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Database: PDB
Entry: 1GHQ
LinkDB: 1GHQ
Original site: 1GHQ 
HEADER    IMMUNE SYSTEM/VIRAL PROTEIN RECEPTOR    11-JAN-01   1GHQ              
TITLE     CR2-C3D COMPLEX STRUCTURE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C3;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: FRAGMENT OF ALPHA CHAIN;                                   
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CR2/CD121/C3D/EPSTEIN-BARR VIRUS RECEPTOR;                 
COMPND   8 CHAIN: B, C;                                                         
COMPND   9 FRAGMENT: SEQUENCE DATABASE RESIDUES 21-153                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606                                                 
KEYWDS    CR2, C3D, IMMUNE SYSTEM-VIRAL PROTEIN RECEPTOR COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SZAKONYI,J.M.GUTHRIDGE,D.LI,V.M.HOLERS,X.S.CHEN                     
REVDAT   4   27-OCT-21 1GHQ    1       REMARK SEQADV HETSYN                     
REVDAT   3   29-JUL-20 1GHQ    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE   ATOM                       
REVDAT   2   24-FEB-09 1GHQ    1       VERSN                                    
REVDAT   1   13-JUN-01 1GHQ    0                                                
JRNL        AUTH   G.SZAKONYI,J.M.GUTHRIDGE,D.LI,K.YOUNG,V.M.HOLERS,X.S.CHEN    
JRNL        TITL   STRUCTURE OF COMPLEMENT RECEPTOR 2 IN COMPLEX WITH ITS C3D   
JRNL        TITL 2 LIGAND.                                                      
JRNL        REF    SCIENCE                       V. 292  1725 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11387479                                                     
JRNL        DOI    10.1126/SCIENCE.1059118                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 255000                         
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 SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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            : 4434                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 666                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.90                          
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 15.00                           
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1GHQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000001525.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 287; NULL                          
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; NSLS                          
REMARK 200  BEAMLINE                       : 14-BM-C; X4A                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; NULL                          
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL; NULL                         
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 260000                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
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; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       85.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       49.07477            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       58.00000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       85.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       49.07477            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       58.00000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       85.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       49.07477            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       58.00000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       85.00000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       49.07477            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       58.00000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       85.00000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       49.07477            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       58.00000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       85.00000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       49.07477            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       58.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       98.14955            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      116.00000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       98.14955            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      116.00000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       98.14955            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      116.00000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       98.14955            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      116.00000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       98.14955            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      116.00000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       98.14955            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      116.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A   308                                                      
REMARK 465     VAL B   130                                                      
REMARK 465     PHE B   131                                                      
REMARK 465     PRO B   132                                                      
REMARK 465     LEU B   133                                                      
REMARK 465     GLU B   134                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A   1    CG   SD   CE                                        
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     LEU C  124   CD2                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU C   133     N    GLU C   134              1.60            
REMARK 500   ND1  HIS A   133     OE2  GLU A   135              2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C   757     O    HOH C   757     4555     1.41            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 135   CB    GLU A 135   CG      0.267                       
REMARK 500    GLU A 135   CG    GLU A 135   CD      0.149                       
REMARK 500    GLU A 135   CD    GLU A 135   OE1    -0.070                       
REMARK 500    SER C   6   CB    SER C   6   OG     -0.135                       
REMARK 500    PRO C  21   CD    PRO C  21   N      -0.252                       
REMARK 500    SER C  33   CA    SER C  33   CB      0.102                       
REMARK 500    GLU C  74   CB    GLU C  74   CG     -0.214                       
REMARK 500    LEU C 133   C     GLU C 134   N      -0.327                       
REMARK 500    GLU C 134   C     GLU C 134   O       0.244                       
REMARK 500    GLU C 134   C     GLU C 134   OXT    -0.129                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 135   CG  -  CD  -  OE1 ANGL. DEV. = -13.0 DEGREES          
REMARK 500    GLU A 135   CG  -  CD  -  OE2 ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO C  21   N   -  CD  -  CG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    SER C  33   CB  -  CA  -  C   ANGL. DEV. =  20.8 DEGREES          
REMARK 500    GLU C  74   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LYS C 100   O   -  C   -  N   ANGL. DEV. =   9.9 DEGREES          
REMARK 500    THR C 101   O   -  C   -  N   ANGL. DEV. = -11.4 DEGREES          
REMARK 500    LEU C 133   CA  -  C   -  N   ANGL. DEV. =  30.9 DEGREES          
REMARK 500    LEU C 133   O   -  C   -  N   ANGL. DEV. = -31.6 DEGREES          
REMARK 500    GLU C 134   C   -  N   -  CA  ANGL. DEV. =  51.1 DEGREES          
REMARK 500    GLU C 134   CA  -  C   -  O   ANGL. DEV. = -14.7 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    SER A  71        4.77     81.49                                   
REMARK 500    ALA A 129       84.63   -150.67                                   
REMARK 500    GLU A 145       35.64     70.28                                   
REMARK 500    LYS A 224       19.05     54.84                                   
REMARK 500    LYS A 232       61.93     65.44                                   
REMARK 500    GLN A 233       43.38    -85.17                                   
REMARK 500    SER B  33      179.71    -53.71                                   
REMARK 500    VAL B  52      -52.46   -127.09                                   
REMARK 500    VAL C  52      -56.63   -127.58                                   
REMARK 500    ASN C 102        9.89     80.28                                   
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 802  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 117   OE2                                                    
REMARK 620 2 GLU A 117   OE1  52.5                                              
REMARK 620 3 HOH A1108   O    85.7  79.4                                        
REMARK 620 4 HOH B 922   O   100.9 153.2  96.7                                  
REMARK 620 N                    1     2     3                                   
DBREF  1GHQ A    3   308  UNP    P01024   CO3_HUMAN      996   1300             
DBREF  1GHQ B    2   134  UNP    P20023   CR2_HUMAN       21    153             
DBREF  1GHQ C    2   134  UNP    P20023   CR2_HUMAN       21    153             
SEQADV 1GHQ MET A    1  UNP  P01024              CLONING ARTIFACT               
SEQADV 1GHQ LEU A    2  UNP  P01024              CLONING ARTIFACT               
SEQADV 1GHQ ALA A   17  UNP  P01024    CYS  1010 ENGINEERED MUTATION            
SEQADV 1GHQ SER A  295  UNP  P01024              INSERTION                      
SEQADV 1GHQ ALA B    1  UNP  P20023              CLONING ARTIFACT               
SEQADV 1GHQ ALA C    1  UNP  P20023              CLONING ARTIFACT               
SEQRES   1 A  308  MET LEU ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR          
SEQRES   2 A  308  PRO SER GLY ALA GLY GLU GLN ASN MET ILE GLY MET THR          
SEQRES   3 A  308  PRO THR VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU          
SEQRES   4 A  308  GLN TRP GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA          
SEQRES   5 A  308  LEU GLU LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA          
SEQRES   6 A  308  PHE ARG GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS          
SEQRES   7 A  308  ARG ALA PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS          
SEQRES   8 A  308  VAL PHE SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER          
SEQRES   9 A  308  GLN VAL LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU          
SEQRES  10 A  308  LYS GLN LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO          
SEQRES  11 A  308  VAL ILE HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN          
SEQRES  12 A  308  ASN GLU LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE          
SEQRES  13 A  308  SER LEU GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL          
SEQRES  14 A  308  ASN SER LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE          
SEQRES  15 A  308  LEU GLU ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR          
SEQRES  16 A  308  VAL ALA ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG          
SEQRES  17 A  308  LEU LYS GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA          
SEQRES  18 A  308  LYS ASP LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU          
SEQRES  19 A  308  TYR ASN VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU          
SEQRES  20 A  308  LEU GLN LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL          
SEQRES  21 A  308  ARG TRP LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR          
SEQRES  22 A  308  GLY SER THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU          
SEQRES  23 A  308  ALA GLN TYR GLN LYS ASP ALA PRO SER ASP HIS GLN GLU          
SEQRES  24 A  308  LEU ASN LEU ASP VAL SER LEU GLN LEU                          
SEQRES   1 B  134  ALA ILE SER CYS GLY SER PRO PRO PRO ILE LEU ASN GLY          
SEQRES   2 B  134  ARG ILE SER TYR TYR SER THR PRO ILE ALA VAL GLY THR          
SEQRES   3 B  134  VAL ILE ARG TYR SER CYS SER GLY THR PHE ARG LEU ILE          
SEQRES   4 B  134  GLY GLU LYS SER LEU LEU CYS ILE THR LYS ASP LYS VAL          
SEQRES   5 B  134  ASP GLY THR TRP ASP LYS PRO ALA PRO LYS CYS GLU TYR          
SEQRES   6 B  134  PHE ASN LYS TYR SER SER CYS PRO GLU PRO ILE VAL PRO          
SEQRES   7 B  134  GLY GLY TYR LYS ILE ARG GLY SER THR PRO TYR ARG HIS          
SEQRES   8 B  134  GLY ASP SER VAL THR PHE ALA CYS LYS THR ASN PHE SER          
SEQRES   9 B  134  MET ASN GLY ASN LYS SER VAL TRP CYS GLN ALA ASN ASN          
SEQRES  10 B  134  MET TRP GLY PRO THR ARG LEU PRO THR CYS VAL SER VAL          
SEQRES  11 B  134  PHE PRO LEU GLU                                              
SEQRES   1 C  134  ALA ILE SER CYS GLY SER PRO PRO PRO ILE LEU ASN GLY          
SEQRES   2 C  134  ARG ILE SER TYR TYR SER THR PRO ILE ALA VAL GLY THR          
SEQRES   3 C  134  VAL ILE ARG TYR SER CYS SER GLY THR PHE ARG LEU ILE          
SEQRES   4 C  134  GLY GLU LYS SER LEU LEU CYS ILE THR LYS ASP LYS VAL          
SEQRES   5 C  134  ASP GLY THR TRP ASP LYS PRO ALA PRO LYS CYS GLU TYR          
SEQRES   6 C  134  PHE ASN LYS TYR SER SER CYS PRO GLU PRO ILE VAL PRO          
SEQRES   7 C  134  GLY GLY TYR LYS ILE ARG GLY SER THR PRO TYR ARG HIS          
SEQRES   8 C  134  GLY ASP SER VAL THR PHE ALA CYS LYS THR ASN PHE SER          
SEQRES   9 C  134  MET ASN GLY ASN LYS SER VAL TRP CYS GLN ALA ASN ASN          
SEQRES  10 C  134  MET TRP GLY PRO THR ARG LEU PRO THR CYS VAL SER VAL          
SEQRES  11 C  134  PHE PRO LEU GLU                                              
HET     ZN  A 802       1                                                       
HET    NDG  B 702      15                                                       
HET     ZN  B 801       1                                                       
HET    NDG  C 701      15                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                        
HETSYN     NDG N-ACETYL-ALPHA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-               
HETSYN   2 NDG  ALPHA-D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-              
HETSYN   3 NDG  ACETAMIDO-2-DEOXY-GLUCOSE; 2-(ACETYLAMINO)-2-DEOXY-A-           
HETSYN   4 NDG  D-GLUCOPYRANOSE                                                 
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5  NDG    2(C8 H15 N O6)                                               
FORMUL   8  HOH   *666(H2 O)                                                    
HELIX    1   1 ASP A    3  HIS A    9  1                                   7    
HELIX    2   2 GLU A   19  GLU A   39  1                                  21    
HELIX    3   3 GLN A   40  GLY A   45  1                                   6    
HELIX    4   4 LYS A   48  ALA A   65  1                                  18    
HELIX    5   5 SER A   82  VAL A   97  1                                  16    
HELIX    6   6 ASP A  103  GLN A  119  1                                  17    
HELIX    7   7 HIS A  133  GLY A  138  5                                   6    
HELIX    8   8 ILE A  137  ASN A  142  5                                   6    
HELIX    9   9 GLU A  145  GLU A  166  1                                  22    
HELIX   10  10 SER A  171  TYR A  187  1                                  17    
HELIX   11  11 MET A  188  LEU A  190  5                                   3    
HELIX   12  12 ARG A  192  MET A  206  1                                  15    
HELIX   13  13 LYS A  210  ALA A  221  1                                  12    
HELIX   14  14 ASP A  223  ASN A  225  5                                   3    
HELIX   15  15 TYR A  235  LYS A  251  1                                  17    
HELIX   16  16 PHE A  255  GLN A  266  1                                  12    
HELIX   17  17 SER A  275  ALA A  293  1                                  19    
HELIX   18  18 PRO A  294  ASP A  296  5                                   3    
SHEET    1   A 2 SER B   3  CYS B   4  0                                        
SHEET    2   A 2 ILE B  22  ALA B  23 -1  O  ILE B  22   N  CYS B   4           
SHEET    1   B 4 GLY B  13  ILE B  15  0                                        
SHEET    2   B 4 VAL B  27  CYS B  32 -1  O  SER B  31   N  ARG B  14           
SHEET    3   B 4 SER B  43  ILE B  47 -1  O  LEU B  44   N  ILE B  28           
SHEET    4   B 4 THR B  55  TRP B  56 -1  O  THR B  55   N  ILE B  47           
SHEET    1   C 2 PHE B  36  ILE B  39  0                                        
SHEET    2   C 2 LYS B  62  TYR B  65 -1  O  LYS B  62   N  ILE B  39           
SHEET    1   D 3 GLY B  80  ARG B  84  0                                        
SHEET    2   D 3 SER B  94  CYS B  99 -1  O  THR B  96   N  ILE B  83           
SHEET    3   D 3 SER B 110  TRP B 112 -1  O  VAL B 111   N  VAL B  95           
SHEET    1   E 2 SER B 104  ASN B 106  0                                        
SHEET    2   E 2 THR B 126  VAL B 128 -1  N  THR B 126   O  ASN B 106           
SHEET    1   F 2 SER C   3  CYS C   4  0                                        
SHEET    2   F 2 ILE C  22  ALA C  23 -1  O  ILE C  22   N  CYS C   4           
SHEET    1   G 4 GLY C  13  ILE C  15  0                                        
SHEET    2   G 4 VAL C  27  CYS C  32 -1  O  SER C  31   N  ARG C  14           
SHEET    3   G 4 SER C  43  ILE C  47 -1  O  LEU C  44   N  ILE C  28           
SHEET    4   G 4 THR C  55  TRP C  56 -1  N  THR C  55   O  ILE C  47           
SHEET    1   H 2 PHE C  36  ILE C  39  0                                        
SHEET    2   H 2 LYS C  62  TYR C  65 -1  O  LYS C  62   N  ILE C  39           
SHEET    1   I 2 SER C  71  CYS C  72  0                                        
SHEET    2   I 2 TYR C  89  ARG C  90 -1  O  TYR C  89   N  CYS C  72           
SHEET    1   J 3 GLY C  80  ARG C  84  0                                        
SHEET    2   J 3 SER C  94  CYS C  99 -1  O  THR C  96   N  ILE C  83           
SHEET    3   J 3 SER C 110  TRP C 112 -1  N  VAL C 111   O  VAL C  95           
SHEET    1   K 2 PHE C 103  ASN C 106  0                                        
SHEET    2   K 2 THR C 126  SER C 129 -1  O  THR C 126   N  ASN C 106           
SSBOND   1 CYS A  108    CYS A  165                          1555   1555  2.04  
SSBOND   2 CYS B    4    CYS B   46                          1555   1555  2.03  
SSBOND   3 CYS B   32    CYS B   63                          1555   1555  2.02  
SSBOND   4 CYS B   72    CYS B  113                          1555   1555  2.04  
SSBOND   5 CYS B   99    CYS B  127                          1555   1555  2.03  
SSBOND   6 CYS C    4    CYS C   46                          1555   1555  2.04  
SSBOND   7 CYS C   32    CYS C   63                          1555   1555  2.01  
SSBOND   8 CYS C   72    CYS C  113                          1555   1555  2.04  
SSBOND   9 CYS C   99    CYS C  127                          1555   1555  2.02  
LINK         OE2 GLU A 117                ZN    ZN A 802     1555   1555  2.58  
LINK         OE1 GLU A 117                ZN    ZN A 802     1555   1555  2.40  
LINK        ZN    ZN A 802                 O   HOH A1108     1555   1555  2.35  
LINK        ZN    ZN A 802                 O   HOH B 922     1555   1555  2.44  
CISPEP   1 THR B   20    PRO B   21          0         0.44                     
CISPEP   2 THR B   87    PRO B   88          0        -0.49                     
CISPEP   3 THR C   20    PRO C   21          0         4.17                     
CISPEP   4 THR C   87    PRO C   88          0        -0.24                     
CISPEP   5 LEU C  133    GLU C  134          0        27.21                     
CRYST1  170.000  170.000  174.000  90.00  90.00 120.00 H 3 2        36          
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      0.005882  0.003396  0.000000        0.00000                         
SCALE2      0.000000  0.006792  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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