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Database: PDB
Entry: 1ICF
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Original site: 1ICF 
HEADER    HYDROLASE                               07-JAN-99   1ICF              
TITLE     CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN       
TITLE    2 COMPLEX WITH CATHEPSIN L                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CATHEPSIN L: HEAVY CHAIN);                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 EC: 3.4.22.15;                                                       
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PROTEIN (CATHEPSIN L: LIGHT CHAIN);                        
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 EC: 3.4.22.15;                                                       
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: PROTEIN (INVARIANT CHAIN);                                 
COMPND  11 CHAIN: I, J;                                                         
COMPND  12 FRAGMENT: THYROGLOBULIN TYPE-1 DOMAIN;                               
COMPND  13 SYNONYM: II FRAGMENT, CD74 FRAGMENT                                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: KIDNEY;                                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 ORGAN: KIDNEY;                                                       
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 ORGAN: KIDNEY                                                        
KEYWDS    CYSTEINE PROTEINASE, CATHEPSIN, MHC CLASS II, INVARIANT CHAIN,        
KEYWDS   2 THYROGLOBULIN TYPE-1 DOMAIN, HYDROLASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.GUNCAR,G.PUNGERCIC,I.KLEMENCIC,V.TURK,D.TURK                        
REVDAT   5   29-JUL-20 1ICF    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   13-JUL-11 1ICF    1       VERSN                                    
REVDAT   3   24-FEB-09 1ICF    1       VERSN                                    
REVDAT   2   01-APR-03 1ICF    1       JRNL                                     
REVDAT   1   12-JAN-00 1ICF    0                                                
JRNL        AUTH   G.GUNCAR,G.PUNGERCIC,I.KLEMENCIC,V.TURK,D.TURK               
JRNL        TITL   CRYSTAL STRUCTURE OF MHC CLASS II-ASSOCIATED P41 II FRAGMENT 
JRNL        TITL 2 BOUND TO CATHEPSIN L REVEALS THE STRUCTURAL BASIS FOR        
JRNL        TITL 3 DIFFERENTIATION BETWEEN CATHEPSINS L AND S.                  
JRNL        REF    EMBO J.                       V.  18   793 1999              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   10022822                                                     
JRNL        DOI    10.1093/EMBOJ/18.4.793                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : MAIN                                                 
REMARK   3   AUTHORS     : TURK                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 41514                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4364                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 668                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.380                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : 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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ICF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000007124.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 289                                
REMARK 200  PH                             : 6.1                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42072                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 3.160                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1CJL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOR DIFFUSION METHOD      
REMARK 280  RESERVOIR CONTAINED 1ML OF 0.2 M NA- ACETATE TRIHYDRATE, 30% W/V    
REMARK 280  PEG 8K AND 0.1M MES, PH 6.1. DROP WAS COMPOSED OF 2 MICRO L OF      
REMARK 280  RESERVOIR SOLUTION AND 2 MICRO L OF THE COMPLEX (10 MG/ML) IN       
REMARK 280  20MM NA-ACETATE AND 1MM EDTA, PH 5.0.                               
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       40.29700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 6970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J                               
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I                               
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 APPLY THE FOLLOWING TO CHAINS: C, D, J                               
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       62.59200            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       40.29700            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     SER A   174                                                      
REMARK 475     THR A   175                                                      
REMARK 475     ASN B   179                                                      
REMARK 475     SER C   174                                                      
REMARK 475     THR C   175                                                      
REMARK 475     ASN D   179                                                      
REMARK 475     ASN D   180                                                      
REMARK 475     SER J   258                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A    3   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ARG A   44   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS A  120   CG   CD   CE   NZ                                   
REMARK 480     GLU A  148   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU B  191   CD   OE1  OE2                                       
REMARK 480     GLU B  192   CG   CD   OE1  OE2                                  
REMARK 480     ARG C   44   CZ   NH1  NH2                                       
REMARK 480     LYS C   99   CB   CG   CD   CE   NZ                              
REMARK 480     LYS C  103   CG   CD   CE   NZ                                   
REMARK 480     LYS C  117   CD   CE   NZ                                        
REMARK 480     LYS C  120   CD   CE   NZ                                        
REMARK 480     GLU C  159   CG   CD   OE1  OE2                                  
REMARK 480     GLU D  191   CG   CD   OE1  OE2                                  
REMARK 480     GLU D  192   CG   CD   OE1  OE2                                  
REMARK 480     LYS I  215   CD   CE   NZ                                        
REMARK 480     GLU I  218   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU J  218   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU J  257   CB   CG   CD   OE1  OE2                             
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    ARG B   206     OG   SER J   258     2656     0.88            
REMARK 500   CB   ASN B   207     OXT  SER J   258     2656     1.36            
REMARK 500   OXT  THR A   175     CE   MET C    38     1656     1.46            
REMARK 500   CB   SER J   258     O    HOH B   235     2646     1.57            
REMARK 500   N    ASN B   207     OXT  SER J   258     2656     1.77            
REMARK 500   CA   ASN B   207     OXT  SER J   258     2656     1.84            
REMARK 500   C    ARG B   206     OG   SER J   258     2656     1.87            
REMARK 500   O    SER A   174     CG2  THR C    42     1656     1.91            
REMARK 500   OXT  SER I   258     O    HOH C   324     2655     2.00            
REMARK 500   C    ARG B   206     OXT  SER J   258     2656     2.02            
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    GLN A  21       49.04    -99.55                                   
REMARK 500    GLU A  96     -169.40   -127.54                                   
REMARK 500    LYS A 147      -52.18   -123.67                                   
REMARK 500    SER A 174      165.71    -46.79                                   
REMARK 500    GLN C  21       51.22    -99.27                                   
REMARK 500    TYR C  89       75.84   -153.68                                   
REMARK 500    GLU C  96     -165.78   -126.20                                   
REMARK 500    ALA D 214       58.51   -151.46                                   
REMARK 500    GLU I 257     -169.01   -125.60                                   
REMARK 500    GLU J 257     -156.81   -102.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH C   365                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE                                        
DBREF  1ICF A    1   175  UNP    P07711   CATL_HUMAN     114    288             
DBREF  1ICF B  179   220  UNP    P07711   CATL_HUMAN     292    333             
DBREF  1ICF C    1   175  UNP    P07711   CATL_HUMAN     114    288             
DBREF  1ICF D  179   220  UNP    P07711   CATL_HUMAN     292    333             
DBREF  1ICF I  194   258  UNP    P04233   HG2A_HUMAN     210    274             
DBREF  1ICF J  194   258  UNP    P04233   HG2A_HUMAN     210    274             
SEQRES   1 A  175  ALA PRO ARG SER VAL ASP TRP ARG GLU LYS GLY TYR VAL          
SEQRES   2 A  175  THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP          
SEQRES   3 A  175  ALA PHE SER ALA THR GLY ALA LEU GLU GLY GLN MET PHE          
SEQRES   4 A  175  ARG LYS THR GLY ARG LEU ILE SER LEU SER GLU GLN ASN          
SEQRES   5 A  175  LEU VAL ASP CYS SER GLY PRO GLN GLY ASN GLU GLY CYS          
SEQRES   6 A  175  ASN GLY GLY LEU MET ASP TYR ALA PHE GLN TYR VAL GLN          
SEQRES   7 A  175  ASP ASN GLY GLY LEU ASP SER GLU GLU SER TYR PRO TYR          
SEQRES   8 A  175  GLU ALA THR GLU GLU SER CYS LYS TYR ASN PRO LYS TYR          
SEQRES   9 A  175  SER VAL ALA ASN ASP THR GLY PHE VAL ASP ILE PRO LYS          
SEQRES  10 A  175  GLN GLU LYS ALA LEU MET LYS ALA VAL ALA THR VAL GLY          
SEQRES  11 A  175  PRO ILE SER VAL ALA ILE ASP ALA GLY HIS GLU SER PHE          
SEQRES  12 A  175  LEU PHE TYR LYS GLU GLY ILE TYR PHE GLU PRO ASP CYS          
SEQRES  13 A  175  SER SER GLU ASP MET ASP HIS GLY VAL LEU VAL VAL GLY          
SEQRES  14 A  175  TYR GLY PHE GLU SER THR                                      
SEQRES   1 B   42  ASN ASN LYS TYR TRP LEU VAL LYS ASN SER TRP GLY GLU          
SEQRES   2 B   42  GLU TRP GLY MET GLY GLY TYR VAL LYS MET ALA LYS ASP          
SEQRES   3 B   42  ARG ARG ASN HIS CYS GLY ILE ALA SER ALA ALA SER TYR          
SEQRES   4 B   42  PRO THR VAL                                                  
SEQRES   1 C  175  ALA PRO ARG SER VAL ASP TRP ARG GLU LYS GLY TYR VAL          
SEQRES   2 C  175  THR PRO VAL LYS ASN GLN GLY GLN CYS GLY SER CYS TRP          
SEQRES   3 C  175  ALA PHE SER ALA THR GLY ALA LEU GLU GLY GLN MET PHE          
SEQRES   4 C  175  ARG LYS THR GLY ARG LEU ILE SER LEU SER GLU GLN ASN          
SEQRES   5 C  175  LEU VAL ASP CYS SER GLY PRO GLN GLY ASN GLU GLY CYS          
SEQRES   6 C  175  ASN GLY GLY LEU MET ASP TYR ALA PHE GLN TYR VAL GLN          
SEQRES   7 C  175  ASP ASN GLY GLY LEU ASP SER GLU GLU SER TYR PRO TYR          
SEQRES   8 C  175  GLU ALA THR GLU GLU SER CYS LYS TYR ASN PRO LYS TYR          
SEQRES   9 C  175  SER VAL ALA ASN ASP THR GLY PHE VAL ASP ILE PRO LYS          
SEQRES  10 C  175  GLN GLU LYS ALA LEU MET LYS ALA VAL ALA THR VAL GLY          
SEQRES  11 C  175  PRO ILE SER VAL ALA ILE ASP ALA GLY HIS GLU SER PHE          
SEQRES  12 C  175  LEU PHE TYR LYS GLU GLY ILE TYR PHE GLU PRO ASP CYS          
SEQRES  13 C  175  SER SER GLU ASP MET ASP HIS GLY VAL LEU VAL VAL GLY          
SEQRES  14 C  175  TYR GLY PHE GLU SER THR                                      
SEQRES   1 D   42  ASN ASN LYS TYR TRP LEU VAL LYS ASN SER TRP GLY GLU          
SEQRES   2 D   42  GLU TRP GLY MET GLY GLY TYR VAL LYS MET ALA LYS ASP          
SEQRES   3 D   42  ARG ARG ASN HIS CYS GLY ILE ALA SER ALA ALA SER TYR          
SEQRES   4 D   42  PRO THR VAL                                                  
SEQRES   1 I   65  LEU THR LYS CYS GLN GLU GLU VAL SER HIS ILE PRO ALA          
SEQRES   2 I   65  VAL HIS PRO GLY SER PHE ARG PRO LYS CYS ASP GLU ASN          
SEQRES   3 I   65  GLY ASN TYR LEU PRO LEU GLN CYS TYR GLY SER ILE GLY          
SEQRES   4 I   65  TYR CYS TRP CYS VAL PHE PRO ASN GLY THR GLU VAL PRO          
SEQRES   5 I   65  ASN THR ARG SER ARG GLY HIS HIS ASN CYS SER GLU SER          
SEQRES   1 J   65  LEU THR LYS CYS GLN GLU GLU VAL SER HIS ILE PRO ALA          
SEQRES   2 J   65  VAL HIS PRO GLY SER PHE ARG PRO LYS CYS ASP GLU ASN          
SEQRES   3 J   65  GLY ASN TYR LEU PRO LEU GLN CYS TYR GLY SER ILE GLY          
SEQRES   4 J   65  TYR CYS TRP CYS VAL PHE PRO ASN GLY THR GLU VAL PRO          
SEQRES   5 J   65  ASN THR ARG SER ARG GLY HIS HIS ASN CYS SER GLU SER          
MODRES 1ICF ASN I  240  ASN  GLYCOSYLATION SITE                                 
MODRES 1ICF ASN J  240  ASN  GLYCOSYLATION SITE                                 
HET    NAG  I 100      14                                                       
HET    NAG  J 100      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   7  NAG    2(C8 H15 N O6)                                               
FORMUL   9  HOH   *668(H2 O)                                                    
HELIX    1   1 CYS A   25  THR A   42  1                                  18    
HELIX    2   2 GLU A   50  CYS A   56  1                                   7    
HELIX    3   3 GLY A   58  GLN A   60  5                                   3    
HELIX    4   4 GLY A   64  ASN A   66  5                                   3    
HELIX    5   5 MET A   70  ASN A   80  1                                  11    
HELIX    6   6 PRO A  102  TYR A  104  5                                   3    
HELIX    7   7 GLU A  119  THR A  128  1                                  10    
HELIX    8   8 GLU A  141  LEU A  144  1                                   4    
HELIX    9   9 HIS B  208  GLY B  210  5                                   3    
HELIX   10  10 CYS C   25  THR C   42  1                                  18    
HELIX   11  11 GLU C   50  CYS C   56  1                                   7    
HELIX   12  12 GLY C   58  GLN C   60  5                                   3    
HELIX   13  13 GLY C   64  ASN C   66  5                                   3    
HELIX   14  14 MET C   70  ASN C   80  1                                  11    
HELIX   15  15 PRO C  102  TYR C  104  5                                   3    
HELIX   16  16 GLU C  119  THR C  128  1                                  10    
HELIX   17  17 GLU C  141  LEU C  144  1                                   4    
HELIX   18  18 HIS D  208  GLY D  210  5                                   3    
HELIX   19  19 LYS I  196  HIS I  203  1                                   8    
HELIX   20  20 LYS J  196  HIS J  203  1                                   8    
SHEET    1   A 2 ILE A 132  ILE A 136  0                                        
SHEET    2   A 2 HIS A 163  VAL A 167 -1  N  VAL A 167   O  ILE A 132           
SHEET    1   B 2 TYR B 182  LYS B 186  0                                        
SHEET    2   B 2 TYR B 198  ALA B 202 -1  N  MET B 201   O  TRP B 183           
SHEET    1   C 2 ILE C 132  ILE C 136  0                                        
SHEET    2   C 2 HIS C 163  VAL C 167 -1  N  VAL C 167   O  ILE C 132           
SHEET    1   D 2 TYR D 182  LYS D 186  0                                        
SHEET    2   D 2 TYR D 198  ALA D 202 -1  N  MET D 201   O  TRP D 183           
SHEET    1   E 2 LEU I 225  TYR I 228  0                                        
SHEET    2   E 2 TYR I 233  CYS I 236 -1  N  TRP I 235   O  GLN I 226           
SHEET    1   F 2 LEU J 225  TYR J 228  0                                        
SHEET    2   F 2 TYR J 233  CYS J 236 -1  N  TRP J 235   O  GLN J 226           
SSBOND   1 CYS A   22    CYS A   65                          1555   1555  2.03  
SSBOND   2 CYS A   56    CYS A   98                          1555   1555  2.04  
SSBOND   3 CYS A  156    CYS B  209                          1555   1555  2.12  
SSBOND   4 CYS C   22    CYS C   65                          1555   1555  2.03  
SSBOND   5 CYS C   56    CYS C   98                          1555   1555  2.04  
SSBOND   6 CYS C  156    CYS D  209                          1555   1555  2.18  
SSBOND   7 CYS I  197    CYS I  216                          1555   1555  2.03  
SSBOND   8 CYS I  227    CYS I  234                          1555   1555  2.05  
SSBOND   9 CYS I  236    CYS I  255                          1555   1555  2.02  
SSBOND  10 CYS J  197    CYS J  216                          1555   1555  2.02  
SSBOND  11 CYS J  227    CYS J  234                          1555   1555  2.03  
SSBOND  12 CYS J  236    CYS J  255                          1555   1555  2.02  
LINK         C1  NAG I 100                 ND2 ASN I 240     1555   1555  1.46  
LINK         C1  NAG J 100                 ND2 ASN J 240     1555   1555  1.45  
SITE     1 ACT  4 CYS A  25  HIS A 163  CYS C  25  HIS C 163                    
CRYST1   62.592   80.594   64.245  90.00  96.77  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015976  0.000000  0.001896        0.00000                         
SCALE2      0.000000  0.012408  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015675        0.00000                         
MTRIX1   1  0.967984 -0.116869  0.222146      -27.30000    1                    
MTRIX2   1 -0.108483 -0.992859 -0.049626      -12.94000    1                    
MTRIX3   1  0.226359  0.023938 -0.973750       22.04000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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