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Database: PDB
Entry: 5JNC
LinkDB: 5JNC
Original site: 5JNC 
HEADER    LYASE/LYASE INHIBITOR                   29-APR-16   5JNC              
TITLE     CRYSTAL STRUCTURE FOR THE COMPLEX OF HUMAN CARBONIC ANHYDRASE IV AND  
TITLE    2 4-AMINOMETHYLBENZENE SULFONAMIDE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 4;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE IV,CARBONIC ANHYDRASE IV,CA-IV;       
COMPND   5 EC: 4.2.1.1;                                                         
COMPND   6 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: CA4;                                                           
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    CARBONIC ANHYDRASE, LYASE, INHIBITOR BINDING, LYASE-LYASE INHIBITOR   
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHEN,A.WAHEED,E.DI CERA,W.S.SLY                                     
REVDAT   3   06-FEB-19 5JNC    1       JRNL                                     
REVDAT   2   20-SEP-17 5JNC    1       REMARK                                   
REVDAT   1   03-MAY-17 5JNC    0                                                
JRNL        AUTH   A.MICKEVICIUTE,D.D.TIMM,M.GEDGAUDAS,V.LINKUVIENE,Z.CHEN,     
JRNL        AUTH 2 A.WAHEED,V.MICHAILOVIENE,A.ZUBRIENE,A.SMIRNOV,               
JRNL        AUTH 3 E.CAPKAUSKAITE,L.BARANAUSKIENE,J.JACHNO,J.REVUCKIENE,        
JRNL        AUTH 4 E.MANAKOVA,S.GRAZULIS,J.MATULIENE,E.DI CERA,W.S.SLY,         
JRNL        AUTH 5 D.MATULIS                                                    
JRNL        TITL   INTRINSIC THERMODYNAMICS OF HIGH AFFINITY INHIBITOR BINDING  
JRNL        TITL 2 TO RECOMBINANT HUMAN CARBONIC ANHYDRASE IV.                  
JRNL        REF    EUR. BIOPHYS. J.              V.  47   271 2018              
JRNL        REFN                   ISSN 1432-1017                               
JRNL        PMID   28975383                                                     
JRNL        DOI    10.1007/S00249-017-1256-0                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.STAMS,S.K.NAIR,T.OKUYAMA,A.WAHEED,W.S.SLY,D.W.CHRISTIANSON 
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE SECRETORY FORM OF                   
REMARK   1  TITL 2 MEMBRANE-ASSOCIATED HUMAN CARBONIC ANHYDRASE IV AT 2.8 A     
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    PNAS                          V.  93 13589 1996              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   8942978                                                      
REMARK   1  DOI    10.1073/PNAS.93.24.13589                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0107                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -0.500                         
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 76144                          
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4039                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5266                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 275                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8360                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 937                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.178         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.133         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.192         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8698 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8207 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11743 ; 1.579 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18972 ; 0.987 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1027 ; 6.806 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   403 ;35.811 ;24.938       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1551 ;14.991 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;15.585 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1267 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9587 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1941 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4154 ; 1.596 ; 2.212       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4149 ; 1.593 ; 2.210       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5157 ; 2.601 ; 3.302       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5158 ; 2.601 ; 3.303       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4544 ; 2.421 ; 2.582       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4544 ; 2.417 ; 2.582       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6585 ; 3.970 ; 3.734       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10403 ; 7.424 ;19.257       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10003 ; 7.053 ;18.667       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5JNC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220895.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80221                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ID 1ZNC                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA ACETATE, 200 MM AMSO4 AND      
REMARK 280  16% PEG 3350, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.38750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.70000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.89800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.70000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.38750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.89800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG A   129                                                      
REMARK 465     ASN A   130                                                      
REMARK 465     VAL A   131                                                      
REMARK 465     LYS A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     ALA A   134                                                      
REMARK 465     GLN A   135                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B   128                                                      
REMARK 465     ARG B   129                                                      
REMARK 465     ASN B   130                                                      
REMARK 465     VAL B   131                                                      
REMARK 465     LYS B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     GLN B   135                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     SER D     3                                                      
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. =   3.3 DEGREES          
REMARK 500    ARG A  27   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 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       53.39   -119.06                                   
REMARK 500    ARG A  27       50.72   -117.13                                   
REMARK 500    ASN A  72        7.22     54.39                                   
REMARK 500    SER A  98     -156.98   -125.52                                   
REMARK 500    GLU A 178      126.00    -28.26                                   
REMARK 500    LYS A 206       27.32   -143.27                                   
REMARK 500    SER B  98     -159.67   -132.07                                   
REMARK 500    ARG C  27       59.65   -119.95                                   
REMARK 500    ASN C  72       13.02     56.92                                   
REMARK 500    SER C  98     -157.41   -128.86                                   
REMARK 500    SER D  98     -159.96   -126.19                                   
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 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  94   NE2                                                    
REMARK 620 2 HIS A  96   NE2 109.5                                              
REMARK 620 3 HIS A 119   ND1 114.1  99.6                                        
REMARK 620 4 6LH A 302   S1   92.1 140.4 101.1                                  
REMARK 620 5 6LH A 302   N2  106.6 111.8 115.2  28.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  94   NE2                                                    
REMARK 620 2 HIS B  96   NE2 101.5                                              
REMARK 620 3 HIS B 119   ND1 113.9  99.1                                        
REMARK 620 4 6LH B 302   S1  101.7 139.2 101.6                                  
REMARK 620 5 6LH B 302   N2  110.9 111.0 118.5  28.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  94   NE2                                                    
REMARK 620 2 HIS C  96   NE2 109.0                                              
REMARK 620 3 HIS C 119   ND1 112.3  99.9                                        
REMARK 620 4 6LH C 302   N2  107.0 108.1 119.9                                  
REMARK 620 5 6LH C 302   S1   94.4 138.0 102.7  30.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 301  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  94   NE2                                                    
REMARK 620 2 HIS D  96   NE2 102.4                                              
REMARK 620 3 HIS D 119   ND1 113.3  96.0                                        
REMARK 620 4 6LH D 302   S1   99.7 144.2 100.6                                  
REMARK 620 5 6LH D 302   N2  111.7 114.3 117.2  30.2                            
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 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LH A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LH B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LH C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6LH D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JND   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5JNA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5JN8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5JN9   RELATED DB: PDB                                   
DBREF  5JNC A    1   259  UNP    P22748   CAH4_HUMAN      19    284             
DBREF  5JNC B    1   259  UNP    P22748   CAH4_HUMAN      19    284             
DBREF  5JNC C    1   259  UNP    P22748   CAH4_HUMAN      19    284             
DBREF  5JNC D    1   259  UNP    P22748   CAH4_HUMAN      19    284             
SEQRES   1 A  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER          
SEQRES   2 A  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY          
SEQRES   3 A  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL          
SEQRES   4 A  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE          
SEQRES   5 A  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL          
SEQRES   6 A  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN          
SEQRES   7 A  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR          
SEQRES   8 A  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO          
SEQRES   9 A  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE          
SEQRES  10 A  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY          
SEQRES  11 A  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP          
SEQRES  12 A  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR          
SEQRES  13 A  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU          
SEQRES  14 A  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA          
SEQRES  15 A  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS          
SEQRES  16 A  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR          
SEQRES  17 A  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG          
SEQRES  18 A  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE          
SEQRES  19 A  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER          
SEQRES  20 A  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN          
SEQRES  21 A  266  ARG THR VAL ILE LYS SER                                      
SEQRES   1 B  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER          
SEQRES   2 B  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY          
SEQRES   3 B  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL          
SEQRES   4 B  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE          
SEQRES   5 B  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL          
SEQRES   6 B  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN          
SEQRES   7 B  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR          
SEQRES   8 B  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO          
SEQRES   9 B  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE          
SEQRES  10 B  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY          
SEQRES  11 B  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP          
SEQRES  12 B  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR          
SEQRES  13 B  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU          
SEQRES  14 B  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA          
SEQRES  15 B  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS          
SEQRES  16 B  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR          
SEQRES  17 B  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG          
SEQRES  18 B  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE          
SEQRES  19 B  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER          
SEQRES  20 B  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN          
SEQRES  21 B  266  ARG THR VAL ILE LYS SER                                      
SEQRES   1 C  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER          
SEQRES   2 C  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY          
SEQRES   3 C  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL          
SEQRES   4 C  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE          
SEQRES   5 C  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL          
SEQRES   6 C  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN          
SEQRES   7 C  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR          
SEQRES   8 C  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO          
SEQRES   9 C  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE          
SEQRES  10 C  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY          
SEQRES  11 C  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP          
SEQRES  12 C  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR          
SEQRES  13 C  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU          
SEQRES  14 C  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA          
SEQRES  15 C  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS          
SEQRES  16 C  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR          
SEQRES  17 C  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG          
SEQRES  18 C  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE          
SEQRES  19 C  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER          
SEQRES  20 C  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN          
SEQRES  21 C  266  ARG THR VAL ILE LYS SER                                      
SEQRES   1 D  266  ALA GLU SER HIS TRP CYS TYR GLU VAL GLN ALA GLU SER          
SEQRES   2 D  266  SER ASN TYR PRO CYS LEU VAL PRO VAL LYS TRP GLY GLY          
SEQRES   3 D  266  ASN CYS GLN LYS ASP ARG GLN SER PRO ILE ASN ILE VAL          
SEQRES   4 D  266  THR THR LYS ALA LYS VAL ASP LYS LYS LEU GLY ARG PHE          
SEQRES   5 D  266  PHE PHE SER GLY TYR ASP LYS LYS GLN THR TRP THR VAL          
SEQRES   6 D  266  GLN ASN ASN GLY HIS SER VAL MET MET LEU LEU GLU ASN          
SEQRES   7 D  266  LYS ALA SER ILE SER GLY GLY GLY LEU PRO ALA PRO TYR          
SEQRES   8 D  266  GLN ALA LYS GLN LEU HIS LEU HIS TRP SER ASP LEU PRO          
SEQRES   9 D  266  TYR LYS GLY SER GLU HIS SER LEU ASP GLY GLU HIS PHE          
SEQRES  10 D  266  ALA MET GLU MET HIS ILE VAL HIS GLU LYS GLU LYS GLY          
SEQRES  11 D  266  THR SER ARG ASN VAL LYS GLU ALA GLN ASP PRO GLU ASP          
SEQRES  12 D  266  GLU ILE ALA VAL LEU ALA PHE LEU VAL GLU ALA GLY THR          
SEQRES  13 D  266  GLN VAL ASN GLU GLY PHE GLN PRO LEU VAL GLU ALA LEU          
SEQRES  14 D  266  SER ASN ILE PRO LYS PRO GLU MET SER THR THR MET ALA          
SEQRES  15 D  266  GLU SER SER LEU LEU ASP LEU LEU PRO LYS GLU GLU LYS          
SEQRES  16 D  266  LEU ARG HIS TYR PHE ARG TYR LEU GLY SER LEU THR THR          
SEQRES  17 D  266  PRO THR CYS ASP GLU LYS VAL VAL TRP THR VAL PHE ARG          
SEQRES  18 D  266  GLU PRO ILE GLN LEU HIS ARG GLU GLN ILE LEU ALA PHE          
SEQRES  19 D  266  SER GLN LYS LEU TYR TYR ASP LYS GLU GLN THR VAL SER          
SEQRES  20 D  266  MET LYS ASP ASN VAL ARG PRO LEU GLN GLN LEU GLY GLN          
SEQRES  21 D  266  ARG THR VAL ILE LYS SER                                      
HET     ZN  A 301       1                                                       
HET    6LH  A 302      12                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET    ACT  A 305       4                                                       
HET    GOL  A 306       6                                                       
HET    GOL  A 307       6                                                       
HET     ZN  B 301       1                                                       
HET    6LH  B 302      12                                                       
HET    SO4  B 303       5                                                       
HET    SO4  B 304       5                                                       
HET    ACT  B 305       4                                                       
HET    GOL  B 306       6                                                       
HET     ZN  C 301       1                                                       
HET    6LH  C 302      12                                                       
HET    SO4  C 303       5                                                       
HET    SO4  C 304       5                                                       
HET    ACT  C 305       4                                                       
HET    GOL  C 306       6                                                       
HET    GOL  C 307       6                                                       
HET     ZN  D 301       1                                                       
HET    6LH  D 302      12                                                       
HET    SO4  D 303       5                                                       
HET    SO4  D 304       5                                                       
HET    ACT  D 305       4                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     6LH 4-(AMINOMETHYL)BENZENE-1-SULFONAMIDE                             
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6  6LH    4(C7 H10 N2 O2 S)                                            
FORMUL   7  SO4    8(O4 S 2-)                                                   
FORMUL   9  ACT    4(C2 H3 O2 1-)                                               
FORMUL  10  GOL    5(C3 H8 O3)                                                  
FORMUL  30  HOH   *937(H2 O)                                                    
HELIX    1 AA1 TYR A    7  SER A   11C 1                                   8    
HELIX    2 AA2 VAL A   12  TRP A   16  5                                   5    
HELIX    3 AA3 VAL A   34  ALA A   38  5                                   5    
HELIX    4 AA4 ASN A  154  GLY A  156  5                                   3    
HELIX    5 AA5 PHE A  157  SER A  165  1                                   9    
HELIX    6 AA6 LEU A  181  LEU A  185  5                                   5    
HELIX    7 AA7 LYS A  187  ARG A  189A 5                                   6    
HELIX    8 AA8 ARG A  220  LEU A  229  1                                  11    
HELIX    9 AA9 TYR B    7  SER B   11B 1                                   7    
HELIX   10 AB1 VAL B   12  TRP B   16  5                                   5    
HELIX   11 AB2 GLY B   20  LYS B   25  5                                   6    
HELIX   12 AB3 VAL B   34  ALA B   38  5                                   5    
HELIX   13 AB4 ASN B  154  GLY B  156  5                                   3    
HELIX   14 AB5 PHE B  157  LEU B  164  1                                   8    
HELIX   15 AB6 SER B  165  ILE B  167  5                                   3    
HELIX   16 AB7 LEU B  181  LEU B  185  5                                   5    
HELIX   17 AB8 LYS B  187  ARG B  189A 5                                   6    
HELIX   18 AB9 ARG B  220  LEU B  229  1                                  11    
HELIX   19 AC1 TYR C    7  SER C   11B 1                                   7    
HELIX   20 AC2 VAL C   12  TRP C   16  5                                   5    
HELIX   21 AC3 VAL C   34  ALA C   38  5                                   5    
HELIX   22 AC4 ASN C  130  GLN C  135  1                                   6    
HELIX   23 AC5 ASP C  136  ASP C  139  5                                   4    
HELIX   24 AC6 ASN C  154  GLY C  156  5                                   3    
HELIX   25 AC7 PHE C  157  SER C  165  1                                   9    
HELIX   26 AC8 LEU C  181  LEU C  185  5                                   5    
HELIX   27 AC9 LYS C  187  ARG C  189A 5                                   6    
HELIX   28 AD1 ARG C  220  LEU C  229  1                                  11    
HELIX   29 AD2 TYR D    7  SER D   11B 1                                   7    
HELIX   30 AD3 VAL D   12  TRP D   16  5                                   5    
HELIX   31 AD4 ASN D  130  ASP D  136  1                                   7    
HELIX   32 AD5 PRO D  137  ASP D  139  5                                   3    
HELIX   33 AD6 ASN D  154  GLY D  156  5                                   3    
HELIX   34 AD7 PHE D  157  LEU D  164  1                                   8    
HELIX   35 AD8 SER D  165  ILE D  167  5                                   3    
HELIX   36 AD9 LEU D  181  LEU D  185  5                                   5    
HELIX   37 AE1 LYS D  187  ARG D  189A 5                                   6    
HELIX   38 AE2 ARG D  220  LEU D  229  1                                  11    
SHEET    1 AA1 2 ASN A  32  ILE A  33  0                                        
SHEET    2 AA1 2 SER A 108  LEU A 109  1  O  SER A 108   N  ILE A  33           
SHEET    1 AA210 LYS A  39  VAL A  40  0                                        
SHEET    2 AA210 ILE A 257  LYS A 258  1  O  LYS A 258   N  LYS A  39           
SHEET    3 AA210 TYR A 191  GLY A 196 -1  N  ARG A 193   O  ILE A 257           
SHEET    4 AA210 VAL A 207  PHE A 212 -1  O  VAL A 207   N  GLY A 196           
SHEET    5 AA210 ILE A 141  GLY A 151  1  N  ILE A 141   O  VAL A 208           
SHEET    6 AA210 MET A 116  LYS A 124 -1  N  MET A 118   O  PHE A 146           
SHEET    7 AA210 TYR A  88  TRP A  97 -1  N  GLN A  92   O  VAL A 121           
SHEET    8 AA210 VAL A  66  LEU A  69 -1  N  MET A  68   O  LEU A  93           
SHEET    9 AA210 THR A  58  ASN A  61 -1  N  THR A  58   O  LEU A  69           
SHEET   10 AA210 SER A 173  THR A 175 -1  O  THR A 174   N  VAL A  59           
SHEET    1 AA3 6 PHE A  47  SER A  50  0                                        
SHEET    2 AA3 6 SER A  78  GLY A  81 -1  O  SER A  80   N  PHE A  48           
SHEET    3 AA3 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  ILE A  79           
SHEET    4 AA3 6 MET A 116  LYS A 124 -1  O  VAL A 121   N  GLN A  92           
SHEET    5 AA3 6 ILE A 141  GLY A 151 -1  O  PHE A 146   N  MET A 118           
SHEET    6 AA3 6 ILE A 216  HIS A 219  1  O  ILE A 216   N  LEU A 147           
SHEET    1 AA4 2 ASN B  32  ILE B  33  0                                        
SHEET    2 AA4 2 SER B 108  LEU B 109  1  O  SER B 108   N  ILE B  33           
SHEET    1 AA510 LYS B  39  VAL B  40  0                                        
SHEET    2 AA510 ILE B 257  LYS B 258  1  O  LYS B 258   N  LYS B  39           
SHEET    3 AA510 TYR B 191  GLY B 196 -1  N  ARG B 193   O  ILE B 257           
SHEET    4 AA510 VAL B 207  PHE B 212 -1  O  VAL B 207   N  GLY B 196           
SHEET    5 AA510 ILE B 141  GLY B 151  1  N  ALA B 145   O  THR B 210           
SHEET    6 AA510 MET B 116  LYS B 124 -1  N  MET B 118   O  PHE B 146           
SHEET    7 AA510 TYR B  88  TRP B  97 -1  N  LYS B  91   O  VAL B 121           
SHEET    8 AA510 VAL B  66  LEU B  69 -1  N  MET B  68   O  LEU B  93           
SHEET    9 AA510 THR B  58  ASN B  61 -1  N  THR B  58   O  LEU B  69           
SHEET   10 AA510 SER B 173  THR B 175 -1  O  THR B 174   N  VAL B  59           
SHEET    1 AA6 6 PHE B  47  SER B  50  0                                        
SHEET    2 AA6 6 SER B  78  GLY B  81 -1  O  SER B  80   N  PHE B  48           
SHEET    3 AA6 6 TYR B  88  TRP B  97 -1  O  TYR B  88   N  ILE B  79           
SHEET    4 AA6 6 MET B 116  LYS B 124 -1  O  VAL B 121   N  LYS B  91           
SHEET    5 AA6 6 ILE B 141  GLY B 151 -1  O  PHE B 146   N  MET B 118           
SHEET    6 AA6 6 ILE B 216  HIS B 219  1  O  LEU B 218   N  GLY B 151           
SHEET    1 AA7 2 ASN C  32  ILE C  33  0                                        
SHEET    2 AA7 2 SER C 108  LEU C 109  1  O  SER C 108   N  ILE C  33           
SHEET    1 AA810 LYS C  39  VAL C  40  0                                        
SHEET    2 AA810 ILE C 257  LYS C 258  1  O  LYS C 258   N  LYS C  39           
SHEET    3 AA810 TYR C 191  GLY C 196 -1  N  ARG C 193   O  ILE C 257           
SHEET    4 AA810 VAL C 207  PHE C 212 -1  O  TRP C 209   N  TYR C 194           
SHEET    5 AA810 ILE C 141  GLY C 151  1  N  ILE C 141   O  VAL C 208           
SHEET    6 AA810 MET C 116  LYS C 124 -1  N  HIS C 122   O  ALA C 142           
SHEET    7 AA810 TYR C  88  TRP C  97 -1  N  GLN C  92   O  VAL C 121           
SHEET    8 AA810 VAL C  66  LEU C  69 -1  N  MET C  68   O  LEU C  93           
SHEET    9 AA810 THR C  58  ASN C  61 -1  N  GLN C  60   O  MET C  67           
SHEET   10 AA810 MET C 172  THR C 175 -1  O  MET C 172   N  ASN C  61           
SHEET    1 AA9 6 PHE C  47  SER C  50  0                                        
SHEET    2 AA9 6 SER C  78  GLY C  81 -1  O  SER C  78   N  SER C  50           
SHEET    3 AA9 6 TYR C  88  TRP C  97 -1  O  TYR C  88   N  ILE C  79           
SHEET    4 AA9 6 MET C 116  LYS C 124 -1  O  VAL C 121   N  GLN C  92           
SHEET    5 AA9 6 ILE C 141  GLY C 151 -1  O  ALA C 142   N  HIS C 122           
SHEET    6 AA9 6 ILE C 216  HIS C 219  1  O  ILE C 216   N  LEU C 147           
SHEET    1 AB1 2 ASN D  32  ILE D  33  0                                        
SHEET    2 AB1 2 SER D 108  LEU D 109  1  O  SER D 108   N  ILE D  33           
SHEET    1 AB210 LYS D  39  VAL D  40  0                                        
SHEET    2 AB210 ILE D 257  LYS D 258  1  O  LYS D 258   N  LYS D  39           
SHEET    3 AB210 TYR D 191  GLY D 196 -1  N  ARG D 193   O  ILE D 257           
SHEET    4 AB210 VAL D 207  PHE D 212 -1  O  VAL D 207   N  GLY D 196           
SHEET    5 AB210 ILE D 141  GLY D 151  1  N  ALA D 145   O  THR D 210           
SHEET    6 AB210 MET D 116  LYS D 124 -1  N  MET D 118   O  PHE D 146           
SHEET    7 AB210 TYR D  88  TRP D  97 -1  N  GLN D  92   O  VAL D 121           
SHEET    8 AB210 VAL D  66  LEU D  69 -1  N  MET D  68   O  LEU D  93           
SHEET    9 AB210 THR D  58  ASN D  61 -1  N  GLN D  60   O  MET D  67           
SHEET   10 AB210 MET D 172  THR D 175 -1  O  THR D 174   N  VAL D  59           
SHEET    1 AB3 6 PHE D  47  SER D  50  0                                        
SHEET    2 AB3 6 SER D  78  GLY D  81 -1  O  SER D  78   N  SER D  50           
SHEET    3 AB3 6 TYR D  88  TRP D  97 -1  O  TYR D  88   N  ILE D  79           
SHEET    4 AB3 6 MET D 116  LYS D 124 -1  O  VAL D 121   N  GLN D  92           
SHEET    5 AB3 6 ILE D 141  GLY D 151 -1  O  PHE D 146   N  MET D 118           
SHEET    6 AB3 6 ILE D 216  HIS D 219  1  O  ILE D 216   N  GLU D 149           
SSBOND   1 CYS A    6    CYS A   11G                         1555   1555  2.13  
SSBOND   2 CYS A   23    CYS A  203                          1555   1555  2.09  
SSBOND   3 CYS B    6    CYS B   11G                         1555   1555  2.09  
SSBOND   4 CYS B   23    CYS B  203                          1555   1555  2.11  
SSBOND   5 CYS C    6    CYS C   11G                         1555   1555  2.14  
SSBOND   6 CYS C   23    CYS C  203                          1555   1555  2.11  
SSBOND   7 CYS D    6    CYS D   11G                         1555   1555  2.10  
SSBOND   8 CYS D   23    CYS D  203                          1555   1555  2.11  
LINK         NE2 HIS A  94                ZN    ZN A 301     1555   1555  2.18  
LINK         NE2 HIS A  96                ZN    ZN A 301     1555   1555  2.18  
LINK         ND1 HIS A 119                ZN    ZN A 301     1555   1555  2.18  
LINK         NE2 HIS B  94                ZN    ZN B 301     1555   1555  2.00  
LINK         NE2 HIS B  96                ZN    ZN B 301     1555   1555  2.16  
LINK         ND1 HIS B 119                ZN    ZN B 301     1555   1555  2.11  
LINK         NE2 HIS C  94                ZN    ZN C 301     1555   1555  2.11  
LINK         NE2 HIS C  96                ZN    ZN C 301     1555   1555  2.15  
LINK         ND1 HIS C 119                ZN    ZN C 301     1555   1555  2.12  
LINK         NE2 HIS D  94                ZN    ZN D 301     1555   1555  2.09  
LINK         NE2 HIS D  96                ZN    ZN D 301     1555   1555  2.16  
LINK         ND1 HIS D 119                ZN    ZN D 301     1555   1555  2.11  
LINK        ZN    ZN A 301                 S1  6LH A 302     1555   1555  2.94  
LINK        ZN    ZN A 301                 N2  6LH A 302     1555   1555  1.93  
LINK        ZN    ZN B 301                 S1  6LH B 302     1555   1555  2.94  
LINK        ZN    ZN B 301                 N2  6LH B 302     1555   1555  1.91  
LINK        ZN    ZN C 301                 N2  6LH C 302     1555   1555  2.03  
LINK        ZN    ZN C 301                 S1  6LH C 302     1555   1555  2.93  
LINK        ZN    ZN D 301                 S1  6LH D 302     1555   1555  2.90  
LINK        ZN    ZN D 301                 N2  6LH D 302     1555   1555  1.98  
CISPEP   1 SER A   29    PRO A   30          0         4.89                     
CISPEP   2 PRO A  201    THR A  202          0        11.14                     
CISPEP   3 SER B   29    PRO B   30          0         3.92                     
CISPEP   4 PRO B  201    THR B  202          0        11.52                     
CISPEP   5 SER C   29    PRO C   30          0         2.10                     
CISPEP   6 PRO C  201    THR C  202          0         9.13                     
CISPEP   7 SER D   29    PRO D   30          0         2.41                     
CISPEP   8 PRO D  201    THR D  202          0        11.97                     
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  6LH A 302                    
SITE     1 AC2 10 GLN A  92  HIS A  94  HIS A  96  HIS A 119                    
SITE     2 AC2 10 LEU A 198  THR A 199  THR A 200   ZN A 301                    
SITE     3 AC2 10 HOH A 402  HOH A 572                                          
SITE     1 AC3  7 ARG A  27  LEU A 195  ARG A 254  THR A 255                    
SITE     2 AC3  7 HOH A 491  HOH A 502  HOH A 569                               
SITE     1 AC4  6 SER A  50  GLY A  50A TYR A  51  ASP A  52                    
SITE     2 AC4  6 LYS A  53  HOH A 548                                          
SITE     1 AC5  3 GLN A  92  GLU A 123  HOH A 517                               
SITE     1 AC6  6 PHE A  48  SER A  50  SER A  78  ILE A  79                    
SITE     2 AC6  6 SER A  80  GLN C  60                                          
SITE     1 AC7  4 ARG A  46  GLU A 187A ASN C  72  LYS C  91                    
SITE     1 AC8  4 HIS B  94  HIS B  96  HIS B 119  6LH B 302                    
SITE     1 AC9 10 GLN B  92  HIS B  94  HIS B  96  HIS B 119                    
SITE     2 AC9 10 LEU B 198  THR B 199  THR B 200  TRP B 209                    
SITE     3 AC9 10  ZN B 301  HOH B 419                                          
SITE     1 AD1  6 ARG B  27  LEU B 195  ARG B 254  THR B 255                    
SITE     2 AD1  6 HOH B 410  HOH B 465                                          
SITE     1 AD2  6 SER B  50  GLY B  50A TYR B  51  ASP B  52                    
SITE     2 AD2  6 LYS B  53  HOH B 402                                          
SITE     1 AD3  4 LYS B  15  GLU D 155  GLN D 158  GLU D 162                    
SITE     1 AD4  7 PHE B  48  SER B  78  ILE B  79  SER B  80                    
SITE     2 AD4  7 HOH B 423  HOH B 494  GLN D  60                               
SITE     1 AD5  4 HIS C  94  HIS C  96  HIS C 119  6LH C 302                    
SITE     1 AD6  8 GLN C  92  HIS C  94  HIS C  96  HIS C 119                    
SITE     2 AD6  8 LEU C 198  THR C 199  THR C 200   ZN C 301                    
SITE     1 AD7  4 ARG C  27  ARG C 254  THR C 255  HOH C 492                    
SITE     1 AD8  6 GLY C  50A TYR C  51  ASP C  52  LYS C  53                    
SITE     2 AD8  6 HOH C 514  HOH C 516                                          
SITE     1 AD9  4 ARG A  46  ARG A 189A ASN C  72  GLN C  89                    
SITE     1 AE1  9 LYS C 103  ASP C 243  VAL C 245  PRO C 247                    
SITE     2 AE1  9 HOH C 415  HOH C 425  HOH C 445  HOH C 495                    
SITE     3 AE1  9 HOH C 507                                                     
SITE     1 AE2  5 SER C  50  LYS C  53  ASN C  72  ALA C  77                    
SITE     2 AE2  5 SER C  78                                                     
SITE     1 AE3  4 HIS D  94  HIS D  96  HIS D 119  6LH D 302                    
SITE     1 AE4 11 GLN D  92  HIS D  94  HIS D  96  HIS D 119                    
SITE     2 AE4 11 LEU D 198  THR D 199  THR D 200  TRP D 209                    
SITE     3 AE4 11  ZN D 301  HOH D 435  HOH D 500                               
SITE     1 AE5  4 ARG D  27  ARG D 254  THR D 255  HOH D 479                    
SITE     1 AE6  6 GLU A   2  GLY D  50A TYR D  51  ASP D  52                    
SITE     2 AE6  6 LYS D  53  HOH D 520                                          
SITE     1 AE7  9 SER D  98  ASP D  99  LEU D 100  PRO D 101                    
SITE     2 AE7  9 ALA D 115  ALA D 150  ILE D 223  LEU D 224                    
SITE     3 AE7  9 HOH D 433                                                     
CRYST1   64.775  123.796  151.400  90.00  90.00  90.00 P 21 21 21   16          
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      0.015438  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008078  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006605        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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