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Database: PDB
Entry: 5NXP
LinkDB: 5NXP
Original site: 5NXP 
HEADER    LYASE                                   10-MAY-17   5NXP              
TITLE     CARBONIC ANHYDRASE II INHIBITOR RA7                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II,CARBONIC ANHYDRASE C,CAC,CARBONIC  
COMPND   5 ANHYDRASE II,CA-II;                                                  
COMPND   6 EC: 4.2.1.1;                                                         
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: CA2;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CARBONIC ANHYDRASE II, CA INHIBITOR, LYASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BRYNDA,P.REZACOVA,M.HOREJSI,J.FANFRLIK                              
REVDAT   2   18-APR-18 5NXP    1       JRNL                                     
REVDAT   1   17-JAN-18 5NXP    0                                                
JRNL        AUTH   A.PECINA,J.BRYNDA,L.VRZAL,R.GNANASEKARAN,M.HOREJSI,          
JRNL        AUTH 2 S.M.EYRILMEZ,J.REZAC,M.LEPSIK,P.REZACOVA,P.HOBZA,P.MAJER,    
JRNL        AUTH 3 V.VEVERKA,J.FANFRLIK                                         
JRNL        TITL   RANKING POWER OF THE SQM/COSMO SCORING FUNCTION ON CARBONIC  
JRNL        TITL 2 ANHYDRASE II-INHIBITOR COMPLEXES.                            
JRNL        REF    CHEMPHYSCHEM                  V.  19   873 2018              
JRNL        REFN                   ISSN 1439-7641                               
JRNL        PMID   29316128                                                     
JRNL        DOI    10.1002/CPHC.201701104                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.8.0103                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 60006                          
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) : 0.129                           
REMARK   3   R VALUE            (WORKING SET) : 0.128                           
REMARK   3   FREE R VALUE                     : 0.162                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1001                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2019                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 280                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14000                                              
REMARK   3    B22 (A**2) : -0.92000                                             
REMARK   3    B33 (A**2) : 0.65000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.09000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.044         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.044         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.033         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.756         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
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  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5NXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004898.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61012                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 2.064                              
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.7800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.87                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.210                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3PO6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS 1.6 M NATRIUM CITRATE, PH     
REMARK 280  7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
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       20.52000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 11410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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   9    CG   CD   CE   NZ                                   
REMARK 470     LYS A  39    CD   CE   NZ                                        
REMARK 470     LYS A  45    CE   NZ                                             
REMARK 470     LYS A  80    CE   NZ                                             
REMARK 470     LYS A 133    CD   CE   NZ                                        
REMARK 470     LYS A 149    NZ                                                  
REMARK 470     LYS A 159    CD   CE   NZ                                        
REMARK 470     LYS A 170    NZ                                                  
REMARK 470     LYS A 172    CD   CE   NZ                                        
REMARK 470     LYS A 213    CD   CE   NZ                                        
REMARK 470     LYS A 228    CE   NZ                                             
REMARK 470     GLU A 236    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 255    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 261    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CD2  HIS A    36     O    HOH A   409              1.91            
REMARK 500   O    HOH A   543     O    HOH A   576              1.97            
REMARK 500   O    LYS A    76     O    HOH A   405              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   461     O    HOH A   639     2546     2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    THR A 125   C     LYS A 127   N       0.158                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  27   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 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    ARG A  27       52.76   -141.11                                   
REMARK 500    ALA A  77       86.54     49.08                                   
REMARK 500    LYS A 111       -4.56     71.65                                   
REMARK 500    PHE A 176       67.01   -150.20                                   
REMARK 500    ASN A 244       45.27    -93.25                                   
REMARK 500    LYS A 252     -132.38     53.13                                   
REMARK 500    ASN A 253       58.87    -93.61                                   
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 680        DISTANCE =  6.60 ANGSTROMS                       
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 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  94   NE2                                                    
REMARK 620 2 HIS A  96   NE2 105.1                                              
REMARK 620 3 HIS A 119   ND1 112.9  98.4                                        
REMARK 620 4 9DH A 302   NAP 108.9 115.2 115.6                                  
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 ZN A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 9DH A 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5NXG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NXI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NXM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5NXO   RELATED DB: PDB                                   
DBREF  5NXP A    3   261  UNP    P00918   CAH2_HUMAN       3    260             
SEQRES   1 A  258  HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO GLU HIS          
SEQRES   2 A  258  TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU ARG GLN          
SEQRES   3 A  258  SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS TYR ASP          
SEQRES   4 A  258  PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP GLN ALA          
SEQRES   5 A  258  THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA PHE ASN          
SEQRES   6 A  258  VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL LEU LYS          
SEQRES   7 A  258  GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE GLN PHE          
SEQRES   8 A  258  HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY SER GLU          
SEQRES   9 A  258  HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU LEU HIS          
SEQRES  10 A  258  LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE GLY LYS          
SEQRES  11 A  258  ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU GLY ILE          
SEQRES  12 A  258  PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU GLN LYS          
SEQRES  13 A  258  VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS GLY LYS          
SEQRES  14 A  258  SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY LEU LEU          
SEQRES  15 A  258  PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY SER LEU          
SEQRES  16 A  258  THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP ILE VAL          
SEQRES  17 A  258  LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN VAL LEU          
SEQRES  18 A  258  LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY GLU PRO          
SEQRES  19 A  258  GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA GLN PRO          
SEQRES  20 A  258  LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS                  
HET     ZN  A 301       1                                                       
HET    9DH  A 302      35                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     9DH 2-[METHYL(PHENYL)AMINO]-~{N}-(4-SULFAMOYLPHENYL)                 
HETNAM   2 9DH  ETHANAMIDE                                                      
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  9DH    C15 H17 N3 O3 S                                              
FORMUL   4  HOH   *280(H2 O)                                                    
HELIX    1 AA1 GLY A   12  TRP A   16  5                                   5    
HELIX    2 AA2 PHE A   20  GLY A   25  5                                   6    
HELIX    3 AA3 LYS A  127  GLY A  129  5                                   3    
HELIX    4 AA4 ASP A  130  VAL A  135  1                                   6    
HELIX    5 AA5 LYS A  154  GLY A  156  5                                   3    
HELIX    6 AA6 LEU A  157  LEU A  164  1                                   8    
HELIX    7 AA7 ASP A  165  LYS A  168  5                                   4    
HELIX    8 AA8 ASP A  180  LEU A  185  5                                   6    
HELIX    9 AA9 SER A  219  ARG A  227  1                                   9    
SHEET    1 AA1 2 ASP A  32  ILE A  33  0                                        
SHEET    2 AA1 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33           
SHEET    1 AA210 LYS A  39  TYR A  40  0                                        
SHEET    2 AA210 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39           
SHEET    3 AA210 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257           
SHEET    4 AA210 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196           
SHEET    5 AA210 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210           
SHEET    6 AA210 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146           
SHEET    7 AA210 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119           
SHEET    8 AA210 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93           
SHEET    9 AA210 SER A  56  ASN A  61 -1  N  ARG A  58   O  GLU A  69           
SHEET   10 AA210 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59           
SHEET    1 AA3 6 LEU A  47  SER A  50  0                                        
SHEET    2 AA3 6 VAL A  78  GLY A  81 -1  O  LYS A  80   N  SER A  48           
SHEET    3 AA3 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79           
SHEET    4 AA3 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94           
SHEET    5 AA3 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118           
SHEET    6 AA3 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147           
LINK         NE2 HIS A  94                ZN    ZN A 301     1555   1555  2.06  
LINK         NE2 HIS A  96                ZN    ZN A 301     1555   1555  2.05  
LINK         ND1 HIS A 119                ZN    ZN A 301     1555   1555  2.07  
LINK        ZN    ZN A 301                 NAP 9DH A 302     1555   1555  2.01  
CISPEP   1 SER A   29    PRO A   30          0        -3.05                     
CISPEP   2 PRO A  201    PRO A  202          0        13.97                     
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  9DH A 302                    
SITE     1 AC2 15 GLN A  92  HIS A  94  HIS A  96  HIS A 119                    
SITE     2 AC2 15 PHE A 131  VAL A 143  LEU A 198  THR A 199                    
SITE     3 AC2 15 THR A 200  PRO A 202  TRP A 209   ZN A 301                    
SITE     4 AC2 15 HOH A 403  HOH A 414  HOH A 565                               
CRYST1   41.911   41.040   71.519  90.00 104.31  90.00 P 1 21 1      2          
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      0.023860  0.000000  0.006085        0.00000                         
SCALE2      0.000000  0.024366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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