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Database: PDB
Entry: 4ZRQ
LinkDB: 4ZRQ
Original site: 4ZRQ 
HEADER    TRANSPORT PROTEIN                       12-MAY-15   4ZRQ              
TITLE     E88 DELETION MUTANT OF CD320 IN COMPLEX WITH TC2                      
CAVEAT     4ZRQ                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCOBALAMIN-2;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TC-2,TRANSCOBALAMIN II,TCII;                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CD320 ANTIGEN;                                             
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: RESIDUES 53-171;                                           
COMPND  10 SYNONYM: 8D6 ANTIGEN,FDC-SIGNALING MOLECULE 8D6,FDC-SM-8D6,          
COMPND  11 TRANSCOBALAMIN RECEPTOR,TCBLR;                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 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: TCN2, TC2;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: UNIDENTIFIED BACULOVIRUS;                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: CD320, 8D6A, UNQ198/PRO224;                                    
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  18 EXPRESSION_SYSTEM_VECTOR: UNIDENTIFIED BACULOVIRUS                   
KEYWDS    LDLR-R, VITAMIN TRANSPORTER, TRANSPORT PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ALAM,K.P.LOCHER                                                     
REVDAT   3   10-OCT-18 4ZRQ    1       COMPND SOURCE                            
REVDAT   2   27-JUL-16 4ZRQ    1       JRNL                                     
REVDAT   1   20-JUL-16 4ZRQ    0                                                
JRNL        AUTH   A.ALAM,J.S.WOO,J.SCHMITZ,B.PRINZ,K.ROOT,F.CHEN,J.S.BLOCH,    
JRNL        AUTH 2 R.ZENOBI,K.P.LOCHER                                          
JRNL        TITL   STRUCTURAL BASIS OF TRANSCOBALAMIN RECOGNITION BY HUMAN      
JRNL        TITL 2 CD320 RECEPTOR.                                              
JRNL        REF    NAT COMMUN                    V.   7 12100 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   27411955                                                     
JRNL        DOI    10.1038/NCOMMS12100                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 54979                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2731                            
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 29.4359 -  7.0270    0.99     2856   161  0.1456 0.1555        
REMARK   3     2  7.0270 -  5.5901    1.00     2732   135  0.1936 0.2405        
REMARK   3     3  5.5901 -  4.8871    1.00     2645   167  0.1770 0.2148        
REMARK   3     4  4.8871 -  4.4419    1.00     2663   129  0.1499 0.1895        
REMARK   3     5  4.4419 -  4.1244    1.00     2649   113  0.1638 0.1810        
REMARK   3     6  4.1244 -  3.8818    1.00     2617   149  0.1670 0.1992        
REMARK   3     7  3.8818 -  3.6878    1.00     2599   137  0.1958 0.2192        
REMARK   3     8  3.6878 -  3.5276    1.00     2615   127  0.2076 0.2376        
REMARK   3     9  3.5276 -  3.3920    1.00     2582   127  0.2290 0.2778        
REMARK   3    10  3.3920 -  3.2751    1.00     2595   144  0.2439 0.2797        
REMARK   3    11  3.2751 -  3.1728    1.00     2557   145  0.2442 0.2768        
REMARK   3    12  3.1728 -  3.0822    1.00     2584   142  0.2607 0.2967        
REMARK   3    13  3.0822 -  3.0011    1.00     2607   133  0.2587 0.3019        
REMARK   3    14  3.0011 -  2.9280    1.00     2593   108  0.2624 0.3016        
REMARK   3    15  2.9280 -  2.8615    1.00     2551   161  0.2808 0.3093        
REMARK   3    16  2.8615 -  2.8006    1.00     2559   130  0.2788 0.3394        
REMARK   3    17  2.8006 -  2.7446    1.00     2583   122  0.2756 0.2960        
REMARK   3    18  2.7446 -  2.6929    1.00     2556   147  0.2851 0.3417        
REMARK   3    19  2.6929 -  2.6448    1.00     2555   119  0.2939 0.3073        
REMARK   3    20  2.6448 -  2.6000    1.00     2550   135  0.3081 0.3898        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.520           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.47                          
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      :  0.007           7702                                  
REMARK   3   ANGLE     :  1.886          10490                                  
REMARK   3   CHIRALITY :  0.122           1178                                  
REMARK   3   PLANARITY :  0.008           1332                                  
REMARK   3   DIHEDRAL  : 13.699           2808                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 409 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1962 -47.2355 -39.7263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5598 T22:   0.3196                                     
REMARK   3      T33:   0.2860 T12:   0.0504                                     
REMARK   3      T13:   0.0045 T23:   0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0841 L22:   1.7106                                     
REMARK   3      L33:   2.9400 L12:   1.3772                                     
REMARK   3      L13:   1.5916 L23:   0.7957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1932 S12:  -0.2816 S13:  -0.0873                       
REMARK   3      S21:   0.2175 S22:  -0.1365 S23:   0.0455                       
REMARK   3      S31:   0.1309 S32:   0.0117 S33:  -0.0538                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 409 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7640 -28.8161  -0.9100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3985 T22:   0.4652                                     
REMARK   3      T33:   0.2952 T12:   0.0163                                     
REMARK   3      T13:  -0.0113 T23:   0.0730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3661 L22:   3.0353                                     
REMARK   3      L33:   4.5354 L12:   1.5827                                     
REMARK   3      L13:   1.4207 L23:   1.7117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1539 S12:   0.0987 S13:   0.1789                       
REMARK   3      S21:  -0.3773 S22:   0.0914 S23:   0.0356                       
REMARK   3      S31:  -0.0690 S32:   0.2212 S33:   0.0673                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 53 THROUGH 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6599 -68.1179 -27.0565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3868 T22:   1.1503                                     
REMARK   3      T33:   1.7086 T12:   0.1842                                     
REMARK   3      T13:  -0.1072 T23:   0.3592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1465 L22:   8.1804                                     
REMARK   3      L33:   5.7063 L12:   6.0698                                     
REMARK   3      L13:   1.5943 L23:  -1.6735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1239 S12:  -1.4070 S13:  -2.8628                       
REMARK   3      S21:   1.9065 S22:  -0.3786 S23:  -2.3962                       
REMARK   3      S31:   1.3346 S32:   0.7814 S33:   0.2550                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 171 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7629 -40.8478 -38.4217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8006 T22:   1.0188                                     
REMARK   3      T33:   0.7890 T12:  -0.0070                                     
REMARK   3      T13:   0.0530 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8087 L22:   7.8048                                     
REMARK   3      L33:   2.0091 L12:  -3.9920                                     
REMARK   3      L13:  -5.2405 L23:   4.1239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4724 S12:   0.2942 S13:  -0.0213                       
REMARK   3      S21:  -0.6662 S22:   0.0643 S23:  -1.8256                       
REMARK   3      S31:  -0.9970 S32:   1.3860 S33:  -0.5179                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 53 THROUGH 85 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1109 -53.1267 -16.3080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0147 T22:   1.4243                                     
REMARK   3      T33:   1.2252 T12:   0.1416                                     
REMARK   3      T13:   0.1372 T23:  -0.3821                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5830 L22:   9.9825                                     
REMARK   3      L33:   6.2584 L12:   4.3647                                     
REMARK   3      L13:  -3.8232 L23:   0.5897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3264 S12:   1.8625 S13:  -1.5796                       
REMARK   3      S21:  -1.0258 S22:   0.7125 S23:  -2.3199                       
REMARK   3      S31:   0.9619 S32:   0.7462 S33:  -0.3887                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 129 THROUGH 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4167 -59.8983  -3.2384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1167 T22:   0.7521                                     
REMARK   3      T33:   0.6902 T12:  -0.1511                                     
REMARK   3      T13:  -0.1287 T23:   0.1058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3452 L22:   6.7478                                     
REMARK   3      L33:   3.8454 L12:  -3.6515                                     
REMARK   3      L13:   1.3321 L23:  -2.2009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3482 S12:  -0.5253 S13:  -1.4076                       
REMARK   3      S21:  -0.1183 S22:   0.4472 S23:   0.4027                       
REMARK   3      S31:   2.0794 S32:  -0.4207 S33:  -0.7922                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 3651                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 594                                         
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4ZRQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209772.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54979                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.434                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.62000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
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   (%): 66.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, L-PROLINE, HEPES, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      178.17050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       49.20200            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.20200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      267.25575            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.20200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       49.20200            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       89.08525            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       49.20200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.20200            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      267.25575            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       49.20200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.20200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       89.08525            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      178.17050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     PHE A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     ASP A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     ASP A    77                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     SER B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     PHE B    71                                                      
REMARK 465     SER B    72                                                      
REMARK 465     GLU B    73                                                      
REMARK 465     ASP B    74                                                      
REMARK 465     ASP B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     ASP B    77                                                      
REMARK 465     GLU C    87                                                      
REMARK 465     GLU C    88                                                      
REMARK 465     CYS C    89                                                      
REMARK 465     ARG C    90                                                      
REMARK 465     ILE C    91                                                      
REMARK 465     GLU C    92                                                      
REMARK 465     PRO C    93                                                      
REMARK 465     CYS C    94                                                      
REMARK 465     THR C    95                                                      
REMARK 465     GLN C    96                                                      
REMARK 465     LYS C    97                                                      
REMARK 465     GLY C    98                                                      
REMARK 465     GLN C    99                                                      
REMARK 465     CYS C   100                                                      
REMARK 465     PRO C   101                                                      
REMARK 465     PRO C   102                                                      
REMARK 465     PRO C   103                                                      
REMARK 465     PRO C   104                                                      
REMARK 465     GLY C   105                                                      
REMARK 465     LEU C   106                                                      
REMARK 465     PRO C   107                                                      
REMARK 465     CYS C   108                                                      
REMARK 465     PRO C   109                                                      
REMARK 465     CYS C   110                                                      
REMARK 465     THR C   111                                                      
REMARK 465     GLY C   112                                                      
REMARK 465     VAL C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     ASP C   115                                                      
REMARK 465     CYS C   116                                                      
REMARK 465     SER C   117                                                      
REMARK 465     GLY C   118                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     THR C   120                                                      
REMARK 465     ASP C   121                                                      
REMARK 465     LYS C   122                                                      
REMARK 465     LYS C   123                                                      
REMARK 465     LEU C   124                                                      
REMARK 465     ARG C   125                                                      
REMARK 465     ASN C   126                                                      
REMARK 465     CYS C   127                                                      
REMARK 465     SER C   128                                                      
REMARK 465     GLU D    87                                                      
REMARK 465     GLU D    88                                                      
REMARK 465     CYS D    89                                                      
REMARK 465     ARG D    90                                                      
REMARK 465     ILE D    91                                                      
REMARK 465     GLU D    92                                                      
REMARK 465     PRO D    93                                                      
REMARK 465     CYS D    94                                                      
REMARK 465     THR D    95                                                      
REMARK 465     GLN D    96                                                      
REMARK 465     LYS D    97                                                      
REMARK 465     GLY D    98                                                      
REMARK 465     GLN D    99                                                      
REMARK 465     CYS D   100                                                      
REMARK 465     PRO D   101                                                      
REMARK 465     PRO D   102                                                      
REMARK 465     PRO D   103                                                      
REMARK 465     PRO D   104                                                      
REMARK 465     GLY D   105                                                      
REMARK 465     LEU D   106                                                      
REMARK 465     PRO D   107                                                      
REMARK 465     CYS D   108                                                      
REMARK 465     PRO D   109                                                      
REMARK 465     CYS D   110                                                      
REMARK 465     THR D   111                                                      
REMARK 465     GLY D   112                                                      
REMARK 465     VAL D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     ASP D   115                                                      
REMARK 465     CYS D   116                                                      
REMARK 465     SER D   117                                                      
REMARK 465     GLY D   118                                                      
REMARK 465     GLY D   119                                                      
REMARK 465     THR D   120                                                      
REMARK 465     ASP D   121                                                      
REMARK 465     LYS D   122                                                      
REMARK 465     LYS D   123                                                      
REMARK 465     LEU D   124                                                      
REMARK 465     ARG D   125                                                      
REMARK 465     ASN D   126                                                      
REMARK 465     CYS D   127                                                      
REMARK 465     SER D   128                                                      
REMARK 465     GLU D   171                                                      
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     GLN A  79    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 126    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 129    CG   CD   CE   NZ                                   
REMARK 470     GLN A 170    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 309    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  79    CG   CD   OE1  NE2                                  
REMARK 470     HIS B 126    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 129    CG   CD   CE   NZ                                   
REMARK 470     GLU B 299    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  58    CG   CD   CE   NZ                                   
REMARK 470     GLN C  60    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C  66    CG   CD1  CD2                                       
REMARK 470     ARG C  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 171    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  58    CG   CD   CE   NZ                                   
REMARK 470     GLN D  60    CG   CD   OE1  NE2                                  
REMARK 470     ARG D  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  76    CG   CD   NE   CZ   NH1  NH2                        
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   OD2  ASP C    82     OG   SER C    84              1.92            
REMARK 500   NE2  GLN B   389     O    HOH B   603              1.94            
REMARK 500   OE2  GLU B     1     O    HOH B   601              2.09            
REMARK 500   ND1  HIS A   104     OD2  ASP C    77              2.10            
REMARK 500   OE1  GLU B   353     O    HOH B   604              2.12            
REMARK 500   O63  CNC B   501     O    HOH B   605              2.16            
REMARK 500   O44  CNC B   501     O    HOH B   606              2.17            
REMARK 500   SG   CYS A    65     CB   CYS A    78              2.18            
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    CYS A  78   CB    CYS A  78   SG      0.200                       
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    ILE B 329   CG1 -  CB  -  CG2 ANGL. DEV. = -27.6 DEGREES          
REMARK 500    LYS B 343   CD  -  CE  -  NZ  ANGL. DEV. = -18.7 DEGREES          
REMARK 500    ASP B 382   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    LEU C  70   CA  -  CB  -  CG  ANGL. DEV. =  23.1 DEGREES          
REMARK 500    SER C  81   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES          
REMARK 500    CYS D  67   CA  -  CB  -  SG  ANGL. DEV. =   7.1 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    GLN A  79      -81.56   -119.05                                   
REMARK 500    THR A 134      -88.51   -109.97                                   
REMARK 500    THR B 134      -88.31   -110.20                                   
REMARK 500    PHE B 168       64.88   -105.44                                   
REMARK 500    ARG C  62       -7.19     82.43                                   
REMARK 500    ASP C  75       43.07    -88.37                                   
REMARK 500    SER C  81      -77.53     14.31                                   
REMARK 500    SER C  84       86.24    -66.58                                   
REMARK 500    THR D  57       46.87   -103.65                                   
REMARK 500    ASP D  75       39.46    -90.67                                   
REMARK 500    SER D  84       55.85   -115.36                                   
REMARK 500    THR D 169      -63.01   -106.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU B  166     PRO B  167                 -149.17                    
REMARK 500 CYS C   80     SER C   81                  135.46                    
REMARK 500 THR D   57     LYS D   58                  146.84                    
REMARK 500 THR D  169     ASN D  170                 -134.64                    
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 C 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP C  72   O                                                      
REMARK 620 2 ASP C  75   OD1  76.4                                              
REMARK 620 3 ASP C  77   O   142.8  79.6                                        
REMARK 620 4 ASP C  79   OD2  74.4  76.2  72.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP C 150   O                                                      
REMARK 620 2 ASP C 153   OD1  78.0                                              
REMARK 620 3 HIS C 155   O   166.0  88.1                                        
REMARK 620 4 ASP C 157   OD2 102.0  97.7  81.4                                  
REMARK 620 5 ASP C 163   OD2 104.7 170.5  88.8  90.6                            
REMARK 620 6 GLU C 164   OE2  89.4  70.7  84.2 161.9 100.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 202  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP D  72   O                                                      
REMARK 620 2 ASP D  75   OD1  89.5                                              
REMARK 620 3 ASP D  77   O   176.8  89.4                                        
REMARK 620 4 ASP D  79   OD2  99.7  87.5  83.3                                  
REMARK 620 5 ASP D  85   OD1  72.0 160.0 109.5  88.5                            
REMARK 620 6 ASP D  85   OD2 118.0 141.8  64.4  63.5  50.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 201  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP D 150   O                                                      
REMARK 620 2 ASP D 153   OD1  80.4                                              
REMARK 620 3 HIS D 155   O   167.5  87.1                                        
REMARK 620 4 ASP D 157   OD2 100.9  95.7  81.2                                  
REMARK 620 5 ASP D 163   OD2 109.1 168.8  83.2  88.2                            
REMARK 620 6 GLU D 164   OE2  90.8  75.2  85.0 163.8  98.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CNC A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CNC B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 202                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZRP   RELATED DB: PDB                                   
DBREF  4ZRQ A    1   409  UNP    P20062   TCO2_HUMAN      19    427             
DBREF  4ZRQ B    1   409  UNP    P20062   TCO2_HUMAN      19    427             
DBREF  4ZRQ C   53   171  UNP    Q9NPF0   CD320_HUMAN     53    171             
DBREF  4ZRQ D   53   171  UNP    Q9NPF0   CD320_HUMAN     53    171             
SEQADV 4ZRQ GLN A  209  UNP  P20062    ARG   227 CONFLICT                       
SEQADV 4ZRQ GLN B  209  UNP  P20062    ARG   227 CONFLICT                       
SEQADV 4ZRQ     C       UNP  Q9NPF0    GLU    86 DELETION                       
SEQADV 4ZRQ     D       UNP  Q9NPF0    GLU    86 DELETION                       
SEQRES   1 A  409  GLU MET CYS GLU ILE PRO GLU MET ASP SER HIS LEU VAL          
SEQRES   2 A  409  GLU LYS LEU GLY GLN HIS LEU LEU PRO TRP MET ASP ARG          
SEQRES   3 A  409  LEU SER LEU GLU HIS LEU ASN PRO SER ILE TYR VAL GLY          
SEQRES   4 A  409  LEU ARG LEU SER SER LEU GLN ALA GLY THR LYS GLU ASP          
SEQRES   5 A  409  LEU TYR LEU HIS SER LEU LYS LEU GLY TYR GLN GLN CYS          
SEQRES   6 A  409  LEU LEU GLY SER ALA PHE SER GLU ASP ASP GLY ASP CYS          
SEQRES   7 A  409  GLN GLY LYS PRO SER MET GLY GLN LEU ALA LEU TYR LEU          
SEQRES   8 A  409  LEU ALA LEU ARG ALA ASN CYS GLU PHE VAL ARG GLY HIS          
SEQRES   9 A  409  LYS GLY ASP ARG LEU VAL SER GLN LEU LYS TRP PHE LEU          
SEQRES  10 A  409  GLU ASP GLU LYS ARG ALA ILE GLY HIS ASP HIS LYS GLY          
SEQRES  11 A  409  HIS PRO HIS THR SER TYR TYR GLN TYR GLY LEU GLY ILE          
SEQRES  12 A  409  LEU ALA LEU CYS LEU HIS GLN LYS ARG VAL HIS ASP SER          
SEQRES  13 A  409  VAL VAL ASP LYS LEU LEU TYR ALA VAL GLU PRO PHE HIS          
SEQRES  14 A  409  GLN GLY HIS HIS SER VAL ASP THR ALA ALA MET ALA GLY          
SEQRES  15 A  409  LEU ALA PHE THR CYS LEU LYS ARG SER ASN PHE ASN PRO          
SEQRES  16 A  409  GLY ARG ARG GLN ARG ILE THR MET ALA ILE ARG THR VAL          
SEQRES  17 A  409  GLN GLU GLU ILE LEU LYS ALA GLN THR PRO GLU GLY HIS          
SEQRES  18 A  409  PHE GLY ASN VAL TYR SER THR PRO LEU ALA LEU GLN PHE          
SEQRES  19 A  409  LEU MET THR SER PRO MET ARG GLY ALA GLU LEU GLY THR          
SEQRES  20 A  409  ALA CYS LEU LYS ALA ARG VAL ALA LEU LEU ALA SER LEU          
SEQRES  21 A  409  GLN ASP GLY ALA PHE GLN ASN ALA LEU MET ILE SER GLN          
SEQRES  22 A  409  LEU LEU PRO VAL LEU ASN HIS LYS THR TYR ILE ASP LEU          
SEQRES  23 A  409  ILE PHE PRO ASP CYS LEU ALA PRO ARG VAL MET LEU GLU          
SEQRES  24 A  409  PRO ALA ALA GLU THR ILE PRO GLN THR GLN GLU ILE ILE          
SEQRES  25 A  409  SER VAL THR LEU GLN VAL LEU SER LEU LEU PRO PRO TYR          
SEQRES  26 A  409  ARG GLN SER ILE SER VAL LEU ALA GLY SER THR VAL GLU          
SEQRES  27 A  409  ASP VAL LEU LYS LYS ALA HIS GLU LEU GLY GLY PHE THR          
SEQRES  28 A  409  TYR GLU THR GLN ALA SER LEU SER GLY PRO TYR LEU THR          
SEQRES  29 A  409  SER VAL MET GLY LYS ALA ALA GLY GLU ARG GLU PHE TRP          
SEQRES  30 A  409  GLN LEU LEU ARG ASP PRO ASN THR PRO LEU LEU GLN GLY          
SEQRES  31 A  409  ILE ALA ASP TYR ARG PRO LYS ASP GLY GLU THR ILE GLU          
SEQRES  32 A  409  LEU ARG LEU VAL SER TRP                                      
SEQRES   1 B  409  GLU MET CYS GLU ILE PRO GLU MET ASP SER HIS LEU VAL          
SEQRES   2 B  409  GLU LYS LEU GLY GLN HIS LEU LEU PRO TRP MET ASP ARG          
SEQRES   3 B  409  LEU SER LEU GLU HIS LEU ASN PRO SER ILE TYR VAL GLY          
SEQRES   4 B  409  LEU ARG LEU SER SER LEU GLN ALA GLY THR LYS GLU ASP          
SEQRES   5 B  409  LEU TYR LEU HIS SER LEU LYS LEU GLY TYR GLN GLN CYS          
SEQRES   6 B  409  LEU LEU GLY SER ALA PHE SER GLU ASP ASP GLY ASP CYS          
SEQRES   7 B  409  GLN GLY LYS PRO SER MET GLY GLN LEU ALA LEU TYR LEU          
SEQRES   8 B  409  LEU ALA LEU ARG ALA ASN CYS GLU PHE VAL ARG GLY HIS          
SEQRES   9 B  409  LYS GLY ASP ARG LEU VAL SER GLN LEU LYS TRP PHE LEU          
SEQRES  10 B  409  GLU ASP GLU LYS ARG ALA ILE GLY HIS ASP HIS LYS GLY          
SEQRES  11 B  409  HIS PRO HIS THR SER TYR TYR GLN TYR GLY LEU GLY ILE          
SEQRES  12 B  409  LEU ALA LEU CYS LEU HIS GLN LYS ARG VAL HIS ASP SER          
SEQRES  13 B  409  VAL VAL ASP LYS LEU LEU TYR ALA VAL GLU PRO PHE HIS          
SEQRES  14 B  409  GLN GLY HIS HIS SER VAL ASP THR ALA ALA MET ALA GLY          
SEQRES  15 B  409  LEU ALA PHE THR CYS LEU LYS ARG SER ASN PHE ASN PRO          
SEQRES  16 B  409  GLY ARG ARG GLN ARG ILE THR MET ALA ILE ARG THR VAL          
SEQRES  17 B  409  GLN GLU GLU ILE LEU LYS ALA GLN THR PRO GLU GLY HIS          
SEQRES  18 B  409  PHE GLY ASN VAL TYR SER THR PRO LEU ALA LEU GLN PHE          
SEQRES  19 B  409  LEU MET THR SER PRO MET ARG GLY ALA GLU LEU GLY THR          
SEQRES  20 B  409  ALA CYS LEU LYS ALA ARG VAL ALA LEU LEU ALA SER LEU          
SEQRES  21 B  409  GLN ASP GLY ALA PHE GLN ASN ALA LEU MET ILE SER GLN          
SEQRES  22 B  409  LEU LEU PRO VAL LEU ASN HIS LYS THR TYR ILE ASP LEU          
SEQRES  23 B  409  ILE PHE PRO ASP CYS LEU ALA PRO ARG VAL MET LEU GLU          
SEQRES  24 B  409  PRO ALA ALA GLU THR ILE PRO GLN THR GLN GLU ILE ILE          
SEQRES  25 B  409  SER VAL THR LEU GLN VAL LEU SER LEU LEU PRO PRO TYR          
SEQRES  26 B  409  ARG GLN SER ILE SER VAL LEU ALA GLY SER THR VAL GLU          
SEQRES  27 B  409  ASP VAL LEU LYS LYS ALA HIS GLU LEU GLY GLY PHE THR          
SEQRES  28 B  409  TYR GLU THR GLN ALA SER LEU SER GLY PRO TYR LEU THR          
SEQRES  29 B  409  SER VAL MET GLY LYS ALA ALA GLY GLU ARG GLU PHE TRP          
SEQRES  30 B  409  GLN LEU LEU ARG ASP PRO ASN THR PRO LEU LEU GLN GLY          
SEQRES  31 B  409  ILE ALA ASP TYR ARG PRO LYS ASP GLY GLU THR ILE GLU          
SEQRES  32 B  409  LEU ARG LEU VAL SER TRP                                      
SEQRES   1 C  118  SER CYS PRO PRO THR LYS PHE GLN CYS ARG THR SER GLY          
SEQRES   2 C  118  LEU CYS VAL PRO LEU THR TRP ARG CYS ASP ARG ASP LEU          
SEQRES   3 C  118  ASP CYS SER ASP GLY SER ASP GLU GLU CYS ARG ILE GLU          
SEQRES   4 C  118  PRO CYS THR GLN LYS GLY GLN CYS PRO PRO PRO PRO GLY          
SEQRES   5 C  118  LEU PRO CYS PRO CYS THR GLY VAL SER ASP CYS SER GLY          
SEQRES   6 C  118  GLY THR ASP LYS LYS LEU ARG ASN CYS SER ARG LEU ALA          
SEQRES   7 C  118  CYS LEU ALA GLY GLU LEU ARG CYS THR LEU SER ASP ASP          
SEQRES   8 C  118  CYS ILE PRO LEU THR TRP ARG CYS ASP GLY HIS PRO ASP          
SEQRES   9 C  118  CYS PRO ASP SER SER ASP GLU LEU GLY CYS GLY THR ASN          
SEQRES  10 C  118  GLU                                                          
SEQRES   1 D  118  SER CYS PRO PRO THR LYS PHE GLN CYS ARG THR SER GLY          
SEQRES   2 D  118  LEU CYS VAL PRO LEU THR TRP ARG CYS ASP ARG ASP LEU          
SEQRES   3 D  118  ASP CYS SER ASP GLY SER ASP GLU GLU CYS ARG ILE GLU          
SEQRES   4 D  118  PRO CYS THR GLN LYS GLY GLN CYS PRO PRO PRO PRO GLY          
SEQRES   5 D  118  LEU PRO CYS PRO CYS THR GLY VAL SER ASP CYS SER GLY          
SEQRES   6 D  118  GLY THR ASP LYS LYS LEU ARG ASN CYS SER ARG LEU ALA          
SEQRES   7 D  118  CYS LEU ALA GLY GLU LEU ARG CYS THR LEU SER ASP ASP          
SEQRES   8 D  118  CYS ILE PRO LEU THR TRP ARG CYS ASP GLY HIS PRO ASP          
SEQRES   9 D  118  CYS PRO ASP SER SER ASP GLU LEU GLY CYS GLY THR ASN          
SEQRES  10 D  118  GLU                                                          
HET    CNC  A 501      93                                                       
HET    GOL  A 502       6                                                       
HET    GOL  A 503       6                                                       
HET    GOL  A 504       6                                                       
HET    CNC  B 501      93                                                       
HET    GOL  B 502       6                                                       
HET     CA  C 201       1                                                       
HET     CA  C 202       1                                                       
HET     CA  D 201       1                                                       
HET     CA  D 202       1                                                       
HETNAM     CNC CO-CYANOCOBALAMIN                                                
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  CNC    2(C63 H88 CO N14 O14 P 1+)                                   
FORMUL   6  GOL    4(C3 H8 O3)                                                  
FORMUL  11   CA    4(CA 2+)                                                     
FORMUL  15  HOH   *44(H2 O)                                                     
HELIX    1 AA1 ASP A    9  LEU A   21  1                                  13    
HELIX    2 AA2 PRO A   22  ARG A   26  5                                   5    
HELIX    3 AA3 ASN A   33  LEU A   42  1                                  10    
HELIX    4 AA4 GLY A   48  LEU A   66  1                                  19    
HELIX    5 AA5 SER A   83  ASN A   97  1                                  15    
HELIX    6 AA6 ARG A  102  GLY A  125  1                                  24    
HELIX    7 AA7 SER A  135  HIS A  149  1                                  15    
HELIX    8 AA8 HIS A  154  GLU A  166  1                                  13    
HELIX    9 AA9 SER A  174  ASN A  192  1                                  19    
HELIX   10 AB1 ASN A  194  GLY A  196  5                                   3    
HELIX   11 AB2 ARG A  197  ALA A  215  1                                  19    
HELIX   12 AB3 SER A  227  THR A  237  1                                  11    
HELIX   13 AB4 GLU A  244  ASP A  262  1                                  19    
HELIX   14 AB5 ASN A  267  ASN A  279  1                                  13    
HELIX   15 AB6 THR A  282  ILE A  287  5                                   6    
HELIX   16 AB7 THR A  336  LEU A  347  1                                  12    
HELIX   17 AB8 ASP B    9  LEU B   21  1                                  13    
HELIX   18 AB9 PRO B   22  ARG B   26  5                                   5    
HELIX   19 AC1 ASN B   33  LEU B   42  1                                  10    
HELIX   20 AC2 GLY B   48  LEU B   67  1                                  20    
HELIX   21 AC3 SER B   83  ALA B   96  1                                  14    
HELIX   22 AC4 ARG B  102  GLY B  125  1                                  24    
HELIX   23 AC5 SER B  135  HIS B  149  1                                  15    
HELIX   24 AC6 HIS B  154  GLU B  166  1                                  13    
HELIX   25 AC7 SER B  174  SER B  191  1                                  18    
HELIX   26 AC8 ASN B  194  GLY B  196  5                                   3    
HELIX   27 AC9 ARG B  197  ALA B  215  1                                  19    
HELIX   28 AD1 SER B  227  MET B  236  1                                  10    
HELIX   29 AD2 GLU B  244  ASP B  262  1                                  19    
HELIX   30 AD3 ASN B  267  ASN B  279  1                                  13    
HELIX   31 AD4 THR B  282  ILE B  287  5                                   6    
HELIX   32 AD5 THR B  336  LEU B  347  1                                  12    
HELIX   33 AD6 THR C  149  ARG C  151  5                                   3    
HELIX   34 AD7 SER C  161  LEU C  165  5                                   5    
HELIX   35 AD8 THR D  149  ARG D  151  5                                   3    
HELIX   36 AD9 SER D  161  LEU D  165  5                                   5    
SHEET    1 AA1 2 LEU A  45  GLN A  46  0                                        
SHEET    2 AA1 2 VAL A 296  MET A 297  1  O  VAL A 296   N  GLN A  46           
SHEET    1 AA2 5 TYR A 325  LEU A 332  0                                        
SHEET    2 AA2 5 ILE A 311  VAL A 318 -1  N  VAL A 314   O  ILE A 329           
SHEET    3 AA2 5 THR A 401  SER A 408  1  O  ILE A 402   N  THR A 315           
SHEET    4 AA2 5 GLU A 375  ARG A 381 -1  N  GLN A 378   O  ARG A 405           
SHEET    5 AA2 5 THR A 385  PRO A 386 -1  O  THR A 385   N  ARG A 381           
SHEET    1 AA3 3 TYR A 352  GLN A 355  0                                        
SHEET    2 AA3 3 TYR A 362  VAL A 366 -1  O  TYR A 362   N  GLN A 355           
SHEET    3 AA3 3 LYS A 369  ALA A 370 -1  O  LYS A 369   N  VAL A 366           
SHEET    1 AA4 2 LEU B  45  GLN B  46  0                                        
SHEET    2 AA4 2 VAL B 296  MET B 297  1  O  VAL B 296   N  GLN B  46           
SHEET    1 AA5 5 TYR B 325  LEU B 332  0                                        
SHEET    2 AA5 5 ILE B 311  VAL B 318 -1  N  VAL B 314   O  ILE B 329           
SHEET    3 AA5 5 THR B 401  SER B 408  1  O  ILE B 402   N  THR B 315           
SHEET    4 AA5 5 GLU B 375  ARG B 381 -1  N  GLN B 378   O  ARG B 405           
SHEET    5 AA5 5 THR B 385  PRO B 386 -1  O  THR B 385   N  ARG B 381           
SHEET    1 AA6 3 TYR B 352  GLN B 355  0                                        
SHEET    2 AA6 3 TYR B 362  VAL B 366 -1  O  TYR B 362   N  GLN B 355           
SHEET    3 AA6 3 LYS B 369  ALA B 370 -1  O  LYS B 369   N  VAL B 366           
SHEET    1 AA7 2 GLU C 136  ARG C 138  0                                        
SHEET    2 AA7 2 CYS C 145  PRO C 147 -1  O  ILE C 146   N  LEU C 137           
SHEET    1 AA8 2 GLU D 136  ARG D 138  0                                        
SHEET    2 AA8 2 CYS D 145  PRO D 147 -1  O  ILE D 146   N  LEU D 137           
SSBOND   1 CYS A    3    CYS A  249                          1555   1555  2.03  
SSBOND   2 CYS A   65    CYS A   78                          1555   1555  2.09  
SSBOND   3 CYS A   98    CYS A  291                          1555   1555  2.03  
SSBOND   4 CYS A  147    CYS A  187                          1555   1555  2.03  
SSBOND   5 CYS B    3    CYS B  249                          1555   1555  2.03  
SSBOND   6 CYS B   65    CYS B   78                          1555   1555  2.04  
SSBOND   7 CYS B   98    CYS B  291                          1555   1555  2.03  
SSBOND   8 CYS B  147    CYS B  187                          1555   1555  2.03  
SSBOND   9 CYS C   54    CYS C   67                          1555   1555  2.04  
SSBOND  10 CYS C   61    CYS C   80                          1555   1555  2.05  
SSBOND  11 CYS C  132    CYS C  145                          1555   1555  2.03  
SSBOND  12 CYS C  139    CYS C  158                          1555   1555  2.03  
SSBOND  13 CYS C  152    CYS C  167                          1555   1555  2.03  
SSBOND  14 CYS D   54    CYS D   67                          1555   1555  2.07  
SSBOND  15 CYS D   61    CYS D   80                          1555   1555  2.03  
SSBOND  16 CYS D  132    CYS D  145                          1555   1555  2.03  
SSBOND  17 CYS D  139    CYS D  158                          1555   1555  2.03  
SSBOND  18 CYS D  152    CYS D  167                          1555   1555  2.03  
LINK         O   TRP C  72                CA    CA C 202     1555   1555  2.80  
LINK         OD1 ASP C  75                CA    CA C 202     1555   1555  2.51  
LINK         O   ASP C  77                CA    CA C 202     1555   1555  2.57  
LINK         OD2 ASP C  79                CA    CA C 202     1555   1555  2.37  
LINK         O   TRP C 150                CA    CA C 201     1555   1555  2.34  
LINK         OD1 ASP C 153                CA    CA C 201     1555   1555  2.45  
LINK         O   HIS C 155                CA    CA C 201     1555   1555  2.35  
LINK         OD2 ASP C 157                CA    CA C 201     1555   1555  2.41  
LINK         OD2 ASP C 163                CA    CA C 201     1555   1555  2.32  
LINK         OE2 GLU C 164                CA    CA C 201     1555   1555  2.48  
LINK         O   TRP D  72                CA    CA D 202     1555   1555  2.73  
LINK         OD1 ASP D  75                CA    CA D 202     1555   1555  2.30  
LINK         O   ASP D  77                CA    CA D 202     1555   1555  2.52  
LINK         OD2 ASP D  79                CA    CA D 202     1555   1555  2.52  
LINK         OD1 ASP D  85                CA    CA D 202     1555   1555  2.26  
LINK         OD2 ASP D  85                CA    CA D 202     1555   1555  2.80  
LINK         O   TRP D 150                CA    CA D 201     1555   1555  2.30  
LINK         OD1 ASP D 153                CA    CA D 201     1555   1555  2.38  
LINK         O   HIS D 155                CA    CA D 201     1555   1555  2.31  
LINK         OD2 ASP D 157                CA    CA D 201     1555   1555  2.38  
LINK         OD2 ASP D 163                CA    CA D 201     1555   1555  2.46  
LINK         OE2 GLU D 164                CA    CA D 201     1555   1555  2.37  
CISPEP   1 LEU A  322    PRO A  323          0        -4.40                     
CISPEP   2 ASP A  382    PRO A  383          0         1.32                     
CISPEP   3 ARG B  241    GLY B  242          0         5.99                     
CISPEP   4 LEU B  322    PRO B  323          0        -4.82                     
CISPEP   5 ASP B  382    PRO B  383          0         3.76                     
CISPEP   6 ARG C   73    CYS C   74          0       -12.50                     
CISPEP   7 CYS C  167    GLY C  168          0         6.11                     
CISPEP   8 ARG D   73    CYS D   74          0       -16.41                     
SITE     1 AC1 27 GLY A  85  GLN A  86  THR A 134  TYR A 137                    
SITE     2 AC1 27 GLN A 138  ASP A 176  ASN A 224  TYR A 226                    
SITE     3 AC1 27 SER A 227  MET A 270  GLN A 273  SER A 357                    
SITE     4 AC1 27 LEU A 358  SER A 359  GLY A 360  PRO A 361                    
SITE     5 AC1 27 TYR A 362  LEU A 363  PHE A 376  TRP A 377                    
SITE     6 AC1 27 GLN A 378  LEU A 379  LEU A 387  LEU A 388                    
SITE     7 AC1 27 GLY A 390  TRP A 409  HOH A 605                               
SITE     1 AC2  5 SER A 174  THR A 177  TRP A 409  HOH A 609                    
SITE     2 AC2  5 HOH A 610                                                     
SITE     1 AC3  5 HIS A 169  HIS A 172  HIS A 173  GLU A 211                    
SITE     2 AC3  5 HOH A 612                                                     
SITE     1 AC4  5 GLY A 372  GLU A 373  GLU A 375  GLY B 372                    
SITE     2 AC4  5 GLU B 375                                                     
SITE     1 AC5 28 GLY B  85  GLN B  86  THR B 134  TYR B 137                    
SITE     2 AC5 28 GLN B 138  ASP B 176  ASN B 224  TYR B 226                    
SITE     3 AC5 28 SER B 227  MET B 270  GLN B 273  SER B 357                    
SITE     4 AC5 28 LEU B 358  SER B 359  GLY B 360  PRO B 361                    
SITE     5 AC5 28 TYR B 362  LEU B 363  PHE B 376  TRP B 377                    
SITE     6 AC5 28 GLN B 378  LEU B 379  LEU B 387  LEU B 388                    
SITE     7 AC5 28 GLY B 390  TRP B 409  HOH B 606  HOH B 607                    
SITE     1 AC6  7 GLN B  63  ARG B 102  GLY B 103  LYS B 105                    
SITE     2 AC6  7 ASP D  77  LEU D  78  ASP D  79                               
SITE     1 AC7  6 TRP C 150  ASP C 153  HIS C 155  ASP C 157                    
SITE     2 AC7  6 ASP C 163  GLU C 164                                          
SITE     1 AC8  6 TRP C  72  CYS C  74  ASP C  75  ASP C  77                    
SITE     2 AC8  6 ASP C  79  ASP C  85                                          
SITE     1 AC9  6 TRP D 150  ASP D 153  HIS D 155  ASP D 157                    
SITE     2 AC9  6 ASP D 163  GLU D 164                                          
SITE     1 AD1  5 TRP D  72  ASP D  75  ASP D  77  ASP D  79                    
SITE     2 AD1  5 ASP D  85                                                     
CRYST1   98.404   98.404  356.341  90.00  90.00  90.00 P 43 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010162  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010162  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002806        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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