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Database: PDB
Entry: 1QY0
LinkDB: 1QY0
Original site: 1QY0 
HEADER    TRANSPORT PROTEIN                       09-SEP-03   1QY0              
TITLE     THERMODYNAMICS OF BINDING OF 2-METHOXY-3-ISOPROPYLPYRAZINE AND 2-     
TITLE    2 METHOXY-3-ISOBUTYLPYRAZINE TO THE MAJOR URINARY PROTEIN              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAJOR URINARY PROTEIN;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 STRAIN: SWISS;                                                       
SOURCE   6 GENE: MUP1;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SG13009;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    LIPOCALIN, BETA-BARREL, TRANSPORT PROTEIN                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.J.BINGHAM,J.B.C.FINDLAY,S.-Y.HSIEH,A.P.KALVERDA,A.KJELLBERG,        
AUTHOR   2 C.PERAZZOLO,S.E.V.PHILLIPS,K.SESHADRI,C.H.TRINH,W.B.TURNBULL,        
AUTHOR   3 G.BODENHAUSEN,S.W.HOMANS                                             
REVDAT   5   23-AUG-23 1QY0    1       REMARK SEQADV LINK                       
REVDAT   4   16-NOV-11 1QY0    1       HETATM                                   
REVDAT   3   13-JUL-11 1QY0    1       VERSN                                    
REVDAT   2   24-FEB-09 1QY0    1       VERSN                                    
REVDAT   1   24-FEB-04 1QY0    0                                                
JRNL        AUTH   R.J.BINGHAM,J.B.C.FINDLAY,S.-Y.HSIEH,A.P.KALVERDA,           
JRNL        AUTH 2 A.KJELLBERG,C.PERAZZOLO,S.E.V.PHILLIPS,K.SESHADRI,C.H.TRINH, 
JRNL        AUTH 3 W.B.TURNBULL,G.BODENHAUSEN,S.W.HOMANS                        
JRNL        TITL   THERMODYNAMICS OF BINDING OF 2-METHOXY-3-ISOPROPYLPYRAZINE   
JRNL        TITL 2 AND 2-METHOXY-3-ISOBUTYLPYRAZINE TO THE MAJOR URINARY        
JRNL        TITL 3 PROTEIN.                                                     
JRNL        REF    J.AM.CHEM.SOC.                V. 126  1675 2004              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   14871097                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
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)   (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 18006                          
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) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 921                             
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 97                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1272                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 208                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.19                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.80000                                             
REMARK   3    B22 (A**2) : -3.80000                                             
REMARK   3    B33 (A**2) : 7.60000                                              
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) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
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) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.760                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.060                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
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 1QY0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020206.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.49                               
REMARK 200  MONOCHROMATOR                  : LIQUID GALLIUM COOLED, BENT,       
REMARK 200                                   TRIANGULAR, SI 111                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18006                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1I06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CADMIUM CHLORIDE, MALATE/HCL, PH 4.9,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
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       68.50400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       26.81350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       26.81350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      102.75600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       26.81350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       26.81350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       34.25200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       26.81350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.81350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      102.75600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       26.81350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.81350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       34.25200            
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       68.50400            
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: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 611  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 612  LIES ON A SPECIAL POSITION.                          
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     MET A   -11                                                      
REMARK 465     ARG A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     GLN A   159                                                      
REMARK 465     ALA A   160                                                      
REMARK 465     ARG A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  74     -168.04   -105.13                                   
REMARK 500    TYR A  84      116.12   -166.18                                   
REMARK 500    TYR A  97      -43.17     67.19                                   
REMARK 500    ASN A  99      -54.78   -125.46                                   
REMARK 500    ALA A 154       18.02   -155.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 201  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  13   OE2                                                    
REMARK 620 2 GLU A  13   OE1  55.0                                              
REMARK 620 3 ASP A 110   OD2  82.3 118.3                                        
REMARK 620 4 HOH A 438   O   115.4  84.3  76.1                                  
REMARK 620 5 HOH A 494   O   132.9  84.8 143.5  78.9                            
REMARK 620 6 HOH A 517   O   154.8 142.4  95.1  87.9  57.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A 200  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  18   OE2                                                    
REMARK 620 2 GLU A  18   OE1  54.7                                              
REMARK 620 3 GLU A 139   OE1 164.0 140.3                                        
REMARK 620 4 GLU A 139   OE2 141.8  87.2  53.2                                  
REMARK 620 5 HOH A 423   O    92.1  89.0  83.7  83.6                            
REMARK 620 6 HOH A 516   O    82.2 136.9  82.5 135.8  92.0                      
REMARK 620 7 HOH A 542   O    91.4  80.7  96.7  84.2 164.4 103.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 202  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  30   OE1                                                    
REMARK 620 2 GLU A  30   OE2  46.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 204  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 125   OD2                                                    
REMARK 620 2 HOH A 463   O   104.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 203  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 140   OE2                                                    
REMARK 620 2 HOH A 459   O   106.0                                              
REMARK 620 3 HOH A 512   O   151.9  89.6                                        
REMARK 620 4 HOH A 555   O    86.3  74.8 120.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QY1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QY2   RELATED DB: PDB                                   
DBREF  1QY0 A    1   162  UNP    P11588   MUP1_MOUSE      19    180             
SEQADV 1QY0 MET A  -11  UNP  P11588              CLONING ARTIFACT               
SEQADV 1QY0 ARG A  -10  UNP  P11588              CLONING ARTIFACT               
SEQADV 1QY0 GLY A   -9  UNP  P11588              CLONING ARTIFACT               
SEQADV 1QY0 SER A    4  UNP  P11588              CLONING ARTIFACT               
SEQADV 1QY0 HIS A   -7  UNP  P11588              EXPRESSION TAG                 
SEQADV 1QY0 HIS A   -6  UNP  P11588              EXPRESSION TAG                 
SEQADV 1QY0 HIS A   -5  UNP  P11588              EXPRESSION TAG                 
SEQADV 1QY0 HIS A   -4  UNP  P11588              EXPRESSION TAG                 
SEQADV 1QY0 HIS A   -3  UNP  P11588              EXPRESSION TAG                 
SEQADV 1QY0 HIS A   -2  UNP  P11588              EXPRESSION TAG                 
SEQADV 1QY0 GLY A   -1  UNP  P11588              CLONING ARTIFACT               
SEQADV 1QY0 SER A    0  UNP  P11588              CLONING ARTIFACT               
SEQRES   1 A  174  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU          
SEQRES   2 A  174  GLU ALA SER SER THR GLY ARG ASN PHE ASN VAL GLU LYS          
SEQRES   3 A  174  ILE ASN GLY GLU TRP HIS THR ILE ILE LEU ALA SER ASP          
SEQRES   4 A  174  LYS ARG GLU LYS ILE GLU ASP ASN GLY ASN PHE ARG LEU          
SEQRES   5 A  174  PHE LEU GLU GLN ILE HIS VAL LEU GLU LYS SER LEU VAL          
SEQRES   6 A  174  LEU LYS PHE HIS THR VAL ARG ASP GLU GLU CYS SER GLU          
SEQRES   7 A  174  LEU SER MET VAL ALA ASP LYS THR GLU LYS ALA GLY GLU          
SEQRES   8 A  174  TYR SER VAL THR TYR ASP GLY PHE ASN THR PHE THR ILE          
SEQRES   9 A  174  PRO LYS THR ASP TYR ASP ASN PHE LEU MET ALA HIS LEU          
SEQRES  10 A  174  ILE ASN GLU LYS ASP GLY GLU THR PHE GLN LEU MET GLY          
SEQRES  11 A  174  LEU TYR GLY ARG GLU PRO ASP LEU SER SER ASP ILE LYS          
SEQRES  12 A  174  GLU ARG PHE ALA GLN LEU CYS GLU GLU HIS GLY ILE LEU          
SEQRES  13 A  174  ARG GLU ASN ILE ILE ASP LEU SER ASN ALA ASN ARG CYS          
SEQRES  14 A  174  LEU GLN ALA ARG GLU                                          
HET     CD  A 200       1                                                       
HET     CD  A 201       1                                                       
HET     NA  A 202       1                                                       
HET     NA  A 203       1                                                       
HET     NA  A 204       1                                                       
HET    GOL  A 300       6                                                       
HETNAM      CD CADMIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   CD    2(CD 2+)                                                     
FORMUL   4   NA    3(NA 1+)                                                     
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *208(H2 O)                                                    
HELIX    1   1 ASN A   11  ASN A   16  5                                   6    
HELIX    2   2 LYS A   28  GLU A   33  5                                   6    
HELIX    3   3 SER A  127  GLU A  140  1                                  14    
HELIX    4   4 LEU A  144  GLU A  146  5                                   3    
SHEET    1   A10 GLY A  17  GLU A  18  0                                        
SHEET    2   A10 PHE A  41  VAL A  47 -1  O  ILE A  45   N  GLY A  17           
SHEET    3   A10 SER A  51  ARG A  60 -1  O  VAL A  53   N  HIS A  46           
SHEET    4   A10 GLU A  63  LYS A  73 -1  O  LEU A  67   N  PHE A  56           
SHEET    5   A10 TYR A  80  THR A  83 -1  O  SER A  81   N  ASP A  72           
SHEET    6   A10 PHE A  87  THR A  95 -1  O  PHE A  90   N  TYR A  80           
SHEET    7   A10 PHE A 100  LYS A 109 -1  O  GLU A 108   N  PHE A  87           
SHEET    8   A10 GLU A 112  GLY A 121 -1  O  LEU A 116   N  LEU A 105           
SHEET    9   A10 HIS A  20  SER A  26 -1  N  ALA A  25   O  MET A 117           
SHEET   10   A10 ILE A 148  ASP A 150 -1  O  ILE A 149   N  LEU A  24           
SSBOND   1 CYS A   64    CYS A  157                          1555   1555  2.05  
LINK         OE2 GLU A  13                CD    CD A 201     1555   1555  2.50  
LINK         OE1 GLU A  13                CD    CD A 201     1555   1555  2.34  
LINK         OE2 GLU A  18                CD    CD A 200     5645   1555  2.30  
LINK         OE1 GLU A  18                CD    CD A 200     5645   1555  2.52  
LINK         OE1 GLU A  30                NA    NA A 202     1555   1555  2.53  
LINK         OE2 GLU A  30                NA    NA A 202     1555   1555  2.95  
LINK         OD2 ASP A 110                CD    CD A 201     8675   1555  2.33  
LINK         OD2 ASP A 125                NA    NA A 204     1555   1555  2.52  
LINK         OE1 GLU A 139                CD    CD A 200     1555   1555  2.30  
LINK         OE2 GLU A 139                CD    CD A 200     1555   1555  2.52  
LINK         OE2 GLU A 140                NA    NA A 203     1555   1555  2.59  
LINK        CD    CD A 200                 O   HOH A 423     1555   5645  2.38  
LINK        CD    CD A 200                 O   HOH A 516     1555   1555  2.37  
LINK        CD    CD A 200                 O   HOH A 542     1555   1555  2.44  
LINK        CD    CD A 201                 O   HOH A 438     1555   8675  2.33  
LINK        CD    CD A 201                 O   HOH A 494     1555   8675  3.08  
LINK        CD    CD A 201                 O   HOH A 517     1555   8675  2.44  
LINK        NA    NA A 203                 O   HOH A 459     1555   1555  2.53  
LINK        NA    NA A 203                 O   HOH A 512     1555   1555  2.41  
LINK        NA    NA A 203                 O   HOH A 555     1555   1555  2.37  
LINK        NA    NA A 204                 O   HOH A 463     1555   1555  2.80  
SITE     1 AC1  5 GLU A  18  GLU A 139  HOH A 423  HOH A 516                    
SITE     2 AC1  5 HOH A 542                                                     
SITE     1 AC2  5 GLU A  13  ASP A 110  HOH A 438  HOH A 494                    
SITE     2 AC2  5 HOH A 517                                                     
SITE     1 AC3  2 GLU A  30  GLU A  49                                          
SITE     1 AC4  5 LYS A  76  GLU A 140  HOH A 459  HOH A 512                    
SITE     2 AC4  5 HOH A 555                                                     
SITE     1 AC5  5 LYS A 109  ASP A 110  ASP A 125  HOH A 463                    
SITE     2 AC5  5 HOH A 517                                                     
SITE     1 AC6  3 ALA A 103  LEU A 105  TYR A 120                               
CRYST1   53.627   53.627  137.008  90.00  90.00  90.00 P 43 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      0.018647  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018647  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007299        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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