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Database: PDB
Entry: 3AQE
LinkDB: 3AQE
Original site: 3AQE 
HEADER    TRANSPORT PROTEIN                       29-OCT-10   3AQE              
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF HUMAN RAMP2          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR ACTIVITY-MODIFYING PROTEIN 2;                     
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 56-139;                 
COMPND   5 SYNONYM: CALCITONIN-RECEPTOR-LIKE RECEPTOR ACTIVITY-MODIFYING PROTEIN
COMPND   6 2, CRLR ACTIVITY-MODIFYING PROTEIN 2;                                
COMPND   7 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                               
KEYWDS    TRANSMEMBRANE, GPCR, ADRENOMEDULLIN, TRAFFICKING, CLR, CGRP,          
KEYWDS   2 ENDOPLASMIC RETICULUM, DISEASE, NEOVASCULARIZATION, HELIX BUNDLE,    
KEYWDS   3 CALCITONIN RECEPTOR-LIKE RECEPTOR (CRLR), ENDOPLASMIC RETICULUM      
KEYWDS   4 (ER), CELL MEMBRANE, TRANSPORT PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KUSANO,M.KUKIMOTO-NIINO,M.SHIROUZU,T.SHINDO,S.YOKOYAMA              
REVDAT   2   25-JUL-12 3AQE    1       JRNL                                     
REVDAT   1   09-NOV-11 3AQE    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.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.41                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33465                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1696                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.4142 -  4.5685    0.98     2796   175  0.2240 0.2454        
REMARK   3     2  4.5685 -  3.6272    0.99     2759   134  0.1861 0.2335        
REMARK   3     3  3.6272 -  3.1690    0.99     2699   149  0.2102 0.2394        
REMARK   3     4  3.1690 -  2.8794    1.00     2706   136  0.2345 0.2832        
REMARK   3     5  2.8794 -  2.6731    1.00     2712   138  0.2335 0.2698        
REMARK   3     6  2.6731 -  2.5155    1.00     2685   150  0.2342 0.3010        
REMARK   3     7  2.5155 -  2.3896    1.00     2658   133  0.2303 0.2973        
REMARK   3     8  2.3896 -  2.2856    0.96     2574   138  0.2552 0.3434        
REMARK   3     9  2.2856 -  2.1976    0.86     2284   141  0.3522 0.3987        
REMARK   3    10  2.1976 -  2.1218    0.98     2632   143  0.2658 0.3253        
REMARK   3    11  2.1218 -  2.0554    1.00     2676   126  0.2530 0.3176        
REMARK   3    12  2.0554 -  1.9967    0.98     2588   133  0.2344 0.2623        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 35.94                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.91880                                             
REMARK   3    B22 (A**2) : 10.52640                                             
REMARK   3    B33 (A**2) : -2.60760                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           3959                                  
REMARK   3   ANGLE     :  0.942           5375                                  
REMARK   3   CHIRALITY :  0.071            537                                  
REMARK   3   PLANARITY :  0.004            705                                  
REMARK   3   DIHEDRAL  : 15.924           1397                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AQE 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 RCSB029565.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
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) : 0.9788, 0.9792, 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   : 33866                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.620                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.3000                            
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     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.24000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.700                              
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   (%): 36.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM-HEPES, 25% (V/V) PEG 400,    
REMARK 280  0.2M CALCIUM CHLORIDE DI-HYDRATE, 0.15% AGAROSE , PH 7.2, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       29.78550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.99900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.86450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.99900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.78550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.86450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
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     GLY A    56                                                      
REMARK 465     THR A    57                                                      
REMARK 465     VAL A    58                                                      
REMARK 465     LYS A    59                                                      
REMARK 465     PRO A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     PHE A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     GLY B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     SER B    53                                                      
REMARK 465     SER B    54                                                      
REMARK 465     GLY B    55                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     THR B    57                                                      
REMARK 465     VAL B    58                                                      
REMARK 465     LYS B    59                                                      
REMARK 465     PRO B   136                                                      
REMARK 465     THR B   137                                                      
REMARK 465     PHE B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     GLY C    49                                                      
REMARK 465     SER C    50                                                      
REMARK 465     SER C    51                                                      
REMARK 465     GLY C    52                                                      
REMARK 465     SER C    53                                                      
REMARK 465     SER C    54                                                      
REMARK 465     GLY C    55                                                      
REMARK 465     GLY C    56                                                      
REMARK 465     THR C    57                                                      
REMARK 465     VAL C    58                                                      
REMARK 465     LYS C    59                                                      
REMARK 465     LEU C   133                                                      
REMARK 465     VAL C   134                                                      
REMARK 465     GLN C   135                                                      
REMARK 465     PRO C   136                                                      
REMARK 465     THR C   137                                                      
REMARK 465     PHE C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     GLY D    49                                                      
REMARK 465     SER D    50                                                      
REMARK 465     SER D    51                                                      
REMARK 465     GLY D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     SER D    54                                                      
REMARK 465     GLY D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     THR D    57                                                      
REMARK 465     VAL D    58                                                      
REMARK 465     LYS D    59                                                      
REMARK 465     VAL D   134                                                      
REMARK 465     GLN D   135                                                      
REMARK 465     PRO D   136                                                      
REMARK 465     THR D   137                                                      
REMARK 465     PHE D   138                                                      
REMARK 465     SER D   139                                                      
REMARK 465     GLY E    49                                                      
REMARK 465     SER E    50                                                      
REMARK 465     SER E    51                                                      
REMARK 465     GLY E    52                                                      
REMARK 465     SER E    53                                                      
REMARK 465     SER E    54                                                      
REMARK 465     GLY E    55                                                      
REMARK 465     GLY E    56                                                      
REMARK 465     THR E    57                                                      
REMARK 465     VAL E    58                                                      
REMARK 465     LYS E    59                                                      
REMARK 465     PRO E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     PHE E   138                                                      
REMARK 465     SER E   139                                                      
REMARK 465     GLY F    49                                                      
REMARK 465     SER F    50                                                      
REMARK 465     SER F    51                                                      
REMARK 465     GLY F    52                                                      
REMARK 465     SER F    53                                                      
REMARK 465     SER F    54                                                      
REMARK 465     GLY F    55                                                      
REMARK 465     GLY F    56                                                      
REMARK 465     THR F    57                                                      
REMARK 465     VAL F    58                                                      
REMARK 465     LYS F    59                                                      
REMARK 465     GLN F   135                                                      
REMARK 465     PRO F   136                                                      
REMARK 465     THR F   137                                                      
REMARK 465     PHE F   138                                                      
REMARK 465     SER F   139                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   200     O    HOH B   252              1.86            
REMARK 500   O    HOH F   185     O    HOH F   244              1.87            
REMARK 500   O    HOH C   145     O    HOH D   220              1.89            
REMARK 500   OD1  ASP A    82     O    HOH A   237              1.97            
REMARK 500   O    HOH D    46     O    HOH D   153              1.99            
REMARK 500   OE1  GLU C   101     O    HOH C   233              1.99            
REMARK 500   OE2  GLU F   105     O    HOH F   166              2.01            
REMARK 500   O    HOH A   182     O    HOH C    44              2.04            
REMARK 500   OD1  ASP D    85     O    HOH D   242              2.06            
REMARK 500   OD1  ASP A    74     O    HOH A   273              2.07            
REMARK 500   O    HOH F   151     O    HOH F   230              2.08            
REMARK 500   OG1  THR E    95     O    HOH E   143              2.10            
REMARK 500   O    HOH F     1     O    HOH F   166              2.14            
REMARK 500   O    HOH A   229     O    HOH A   232              2.15            
REMARK 500   OE2  GLU F   105     O    HOH F     1              2.15            
REMARK 500   OD1  ASP D    82     O    HOH D   281              2.17            
REMARK 500   OE2  GLU A   105     O    HOH A   154              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   149     O    HOH E   161     1455     2.11            
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    ILE C  79       36.26    -98.91                                   
REMARK 500    ILE F  79       40.03   -106.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AQF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CRLR/RAMP2 EXTRACELLULAR              
REMARK 900 COMPLEX                                                              
DBREF  3AQE A   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
DBREF  3AQE B   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
DBREF  3AQE C   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
DBREF  3AQE D   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
DBREF  3AQE E   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
DBREF  3AQE F   56   139  UNP    O60895   RAMP2_HUMAN     56    139             
SEQADV 3AQE GLY A   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER A   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER A   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY A   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER A   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER A   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY A   55  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY B   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER B   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER B   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY B   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER B   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER B   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY B   55  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY C   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER C   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER C   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY C   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER C   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER C   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY C   55  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY D   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER D   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER D   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY D   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER D   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER D   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY D   55  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY E   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER E   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER E   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY E   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER E   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER E   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY E   55  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY F   49  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER F   50  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER F   51  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY F   52  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER F   53  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE SER F   54  UNP  O60895              EXPRESSION TAG                 
SEQADV 3AQE GLY F   55  UNP  O60895              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   91  GLY SER SER GLY SER SER GLY GLY THR VAL LYS ASN TYR          
SEQRES   2 B   91  GLU THR ALA VAL GLN PHE CYS TRP ASN HIS TYR LYS ASP          
SEQRES   3 B   91  GLN MSE ASP PRO ILE GLU LYS ASP TRP CYS ASP TRP ALA          
SEQRES   4 B   91  MSE ILE SER ARG PRO TYR SER THR LEU ARG ASP CYS LEU          
SEQRES   5 B   91  GLU HIS PHE ALA GLU LEU PHE ASP LEU GLY PHE PRO ASN          
SEQRES   6 B   91  PRO LEU ALA GLU ARG ILE ILE PHE GLU THR HIS GLN ILE          
SEQRES   7 B   91  HIS PHE ALA ASN CYS SER LEU VAL GLN PRO THR PHE SER          
SEQRES   1 C   91  GLY SER SER GLY SER SER GLY GLY THR VAL LYS ASN TYR          
SEQRES   2 C   91  GLU THR ALA VAL GLN PHE CYS TRP ASN HIS TYR LYS ASP          
SEQRES   3 C   91  GLN MSE ASP PRO ILE GLU LYS ASP TRP CYS ASP TRP ALA          
SEQRES   4 C   91  MSE ILE SER ARG PRO TYR SER THR LEU ARG ASP CYS LEU          
SEQRES   5 C   91  GLU HIS PHE ALA GLU LEU PHE ASP LEU GLY PHE PRO ASN          
SEQRES   6 C   91  PRO LEU ALA GLU ARG ILE ILE PHE GLU THR HIS GLN ILE          
SEQRES   7 C   91  HIS PHE ALA ASN CYS SER LEU VAL GLN PRO THR PHE SER          
SEQRES   1 D   91  GLY SER SER GLY SER SER GLY GLY THR VAL LYS ASN TYR          
SEQRES   2 D   91  GLU THR ALA VAL GLN PHE CYS TRP ASN HIS TYR LYS ASP          
SEQRES   3 D   91  GLN MSE ASP PRO ILE GLU LYS ASP TRP CYS ASP TRP ALA          
SEQRES   4 D   91  MSE ILE SER ARG PRO TYR SER THR LEU ARG ASP CYS LEU          
SEQRES   5 D   91  GLU HIS PHE ALA GLU LEU PHE ASP LEU GLY PHE PRO ASN          
SEQRES   6 D   91  PRO LEU ALA GLU ARG ILE ILE PHE GLU THR HIS GLN ILE          
SEQRES   7 D   91  HIS PHE ALA ASN CYS SER LEU VAL GLN PRO THR PHE SER          
SEQRES   1 E   91  GLY SER SER GLY SER SER GLY GLY THR VAL LYS ASN TYR          
SEQRES   2 E   91  GLU THR ALA VAL GLN PHE CYS TRP ASN HIS TYR LYS ASP          
SEQRES   3 E   91  GLN MSE ASP PRO ILE GLU LYS ASP TRP CYS ASP TRP ALA          
SEQRES   4 E   91  MSE ILE SER ARG PRO TYR SER THR LEU ARG ASP CYS LEU          
SEQRES   5 E   91  GLU HIS PHE ALA GLU LEU PHE ASP LEU GLY PHE PRO ASN          
SEQRES   6 E   91  PRO LEU ALA GLU ARG ILE ILE PHE GLU THR HIS GLN ILE          
SEQRES   7 E   91  HIS PHE ALA ASN CYS SER LEU VAL GLN PRO THR PHE SER          
SEQRES   1 F   91  GLY SER SER GLY SER SER GLY GLY THR VAL LYS ASN TYR          
SEQRES   2 F   91  GLU THR ALA VAL GLN PHE CYS TRP ASN HIS TYR LYS ASP          
SEQRES   3 F   91  GLN MSE ASP PRO ILE GLU LYS ASP TRP CYS ASP TRP ALA          
SEQRES   4 F   91  MSE ILE SER ARG PRO TYR SER THR LEU ARG ASP CYS LEU          
SEQRES   5 F   91  GLU HIS PHE ALA GLU LEU PHE ASP LEU GLY PHE PRO ASN          
SEQRES   6 F   91  PRO LEU ALA GLU ARG ILE ILE PHE GLU THR HIS GLN ILE          
SEQRES   7 F   91  HIS PHE ALA ASN CYS SER LEU VAL GLN PRO THR PHE SER          
MODRES 3AQE MSE A   76  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE A   88  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE B   76  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE B   88  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE C   76  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE C   88  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE D   76  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE D   88  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE E   76  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE E   88  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE F   76  MET  SELENOMETHIONINE                                   
MODRES 3AQE MSE F   88  MET  SELENOMETHIONINE                                   
HET    MSE  A  76       8                                                       
HET    MSE  A  88       8                                                       
HET    MSE  B  76       8                                                       
HET    MSE  B  88       8                                                       
HET    MSE  C  76       8                                                       
HET    MSE  C  88       8                                                       
HET    MSE  D  76       8                                                       
HET    MSE  D  88       8                                                       
HET    MSE  E  76       8                                                       
HET    MSE  E  88       8                                                       
HET    MSE  F  76       8                                                       
HET    MSE  F  88       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   7  HOH   *282(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 TYR B   61  ASP B   77  1                                  17    
HELIX    6   6 PRO B   78  TRP B   83  5                                   6    
HELIX    7   7 ILE B   89  PHE B  107  1                                  19    
HELIX    8   8 ASN B  113  HIS B  127  1                                  15    
HELIX    9   9 TYR C   61  ASP C   77  1                                  17    
HELIX   10  10 PRO C   78  TRP C   83  5                                   6    
HELIX   11  11 ASP C   85  PHE C  107  1                                  23    
HELIX   12  12 ASN C  113  HIS C  127  1                                  15    
HELIX   13  13 TYR D   61  ASP D   77  1                                  17    
HELIX   14  14 PRO D   78  TRP D   83  5                                   6    
HELIX   15  15 ASP D   85  PHE D  107  1                                  23    
HELIX   16  16 ASN D  113  PHE D  128  1                                  16    
HELIX   17  17 TYR E   61  ASP E   77  1                                  17    
HELIX   18  18 PRO E   78  TRP E   83  5                                   6    
HELIX   19  19 ASP E   85  PHE E  107  1                                  23    
HELIX   20  20 ASN E  113  HIS E  127  1                                  15    
HELIX   21  21 TYR F   61  ASP F   77  1                                  17    
HELIX   22  22 PRO F   78  TRP F   83  5                                   6    
HELIX   23  23 ASP F   85  PHE F  107  1                                  23    
HELIX   24  24 ASN F  113  HIS F  127  1                                  15    
SSBOND   1 CYS A   68    CYS A   99                          1555   1555  2.03  
SSBOND   2 CYS A   84    CYS A  131                          1555   1555  2.03  
SSBOND   3 CYS B   68    CYS B   99                          1555   1555  2.03  
SSBOND   4 CYS B   84    CYS B  131                          1555   1555  2.03  
SSBOND   5 CYS C   68    CYS C   99                          1555   1555  2.03  
SSBOND   6 CYS C   84    CYS C  131                          1555   1555  2.03  
SSBOND   7 CYS D   68    CYS D   99                          1555   1555  2.03  
SSBOND   8 CYS D   84    CYS D  131                          1555   1555  2.03  
SSBOND   9 CYS E   68    CYS E   99                          1555   1555  2.03  
SSBOND  10 CYS E   84    CYS E  131                          1555   1555  2.03  
SSBOND  11 CYS F   68    CYS F   99                          1555   1555  2.03  
SSBOND  12 CYS F   84    CYS F  131                          1555   1555  2.03  
LINK         C   GLN A  75                 N   MSE A  76     1555   1555  1.33  
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   GLN B  75                 N   MSE B  76     1555   1555  1.33  
LINK         C   MSE B  76                 N   ASP B  77     1555   1555  1.33  
LINK         C   ALA B  87                 N   MSE B  88     1555   1555  1.33  
LINK         C   MSE B  88                 N   ILE B  89     1555   1555  1.33  
LINK         C   GLN C  75                 N   MSE C  76     1555   1555  1.33  
LINK         C   MSE C  76                 N   ASP C  77     1555   1555  1.33  
LINK         C   ALA C  87                 N   MSE C  88     1555   1555  1.33  
LINK         C   MSE C  88                 N   ILE C  89     1555   1555  1.33  
LINK         C   GLN D  75                 N   MSE D  76     1555   1555  1.33  
LINK         C   MSE D  76                 N   ASP D  77     1555   1555  1.33  
LINK         C   ALA D  87                 N   MSE D  88     1555   1555  1.33  
LINK         C   MSE D  88                 N   ILE D  89     1555   1555  1.33  
LINK         C   GLN E  75                 N   MSE E  76     1555   1555  1.33  
LINK         C   MSE E  76                 N   ASP E  77     1555   1555  1.33  
LINK         C   ALA E  87                 N   MSE E  88     1555   1555  1.33  
LINK         C   MSE E  88                 N   ILE E  89     1555   1555  1.33  
LINK         C   GLN F  75                 N   MSE F  76     1555   1555  1.33  
LINK         C   MSE F  76                 N   ASP F  77     1555   1555  1.33  
LINK         C   ALA F  87                 N   MSE F  88     1555   1555  1.33  
LINK         C   MSE F  88                 N   ILE F  89     1555   1555  1.33  
CISPEP   1 PHE A  111    PRO A  112          0         3.24                     
CISPEP   2 PHE B  111    PRO B  112          0        -0.41                     
CISPEP   3 PHE C  111    PRO C  112          0         2.65                     
CISPEP   4 PHE D  111    PRO D  112          0         2.43                     
CISPEP   5 PHE E  111    PRO E  112          0        -1.65                     
CISPEP   6 PHE F  111    PRO F  112          0         2.19                     
CRYST1   59.571   89.729   91.998  90.00  90.00  90.00 P 21 21 21   24          
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      0.016787  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011145  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010870        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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