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Database: PDB
Entry: 6RQQ
LinkDB: 6RQQ
Original site: 6RQQ 
HEADER    PROTON TRANSPORT                        16-MAY-19   6RQQ              
TITLE     X-RAY CRYSTAL STRUCTURE OF PROTIATED (H) LARGE MONOCLINIC UNIT CELL CA
TITLE    2 IX SV.                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 9;                                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE IX,CARBONIC ANHYDRASE IX,CAIX,MEMBRANE
COMPND   5 ANTIGEN MN,P54/58N,RENAL CELL CARCINOMA-ASSOCIATED ANTIGEN G250,RCC- 
COMPND   6 ASSOCIATED ANTIGEN G250,PMW1;                                        
COMPND   7 EC: 4.2.1.1;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CA9, G250, MN;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    CARBONIC ANHYDRASE, CA IX, SURFACE VARIANT, PROTON TRANSPORT          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.FISHER,K.KORUZA                                                     
REVDAT   2   16-OCT-19 6RQQ    1       JRNL                                     
REVDAT   1   11-SEP-19 6RQQ    0                                                
JRNL        AUTH   K.KORUZA,B.LAFUMAT,M.NYBLOM,B.P.MAHON,W.KNECHT,R.MCKENNA,    
JRNL        AUTH 2 S.Z.FISHER                                                   
JRNL        TITL   STRUCTURAL COMPARISON OF PROTIATED, H/D-EXCHANGED AND        
JRNL        TITL 2 DEUTERATED HUMAN CARBONIC ANHYDRASE IX.                      
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  75   895 2019              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   31588921                                                     
JRNL        DOI    10.1107/S2059798319010027                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.28 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.12_2829                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.28                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 122062                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6050                            
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 48.9151 -  3.9641    0.96     3912   181  0.1685 0.1644        
REMARK   3     2  3.9641 -  3.1466    0.99     3937   216  0.1526 0.1662        
REMARK   3     3  3.1466 -  2.7489    1.00     3967   185  0.1766 0.2000        
REMARK   3     4  2.7489 -  2.4975    0.99     3907   235  0.1842 0.1883        
REMARK   3     5  2.4975 -  2.3185    1.00     3900   216  0.1765 0.2300        
REMARK   3     6  2.3185 -  2.1818    1.00     3957   196  0.1752 0.1887        
REMARK   3     7  2.1818 -  2.0726    1.00     3982   161  0.1711 0.1955        
REMARK   3     8  2.0726 -  1.9823    0.99     3913   173  0.1612 0.1708        
REMARK   3     9  1.9823 -  1.9060    0.98     3866   215  0.1718 0.1644        
REMARK   3    10  1.9060 -  1.8403    0.99     3917   201  0.1743 0.1911        
REMARK   3    11  1.8403 -  1.7827    0.99     3846   218  0.1824 0.2064        
REMARK   3    12  1.7827 -  1.7317    0.99     3871   185  0.1718 0.1881        
REMARK   3    13  1.7317 -  1.6862    0.99     3909   222  0.1737 0.1968        
REMARK   3    14  1.6862 -  1.6450    0.99     3908   196  0.1804 0.2130        
REMARK   3    15  1.6450 -  1.6076    0.99     3849   212  0.1817 0.2145        
REMARK   3    16  1.6076 -  1.5734    0.99     3825   232  0.1965 0.2062        
REMARK   3    17  1.5734 -  1.5419    0.99     3932   168  0.2001 0.2058        
REMARK   3    18  1.5419 -  1.5128    0.99     3884   196  0.1994 0.2094        
REMARK   3    19  1.5128 -  1.4858    0.98     3874   182  0.2088 0.2066        
REMARK   3    20  1.4858 -  1.4606    0.98     3857   218  0.2149 0.2380        
REMARK   3    21  1.4606 -  1.4371    0.98     3811   214  0.2205 0.2292        
REMARK   3    22  1.4371 -  1.4149    0.98     3835   202  0.2229 0.2409        
REMARK   3    23  1.4149 -  1.3941    0.97     3778   195  0.2352 0.2762        
REMARK   3    24  1.3941 -  1.3745    0.97     3802   219  0.2463 0.2841        
REMARK   3    25  1.3745 -  1.3559    0.98     3789   208  0.2516 0.2467        
REMARK   3    26  1.3559 -  1.3383    0.97     3768   223  0.2617 0.2628        
REMARK   3    27  1.3383 -  1.3216    0.97     3814   168  0.2706 0.2820        
REMARK   3    28  1.3216 -  1.3057    0.97     3834   224  0.2887 0.2929        
REMARK   3    29  1.3057 -  1.2905    0.97     3756   203  0.3061 0.3298        
REMARK   3    30  1.2905 -  1.2760    0.97     3812   186  0.3071 0.3563        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.470           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.007           4397                                  
REMARK   3   ANGLE     :  0.940           6046                                  
REMARK   3   CHIRALITY :  0.089            656                                  
REMARK   3   PLANARITY :  0.007            816                                  
REMARK   3   DIHEDRAL  : 25.252           1678                                  
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 6RQQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102415.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX IV                             
REMARK 200  BEAMLINE                       : BIOMAX                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122208                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.03100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5DVX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (W/V) PEG 4000, 0.2 M AMMONIUM       
REMARK 280  FORMATE, 0.1 M TRIS-HCL PH 8.5, VAPOR DIFFUSION, SITTING DROP,      
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       32.55000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 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 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     TYR C   259                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A 212   CG  -  SD  -  CE  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    MET C 212   CG  -  SD  -  CE  ANGL. DEV. = -17.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 146       79.68     66.07                                   
REMARK 500    PRO A 148      172.38    -53.68                                   
REMARK 500    ALA A 392      -85.47    -54.16                                   
REMARK 500    VAL A 394      -59.50   -139.45                                   
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                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 226   NE2                                                    
REMARK 620 2 HIS A 228   NE2 100.9                                              
REMARK 620 3 HIS A 251   ND1 116.5  93.0                                        
REMARK 620 4 HOH A 540   O   105.6  93.2 135.3                                  
REMARK 620 5 FMT A 402   O2   88.5 170.5  84.4  82.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 226   NE2                                                    
REMARK 620 2 HIS C 228   NE2 100.5                                              
REMARK 620 3 HIS C 251   ND1 116.9  93.0                                        
REMARK 620 4 FMT C 402   O2   87.8 170.4  87.5                                  
REMARK 620 5 HOH C 528   O   107.1  94.6 133.1  78.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 402                 
DBREF  6RQQ A  140   395  UNP    Q16790   CAH9_HUMAN     140    395             
DBREF  6RQQ C  140   395  UNP    Q16790   CAH9_HUMAN     140    395             
SEQADV 6RQQ SER A  174  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 6RQQ SER A  183  UNP  Q16790    LEU   183 ENGINEERED MUTATION            
SEQADV 6RQQ LYS A  213  UNP  Q16790    ALA   213 ENGINEERED MUTATION            
SEQADV 6RQQ LYS A  258  UNP  Q16790    ALA   258 ENGINEERED MUTATION            
SEQADV 6RQQ TYR A  259  UNP  Q16790    PHE   259 ENGINEERED MUTATION            
SEQADV 6RQQ SER A  350  UNP  Q16790    MET   350 ENGINEERED MUTATION            
SEQADV 6RQQ SER C  174  UNP  Q16790    CYS   174 ENGINEERED MUTATION            
SEQADV 6RQQ SER C  183  UNP  Q16790    LEU   183 ENGINEERED MUTATION            
SEQADV 6RQQ LYS C  213  UNP  Q16790    ALA   213 ENGINEERED MUTATION            
SEQADV 6RQQ LYS C  258  UNP  Q16790    ALA   258 ENGINEERED MUTATION            
SEQADV 6RQQ TYR C  259  UNP  Q16790    PHE   259 ENGINEERED MUTATION            
SEQADV 6RQQ SER C  350  UNP  Q16790    MET   350 ENGINEERED MUTATION            
SEQRES   1 A  256  HIS TRP ARG TYR GLY GLY ASP PRO PRO TRP PRO ARG VAL          
SEQRES   2 A  256  SER PRO ALA CYS ALA GLY ARG PHE GLN SER PRO VAL ASP          
SEQRES   3 A  256  ILE ARG PRO GLN LEU ALA ALA PHE SER PRO ALA LEU ARG          
SEQRES   4 A  256  PRO LEU GLU LEU SER GLY PHE GLN LEU PRO PRO LEU PRO          
SEQRES   5 A  256  GLU LEU ARG LEU ARG ASN ASN GLY HIS SER VAL GLN LEU          
SEQRES   6 A  256  THR LEU PRO PRO GLY LEU GLU MET LYS LEU GLY PRO GLY          
SEQRES   7 A  256  ARG GLU TYR ARG ALA LEU GLN LEU HIS LEU HIS TRP GLY          
SEQRES   8 A  256  ALA ALA GLY ARG PRO GLY SER GLU HIS THR VAL GLU GLY          
SEQRES   9 A  256  HIS ARG PHE PRO ALA GLU ILE HIS VAL VAL HIS LEU SER          
SEQRES  10 A  256  THR LYS TYR ALA ARG VAL ASP GLU ALA LEU GLY ARG PRO          
SEQRES  11 A  256  GLY GLY LEU ALA VAL LEU ALA ALA PHE LEU GLU GLU GLY          
SEQRES  12 A  256  PRO GLU GLU ASN SER ALA TYR GLU GLN LEU LEU SER ARG          
SEQRES  13 A  256  LEU GLU GLU ILE ALA GLU GLU GLY SER GLU THR GLN VAL          
SEQRES  14 A  256  PRO GLY LEU ASP ILE SER ALA LEU LEU PRO SER ASP PHE          
SEQRES  15 A  256  SER ARG TYR PHE GLN TYR GLU GLY SER LEU THR THR PRO          
SEQRES  16 A  256  PRO CYS ALA GLN GLY VAL ILE TRP THR VAL PHE ASN GLN          
SEQRES  17 A  256  THR VAL SER LEU SER ALA LYS GLN LEU HIS THR LEU SER          
SEQRES  18 A  256  ASP THR LEU TRP GLY PRO GLY ASP SER ARG LEU GLN LEU          
SEQRES  19 A  256  ASN PHE ARG ALA THR GLN PRO LEU ASN GLY ARG VAL ILE          
SEQRES  20 A  256  GLU ALA SER PHE PRO ALA GLY VAL ASP                          
SEQRES   1 C  256  HIS TRP ARG TYR GLY GLY ASP PRO PRO TRP PRO ARG VAL          
SEQRES   2 C  256  SER PRO ALA CYS ALA GLY ARG PHE GLN SER PRO VAL ASP          
SEQRES   3 C  256  ILE ARG PRO GLN LEU ALA ALA PHE SER PRO ALA LEU ARG          
SEQRES   4 C  256  PRO LEU GLU LEU SER GLY PHE GLN LEU PRO PRO LEU PRO          
SEQRES   5 C  256  GLU LEU ARG LEU ARG ASN ASN GLY HIS SER VAL GLN LEU          
SEQRES   6 C  256  THR LEU PRO PRO GLY LEU GLU MET LYS LEU GLY PRO GLY          
SEQRES   7 C  256  ARG GLU TYR ARG ALA LEU GLN LEU HIS LEU HIS TRP GLY          
SEQRES   8 C  256  ALA ALA GLY ARG PRO GLY SER GLU HIS THR VAL GLU GLY          
SEQRES   9 C  256  HIS ARG PHE PRO ALA GLU ILE HIS VAL VAL HIS LEU SER          
SEQRES  10 C  256  THR LYS TYR ALA ARG VAL ASP GLU ALA LEU GLY ARG PRO          
SEQRES  11 C  256  GLY GLY LEU ALA VAL LEU ALA ALA PHE LEU GLU GLU GLY          
SEQRES  12 C  256  PRO GLU GLU ASN SER ALA TYR GLU GLN LEU LEU SER ARG          
SEQRES  13 C  256  LEU GLU GLU ILE ALA GLU GLU GLY SER GLU THR GLN VAL          
SEQRES  14 C  256  PRO GLY LEU ASP ILE SER ALA LEU LEU PRO SER ASP PHE          
SEQRES  15 C  256  SER ARG TYR PHE GLN TYR GLU GLY SER LEU THR THR PRO          
SEQRES  16 C  256  PRO CYS ALA GLN GLY VAL ILE TRP THR VAL PHE ASN GLN          
SEQRES  17 C  256  THR VAL SER LEU SER ALA LYS GLN LEU HIS THR LEU SER          
SEQRES  18 C  256  ASP THR LEU TRP GLY PRO GLY ASP SER ARG LEU GLN LEU          
SEQRES  19 C  256  ASN PHE ARG ALA THR GLN PRO LEU ASN GLY ARG VAL ILE          
SEQRES  20 C  256  GLU ALA SER PHE PRO ALA GLY VAL ASP                          
HET     ZN  A 401       1                                                       
HET    FMT  A 402       3                                                       
HET     ZN  C 401       1                                                       
HET    FMT  C 402       3                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     FMT FORMIC ACID                                                      
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  FMT    2(C H2 O2)                                                   
FORMUL   7  HOH   *674(H2 O)                                                    
HELIX    1 AA1 SER A  153  GLY A  158  5                                   6    
HELIX    2 AA2 ARG A  167  ALA A  171  5                                   5    
HELIX    3 AA3 ARG A  261  LEU A  266  1                                   6    
HELIX    4 AA4 ASN A  286  SER A  294  1                                   9    
HELIX    5 AA5 ARG A  295  ALA A  300  5                                   6    
HELIX    6 AA6 ASP A  312  LEU A  317  5                                   6    
HELIX    7 AA7 SER A  352  THR A  362  1                                  11    
HELIX    8 AA8 PRO C  148  VAL C  152  5                                   5    
HELIX    9 AA9 SER C  153  GLY C  158  5                                   6    
HELIX   10 AB1 ARG C  167  ALA C  171  5                                   5    
HELIX   11 AB2 ARG C  261  LEU C  266  1                                   6    
HELIX   12 AB3 ASN C  286  SER C  294  1                                   9    
HELIX   13 AB4 ARG C  295  ALA C  300  5                                   6    
HELIX   14 AB5 ASP C  312  LEU C  317  5                                   6    
HELIX   15 AB6 SER C  352  THR C  362  1                                  11    
SHEET    1 AA1 2 ASP A 165  ILE A 166  0                                        
SHEET    2 AA1 2 THR A 240  VAL A 241  1  O  THR A 240   N  ILE A 166           
SHEET    1 AA210 ALA A 172  PHE A 173  0                                        
SHEET    2 AA210 GLU A 387  ALA A 388  1  O  ALA A 388   N  ALA A 172           
SHEET    3 AA210 TYR A 324  SER A 330 -1  N  GLN A 326   O  GLU A 387           
SHEET    4 AA210 GLN A 338  PHE A 345 -1  O  VAL A 340   N  GLY A 329           
SHEET    5 AA210 LEU A 272  GLU A 281  1  N  ALA A 276   O  THR A 343           
SHEET    6 AA210 ALA A 248  SER A 256 -1  N  VAL A 252   O  LEU A 275           
SHEET    7 AA210 ARG A 218  TRP A 229 -1  N  LEU A 223   O  VAL A 253           
SHEET    8 AA210 VAL A 202  THR A 205 -1  N  LEU A 204   O  LEU A 225           
SHEET    9 AA210 LEU A 193  ASN A 197 -1  N  ARG A 194   O  THR A 205           
SHEET   10 AA210 GLU A 305  VAL A 308 -1  O  VAL A 308   N  LEU A 193           
SHEET    1 AA3 6 GLU A 181  SER A 183  0                                        
SHEET    2 AA3 6 GLU A 211  GLY A 215 -1  O  GLU A 211   N  SER A 183           
SHEET    3 AA3 6 ARG A 218  TRP A 229 -1  O  ARG A 218   N  LEU A 214           
SHEET    4 AA3 6 ALA A 248  SER A 256 -1  O  VAL A 253   N  LEU A 223           
SHEET    5 AA3 6 LEU A 272  GLU A 281 -1  O  LEU A 275   N  VAL A 252           
SHEET    6 AA3 6 VAL A 349  LEU A 351  1  O  VAL A 349   N  GLU A 280           
SHEET    1 AA4 2 ASP C 165  ILE C 166  0                                        
SHEET    2 AA4 2 THR C 240  VAL C 241  1  O  THR C 240   N  ILE C 166           
SHEET    1 AA510 ALA C 172  PHE C 173  0                                        
SHEET    2 AA510 GLU C 387  ALA C 388  1  O  ALA C 388   N  ALA C 172           
SHEET    3 AA510 TYR C 324  SER C 330 -1  N  GLN C 326   O  GLU C 387           
SHEET    4 AA510 GLN C 338  PHE C 345 -1  O  VAL C 340   N  GLY C 329           
SHEET    5 AA510 LEU C 272  GLU C 281  1  N  ALA C 276   O  THR C 343           
SHEET    6 AA510 ALA C 248  SER C 256 -1  N  ALA C 248   O  LEU C 279           
SHEET    7 AA510 ARG C 218  TRP C 229 -1  N  LEU C 223   O  VAL C 253           
SHEET    8 AA510 VAL C 202  THR C 205 -1  N  LEU C 204   O  LEU C 225           
SHEET    9 AA510 LEU C 193  ASN C 197 -1  N  ARG C 196   O  GLN C 203           
SHEET   10 AA510 GLU C 305  VAL C 308 -1  O  VAL C 308   N  LEU C 193           
SHEET    1 AA6 6 GLU C 181  SER C 183  0                                        
SHEET    2 AA6 6 GLU C 211  GLY C 215 -1  O  GLU C 211   N  SER C 183           
SHEET    3 AA6 6 ARG C 218  TRP C 229 -1  O  TYR C 220   N  MET C 212           
SHEET    4 AA6 6 ALA C 248  SER C 256 -1  O  VAL C 253   N  LEU C 223           
SHEET    5 AA6 6 LEU C 272  GLU C 281 -1  O  LEU C 279   N  ALA C 248           
SHEET    6 AA6 6 VAL C 349  LEU C 351  1  O  LEU C 351   N  GLU C 280           
SSBOND   1 CYS A  156    CYS A  336                          1555   1555  2.04  
SSBOND   2 CYS C  156    CYS C  336                          1555   1555  2.04  
LINK         NE2 HIS A 226                ZN    ZN A 401     1555   1555  2.04  
LINK         NE2 HIS A 228                ZN    ZN A 401     1555   1555  2.14  
LINK         ND1 HIS A 251                ZN    ZN A 401     1555   1555  2.09  
LINK         NE2 HIS C 226                ZN    ZN C 401     1555   1555  2.05  
LINK         NE2 HIS C 228                ZN    ZN C 401     1555   1555  2.16  
LINK         ND1 HIS C 251                ZN    ZN C 401     1555   1555  2.09  
LINK        ZN    ZN A 401                 O   HOH A 540     1555   1555  1.99  
LINK        ZN    ZN A 401                 O2  FMT A 402     1555   1555  2.48  
LINK        ZN    ZN C 401                 O2  FMT C 402     1555   1555  2.41  
LINK        ZN    ZN C 401                 O   HOH C 528     1555   1555  2.01  
CISPEP   1 GLY A  145    ASP A  146          0         0.01                     
CISPEP   2 ASP A  146    PRO A  147          0        -0.02                     
CISPEP   3 SER A  162    PRO A  163          0        -1.56                     
CISPEP   4 LEU A  190    PRO A  191          0         3.37                     
CISPEP   5 PRO A  334    PRO A  335          0        10.16                     
CISPEP   6 ALA A  392    GLY A  393          0        -3.76                     
CISPEP   7 ASP C  146    PRO C  147          0         2.41                     
CISPEP   8 SER C  162    PRO C  163          0        -1.85                     
CISPEP   9 LEU C  190    PRO C  191          0         2.03                     
CISPEP  10 PRO C  334    PRO C  335          0         8.94                     
SITE     1 AC1  5 HIS A 226  HIS A 228  HIS A 251  FMT A 402                    
SITE     2 AC1  5 HOH A 540                                                     
SITE     1 AC2  6 HIS A 226  HIS A 251  THR A 332   ZN A 401                    
SITE     2 AC2  6 HOH A 540  HOH A 555                                          
SITE     1 AC3  5 HIS C 226  HIS C 228  HIS C 251  FMT C 402                    
SITE     2 AC3  5 HOH C 528                                                     
SITE     1 AC4  6 HIS C 226  HIS C 251  THR C 332   ZN C 401                    
SITE     2 AC4  6 HOH C 528  HOH C 580                                          
CRYST1   48.940   65.100   76.290  90.00  92.86  90.00 P 1 21 1      4          
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      0.020433  0.000000  0.001019        0.00000                         
SCALE2      0.000000  0.015361  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013124        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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