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Database: PDB
Entry: 4OYW
LinkDB: 4OYW
Original site: 4OYW 
HEADER    LYASE                                   13-FEB-14   4OYW              
TITLE     CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLATE CYCLASE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENYLATE CYCLASE TYPE 10;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AH-RELATED PROTEIN, ADENYLATE CYCLASE HOMOLOG, GERM CELL    
COMPND   5 SOLUBLE ADENYLYL CYCLASE, SAC, TESTICULAR SOLUBLE ADENYLYL CYCLASE;  
COMPND   6 EC: 4.6.1.1;                                                         
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: ADCY10, SAC;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ADENYLATE CYCLASE, LYASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.VINKOVIC                                                            
REVDAT   3   27-DEC-23 4OYW    1       SOURCE REMARK CRYST1                     
REVDAT   2   01-OCT-14 4OYW    1       JRNL                                     
REVDAT   1   02-APR-14 4OYW    0                                                
JRNL        AUTH   S.M.SAALAU-BETHELL,V.BERDINI,A.CLEASBY,M.CONGREVE,J.E.COYLE, 
JRNL        AUTH 2 V.LOCK,C.W.MURRAY,M.A.O'BRIEN,S.J.RICH,T.SAMBROOK,           
JRNL        AUTH 3 M.VINKOVIC,J.R.YON,H.JHOTI                                   
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN SOLUBLE ADENYLATE CYCLASE REVEALS 
JRNL        TITL 2 A DISTINCT, HIGHLY FLEXIBLE ALLOSTERIC BICARBONATE BINDING   
JRNL        TITL 3 POCKET.                                                      
JRNL        REF    CHEMMEDCHEM                   V.   9   823 2014              
JRNL        REFN                   ESSN 1860-7187                               
JRNL        PMID   24616449                                                     
JRNL        DOI    10.1002/CMDC.201300480                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 59877                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.184                          
REMARK   3   R VALUE            (WORKING SET)  : 0.182                          
REMARK   3   FREE R VALUE                      : 0.211                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3025                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.70                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.74                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.72                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4448                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2216                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4220                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2205                   
REMARK   3   BIN FREE R VALUE                        : 0.2406                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.13                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 228                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3742                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 420                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.30690                                             
REMARK   3    B22 (A**2) : -0.30690                                             
REMARK   3    B33 (A**2) : 0.61380                                              
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) : 0.222               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.099               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.096               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.097               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.095               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3896   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5276   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1369   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 99     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 576    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3890   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 501    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5179   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.013                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.14                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.17                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.55                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|0 - A|468 }                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   21.8638   25.3748   -2.2701           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0854 T22:   -0.0212                                    
REMARK   3     T33:   -0.0136 T12:    0.0117                                    
REMARK   3     T13:    0.0041 T23:    0.0528                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4195 L22:    0.5369                                    
REMARK   3     L33:    0.5889 L12:   -0.0952                                    
REMARK   3     L13:    0.2401 L23:   -0.1746                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0379 S12:   -0.0274 S13:   -0.0015                     
REMARK   3     S21:    0.0193 S22:    0.1009 S23:    0.1785                     
REMARK   3     S31:   -0.0466 S32:   -0.1788 S33:   -0.0630                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OYW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200282.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97560                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59877                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1UL OF PROTEIN SOLUTION WAS MIXED WITH   
REMARK 280  1UL OF RESERVOIR SOLUTION (0.1M SODIUM ACETATE, PH 4.8, 0.2M        
REMARK 280  TRISODIUM CITRATE, 16-18% PEG4K AND 10% GLYCEROL) AND LEFT TO       
REMARK 280  EQUILIBRATE AT 4C, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       48.69550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       48.69550            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.69550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL                        
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   BIOMT1   2 -0.500000 -0.866025  0.000000       99.42400            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       49.71200            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       86.10371            
REMARK 350   BIOMT3   3  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 734  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1018  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     VAL A   469                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 468    O                                                   
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    HIS A  28       63.89     27.94                                   
REMARK 500    THR A 132       62.26   -107.72                                   
REMARK 500    GLU A 136       22.40     47.11                                   
REMARK 500    GLU A 137      -49.00   -162.16                                   
REMARK 500    ASP A 140       31.47    -76.10                                   
REMARK 500    ASP A 159     -156.09   -127.16                                   
REMARK 500    ASP A 258       95.89   -166.03                                   
REMARK 500    ASP A 305       30.09   -145.78                                   
REMARK 500    LYS A 354      -98.38     12.15                                   
REMARK 500    VAL A 355      117.14     66.66                                   
REMARK 500    LYS A 378       -6.82     82.05                                   
REMARK 500    ASN A 436        0.15     55.03                                   
REMARK 500    ALA A 454      113.45   -163.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 941        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH A 944        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A1018        DISTANCE =  7.57 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OYA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OYZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OZ2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4OZ3   RELATED DB: PDB                                   
DBREF  4OYW A    1   469  UNP    Q96PN6   ADCYA_HUMAN      1    469             
SEQADV 4OYW ACE A    0  UNP  Q96PN6              ACETYLATION                    
SEQRES   1 A  470  ACE MET ASN THR PRO LYS GLU GLU PHE GLN ASP TRP PRO          
SEQRES   2 A  470  ILE VAL ARG ILE ALA ALA HIS LEU PRO ASP LEU ILE VAL          
SEQRES   3 A  470  TYR GLY HIS PHE SER PRO GLU ARG PRO PHE MET ASP TYR          
SEQRES   4 A  470  PHE ASP GLY VAL LEU MET PHE VAL ASP ILE SER GLY PHE          
SEQRES   5 A  470  THR ALA MET THR GLU LYS PHE SER SER ALA MET TYR MET          
SEQRES   6 A  470  ASP ARG GLY ALA GLU GLN LEU VAL GLU ILE LEU ASN TYR          
SEQRES   7 A  470  HIS ILE SER ALA ILE VAL GLU LYS VAL LEU ILE PHE GLY          
SEQRES   8 A  470  GLY ASP ILE LEU LYS PHE ALA GLY ASP ALA LEU LEU ALA          
SEQRES   9 A  470  LEU TRP ARG VAL GLU ARG LYS GLN LEU LYS ASN ILE ILE          
SEQRES  10 A  470  THR VAL VAL ILE LYS CYS SER LEU GLU ILE HIS GLY LEU          
SEQRES  11 A  470  PHE GLU THR GLN GLU TRP GLU GLU GLY LEU ASP ILE ARG          
SEQRES  12 A  470  VAL LYS ILE GLY LEU ALA ALA GLY HIS ILE SER MET LEU          
SEQRES  13 A  470  VAL PHE GLY ASP GLU THR HIS SER HIS PHE LEU VAL ILE          
SEQRES  14 A  470  GLY GLN ALA VAL ASP ASP VAL ARG LEU ALA GLN ASN MET          
SEQRES  15 A  470  ALA GLN MET ASN ASP VAL ILE LEU SER PRO ASN CYS TRP          
SEQRES  16 A  470  GLN LEU CYS ASP ARG SER MET ILE GLU ILE GLU SER VAL          
SEQRES  17 A  470  PRO ASP GLN ARG ALA VAL LYS VAL ASN PHE LEU LYS PRO          
SEQRES  18 A  470  PRO PRO ASN PHE ASN PHE ASP GLU PHE PHE THR LYS CYS          
SEQRES  19 A  470  THR THR PHE MET HIS TYR TYR PRO SER GLY GLU HIS LYS          
SEQRES  20 A  470  ASN LEU LEU ARG LEU ALA CME THR LEU LYS PRO ASP PRO          
SEQRES  21 A  470  GLU LEU GLU MET SER LEU GLN LYS TYR VAL MET GLU SER          
SEQRES  22 A  470  ILE LEU LYS GLN ILE ASP ASN LYS GLN LEU GLN GLY TYR          
SEQRES  23 A  470  LEU SER GLU LEU ARG PRO VAL THR ILE VAL PHE VAL ASN          
SEQRES  24 A  470  LEU MET PHE GLU ASP GLN ASP LYS ALA GLU GLU ILE GLY          
SEQRES  25 A  470  PRO ALA ILE GLN ASP ALA TYR MET HIS ILE THR SER VAL          
SEQRES  26 A  470  LEU LYS ILE PHE GLN GLY GLN ILE ASN LYS VAL PHE MET          
SEQRES  27 A  470  PHE ASP LYS GLY CYS SER PHE LEU CYS VAL PHE GLY PHE          
SEQRES  28 A  470  PRO GLY GLU LYS VAL PRO ASP GLU LEU THR HIS ALA LEU          
SEQRES  29 A  470  GLU CYS ALA MET ASP ILE PHE ASP PHE CYS SER GLN VAL          
SEQRES  30 A  470  HIS LYS ILE GLN THR VAL SER ILE GLY VAL ALA SER GLY          
SEQRES  31 A  470  ILE VAL PHE CYS GLY ILE VAL GLY HIS THR VAL ARG HIS          
SEQRES  32 A  470  GLU TYR THR VAL ILE GLY GLN LYS VAL ASN LEU ALA ALA          
SEQRES  33 A  470  ARG MET MET MET TYR TYR PRO GLY ILE VAL THR CYS ASP          
SEQRES  34 A  470  SER VAL THR TYR ASN GLY SER ASN LEU PRO ALA TYR PHE          
SEQRES  35 A  470  PHE LYS GLU LEU PRO LYS LYS VAL MET LYS GLY VAL ALA          
SEQRES  36 A  470  ASP SER GLY PRO LEU TYR GLN TYR TRP GLY ARG THR GLU          
SEQRES  37 A  470  LYS VAL                                                      
MODRES 4OYW CME A  253  CYS  MODIFIED RESIDUE                                   
HET    ACE  A   0       3                                                       
HET    CME  A 253      10                                                       
HET    GOL  A 501       6                                                       
HET     CL  A 502       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  GOL    C3 H8 O3                                                     
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *420(H2 O)                                                    
HELIX    1 AA1 TRP A   11  ALA A   18  1                                   8    
HELIX    2 AA2 PRO A   21  TYR A   26  1                                   6    
HELIX    3 AA3 ILE A   48  ALA A   53  1                                   6    
HELIX    4 AA4 MET A   54  SER A   59  1                                   6    
HELIX    5 AA5 SER A   60  MET A   64  5                                   5    
HELIX    6 AA6 ARG A   66  PHE A   89  1                                  24    
HELIX    7 AA7 GLU A  108  LYS A  110  5                                   3    
HELIX    8 AA8 GLN A  111  PHE A  130  1                                  20    
HELIX    9 AA9 GLY A  169  ALA A  182  1                                  14    
HELIX   10 AB1 SER A  190  CYS A  197  1                                   8    
HELIX   11 AB2 ASN A  225  THR A  235  1                                  11    
HELIX   12 AB3 SER A  242  LYS A  246  5                                   5    
HELIX   13 AB4 ARG A  250  LEU A  255  5                                   6    
HELIX   14 AB5 ASP A  258  LYS A  267  1                                  10    
HELIX   15 AB6 MET A  270  ASP A  278  1                                   9    
HELIX   16 AB7 LYS A  306  PHE A  328  1                                  23    
HELIX   17 AB8 ASP A  357  SER A  374  1                                  18    
HELIX   18 AB9 GLY A  408  TYR A  421  1                                  14    
HELIX   19 AC1 ASP A  428  ASN A  436  1                                   9    
HELIX   20 AC2 PRO A  438  TYR A  440  5                                   3    
SHEET    1 AA1 5 ASP A  92  PHE A  96  0                                        
SHEET    2 AA1 5 ALA A 100  ARG A 106 -1  O  LEU A 104   N  ASP A  92           
SHEET    3 AA1 5 PHE A  35  ASP A  47 -1  N  VAL A  46   O  LEU A 101           
SHEET    4 AA1 5 LYS A 144  GLY A 158 -1  O  ILE A 152   N  PHE A  39           
SHEET    5 AA1 5 SER A 163  ILE A 168 -1  O  LEU A 166   N  LEU A 155           
SHEET    1 AA2 7 ASP A  92  PHE A  96  0                                        
SHEET    2 AA2 7 ALA A 100  ARG A 106 -1  O  LEU A 104   N  ASP A  92           
SHEET    3 AA2 7 PHE A  35  ASP A  47 -1  N  VAL A  46   O  LEU A 101           
SHEET    4 AA2 7 LYS A 144  GLY A 158 -1  O  ILE A 152   N  PHE A  39           
SHEET    5 AA2 7 VAL A 187  LEU A 189  1  O  ILE A 188   N  LEU A 147           
SHEET    6 AA2 7 VAL A 213  LEU A 218 -1  O  VAL A 213   N  LEU A 189           
SHEET    7 AA2 7 ILE A 202  SER A 206 -1  N  GLU A 205   O  LYS A 214           
SHEET    1 AA3 5 GLN A 331  PHE A 338  0                                        
SHEET    2 AA3 5 GLY A 341  PHE A 348 -1  O  LEU A 345   N  LYS A 334           
SHEET    3 AA3 5 GLU A 288  PHE A 301 -1  N  THR A 293   O  PHE A 348           
SHEET    4 AA3 5 ILE A 379  HIS A 398 -1  O  SER A 383   N  ASN A 298           
SHEET    5 AA3 5 ARG A 401  ILE A 407 -1  O  GLU A 403   N  VAL A 396           
SHEET    1 AA4 7 GLN A 331  PHE A 338  0                                        
SHEET    2 AA4 7 GLY A 341  PHE A 348 -1  O  LEU A 345   N  LYS A 334           
SHEET    3 AA4 7 GLU A 288  PHE A 301 -1  N  THR A 293   O  PHE A 348           
SHEET    4 AA4 7 ILE A 379  HIS A 398 -1  O  SER A 383   N  ASN A 298           
SHEET    5 AA4 7 VAL A 425  CYS A 427  1  O  THR A 426   N  ILE A 384           
SHEET    6 AA4 7 TYR A 460  TYR A 462 -1  O  TYR A 460   N  CYS A 427           
SHEET    7 AA4 7 PHE A 442  GLU A 444 -1  N  LYS A 443   O  GLN A 461           
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.32  
LINK         C   ALA A 252                 N   CME A 253     1555   1555  1.36  
LINK         C   CME A 253                 N   THR A 254     1555   1555  1.33  
CISPEP   1 ARG A   33    PRO A   34          0         3.07                     
CISPEP   2 ALA A  454    ASP A  455          0        -7.17                     
SITE     1 AC1  6 THR A 322  LEU A 325  LYS A 326  GLY A 330                    
SITE     2 AC1  6 HOH A 818  HOH A1007                                          
SITE     1 AC2  3 LYS A  95  VAL A 167  HOH A 863                               
CRYST1   99.424   99.424   97.391  90.00  90.00 120.00 P 63          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010058  0.005807  0.000000        0.00000                         
SCALE2      0.000000  0.011614  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010268        0.00000                         
HETATM    1  C   ACE A   0      63.198  12.741  24.855  1.00 27.70           C  
ANISOU    1  C   ACE A   0     3733   3317   3475    347   -882     53       C  
HETATM    2  O   ACE A   0      63.810  13.735  24.468  1.00 27.19           O  
ANISOU    2  O   ACE A   0     3629   3266   3435    319   -902     42       O  
HETATM    3  CH3 ACE A   0      63.336  12.223  26.330  1.00 29.72           C  
ANISOU    3  CH3 ACE A   0     4054   3551   3686    372   -932     65       C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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