121  GLY SER SER GLY SER SER GLY GLU LEU GLU GLU SER PRO          
SEQRES   2 B  121  GLU ASP SER ILE GLN LEU GLY VAL THR ARG ASN LYS ILE          
SEQRES   3 B  121  MSE THR ALA GLN TYR GLU CYS TYR GLN LYS ILE MSE GLN          
SEQRES   4 B  121  ASP PRO ILE GLN GLN ALA GLU GLY VAL TYR CYS ASN ARG          
SEQRES   5 B  121  THR TRP ASP GLY TRP LEU CYS TRP ASN ASP VAL ALA ALA          
SEQRES   6 B  121  GLY THR GLU SER MSE GLN LEU CYS PRO ASP TYR PHE GLN          
SEQRES   7 B  121  ASP PHE ASP PRO SER GLU LYS VAL THR LYS ILE CYS ASP          
SEQRES   8 B  121  GLN ASP GLY ASN TRP PHE ARG HIS PRO ALA SER ASN ARG          
SEQRES   9 B  121  THR TRP THR ASN TYR THR GLN CYS ASN VAL ASN THR HIS          
SEQRES  10 B  121  GLU LYS VAL LYS                                              
MODRES 3AQF MSE A   76  MET  SELENOMETHIONINE                                   
MODRES 3AQF MSE A   88  MET  SELENOMETHIONINE                                   
MODRES 3AQF MSE B   42  MET  SELENOMETHIONINE                                   
MODRES 3AQF MSE B   53  MET  SELENOMETHIONINE                                   
MODRES 3AQF MSE B   85  MET  SELENOMETHIONINE                                   
HET    MSE  A  76       8                                                       
HET    MSE  A  88       8                                                       
HET    MSE  B  42       8                                                       
HET    MSE  B  53       8                                                       
HET    MSE  B  85       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *30(H2 O)                                                     
HELIX    1   1 ASN A   60  ASP A   77  1                                  18    
HELIX    2   2 PRO A   78  TRP A   83  5                                   6    
HELIX    3   3 ASP A   85  PHE A  107  1                                  23    
HELIX    4   4 ASN A  113  HIS A  127  1                                  15    
HELIX    5   5 VAL B   36  ASP B   55  1                                  20    
HELIX    6   6 ASN B  128  HIS B  132  5                                   5    
SHEET    1   A 2 TYR B  64  CYS B  65  0                                        
SHEET    2   A 2 VAL B  78  ALA B  79 -1  O  VAL B  78   N  CYS B  65           
SHEET    1   B 2 THR B  68  TRP B  69  0                                        
SHEET    2   B 2 CYS B  74  TRP B  75 -1  O  TRP B  75   N  THR B  68           
SHEET    1   C 2 THR B  82  LEU B  87  0                                        
SHEET    2   C 2 LYS B 100  CYS B 105 -1  O  VAL B 101   N  GLN B  86           
SSBOND   1 CYS A   68    CYS A   99                          1555   1555  2.02  
SSBOND   2 CYS A   84    CYS A  131                          1555   1555  2.04  
SSBOND   3 CYS B   48    CYS B   74                          1555   1555  2.05  
SSBOND   4 CYS B   65    CYS B  105                          1555   1555  2.03  
SSBOND   5 CYS B   88    CYS B  127                          1555   1555  2.04  
LINK         C   GLN A  75                 N   MSE A  76     1555   1555  1.32  
LINK         C   MSE A  76                 N   ASP A  77     1555   1555  1.33  
LINK         C   ALA A  87                 N   MSE A  88     1555   1555  1.33  
LINK         C   MSE A  88                 N   ILE A  89     1555   1555  1.33  
LINK         C   ILE B  41                 N   MSE B  42     1555   1555  1.33  
LINK         C   MSE B  42                 N   THR B  43     1555   1555  1.32  
LINK         C   ILE B  52                 N   MSE B  53     1555   1555  1.32  
LINK         C   MSE B  53                 N   GLN B  54     1555   1555  1.33  
LINK         C   SER B  84                 N   MSE B  85     1555   1555  1.33  
LINK         C   MSE B  85                 N   GLN B  86     1555   1555  1.33  
CISPEP   1 PHE A  111    PRO A  112          0         0.04                     
CRYST1   55.424   55.424  119.391  90.00  90.00  90.00 P 41 21 2     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      0.018043  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008376        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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