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Database: PDB
Entry: 5DSU
LinkDB: 5DSU
Original site: 5DSU 
HEADER    SIGNALING PROTEIN                       17-SEP-15   5DSU              
TITLE     CRYSTAL STRUCTURE OF DOUBLE MUTANT OF N-DOMAIN OF HUMAN CALMODULIN    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 3-78;                                         
COMPND   5 SYNONYM: CAM;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,      
SOURCE   6 CAM3, CAMC, CAMIII;                                                  
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET3A                                     
KEYWDS    CA2+ BINDING PROTEIN EF-HAND DOMAIN, SIGNALING PROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ABABOU,M.ZALESKA                                                    
REVDAT   4   10-JAN-24 5DSU    1       REMARK                                   
REVDAT   3   12-APR-17 5DSU    1       JRNL                                     
REVDAT   2   05-APR-17 5DSU    1       JRNL                                     
REVDAT   1   11-JAN-17 5DSU    0                                                
JRNL        AUTH   A.ABABOU,M.ZALESKA,M.PFUHL                                   
JRNL        TITL   ON THE CA(2+) BINDING AND CONFORMATIONAL CHANGE IN EF-HAND   
JRNL        TITL 2 DOMAINS: EXPERIMENTAL EVIDENCE OF CA(2+)-SATURATED           
JRNL        TITL 3 INTERMEDIATES OF N-DOMAIN OF CALMODULIN.                     
JRNL        REF    BIOCHIM. BIOPHYS. ACTA        V.1865   640 2017              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   28288938                                                     
JRNL        DOI    10.1016/J.BBAPAP.2017.03.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 5544                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.550                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 252                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 20.9936 -  2.4310    0.99     2709   133  0.2179 0.2413        
REMARK   3     2  2.4310 -  1.9300    0.99     2583   119  0.2619 0.3478        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.10                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.390           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012            599                                  
REMARK   3   ANGLE     :  1.312            800                                  
REMARK   3   CHIRALITY :  0.084             91                                  
REMARK   3   PLANARITY :  0.004            105                                  
REMARK   3   DIHEDRAL  : 18.653            231                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213741.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5544                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.992                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1CLL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 37% PEG 400, 100 MM HEPES, 250 MM        
REMARK 280  CACL2, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-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       54.13333            
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       27.06667            
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       27.06667            
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       54.13333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 440 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 5260 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     TYR A    78                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   203     O    HOH A   226     2444     2.18            
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                              CA A 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASP A  22   OD1  79.8                                              
REMARK 620 3 ASP A  24   OD1  99.9  81.4                                        
REMARK 620 4 THR A  26   O    88.9 163.6  88.9                                  
REMARK 620 5 GLU A  31   OE1  81.7  70.2 150.9 120.2                            
REMARK 620 6 GLU A  31   OE2  99.2 115.5 156.5  77.9  46.5                      
REMARK 620 7 HOH A 211   O   160.0  82.8  87.1 110.1  83.2  79.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 ASP A  58   OD1  83.0                                              
REMARK 620 3 ASN A  60   OD1  89.4  76.5                                        
REMARK 620 4 THR A  62   O    92.7 155.1  79.0                                  
REMARK 620 5 GLU A  67   OE1 105.2 126.7 153.3  78.1                            
REMARK 620 6 GLU A  67   OE2  92.3  77.3 153.4 127.4  50.2                      
REMARK 620 7 HOH A 237   O   167.2 101.0  79.8  78.6  82.3 100.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 103                 
DBREF  5DSU A    2    77  UNP    P62158   CALM_HUMAN       3     78             
SEQADV 5DSU MET A    1  UNP  P62158              INITIATING METHIONINE          
SEQADV 5DSU TYR A   19  UNP  P62158    PHE    20 ENGINEERED MUTATION            
SEQADV 5DSU LEU A   41  UNP  P62158    GLN    42 ENGINEERED MUTATION            
SEQADV 5DSU ILE A   75  UNP  P62158    LYS    76 ENGINEERED MUTATION            
SEQADV 5DSU TYR A   78  UNP  P62158              EXPRESSION TAG                 
SEQRES   1 A   78  MET ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS          
SEQRES   2 A   78  GLU ALA PHE SER LEU TYR ASP LYS ASP GLY ASP GLY THR          
SEQRES   3 A   78  ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU          
SEQRES   4 A   78  GLY LEU ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE          
SEQRES   5 A   78  ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE          
SEQRES   6 A   78  PRO GLU PHE LEU THR MET MET ALA ARG ILE MET LYS TYR          
HET     CA  A 101       1                                                       
HET     CA  A 102       1                                                       
HET    PGE  A 103      10                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     PGE TRIETHYLENE GLYCOL                                               
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  PGE    C6 H14 O4                                                    
FORMUL   5  HOH   *56(H2 O)                                                     
HELIX    1 AA1 THR A    5  ASP A   20  1                                  16    
HELIX    2 AA2 THR A   28  LEU A   39  1                                  12    
HELIX    3 AA3 THR A   44  ASP A   56  1                                  13    
HELIX    4 AA4 ASP A   64  LYS A   77  1                                  14    
LINK         OD1 ASP A  20                CA    CA A 101     1555   1555  2.16  
LINK         OD1 ASP A  22                CA    CA A 101     1555   1555  2.51  
LINK         OD1 ASP A  24                CA    CA A 101     1555   1555  2.33  
LINK         O   THR A  26                CA    CA A 101     1555   1555  2.33  
LINK         OE1 GLU A  31                CA    CA A 101     1555   1555  2.84  
LINK         OE2 GLU A  31                CA    CA A 101     1555   1555  2.71  
LINK         OD1 ASP A  56                CA    CA A 102     1555   1555  2.28  
LINK         OD1 ASP A  58                CA    CA A 102     1555   1555  2.51  
LINK         OD1 ASN A  60                CA    CA A 102     1555   1555  2.30  
LINK         O   THR A  62                CA    CA A 102     1555   1555  2.38  
LINK         OE1 GLU A  67                CA    CA A 102     1555   1555  2.56  
LINK         OE2 GLU A  67                CA    CA A 102     1555   1555  2.63  
LINK        CA    CA A 101                 O   HOH A 211     1555   1555  2.28  
LINK        CA    CA A 102                 O   HOH A 237     1555   1555  2.66  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 211                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 237                                          
SITE     1 AC3  4 TYR A  19  LEU A  39  MET A  72  ILE A  75                    
CRYST1   38.400   38.400   81.200  90.00  90.00 120.00 P 32 2 1      6          
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      0.026042  0.015035  0.000000        0.00000                         
SCALE2      0.000000  0.030070  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012315        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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