GenomeNet

Database: PDB
Entry: 3KQ4
LinkDB: 3KQ4
Original site: 3KQ4 
HEADER    TRANSPORT PROTEIN                       17-NOV-09   3KQ4              
TITLE     STRUCTURE OF INTRINSIC FACTOR-COBALAMIN BOUND TO ITS RECEPTOR CUBILIN 
CAVEAT     3KQ4    NAG A 2001 HAS WRONG CHIRALITY AT ATOM C1 B12 A 2007 HAS     
CAVEAT   2 3KQ4    WRONG CHIRALITY AT ATOM C19 NAG B 2001 HAS WRONG CHIRALITY   
CAVEAT   3 3KQ4    AT ATOM C1 NAG B 2008 HAS WRONG CHIRALITY AT ATOM C1 NAG C   
CAVEAT   4 3KQ4    2001 HAS WRONG CHIRALITY AT ATOM C1 B12 C 2007 HAS WRONG     
CAVEAT   5 3KQ4    CHIRALITY AT ATOM C19 NAG D 2001 HAS WRONG CHIRALITY AT      
CAVEAT   6 3KQ4    ATOM C1 NAG D 2008 HAS WRONG CHIRALITY AT ATOM C1 NAG E      
CAVEAT   7 3KQ4    2001 HAS WRONG CHIRALITY AT ATOM C1 B12 E 2007 HAS WRONG     
CAVEAT   8 3KQ4    CHIRALITY AT ATOM C19 NAG F 2001 HAS WRONG CHIRALITY AT      
CAVEAT   9 3KQ4    ATOM C1 NAG F 2008 HAS WRONG CHIRALITY AT ATOM C1            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GASTRIC INTRINSIC FACTOR;                                  
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 25-417;                                       
COMPND   5 SYNONYM: INTRINSIC FACTOR, INF, IF;                                  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CUBILIN;                                                   
COMPND   9 CHAIN: B, D, F;                                                      
COMPND  10 FRAGMENT: UNP RESIDUES 932-1388;                                     
COMPND  11 SYNONYM: INTRINSIC FACTOR-COBALAMIN RECEPTOR, INTRINSIC FACTOR-      
COMPND  12 VITAMIN B12 RECEPTOR, 460 KDA RECEPTOR, INTESTINAL INTRINSIC FACTOR  
COMPND  13 RECEPTOR;                                                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GIF, IFMH;                                                     
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CUBN, IFCR;                                                    
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    PROTEIN-PROTEIN COMPLEX, COBALT, COBALT TRANSPORT, DISEASE MUTATION,  
KEYWDS   2 DISULFIDE BOND, GLYCOPROTEIN, SECRETED, TRANSPORT, CHOLESTEROL       
KEYWDS   3 METABOLISM, COBALAMIN, EGF-LIKE DOMAIN, ENDOCYTOSIS, ENDOSOME, LIPID 
KEYWDS   4 METABOLISM, LYSOSOME, MEMBRANE, PROTEIN TRANSPORT, RECEPTOR, STEROID 
KEYWDS   5 METABOLISM, TRANSPORT PROTEIN                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.B.F.ANDERSEN,M.MADSEN,S.K.MOESTRUP,G.R.ANDERSEN                     
REVDAT   5   29-JUL-20 3KQ4    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   07-MAR-18 3KQ4    1       REMARK                                   
REVDAT   3   24-OCT-12 3KQ4    1       FORMUL VERSN                             
REVDAT   2   12-JAN-11 3KQ4    1       JRNL                                     
REVDAT   1   09-MAR-10 3KQ4    0                                                
JRNL        AUTH   C.B.ANDERSEN,M.MADSEN,T.STORM,S.K.MOESTRUP,G.R.ANDERSEN      
JRNL        TITL   STRUCTURAL BASIS FOR RECEPTOR RECOGNITION OF                 
JRNL        TITL 2 VITAMIN-B(12)-INTRINSIC FACTOR COMPLEXES.                    
JRNL        REF    NATURE                        V. 464   445 2010              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   20237569                                                     
JRNL        DOI    10.1038/NATURE08874                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 72265                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.520                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1102                            
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 47.8528 -  6.5950    0.94     8866   178  0.2105 0.2232        
REMARK   3     2  6.5950 -  5.2367    0.96     8826   175  0.1987 0.2370        
REMARK   3     3  5.2367 -  4.5753    0.97     8866   129  0.1736 0.2181        
REMARK   3     4  4.5753 -  4.1573    0.97     8902    95  0.1732 0.1834        
REMARK   3     5  4.1573 -  3.8594    0.98     8977   107  0.1980 0.2132        
REMARK   3     6  3.8594 -  3.6320    0.98     9008    70  0.2317 0.2682        
REMARK   3     7  3.6320 -  3.4501    0.98     8797   178  0.2617 0.3078        
REMARK   3     8  3.4501 -  3.3000    0.98     8921   170  0.2873 0.3565        
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              : 0.30                                          
REMARK   3   B_SOL              : 74.42                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.810           
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      :  0.013          21450                                  
REMARK   3   ANGLE     :  1.930          29349                                  
REMARK   3   CHIRALITY :  0.138           3324                                  
REMARK   3   PLANARITY :  0.007           3660                                  
REMARK   3   DIHEDRAL  : 26.398          12915                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -55.3989  15.1433 -49.3363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4521 T22:   0.3465                                     
REMARK   3      T33:   0.4564 T12:  -0.0535                                     
REMARK   3      T13:  -0.0508 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0141 L22:   0.1055                                     
REMARK   3      L33:   0.4342 L12:  -0.0965                                     
REMARK   3      L13:   0.0719 L23:  -0.1007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0062 S12:  -0.0196 S13:  -0.0100                       
REMARK   3      S21:  -0.0661 S22:  -0.0344 S23:   0.0069                       
REMARK   3      S31:  -0.0361 S32:  -0.0347 S33:   0.0254                       
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 B AND (RESSEQ 932:1388 )              
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 932:1388 )              
REMARK   3     ATOM PAIRS NUMBER  : 3640                                        
REMARK   3     RMSD               : 0.006                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND (RESSEQ 932:1388 )              
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 932:1388 )              
REMARK   3     ATOM PAIRS NUMBER  : 3640                                        
REMARK   3     RMSD               : 0.005                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:281 OR RESSEQ         
REMARK   3                          290:399 )                                   
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 7:281 OR RESSEQ         
REMARK   3                          290:399 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 2737                                        
REMARK   3     RMSD               : 0.004                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 7:281 OR RESSEQ         
REMARK   3                          290:399 )                                   
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 7:281 OR RESSEQ         
REMARK   3                          290:399 )                                   
REMARK   3     ATOM PAIRS NUMBER  : 2737                                        
REMARK   3     RMSD               : 0.005                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000056306.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-09; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SLS; MAX II                        
REMARK 200  BEAMLINE                       : X06SA; I911-3                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9; 1.8                           
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL; NULL                         
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72280                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      205.01150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      205.01150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       58.84200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      102.08950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       58.84200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.08950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      205.01150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       58.84200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      102.08950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      205.01150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       58.84200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      102.08950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H, I                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, J, K, L                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, M, N, O                         
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   300                                                      
REMARK 465     ASN A   301                                                      
REMARK 465     PRO A   302                                                      
REMARK 465     GLY A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     PRO A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     SER C   300                                                      
REMARK 465     ASN C   301                                                      
REMARK 465     PRO C   302                                                      
REMARK 465     GLY C   303                                                      
REMARK 465     PRO C   304                                                      
REMARK 465     GLY C   305                                                      
REMARK 465     PRO C   306                                                      
REMARK 465     THR C   307                                                      
REMARK 465     SER E   300                                                      
REMARK 465     ASN E   301                                                      
REMARK 465     PRO E   302                                                      
REMARK 465     GLY E   303                                                      
REMARK 465     PRO E   304                                                      
REMARK 465     GLY E   305                                                      
REMARK 465     PRO E   306                                                      
REMARK 465     THR E   307                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASN A  330   CG   OD1  ND2                                       
REMARK 480     ASN C  330   CG   OD1  ND2                                       
REMARK 480     ASN E  330   CG   OD1  ND2                                       
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    PRO A 167   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO B 953   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO C 167   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO D 953   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO E 167   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PRO F 953   C   -  N   -  CA  ANGL. DEV. =   9.5 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    CYS A  26       28.93   -152.81                                   
REMARK 500    PRO A  29      122.95    -37.39                                   
REMARK 500    ASN A 119       24.45    -79.90                                   
REMARK 500    PRO A 122     -165.98    -76.33                                   
REMARK 500    SER A 123      -94.88    -92.32                                   
REMARK 500    ALA A 131      -18.41    -49.92                                   
REMARK 500    LYS A 186       35.77   -141.86                                   
REMARK 500    MET A 212       -5.71    -55.61                                   
REMARK 500    ASP A 216       42.99    -71.20                                   
REMARK 500    ASN A 217       13.13   -166.25                                   
REMARK 500    VAL A 235      -30.58   -142.60                                   
REMARK 500    LYS A 241      -76.92    -51.72                                   
REMARK 500    PHE A 262       60.75   -107.14                                   
REMARK 500    SER A 289       67.67     71.82                                   
REMARK 500    ASP A 291       66.03     84.41                                   
REMARK 500    ALA A 309       92.37    154.44                                   
REMARK 500    LEU A 322      -36.16   -139.33                                   
REMARK 500    VAL A 325       63.92   -116.29                                   
REMARK 500    GLU A 326      103.07   -161.05                                   
REMARK 500    PHE A 329        1.72   -150.70                                   
REMARK 500    LYS A 338      179.82     50.94                                   
REMARK 500    SER A 339     -163.14    -66.91                                   
REMARK 500    VAL A 392      -27.95   -148.23                                   
REMARK 500    HIS A 407       45.03   -142.93                                   
REMARK 500    GLU B 938      153.64    -47.73                                   
REMARK 500    HIS B 948      143.60    -38.79                                   
REMARK 500    PRO B 949        0.19    -66.86                                   
REMARK 500    ASN B 950      131.17    166.64                                   
REMARK 500    ASN B 957       23.80   -144.77                                   
REMARK 500    GLN B 965      162.56    -48.88                                   
REMARK 500    PHE B 974       64.59   -164.96                                   
REMARK 500    PHE B 977       87.38   -175.02                                   
REMARK 500    HIS B 982      120.57   -171.27                                   
REMARK 500    ASN B 987      -87.61    -60.36                                   
REMARK 500    TYR B 989      165.28    174.91                                   
REMARK 500    THR B 999      176.98     68.51                                   
REMARK 500    ILE B1009      113.22    169.70                                   
REMARK 500    THR B1026     -159.47   -125.05                                   
REMARK 500    LEU B1030      126.15     88.27                                   
REMARK 500    GLU B1033       -7.51    -57.32                                   
REMARK 500    ILE B1037      109.12   -165.67                                   
REMARK 500    THR B1046        2.91    -54.84                                   
REMARK 500    THR B1053      -32.12   -140.85                                   
REMARK 500    ASP B1054        6.65    -58.05                                   
REMARK 500    ASN B1063      -10.58     69.71                                   
REMARK 500    ASN B1071       17.21     55.21                                   
REMARK 500    PHE B1093       94.84   -166.15                                   
REMARK 500    ASP B1105      120.51     49.98                                   
REMARK 500    GLU B1115        0.21    -68.31                                   
REMARK 500    PRO B1118      151.05    -44.63                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     254 RAMACHANDRAN OUTLIERS.                        
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 B2014  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 980   OE1                                                    
REMARK 620 2 ASP B 988   OD1  88.2                                              
REMARK 620 3 ASP B1027   OD1  91.4  84.0                                        
REMARK 620 4 ASP B1027   O   155.9  90.6  64.6                                  
REMARK 620 5 ASP B1029   O    75.0 161.1  87.7 101.2                            
REMARK 620 6 LEU B1030   O    91.7 101.4 173.8 112.0  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2015  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B1096   OE1                                                    
REMARK 620 2 ASP B1105   OD2  81.8                                              
REMARK 620 3 ASP B1105   OD1  89.6  49.9                                        
REMARK 620 4 ASP B1146   OD2  90.3 110.9  61.5                                  
REMARK 620 5 ILE B1148   O    92.4 166.7 142.5  81.0                            
REMARK 620 6 ASP B1149   O    98.5  87.0 134.7 161.1  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2016  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B1213   OE2                                                    
REMARK 620 2 ASP B1221   OD1  93.0                                              
REMARK 620 3 ASP B1221   OD2  58.0  51.0                                        
REMARK 620 4 ASP B1262   OD1  91.1  88.3  57.1                                  
REMARK 620 5 ASP B1262   O   166.9  94.5 120.1  78.5                            
REMARK 620 6 GLY B1264   O    86.5 174.5 132.2  97.1  87.1                      
REMARK 620 7 GLN B1265   O    76.7  97.0 117.9 166.9 112.9  77.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2017  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B1328   OE2                                                    
REMARK 620 2 ASP B1336   OD2  83.9                                              
REMARK 620 3 ASP B1373   OD1  87.2  95.9                                        
REMARK 620 4 VAL B1375   O    79.5 161.8  90.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2014  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 980   OE1                                                    
REMARK 620 2 ASP D 988   OD1  88.3                                              
REMARK 620 3 ASP D1027   OD1  91.4  84.1                                        
REMARK 620 4 ASP D1027   O   155.9  90.6  64.5                                  
REMARK 620 5 ASP D1029   O    75.1 161.2  87.7 101.1                            
REMARK 620 6 LEU D1030   O    91.8 101.4 173.7 112.0  88.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2015  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D1096   OE1                                                    
REMARK 620 2 ASP D1105   OD2  81.8                                              
REMARK 620 3 ASP D1105   OD1  89.6  49.9                                        
REMARK 620 4 ASP D1146   OD2  90.3 110.9  61.5                                  
REMARK 620 5 ILE D1148   O    92.4 166.7 142.4  81.0                            
REMARK 620 6 ASP D1149   O    98.5  87.1 134.7 161.1  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2016  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D1213   OE2                                                    
REMARK 620 2 ASP D1221   OD1  92.9                                              
REMARK 620 3 ASP D1221   OD2  58.0  51.0                                        
REMARK 620 4 ASP D1262   OD1  91.1  88.3  57.1                                  
REMARK 620 5 ASP D1262   O   166.9  94.5 120.1  78.4                            
REMARK 620 6 GLY D1264   O    86.5 174.5 132.2  97.1  87.1                      
REMARK 620 7 GLN D1265   O    76.7  97.0 117.9 166.9 112.9  77.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2017  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D1328   OE2                                                    
REMARK 620 2 ASP D1336   OD2  84.0                                              
REMARK 620 3 ASP D1373   OD1  87.2  95.9                                        
REMARK 620 4 VAL D1375   O    79.6 161.9  90.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2014  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 980   OE1                                                    
REMARK 620 2 ASP F 988   OD1  88.3                                              
REMARK 620 3 ASP F1027   OD1  91.5  84.1                                        
REMARK 620 4 ASP F1027   O   155.9  90.6  64.5                                  
REMARK 620 5 ASP F1029   O    75.0 161.2  87.8 101.2                            
REMARK 620 6 LEU F1030   O    91.7 101.4 173.8 112.0  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2015  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F1096   OE1                                                    
REMARK 620 2 ASP F1105   OD2  81.8                                              
REMARK 620 3 ASP F1105   OD1  89.6  49.9                                        
REMARK 620 4 ASP F1146   OD2  90.3 110.9  61.6                                  
REMARK 620 5 ILE F1148   O    92.3 166.7 142.5  81.0                            
REMARK 620 6 ASP F1149   O    98.5  87.0 134.7 161.1  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2016  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F1213   OE2                                                    
REMARK 620 2 ASP F1221   OD1  93.0                                              
REMARK 620 3 ASP F1221   OD2  58.0  51.0                                        
REMARK 620 4 ASP F1262   OD1  91.1  88.3  57.0                                  
REMARK 620 5 ASP F1262   O   166.9  94.5 120.1  78.4                            
REMARK 620 6 GLY F1264   O    86.5 174.5 132.2  97.2  87.1                      
REMARK 620 7 GLN F1265   O    76.7  97.0 117.9 166.9 112.9  77.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2017  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F1328   OE2                                                    
REMARK 620 2 ASP F1336   OD2  83.9                                              
REMARK 620 3 ASP F1373   OD1  87.2  95.9                                        
REMARK 620 4 VAL F1375   O    79.5 161.8  90.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2PMW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN INTRINSIC FACTOR-COBALAMIN COMPLEX AT     
REMARK 900 2.6 A RESOLUTION                                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 GLN TO HIS SEQUENCE CONFLICT IN UNP ENTRY P27352                     
DBREF  3KQ4 A   25   417  UNP    P27352   IF_HUMAN        25    417             
DBREF  3KQ4 B  932  1388  UNP    O60494   CUBN_HUMAN     932   1388             
DBREF  3KQ4 C   25   417  UNP    P27352   IF_HUMAN        25    417             
DBREF  3KQ4 D  932  1388  UNP    O60494   CUBN_HUMAN     932   1388             
DBREF  3KQ4 E   25   417  UNP    P27352   IF_HUMAN        25    417             
DBREF  3KQ4 F  932  1388  UNP    O60494   CUBN_HUMAN     932   1388             
SEQADV 3KQ4 HIS A   91  UNP  P27352    GLN    91 SEE REMARK 999                 
SEQADV 3KQ4 HIS C   91  UNP  P27352    GLN    91 SEE REMARK 999                 
SEQADV 3KQ4 HIS E   91  UNP  P27352    GLN    91 SEE REMARK 999                 
SEQRES   1 A  393  SER CYS SER VAL PRO SER ALA GLN GLU PRO LEU VAL ASN          
SEQRES   2 A  393  GLY ILE GLN VAL LEU MET GLU ASN SER VAL THR SER SER          
SEQRES   3 A  393  ALA TYR PRO ASN PRO SER ILE LEU ILE ALA MET ASN LEU          
SEQRES   4 A  393  ALA GLY ALA TYR ASN LEU LYS ALA GLN LYS LEU LEU THR          
SEQRES   5 A  393  TYR GLN LEU MET SER SER ASP ASN ASN ASP LEU THR ILE          
SEQRES   6 A  393  GLY HIS LEU GLY LEU THR ILE MET ALA LEU THR SER SER          
SEQRES   7 A  393  CYS ARG ASP PRO GLY ASP LYS VAL SER ILE LEU GLN ARG          
SEQRES   8 A  393  GLN MET GLU ASN TRP ALA PRO SER SER PRO ASN ALA GLU          
SEQRES   9 A  393  ALA SER ALA PHE TYR GLY PRO SER LEU ALA ILE LEU ALA          
SEQRES  10 A  393  LEU CYS GLN LYS ASN SER GLU ALA THR LEU PRO ILE ALA          
SEQRES  11 A  393  VAL ARG PHE ALA LYS THR LEU LEU ALA ASN SER SER PRO          
SEQRES  12 A  393  PHE ASN VAL ASP THR GLY ALA MET ALA THR LEU ALA LEU          
SEQRES  13 A  393  THR CYS MET TYR ASN LYS ILE PRO VAL GLY SER GLU GLU          
SEQRES  14 A  393  GLY TYR ARG SER LEU PHE GLY GLN VAL LEU LYS ASP ILE          
SEQRES  15 A  393  VAL GLU LYS ILE SER MET LYS ILE LYS ASP ASN GLY ILE          
SEQRES  16 A  393  ILE GLY ASP ILE TYR SER THR GLY LEU ALA MET GLN ALA          
SEQRES  17 A  393  LEU SER VAL THR PRO GLU PRO SER LYS LYS GLU TRP ASN          
SEQRES  18 A  393  CYS LYS LYS THR THR ASP MET ILE LEU ASN GLU ILE LYS          
SEQRES  19 A  393  GLN GLY LYS PHE HIS ASN PRO MET SER ILE ALA GLN ILE          
SEQRES  20 A  393  LEU PRO SER LEU LYS GLY LYS THR TYR LEU ASP VAL PRO          
SEQRES  21 A  393  GLN VAL THR CYS SER PRO ASP HIS GLU VAL GLN PRO THR          
SEQRES  22 A  393  LEU PRO SER ASN PRO GLY PRO GLY PRO THR SER ALA SER          
SEQRES  23 A  393  ASN ILE THR VAL ILE TYR THR ILE ASN ASN GLN LEU ARG          
SEQRES  24 A  393  GLY VAL GLU LEU LEU PHE ASN GLU THR ILE ASN VAL SER          
SEQRES  25 A  393  VAL LYS SER GLY SER VAL LEU LEU VAL VAL LEU GLU GLU          
SEQRES  26 A  393  ALA GLN ARG LYS ASN PRO MET PHE LYS PHE GLU THR THR          
SEQRES  27 A  393  MET THR SER TRP GLY LEU VAL VAL SER SER ILE ASN ASN          
SEQRES  28 A  393  ILE ALA GLU ASN VAL ASN HIS LYS THR TYR TRP GLN PHE          
SEQRES  29 A  393  LEU SER GLY VAL THR PRO LEU ASN GLU GLY VAL ALA ASP          
SEQRES  30 A  393  TYR ILE PRO PHE ASN HIS GLU HIS ILE THR ALA ASN PHE          
SEQRES  31 A  393  THR GLN TYR                                                  
SEQRES   1 B  457  CYS GLY GLU ILE LEU THR GLU SER THR GLY THR ILE GLN          
SEQRES   2 B  457  SER PRO GLY HIS PRO ASN VAL TYR PRO HIS GLY ILE ASN          
SEQRES   3 B  457  CYS THR TRP HIS ILE LEU VAL GLN PRO ASN HIS LEU ILE          
SEQRES   4 B  457  HIS LEU MET PHE GLU THR PHE HIS LEU GLU PHE HIS TYR          
SEQRES   5 B  457  ASN CYS THR ASN ASP TYR LEU GLU VAL TYR ASP THR ASP          
SEQRES   6 B  457  SER GLU THR SER LEU GLY ARG TYR CYS GLY LYS SER ILE          
SEQRES   7 B  457  PRO PRO SER LEU THR SER SER GLY ASN SER LEU MET LEU          
SEQRES   8 B  457  VAL PHE VAL THR ASP SER ASP LEU ALA TYR GLU GLY PHE          
SEQRES   9 B  457  LEU ILE ASN TYR GLU ALA ILE SER ALA ALA THR ALA CYS          
SEQRES  10 B  457  LEU GLN ASP TYR THR ASP ASP LEU GLY THR PHE THR SER          
SEQRES  11 B  457  PRO ASN PHE PRO ASN ASN TYR PRO ASN ASN TRP GLU CYS          
SEQRES  12 B  457  ILE TYR ARG ILE THR VAL ARG THR GLY GLN LEU ILE ALA          
SEQRES  13 B  457  VAL HIS PHE THR ASN PHE SER LEU GLU GLU ALA ILE GLY          
SEQRES  14 B  457  ASN TYR TYR THR ASP PHE LEU GLU ILE ARG ASP GLY GLY          
SEQRES  15 B  457  TYR GLU LYS SER PRO LEU LEU GLY ILE PHE TYR GLY SER          
SEQRES  16 B  457  ASN LEU PRO PRO THR ILE ILE SER HIS SER ASN LYS LEU          
SEQRES  17 B  457  TRP LEU LYS PHE LYS SER ASP GLN ILE ASP THR ARG SER          
SEQRES  18 B  457  GLY PHE SER ALA TYR TRP ASP GLY SER SER THR GLY CYS          
SEQRES  19 B  457  GLY GLY ASN LEU THR THR SER SER GLY THR PHE ILE SER          
SEQRES  20 B  457  PRO ASN TYR PRO MET PRO TYR TYR HIS SER SER GLU CYS          
SEQRES  21 B  457  TYR TRP TRP LEU LYS SER SER HIS GLY SER ALA PHE GLU          
SEQRES  22 B  457  LEU GLU PHE LYS ASP PHE HIS LEU GLU HIS HIS PRO ASN          
SEQRES  23 B  457  CYS THR LEU ASP TYR LEU ALA VAL TYR ASP GLY PRO SER          
SEQRES  24 B  457  SER ASN SER HIS LEU LEU THR GLN LEU CYS GLY ASP GLU          
SEQRES  25 B  457  LYS PRO PRO LEU ILE ARG SER SER GLY ASP SER MET PHE          
SEQRES  26 B  457  ILE LYS LEU ARG THR ASP GLU GLY GLN GLN GLY ARG GLY          
SEQRES  27 B  457  PHE LYS ALA GLU TYR ARG GLN THR CYS GLU ASN VAL VAL          
SEQRES  28 B  457  ILE VAL ASN GLN THR TYR GLY ILE LEU GLU SER ILE GLY          
SEQRES  29 B  457  TYR PRO ASN PRO TYR SER GLU ASN GLN HIS CYS ASN TRP          
SEQRES  30 B  457  THR ILE ARG ALA THR THR GLY ASN THR VAL ASN TYR THR          
SEQRES  31 B  457  PHE LEU ALA PHE ASP LEU GLU HIS HIS ILE ASN CYS SER          
SEQRES  32 B  457  THR ASP TYR LEU GLU LEU TYR ASP GLY PRO ARG GLN MET          
SEQRES  33 B  457  GLY ARG TYR CYS GLY VAL ASP LEU PRO PRO PRO GLY SER          
SEQRES  34 B  457  THR THR SER SER LYS LEU GLN VAL LEU LEU LEU THR ASP          
SEQRES  35 B  457  GLY VAL GLY ARG ARG GLU LYS GLY PHE GLN MET GLN TRP          
SEQRES  36 B  457  PHE VAL                                                      
SEQRES   1 C  393  SER CYS SER VAL PRO SER ALA GLN GLU PRO LEU VAL ASN          
SEQRES   2 C  393  GLY ILE GLN VAL LEU MET GLU ASN SER VAL THR SER SER          
SEQRES   3 C  393  ALA TYR PRO ASN PRO SER ILE LEU ILE ALA MET ASN LEU          
SEQRES   4 C  393  ALA GLY ALA TYR ASN LEU LYS ALA GLN LYS LEU LEU THR          
SEQRES   5 C  393  TYR GLN LEU MET SER SER ASP ASN ASN ASP LEU THR ILE          
SEQRES   6 C  393  GLY HIS LEU GLY LEU THR ILE MET ALA LEU THR SER SER          
SEQRES   7 C  393  CYS ARG ASP PRO GLY ASP LYS VAL SER ILE LEU GLN ARG          
SEQRES   8 C  393  GLN MET GLU ASN TRP ALA PRO SER SER PRO ASN ALA GLU          
SEQRES   9 C  393  ALA SER ALA PHE TYR GLY PRO SER LEU ALA ILE LEU ALA          
SEQRES  10 C  393  LEU CYS GLN LYS ASN SER GLU ALA THR LEU PRO ILE ALA          
SEQRES  11 C  393  VAL ARG PHE ALA LYS THR LEU LEU ALA ASN SER SER PRO          
SEQRES  12 C  393  PHE ASN VAL ASP THR GLY ALA MET ALA THR LEU ALA LEU          
SEQRES  13 C  393  THR CYS MET TYR ASN LYS ILE PRO VAL GLY SER GLU GLU          
SEQRES  14 C  393  GLY TYR ARG SER LEU PHE GLY GLN VAL LEU LYS ASP ILE          
SEQRES  15 C  393  VAL GLU LYS ILE SER MET LYS ILE LYS ASP ASN GLY ILE          
SEQRES  16 C  393  ILE GLY ASP ILE TYR SER THR GLY LEU ALA MET GLN ALA          
SEQRES  17 C  393  LEU SER VAL THR PRO GLU PRO SER LYS LYS GLU TRP ASN          
SEQRES  18 C  393  CYS LYS LYS THR THR ASP MET ILE LEU ASN GLU ILE LYS          
SEQRES  19 C  393  GLN GLY LYS PHE HIS ASN PRO MET SER ILE ALA GLN ILE          
SEQRES  20 C  393  LEU PRO SER LEU LYS GLY LYS THR TYR LEU ASP VAL PRO          
SEQRES  21 C  393  GLN VAL THR CYS SER PRO ASP HIS GLU VAL GLN PRO THR          
SEQRES  22 C  393  LEU PRO SER ASN PRO GLY PRO GLY PRO THR SER ALA SER          
SEQRES  23 C  393  ASN ILE THR VAL ILE TYR THR ILE ASN ASN GLN LEU ARG          
SEQRES  24 C  393  GLY VAL GLU LEU LEU PHE ASN GLU THR ILE ASN VAL SER          
SEQRES  25 C  393  VAL LYS SER GLY SER VAL LEU LEU VAL VAL LEU GLU GLU          
SEQRES  26 C  393  ALA GLN ARG LYS ASN PRO MET PHE LYS PHE GLU THR THR          
SEQRES  27 C  393  MET THR SER TRP GLY LEU VAL VAL SER SER ILE ASN ASN          
SEQRES  28 C  393  ILE ALA GLU ASN VAL ASN HIS LYS THR TYR TRP GLN PHE          
SEQRES  29 C  393  LEU SER GLY VAL THR PRO LEU ASN GLU GLY VAL ALA ASP          
SEQRES  30 C  393  TYR ILE PRO PHE ASN HIS GLU HIS ILE THR ALA ASN PHE          
SEQRES  31 C  393  THR GLN TYR                                                  
SEQRES   1 D  457  CYS GLY GLU ILE LEU THR GLU SER THR GLY THR ILE GLN          
SEQRES   2 D  457  SER PRO GLY HIS PRO ASN VAL TYR PRO HIS GLY ILE ASN          
SEQRES   3 D  457  CYS THR TRP HIS ILE LEU VAL GLN PRO ASN HIS LEU ILE          
SEQRES   4 D  457  HIS LEU MET PHE GLU THR PHE HIS LEU GLU PHE HIS TYR          
SEQRES   5 D  457  ASN CYS THR ASN ASP TYR LEU GLU VAL TYR ASP THR ASP          
SEQRES   6 D  457  SER GLU THR SER LEU GLY ARG TYR CYS GLY LYS SER ILE          
SEQRES   7 D  457  PRO PRO SER LEU THR SER SER GLY ASN SER LEU MET LEU          
SEQRES   8 D  457  VAL PHE VAL THR ASP SER ASP LEU ALA TYR GLU GLY PHE          
SEQRES   9 D  457  LEU ILE ASN TYR GLU ALA ILE SER ALA ALA THR ALA CYS          
SEQRES  10 D  457  LEU GLN ASP TYR THR ASP ASP LEU GLY THR PHE THR SER          
SEQRES  11 D  457  PRO ASN PHE PRO ASN ASN TYR PRO ASN ASN TRP GLU CYS          
SEQRES  12 D  457  ILE TYR ARG ILE THR VAL ARG THR GLY GLN LEU ILE ALA          
SEQRES  13 D  457  VAL HIS PHE THR ASN PHE SER LEU GLU GLU ALA ILE GLY          
SEQRES  14 D  457  ASN TYR TYR THR ASP PHE LEU GLU ILE ARG ASP GLY GLY          
SEQRES  15 D  457  TYR GLU LYS SER PRO LEU LEU GLY ILE PHE TYR GLY SER          
SEQRES  16 D  457  ASN LEU PRO PRO THR ILE ILE SER HIS SER ASN LYS LEU          
SEQRES  17 D  457  TRP LEU LYS PHE LYS SER ASP GLN ILE ASP THR ARG SER          
SEQRES  18 D  457  GLY PHE SER ALA TYR TRP ASP GLY SER SER THR GLY CYS          
SEQRES  19 D  457  GLY GLY ASN LEU THR THR SER SER GLY THR PHE ILE SER          
SEQRES  20 D  457  PRO ASN TYR PRO MET PRO TYR TYR HIS SER SER GLU CYS          
SEQRES  21 D  457  TYR TRP TRP LEU LYS SER SER HIS GLY SER ALA PHE GLU          
SEQRES  22 D  457  LEU GLU PHE LYS ASP PHE HIS LEU GLU HIS HIS PRO ASN          
SEQRES  23 D  457  CYS THR LEU ASP TYR LEU ALA VAL TYR ASP GLY PRO SER          
SEQRES  24 D  457  SER ASN SER HIS LEU LEU THR GLN LEU CYS GLY ASP GLU          
SEQRES  25 D  457  LYS PRO PRO LEU ILE ARG SER SER GLY ASP SER MET PHE          
SEQRES  26 D  457  ILE LYS LEU ARG THR ASP GLU GLY GLN GLN GLY ARG GLY          
SEQRES  27 D  457  PHE LYS ALA GLU TYR ARG GLN THR CYS GLU ASN VAL VAL          
SEQRES  28 D  457  ILE VAL ASN GLN THR TYR GLY ILE LEU GLU SER ILE GLY          
SEQRES  29 D  457  TYR PRO ASN PRO TYR SER GLU ASN GLN HIS CYS ASN TRP          
SEQRES  30 D  457  THR ILE ARG ALA THR THR GLY ASN THR VAL ASN TYR THR          
SEQRES  31 D  457  PHE LEU ALA PHE ASP LEU GLU HIS HIS ILE ASN CYS SER          
SEQRES  32 D  457  THR ASP TYR LEU GLU LEU TYR ASP GLY PRO ARG GLN MET          
SEQRES  33 D  457  GLY ARG TYR CYS GLY VAL ASP LEU PRO PRO PRO GLY SER          
SEQRES  34 D  457  THR THR SER SER LYS LEU GLN VAL LEU LEU LEU THR ASP          
SEQRES  35 D  457  GLY VAL GLY ARG ARG GLU LYS GLY PHE GLN MET GLN TRP          
SEQRES  36 D  457  PHE VAL                                                      
SEQRES   1 E  393  SER CYS SER VAL PRO SER ALA GLN GLU PRO LEU VAL ASN          
SEQRES   2 E  393  GLY ILE GLN VAL LEU MET GLU ASN SER VAL THR SER SER          
SEQRES   3 E  393  ALA TYR PRO ASN PRO SER ILE LEU ILE ALA MET ASN LEU          
SEQRES   4 E  393  ALA GLY ALA TYR ASN LEU LYS ALA GLN LYS LEU LEU THR          
SEQRES   5 E  393  TYR GLN LEU MET SER SER ASP ASN ASN ASP LEU THR ILE          
SEQRES   6 E  393  GLY HIS LEU GLY LEU THR ILE MET ALA LEU THR SER SER          
SEQRES   7 E  393  CYS ARG ASP PRO GLY ASP LYS VAL SER ILE LEU GLN ARG          
SEQRES   8 E  393  GLN MET GLU ASN TRP ALA PRO SER SER PRO ASN ALA GLU          
SEQRES   9 E  393  ALA SER ALA PHE TYR GLY PRO SER LEU ALA ILE LEU ALA          
SEQRES  10 E  393  LEU CYS GLN LYS ASN SER GLU ALA THR LEU PRO ILE ALA          
SEQRES  11 E  393  VAL ARG PHE ALA LYS THR LEU LEU ALA ASN SER SER PRO          
SEQRES  12 E  393  PHE ASN VAL ASP THR GLY ALA MET ALA THR LEU ALA LEU          
SEQRES  13 E  393  THR CYS MET TYR ASN LYS ILE PRO VAL GLY SER GLU GLU          
SEQRES  14 E  393  GLY TYR ARG SER LEU PHE GLY GLN VAL LEU LYS ASP ILE          
SEQRES  15 E  393  VAL GLU LYS ILE SER MET LYS ILE LYS ASP ASN GLY ILE          
SEQRES  16 E  393  ILE GLY ASP ILE TYR SER THR GLY LEU ALA MET GLN ALA          
SEQRES  17 E  393  LEU SER VAL THR PRO GLU PRO SER LYS LYS GLU TRP ASN          
SEQRES  18 E  393  CYS LYS LYS THR THR ASP MET ILE LEU ASN GLU ILE LYS          
SEQRES  19 E  393  GLN GLY LYS PHE HIS ASN PRO MET SER ILE ALA GLN ILE          
SEQRES  20 E  393  LEU PRO SER LEU LYS GLY LYS THR TYR LEU ASP VAL PRO          
SEQRES  21 E  393  GLN VAL THR CYS SER PRO ASP HIS GLU VAL GLN PRO THR          
SEQRES  22 E  393  LEU PRO SER ASN PRO GLY PRO GLY PRO THR SER ALA SER          
SEQRES  23 E  393  ASN ILE THR VAL ILE TYR THR ILE ASN ASN GLN LEU ARG          
SEQRES  24 E  393  GLY VAL GLU LEU LEU PHE ASN GLU THR ILE ASN VAL SER          
SEQRES  25 E  393  VAL LYS SER GLY SER VAL LEU LEU VAL VAL LEU GLU GLU          
SEQRES  26 E  393  ALA GLN ARG LYS ASN PRO MET PHE LYS PHE GLU THR THR          
SEQRES  27 E  393  MET THR SER TRP GLY LEU VAL VAL SER SER ILE ASN ASN          
SEQRES  28 E  393  ILE ALA GLU ASN VAL ASN HIS LYS THR TYR TRP GLN PHE          
SEQRES  29 E  393  LEU SER GLY VAL THR PRO LEU ASN GLU GLY VAL ALA ASP          
SEQRES  30 E  393  TYR ILE PRO PHE ASN HIS GLU HIS ILE THR ALA ASN PHE          
SEQRES  31 E  393  THR GLN TYR                                                  
SEQRES   1 F  457  CYS GLY GLU ILE LEU THR GLU SER THR GLY THR ILE GLN          
SEQRES   2 F  457  SER PRO GLY HIS PRO ASN VAL TYR PRO HIS GLY ILE ASN          
SEQRES   3 F  457  CYS THR TRP HIS ILE LEU VAL GLN PRO ASN HIS LEU ILE          
SEQRES   4 F  457  HIS LEU MET PHE GLU THR PHE HIS LEU GLU PHE HIS TYR          
SEQRES   5 F  457  ASN CYS THR ASN ASP TYR LEU GLU VAL TYR ASP THR ASP          
SEQRES   6 F  457  SER GLU THR SER LEU GLY ARG TYR CYS GLY LYS SER ILE          
SEQRES   7 F  457  PRO PRO SER LEU THR SER SER GLY ASN SER LEU MET LEU          
SEQRES   8 F  457  VAL PHE VAL THR ASP SER ASP LEU ALA TYR GLU GLY PHE          
SEQRES   9 F  457  LEU ILE ASN TYR GLU ALA ILE SER ALA ALA THR ALA CYS          
SEQRES  10 F  457  LEU GLN ASP TYR THR ASP ASP LEU GLY THR PHE THR SER          
SEQRES  11 F  457  PRO ASN PHE PRO ASN ASN TYR PRO ASN ASN TRP GLU CYS          
SEQRES  12 F  457  ILE TYR ARG ILE THR VAL ARG THR GLY GLN LEU ILE ALA          
SEQRES  13 F  457  VAL HIS PHE THR ASN PHE SER LEU GLU GLU ALA ILE GLY          
SEQRES  14 F  457  ASN TYR TYR THR ASP PHE LEU GLU ILE ARG ASP GLY GLY          
SEQRES  15 F  457  TYR GLU LYS SER PRO LEU LEU GLY ILE PHE TYR GLY SER          
SEQRES  16 F  457  ASN LEU PRO PRO THR ILE ILE SER HIS SER ASN LYS LEU          
SEQRES  17 F  457  TRP LEU LYS PHE LYS SER ASP GLN ILE ASP THR ARG SER          
SEQRES  18 F  457  GLY PHE SER ALA TYR TRP ASP GLY SER SER THR GLY CYS          
SEQRES  19 F  457  GLY GLY ASN LEU THR THR SER SER GLY THR PHE ILE SER          
SEQRES  20 F  457  PRO ASN TYR PRO MET PRO TYR TYR HIS SER SER GLU CYS          
SEQRES  21 F  457  TYR TRP TRP LEU LYS SER SER HIS GLY SER ALA PHE GLU          
SEQRES  22 F  457  LEU GLU PHE LYS ASP PHE HIS LEU GLU HIS HIS PRO ASN          
SEQRES  23 F  457  CYS THR LEU ASP TYR LEU ALA VAL TYR ASP GLY PRO SER          
SEQRES  24 F  457  SER ASN SER HIS LEU LEU THR GLN LEU CYS GLY ASP GLU          
SEQRES  25 F  457  LYS PRO PRO LEU ILE ARG SER SER GLY ASP SER MET PHE          
SEQRES  26 F  457  ILE LYS LEU ARG THR ASP GLU GLY GLN GLN GLY ARG GLY          
SEQRES  27 F  457  PHE LYS ALA GLU TYR ARG GLN THR CYS GLU ASN VAL VAL          
SEQRES  28 F  457  ILE VAL ASN GLN THR TYR GLY ILE LEU GLU SER ILE GLY          
SEQRES  29 F  457  TYR PRO ASN PRO TYR SER GLU ASN GLN HIS CYS ASN TRP          
SEQRES  30 F  457  THR ILE ARG ALA THR THR GLY ASN THR VAL ASN TYR THR          
SEQRES  31 F  457  PHE LEU ALA PHE ASP LEU GLU HIS HIS ILE ASN CYS SER          
SEQRES  32 F  457  THR ASP TYR LEU GLU LEU TYR ASP GLY PRO ARG GLN MET          
SEQRES  33 F  457  GLY ARG TYR CYS GLY VAL ASP LEU PRO PRO PRO GLY SER          
SEQRES  34 F  457  THR THR SER SER LYS LEU GLN VAL LEU LEU LEU THR ASP          
SEQRES  35 F  457  GLY VAL GLY ARG ARG GLU LYS GLY PHE GLN MET GLN TRP          
SEQRES  36 F  457  PHE VAL                                                      
MODRES 3KQ4 ASN D 1319  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN E  311  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN C  311  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D 1285  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1285  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1285  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN A  311  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D 1307  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1307  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1307  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1168  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1168  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D 1217  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D 1168  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1217  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1319  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1217  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F  984  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1092  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1092  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B  984  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D 1092  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D  984  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN C  413  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN E  413  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN A  413  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1319  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN B 1332  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN F 1332  ASN  GLYCOSYLATION SITE                                 
MODRES 3KQ4 ASN D 1332  ASN  GLYCOSYLATION SITE                                 
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    BMA  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    MAN  G   5      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    BMA  H   3      11                                                       
HET    MAN  H   4      11                                                       
HET    MAN  H   5      11                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    BMA  J   3      11                                                       
HET    MAN  J   4      11                                                       
HET    MAN  J   5      11                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    BMA  K   3      11                                                       
HET    MAN  K   4      11                                                       
HET    MAN  K   5      11                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    BMA  M   3      11                                                       
HET    MAN  M   4      11                                                       
HET    MAN  M   5      11                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    BMA  N   3      11                                                       
HET    MAN  N   4      11                                                       
HET    MAN  N   5      11                                                       
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    NAG  A2001      14                                                       
HET    B12  A2007      91                                                       
HET    NAG  B2001      14                                                       
HET    NAG  B2007      14                                                       
HET    NAG  B2008      14                                                       
HET    NAG  B2009      14                                                       
HET    NAG  B2012      14                                                       
HET    NAG  B2013      14                                                       
HET     CA  B2014       1                                                       
HET     CA  B2015       1                                                       
HET     CA  B2016       1                                                       
HET     CA  B2017       1                                                       
HET    NAG  C2001      14                                                       
HET    B12  C2007      91                                                       
HET    NAG  D2001      14                                                       
HET    NAG  D2007      14                                                       
HET    NAG  D2008      14                                                       
HET    NAG  D2009      14                                                       
HET    NAG  D2012      14                                                       
HET    NAG  D2013      14                                                       
HET     CA  D2014       1                                                       
HET     CA  D2015       1                                                       
HET     CA  D2016       1                                                       
HET     CA  D2017       1                                                       
HET    NAG  E2001      14                                                       
HET    B12  E2007      91                                                       
HET    NAG  F2001      14                                                       
HET    NAG  F2007      14                                                       
HET    NAG  F2008      14                                                       
HET    NAG  F2009      14                                                       
HET    NAG  F2012      14                                                       
HET    NAG  F2013      14                                                       
HET     CA  F2014       1                                                       
HET     CA  F2015       1                                                       
HET     CA  F2016       1                                                       
HET     CA  F2017       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     B12 COBALAMIN                                                        
HETNAM      CA CALCIUM ION                                                      
FORMUL   7  NAG    39(C8 H15 N O6)                                              
FORMUL   7  BMA    6(C6 H12 O6)                                                 
FORMUL   7  MAN    12(C6 H12 O6)                                                
FORMUL  17  B12    3(C62 H89 CO N13 O14 P 2+)                                   
FORMUL  24   CA    12(CA 2+)                                                    
HELIX    1   1 GLN A   32  ASN A   45  1                                  14    
HELIX    2   2 ASN A   54  GLY A   65  1                                  12    
HELIX    3   3 ASN A   68  SER A   82  1                                  15    
HELIX    4   4 ASP A   83  LEU A   87  5                                   5    
HELIX    5   5 THR A   88  SER A  101  1                                  14    
HELIX    6   6 GLY A  107  ASN A  119  1                                  13    
HELIX    7   7 GLU A  128  ALA A  131  5                                   4    
HELIX    8   8 PHE A  132  ASN A  146  1                                  15    
HELIX    9   9 ASN A  146  ASN A  164  1                                  19    
HELIX   10  10 ASN A  169  ASN A  185  1                                  17    
HELIX   11  11 GLY A  194  MET A  212  1                                  19    
HELIX   12  12 SER A  225  SER A  234  1                                  10    
HELIX   13  13 ASN A  245  GLN A  259  1                                  15    
HELIX   14  14 ASN A  264  LYS A  276  1                                  13    
HELIX   15  15 THR A  279  VAL A  286  5                                   8    
HELIX   16  16 VAL A  342  ASN A  354  1                                  13    
HELIX   17  17 PRO A  355  PHE A  357  5                                   3    
HELIX   18  18 ASN A  379  HIS A  382  5                                   4    
HELIX   19  19 GLN C   32  ASN C   45  1                                  14    
HELIX   20  20 ASN C   54  GLY C   65  1                                  12    
HELIX   21  21 ASN C   68  SER C   82  1                                  15    
HELIX   22  22 ASP C   83  LEU C   87  5                                   5    
HELIX   23  23 THR C   88  SER C  101  1                                  14    
HELIX   24  24 GLY C  107  ASN C  119  1                                  13    
HELIX   25  25 GLU C  128  ALA C  131  5                                   4    
HELIX   26  26 PHE C  132  ASN C  146  1                                  15    
HELIX   27  27 ASN C  146  ASN C  164  1                                  19    
HELIX   28  28 ASN C  169  ASN C  185  1                                  17    
HELIX   29  29 GLY C  194  MET C  212  1                                  19    
HELIX   30  30 SER C  225  SER C  234  1                                  10    
HELIX   31  31 ASN C  245  GLN C  259  1                                  15    
HELIX   32  32 ASN C  264  LYS C  276  1                                  13    
HELIX   33  33 THR C  279  VAL C  286  5                                   8    
HELIX   34  34 VAL C  342  ASN C  354  1                                  13    
HELIX   35  35 PRO C  355  PHE C  357  5                                   3    
HELIX   36  36 ASN C  379  HIS C  382  5                                   4    
HELIX   37  37 GLN E   32  ASN E   45  1                                  14    
HELIX   38  38 ASN E   54  GLY E   65  1                                  12    
HELIX   39  39 ASN E   68  SER E   82  1                                  15    
HELIX   40  40 ASP E   83  LEU E   87  5                                   5    
HELIX   41  41 THR E   88  SER E  101  1                                  14    
HELIX   42  42 GLY E  107  ASN E  119  1                                  13    
HELIX   43  43 GLU E  128  ALA E  131  5                                   4    
HELIX   44  44 PHE E  132  ASN E  146  1                                  15    
HELIX   45  45 ASN E  146  ASN E  164  1                                  19    
HELIX   46  46 ASN E  169  ASN E  185  1                                  17    
HELIX   47  47 GLY E  194  MET E  212  1                                  19    
HELIX   48  48 SER E  225  SER E  234  1                                  10    
HELIX   49  49 ASN E  245  GLN E  259  1                                  15    
HELIX   50  50 ASN E  264  LYS E  276  1                                  13    
HELIX   51  51 THR E  279  VAL E  286  5                                   8    
HELIX   52  52 VAL E  342  ASN E  354  1                                  13    
HELIX   53  53 PRO E  355  PHE E  357  5                                   3    
HELIX   54  54 ASN E  379  HIS E  382  5                                   4    
SHEET    1   A 5 ILE A 333  SER A 336  0                                        
SHEET    2   A 5 ILE A 312  ASN A 320 -1  N  ILE A 312   O  SER A 336           
SHEET    3   A 5 HIS A 409  GLN A 416  1  O  ILE A 410   N  THR A 317           
SHEET    4   A 5 THR A 384  SER A 390 -1  N  GLN A 387   O  ASN A 413           
SHEET    5   A 5 THR A 393  PRO A 394 -1  O  THR A 393   N  SER A 390           
SHEET    1   B 3 PHE A 359  THR A 364  0                                        
SHEET    2   B 3 GLY A 367  ILE A 373 -1  O  SER A 372   N  GLU A 360           
SHEET    3   B 3 ILE A 376  ALA A 377 -1  O  ILE A 376   N  ILE A 373           
SHEET    1   C 5 ILE B 935  LEU B 936  0                                        
SHEET    2   C 5 THR B 959  LEU B 963  1  O  HIS B 961   N  LEU B 936           
SHEET    3   C 5 SER B1019  VAL B1025 -1  O  LEU B1022   N  TRP B 960           
SHEET    4   C 5 TYR B 989  TYR B 993 -1  N  TYR B 993   O  MET B1021           
SHEET    5   C 5 SER B1000  TYR B1004 -1  O  TYR B1004   N  LEU B 990           
SHEET    1   D 4 THR B 940  THR B 942  0                                        
SHEET    2   D 4 ASN B1038  SER B1043 -1  O  TYR B1039   N  GLY B 941           
SHEET    3   D 4 HIS B 968  LEU B 972 -1  N  LEU B 969   O  ILE B1042           
SHEET    4   D 4 LEU B1013  THR B1014 -1  O  LEU B1013   N  LEU B 972           
SHEET    1   E 5 CYS B1048  TYR B1052  0                                        
SHEET    2   E 5 GLU B1073  ILE B1078  1  O  ILE B1075   N  GLN B1050           
SHEET    3   E 5 LEU B1139  LYS B1144 -1  O  LEU B1141   N  TYR B1076           
SHEET    4   E 5 PHE B1106  ARG B1110 -1  N  ARG B1110   O  TRP B1140           
SHEET    5   E 5 LEU B1119  PHE B1123 -1  O  GLY B1121   N  ILE B1109           
SHEET    1   F 4 PHE B1059  THR B1060  0                                        
SHEET    2   F 4 GLY B1153  ASP B1159 -1  O  ALA B1156   N  PHE B1059           
SHEET    3   F 4 ALA B1087  SER B1094 -1  N  THR B1091   O  SER B1155           
SHEET    4   F 4 ILE B1132  ILE B1133 -1  O  ILE B1132   N  VAL B1088           
SHEET    1   G 5 GLY B1166  GLY B1167  0                                        
SHEET    2   G 5 GLU B1190  LEU B1195  1  O  TRP B1194   N  GLY B1167           
SHEET    3   G 5 MET B1255  ARG B1260 -1  O  MET B1255   N  LEU B1195           
SHEET    4   G 5 TYR B1222  ASP B1227 -1  N  ALA B1224   O  LYS B1258           
SHEET    5   G 5 HIS B1234  LEU B1239 -1  O  LEU B1239   N  LEU B1223           
SHEET    1   H 4 SER B1173  ILE B1177  0                                        
SHEET    2   H 4 LYS B1271  GLN B1276 -1  O  ALA B1272   N  PHE B1176           
SHEET    3   H 4 PHE B1203  ASP B1209 -1  N  GLU B1204   O  ARG B1275           
SHEET    4   H 4 ILE B1248  ARG B1249 -1  O  ILE B1248   N  LEU B1205           
SHEET    1   I 5 VAL B1281  ILE B1283  0                                        
SHEET    2   I 5 HIS B1305  ARG B1311  1  O  ARG B1311   N  ILE B1283           
SHEET    3   I 5 LYS B1365  LEU B1371 -1  O  VAL B1368   N  TRP B1308           
SHEET    4   I 5 TYR B1337  ASP B1342 -1  N  GLU B1339   O  LEU B1369           
SHEET    5   I 5 ARG B1345  TYR B1350 -1  O  ARG B1345   N  ASP B1342           
SHEET    1   J 4 GLY B1289  GLU B1292  0                                        
SHEET    2   J 4 GLY B1381  TRP B1386 -1  O  MET B1384   N  LEU B1291           
SHEET    3   J 4 ASN B1319  ASP B1326 -1  N  LEU B1323   O  GLN B1383           
SHEET    4   J 4 GLY B1359  SER B1360 -1  O  GLY B1359   N  TYR B1320           
SHEET    1   K 5 ILE C 333  SER C 336  0                                        
SHEET    2   K 5 ILE C 312  ASN C 320 -1  N  ILE C 312   O  SER C 336           
SHEET    3   K 5 HIS C 409  GLN C 416  1  O  ILE C 410   N  THR C 317           
SHEET    4   K 5 THR C 384  SER C 390 -1  N  GLN C 387   O  ASN C 413           
SHEET    5   K 5 THR C 393  PRO C 394 -1  O  THR C 393   N  SER C 390           
SHEET    1   L 3 PHE C 359  THR C 364  0                                        
SHEET    2   L 3 GLY C 367  ILE C 373 -1  O  SER C 372   N  GLU C 360           
SHEET    3   L 3 ILE C 376  ALA C 377 -1  O  ILE C 376   N  ILE C 373           
SHEET    1   M 5 ILE D 935  LEU D 936  0                                        
SHEET    2   M 5 THR D 959  LEU D 963  1  O  HIS D 961   N  LEU D 936           
SHEET    3   M 5 SER D1019  VAL D1025 -1  O  LEU D1022   N  TRP D 960           
SHEET    4   M 5 TYR D 989  TYR D 993 -1  N  TYR D 993   O  MET D1021           
SHEET    5   M 5 SER D1000  TYR D1004 -1  O  TYR D1004   N  LEU D 990           
SHEET    1   N 4 THR D 940  THR D 942  0                                        
SHEET    2   N 4 ASN D1038  SER D1043 -1  O  TYR D1039   N  GLY D 941           
SHEET    3   N 4 HIS D 968  LEU D 972 -1  N  LEU D 969   O  ILE D1042           
SHEET    4   N 4 LEU D1013  THR D1014 -1  O  LEU D1013   N  LEU D 972           
SHEET    1   O 5 CYS D1048  TYR D1052  0                                        
SHEET    2   O 5 GLU D1073  ILE D1078  1  O  ILE D1075   N  GLN D1050           
SHEET    3   O 5 LEU D1139  LYS D1144 -1  O  LEU D1141   N  TYR D1076           
SHEET    4   O 5 PHE D1106  ARG D1110 -1  N  ARG D1110   O  TRP D1140           
SHEET    5   O 5 LEU D1119  PHE D1123 -1  O  GLY D1121   N  ILE D1109           
SHEET    1   P 4 PHE D1059  THR D1060  0                                        
SHEET    2   P 4 GLY D1153  ASP D1159 -1  O  ALA D1156   N  PHE D1059           
SHEET    3   P 4 ALA D1087  SER D1094 -1  N  THR D1091   O  SER D1155           
SHEET    4   P 4 ILE D1132  ILE D1133 -1  O  ILE D1132   N  VAL D1088           
SHEET    1   Q 5 GLY D1166  GLY D1167  0                                        
SHEET    2   Q 5 GLU D1190  LEU D1195  1  O  TRP D1194   N  GLY D1167           
SHEET    3   Q 5 MET D1255  ARG D1260 -1  O  MET D1255   N  LEU D1195           
SHEET    4   Q 5 TYR D1222  ASP D1227 -1  N  ALA D1224   O  LYS D1258           
SHEET    5   Q 5 HIS D1234  LEU D1239 -1  O  LEU D1239   N  LEU D1223           
SHEET    1   R 4 SER D1173  ILE D1177  0                                        
SHEET    2   R 4 LYS D1271  GLN D1276 -1  O  ALA D1272   N  PHE D1176           
SHEET    3   R 4 PHE D1203  ASP D1209 -1  N  GLU D1204   O  ARG D1275           
SHEET    4   R 4 ILE D1248  ARG D1249 -1  O  ILE D1248   N  LEU D1205           
SHEET    1   S 5 VAL D1281  ILE D1283  0                                        
SHEET    2   S 5 HIS D1305  ARG D1311  1  O  ARG D1311   N  ILE D1283           
SHEET    3   S 5 LYS D1365  LEU D1371 -1  O  VAL D1368   N  TRP D1308           
SHEET    4   S 5 TYR D1337  ASP D1342 -1  N  GLU D1339   O  LEU D1369           
SHEET    5   S 5 ARG D1345  TYR D1350 -1  O  ARG D1345   N  ASP D1342           
SHEET    1   T 4 GLY D1289  GLU D1292  0                                        
SHEET    2   T 4 GLY D1381  TRP D1386 -1  O  MET D1384   N  LEU D1291           
SHEET    3   T 4 ASN D1319  ASP D1326 -1  N  LEU D1323   O  GLN D1383           
SHEET    4   T 4 GLY D1359  SER D1360 -1  O  GLY D1359   N  TYR D1320           
SHEET    1   U 5 ILE E 333  SER E 336  0                                        
SHEET    2   U 5 ILE E 312  ASN E 320 -1  N  ILE E 312   O  SER E 336           
SHEET    3   U 5 HIS E 409  GLN E 416  1  O  ILE E 410   N  THR E 317           
SHEET    4   U 5 THR E 384  SER E 390 -1  N  GLN E 387   O  ASN E 413           
SHEET    5   U 5 THR E 393  PRO E 394 -1  O  THR E 393   N  SER E 390           
SHEET    1   V 3 PHE E 359  THR E 364  0                                        
SHEET    2   V 3 GLY E 367  ILE E 373 -1  O  SER E 372   N  GLU E 360           
SHEET    3   V 3 ILE E 376  ALA E 377 -1  O  ILE E 376   N  ILE E 373           
SHEET    1   W 5 ILE F 935  LEU F 936  0                                        
SHEET    2   W 5 THR F 959  LEU F 963  1  O  HIS F 961   N  LEU F 936           
SHEET    3   W 5 SER F1019  VAL F1025 -1  O  LEU F1022   N  TRP F 960           
SHEET    4   W 5 TYR F 989  TYR F 993 -1  N  TYR F 993   O  MET F1021           
SHEET    5   W 5 SER F1000  TYR F1004 -1  O  TYR F1004   N  LEU F 990           
SHEET    1   X 4 THR F 940  THR F 942  0                                        
SHEET    2   X 4 ASN F1038  SER F1043 -1  O  TYR F1039   N  GLY F 941           
SHEET    3   X 4 HIS F 968  LEU F 972 -1  N  LEU F 969   O  ILE F1042           
SHEET    4   X 4 LEU F1013  THR F1014 -1  O  LEU F1013   N  LEU F 972           
SHEET    1   Y 5 CYS F1048  TYR F1052  0                                        
SHEET    2   Y 5 GLU F1073  ILE F1078  1  O  ILE F1075   N  GLN F1050           
SHEET    3   Y 5 LEU F1139  LYS F1144 -1  O  LEU F1141   N  TYR F1076           
SHEET    4   Y 5 PHE F1106  ARG F1110 -1  N  ARG F1110   O  TRP F1140           
SHEET    5   Y 5 LEU F1119  PHE F1123 -1  O  GLY F1121   N  ILE F1109           
SHEET    1   Z 4 PHE F1059  THR F1060  0                                        
SHEET    2   Z 4 GLY F1153  ASP F1159 -1  O  ALA F1156   N  PHE F1059           
SHEET    3   Z 4 ALA F1087  SER F1094 -1  N  THR F1091   O  SER F1155           
SHEET    4   Z 4 ILE F1132  ILE F1133 -1  O  ILE F1132   N  VAL F1088           
SHEET    1  AA 5 GLY F1166  GLY F1167  0                                        
SHEET    2  AA 5 GLU F1190  LEU F1195  1  O  TRP F1194   N  GLY F1167           
SHEET    3  AA 5 MET F1255  ARG F1260 -1  O  MET F1255   N  LEU F1195           
SHEET    4  AA 5 TYR F1222  ASP F1227 -1  N  ALA F1224   O  LYS F1258           
SHEET    5  AA 5 HIS F1234  LEU F1239 -1  O  LEU F1239   N  LEU F1223           
SHEET    1  AB 4 SER F1173  ILE F1177  0                                        
SHEET    2  AB 4 LYS F1271  GLN F1276 -1  O  ALA F1272   N  PHE F1176           
SHEET    3  AB 4 PHE F1203  ASP F1209 -1  N  GLU F1204   O  ARG F1275           
SHEET    4  AB 4 ILE F1248  ARG F1249 -1  O  ILE F1248   N  LEU F1205           
SHEET    1  AC 5 VAL F1281  ILE F1283  0                                        
SHEET    2  AC 5 HIS F1305  ARG F1311  1  O  ARG F1311   N  ILE F1283           
SHEET    3  AC 5 LYS F1365  LEU F1371 -1  O  VAL F1368   N  TRP F1308           
SHEET    4  AC 5 TYR F1337  ASP F1342 -1  N  GLU F1339   O  LEU F1369           
SHEET    5  AC 5 ARG F1345  TYR F1350 -1  O  ARG F1345   N  ASP F1342           
SHEET    1  AD 4 GLY F1289  GLU F1292  0                                        
SHEET    2  AD 4 GLY F1381  TRP F1386 -1  O  MET F1384   N  LEU F1291           
SHEET    3  AD 4 ASN F1319  ASP F1326 -1  N  LEU F1323   O  GLN F1383           
SHEET    4  AD 4 GLY F1359  SER F1360 -1  O  GLY F1359   N  TYR F1320           
SSBOND   1 CYS A   26    CYS A  246                          1555   1555  2.04  
SSBOND   2 CYS A  103    CYS A  288                          1555   1555  2.06  
SSBOND   3 CYS A  143    CYS A  182                          1555   1555  2.10  
SSBOND   4 CYS B  932    CYS B  958                          1555   1555  2.04  
SSBOND   5 CYS B  985    CYS B 1005                          1555   1555  2.03  
SSBOND   6 CYS B 1048    CYS B 1074                          1555   1555  2.08  
SSBOND   7 CYS B 1165    CYS B 1191                          1555   1555  2.06  
SSBOND   8 CYS B 1218    CYS B 1240                          1555   1555  2.04  
SSBOND   9 CYS B 1278    CYS B 1306                          1555   1555  2.07  
SSBOND  10 CYS B 1333    CYS B 1351                          1555   1555  2.06  
SSBOND  11 CYS C   26    CYS C  246                          1555   1555  2.04  
SSBOND  12 CYS C  103    CYS C  288                          1555   1555  2.06  
SSBOND  13 CYS C  143    CYS C  182                          1555   1555  2.10  
SSBOND  14 CYS D  932    CYS D  958                          1555   1555  2.04  
SSBOND  15 CYS D  985    CYS D 1005                          1555   1555  2.03  
SSBOND  16 CYS D 1048    CYS D 1074                          1555   1555  2.08  
SSBOND  17 CYS D 1165    CYS D 1191                          1555   1555  2.06  
SSBOND  18 CYS D 1218    CYS D 1240                          1555   1555  2.04  
SSBOND  19 CYS D 1278    CYS D 1306                          1555   1555  2.07  
SSBOND  20 CYS D 1333    CYS D 1351                          1555   1555  2.06  
SSBOND  21 CYS E   26    CYS E  246                          1555   1555  2.04  
SSBOND  22 CYS E  103    CYS E  288                          1555   1555  2.06  
SSBOND  23 CYS E  143    CYS E  182                          1555   1555  2.10  
SSBOND  24 CYS F  932    CYS F  958                          1555   1555  2.04  
SSBOND  25 CYS F  985    CYS F 1005                          1555   1555  2.03  
SSBOND  26 CYS F 1048    CYS F 1074                          1555   1555  2.08  
SSBOND  27 CYS F 1165    CYS F 1191                          1555   1555  2.06  
SSBOND  28 CYS F 1218    CYS F 1240                          1555   1555  2.04  
SSBOND  29 CYS F 1278    CYS F 1306                          1555   1555  2.07  
SSBOND  30 CYS F 1333    CYS F 1351                          1555   1555  2.06  
LINK         ND2 ASN A 311                 C1  NAG A2001     1555   1555  1.45  
LINK         ND2 ASN A 413                 C1  NAG G   1     1555   1555  1.46  
LINK         ND2 ASN B 984                 C1  NAG B2001     1555   1555  1.46  
LINK         ND2 ASN B1092                 C1  NAG H   1     1555   1555  1.46  
LINK         ND2 ASN B1168                 C1  NAG B2007     1555   1555  1.45  
LINK         ND2 ASN B1217                 C1  NAG B2008     1555   1555  1.45  
LINK         ND2 ASN B1285                 C1  NAG B2009     1555   1555  1.45  
LINK         ND2 ASN B1307                 C1  NAG I   1     1555   1555  1.45  
LINK         ND2 ASN B1319                 C1  NAG B2012     1555   1555  1.47  
LINK         ND2 ASN B1332                 C1  NAG B2013     1555   1555  1.47  
LINK         ND2 ASN C 311                 C1  NAG C2001     1555   1555  1.44  
LINK         ND2 ASN C 413                 C1  NAG J   1     1555   1555  1.46  
LINK         ND2 ASN D 984                 C1  NAG D2001     1555   1555  1.46  
LINK         ND2 ASN D1092                 C1  NAG K   1     1555   1555  1.46  
LINK         ND2 ASN D1168                 C1  NAG D2007     1555   1555  1.45  
LINK         ND2 ASN D1217                 C1  NAG D2008     1555   1555  1.45  
LINK         ND2 ASN D1285                 C1  NAG D2009     1555   1555  1.45  
LINK         ND2 ASN D1307                 C1  NAG L   1     1555   1555  1.45  
LINK         ND2 ASN D1319                 C1  NAG D2012     1555   1555  1.44  
LINK         ND2 ASN D1332                 C1  NAG D2013     1555   1555  1.47  
LINK         ND2 ASN E 311                 C1  NAG E2001     1555   1555  1.44  
LINK         ND2 ASN E 413                 C1  NAG M   1     1555   1555  1.46  
LINK         ND2 ASN F 984                 C1  NAG F2001     1555   1555  1.46  
LINK         ND2 ASN F1092                 C1  NAG N   1     1555   1555  1.46  
LINK         ND2 ASN F1168                 C1  NAG F2007     1555   1555  1.45  
LINK         ND2 ASN F1217                 C1  NAG F2008     1555   1555  1.45  
LINK         ND2 ASN F1285                 C1  NAG F2009     1555   1555  1.45  
LINK         ND2 ASN F1307                 C1  NAG O   1     1555   1555  1.45  
LINK         ND2 ASN F1319                 C1  NAG F2012     1555   1555  1.45  
LINK         ND2 ASN F1332                 C1  NAG F2013     1555   1555  1.47  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.47  
LINK         O4  NAG G   2                 C1  BMA G   3     1555   1555  1.45  
LINK         O3  BMA G   3                 C1  MAN G   4     1555   1555  1.45  
LINK         O6  BMA G   3                 C1  MAN G   5     1555   1555  1.46  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.44  
LINK         O4  NAG H   2                 C1  BMA H   3     1555   1555  1.46  
LINK         O3  BMA H   3                 C1  MAN H   4     1555   1555  1.45  
LINK         O6  BMA H   3                 C1  MAN H   5     1555   1555  1.45  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.45  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.48  
LINK         O4  NAG J   2                 C1  BMA J   3     1555   1555  1.45  
LINK         O3  BMA J   3                 C1  MAN J   4     1555   1555  1.46  
LINK         O6  BMA J   3                 C1  MAN J   5     1555   1555  1.46  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.44  
LINK         O4  NAG K   2                 C1  BMA K   3     1555   1555  1.46  
LINK         O3  BMA K   3                 C1  MAN K   4     1555   1555  1.45  
LINK         O6  BMA K   3                 C1  MAN K   5     1555   1555  1.45  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.45  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.48  
LINK         O4  NAG M   2                 C1  BMA M   3     1555   1555  1.45  
LINK         O3  BMA M   3                 C1  MAN M   4     1555   1555  1.46  
LINK         O6  BMA M   3                 C1  MAN M   5     1555   1555  1.46  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.44  
LINK         O4  NAG N   2                 C1  BMA N   3     1555   1555  1.46  
LINK         O3  BMA N   3                 C1  MAN N   4     1555   1555  1.45  
LINK         O6  BMA N   3                 C1  MAN N   5     1555   1555  1.45  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.45  
LINK         OE1 GLU B 980                CA    CA B2014     1555   1555  2.29  
LINK         OD1 ASP B 988                CA    CA B2014     1555   1555  2.30  
LINK         OD1 ASP B1027                CA    CA B2014     1555   1555  2.30  
LINK         O   ASP B1027                CA    CA B2014     1555   1555  3.13  
LINK         O   ASP B1029                CA    CA B2014     1555   1555  2.29  
LINK         O   LEU B1030                CA    CA B2014     1555   1555  2.31  
LINK         OE1 GLU B1096                CA    CA B2015     1555   1555  2.29  
LINK         OD2 ASP B1105                CA    CA B2015     1555   1555  2.31  
LINK         OD1 ASP B1105                CA    CA B2015     1555   1555  2.74  
LINK         OD2 ASP B1146                CA    CA B2015     1555   1555  2.29  
LINK         O   ILE B1148                CA    CA B2015     1555   1555  2.30  
LINK         O   ASP B1149                CA    CA B2015     1555   1555  2.28  
LINK         OE2 GLU B1213                CA    CA B2016     1555   1555  2.28  
LINK         OD1 ASP B1221                CA    CA B2016     1555   1555  2.32  
LINK         OD2 ASP B1221                CA    CA B2016     1555   1555  2.67  
LINK         OD1 ASP B1262                CA    CA B2016     1555   1555  2.29  
LINK         O   ASP B1262                CA    CA B2016     1555   1555  2.32  
LINK         O   GLY B1264                CA    CA B2016     1555   1555  2.30  
LINK         O   GLN B1265                CA    CA B2016     1555   1555  2.32  
LINK         OE2 GLU B1328                CA    CA B2017     1555   1555  2.28  
LINK         OD2 ASP B1336                CA    CA B2017     1555   1555  2.30  
LINK         OD1 ASP B1373                CA    CA B2017     1555   1555  2.31  
LINK         O   VAL B1375                CA    CA B2017     1555   1555  2.29  
LINK         OE1 GLU D 980                CA    CA D2014     1555   1555  2.29  
LINK         OD1 ASP D 988                CA    CA D2014     1555   1555  2.30  
LINK         OD1 ASP D1027                CA    CA D2014     1555   1555  2.30  
LINK         O   ASP D1027                CA    CA D2014     1555   1555  3.13  
LINK         O   ASP D1029                CA    CA D2014     1555   1555  2.29  
LINK         O   LEU D1030                CA    CA D2014     1555   1555  2.31  
LINK         OE1 GLU D1096                CA    CA D2015     1555   1555  2.29  
LINK         OD2 ASP D1105                CA    CA D2015     1555   1555  2.31  
LINK         OD1 ASP D1105                CA    CA D2015     1555   1555  2.74  
LINK         OD2 ASP D1146                CA    CA D2015     1555   1555  2.29  
LINK         O   ILE D1148                CA    CA D2015     1555   1555  2.30  
LINK         O   ASP D1149                CA    CA D2015     1555   1555  2.28  
LINK         OE2 GLU D1213                CA    CA D2016     1555   1555  2.29  
LINK         OD1 ASP D1221                CA    CA D2016     1555   1555  2.32  
LINK         OD2 ASP D1221                CA    CA D2016     1555   1555  2.67  
LINK         OD1 ASP D1262                CA    CA D2016     1555   1555  2.29  
LINK         O   ASP D1262                CA    CA D2016     1555   1555  2.32  
LINK         O   GLY D1264                CA    CA D2016     1555   1555  2.30  
LINK         O   GLN D1265                CA    CA D2016     1555   1555  2.32  
LINK         OE2 GLU D1328                CA    CA D2017     1555   1555  2.28  
LINK         OD2 ASP D1336                CA    CA D2017     1555   1555  2.30  
LINK         OD1 ASP D1373                CA    CA D2017     1555   1555  2.31  
LINK         O   VAL D1375                CA    CA D2017     1555   1555  2.29  
LINK         OE1 GLU F 980                CA    CA F2014     1555   1555  2.29  
LINK         OD1 ASP F 988                CA    CA F2014     1555   1555  2.30  
LINK         OD1 ASP F1027                CA    CA F2014     1555   1555  2.30  
LINK         O   ASP F1027                CA    CA F2014     1555   1555  3.13  
LINK         O   ASP F1029                CA    CA F2014     1555   1555  2.29  
LINK         O   LEU F1030                CA    CA F2014     1555   1555  2.31  
LINK         OE1 GLU F1096                CA    CA F2015     1555   1555  2.29  
LINK         OD2 ASP F1105                CA    CA F2015     1555   1555  2.31  
LINK         OD1 ASP F1105                CA    CA F2015     1555   1555  2.74  
LINK         OD2 ASP F1146                CA    CA F2015     1555   1555  2.29  
LINK         O   ILE F1148                CA    CA F2015     1555   1555  2.30  
LINK         O   ASP F1149                CA    CA F2015     1555   1555  2.28  
LINK         OE2 GLU F1213                CA    CA F2016     1555   1555  2.28  
LINK         OD1 ASP F1221                CA    CA F2016     1555   1555  2.32  
LINK         OD2 ASP F1221                CA    CA F2016     1555   1555  2.67  
LINK         OD1 ASP F1262                CA    CA F2016     1555   1555  2.29  
LINK         O   ASP F1262                CA    CA F2016     1555   1555  2.32  
LINK         O   GLY F1264                CA    CA F2016     1555   1555  2.30  
LINK         O   GLN F1265                CA    CA F2016     1555   1555  2.32  
LINK         OE2 GLU F1328                CA    CA F2017     1555   1555  2.28  
LINK         OD2 ASP F1336                CA    CA F2017     1555   1555  2.30  
LINK         OD1 ASP F1373                CA    CA F2017     1555   1555  2.31  
LINK         O   VAL F1375                CA    CA F2017     1555   1555  2.29  
CISPEP   1 HIS B  948    PRO B  949          0         2.87                     
CISPEP   2 ASN B  950    VAL B  951          0       -19.58                     
CISPEP   3 PHE B 1064    PRO B 1065          0         8.49                     
CISPEP   4 TYR B 1181    PRO B 1182          0        -0.82                     
CISPEP   5 TYR B 1296    PRO B 1297          0         6.51                     
CISPEP   6 HIS D  948    PRO D  949          0         2.83                     
CISPEP   7 ASN D  950    VAL D  951          0       -19.58                     
CISPEP   8 PHE D 1064    PRO D 1065          0         8.50                     
CISPEP   9 TYR D 1181    PRO D 1182          0        -0.78                     
CISPEP  10 TYR D 1296    PRO D 1297          0         6.47                     
CISPEP  11 HIS F  948    PRO F  949          0         2.91                     
CISPEP  12 ASN F  950    VAL F  951          0       -19.59                     
CISPEP  13 PHE F 1064    PRO F 1065          0         8.51                     
CISPEP  14 TYR F 1181    PRO F 1182          0        -0.73                     
CISPEP  15 TYR F 1296    PRO F 1297          0         6.51                     
CRYST1  117.684  204.179  410.023  90.00  90.00  90.00 C 2 2 21     24          
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      0.008497  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004898  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002439        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system