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PDBsum entry 3ju4

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Hydrolase PDB id
3ju4
Jmol
Contents
Protein chain
670 a.a.
Ligands
SLB
Metals
_NA
_CL ×5
Waters ×1616
HEADER    HYDROLASE                               14-SEP-09   3JU4
TITLE     CRYSTAL STRUCTURE ANALYSIS OF ENDOSIALIDASENF AT 0.98 A RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ENDO-N-ACETYLNEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 246-910;
COMPND   5 SYNONYM: ENDONF, ENDO-N, ENDOSIALIDASE, G102;
COMPND   6 EC: 3.2.1.129;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE K1F;
SOURCE   3 ORGANISM_COMMON: BACTERIOPHAGE K1F;
SOURCE   4 ORGANISM_TAXID: 344021;
SOURCE   5 STRAIN: K1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET22B+
KEYWDS    ENDONF, POLYSIA, HIGH-RESOLUTION, 1A, GLYCOSIDASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.C.SCHULZ,P.NEUMAN,R.GERARDY-SCHAHN,G.M.SHELDRICK,R.FICNER
REVDAT   2   18-APR-12 3JU4    1       JRNL   VERSN
REVDAT   1   02-FEB-10 3JU4    0
JRNL        AUTH   E.C.SCHULZ,P.NEUMANN,R.GERARDY-SCHAHN,G.M.SHELDRICK,R.FICNER
JRNL        TITL   STRUCTURE ANALYSIS OF ENDOSIALIDASE NF AT 0.98 A RESOLUTION.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   176 2010
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   20124697
JRNL        DOI    10.1107/S0907444909048720
REMARK   2
REMARK   2 RESOLUTION.    0.98 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.98
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.116
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.133
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 25843
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 5260
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 27
REMARK   3   SOLVENT ATOMS      : 1616
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 43
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : NULL
REMARK   3   ANGLE DISTANCES                      (A) : NULL
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3JU4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 516832
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.980
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07300
REMARK 200   FOR THE DATA SET  : 12.4100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.08
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.41500
REMARK 200   FOR SHELL         : 3.420
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1V0E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG 8000, 0.1M TRIS/HCL PH
REMARK 280  7.2, 3% ISOPROPANOL, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z
REMARK 290       3555   -X+Y,-X,Z
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.52000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.36389
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.56333
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       59.52000
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       34.36389
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.56333
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       59.52000
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       34.36389
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.56333
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       68.72778
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      117.12667
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       68.72778
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      117.12667
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       68.72778
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      117.12667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 44390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 65530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -271.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      119.04000
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       59.52000
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      103.09166
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A1087  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A1088  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A2256  LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   OG1  THR A   434     OG1  THR A   443              1.97
REMARK 500   OD1  ASP A   779     O    HOH A  2257              2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 315   CD    GLU A 315   OE1     0.066
REMARK 500    ARG A 421   CZ    ARG A 421   NH1    -0.079
REMARK 500    ARG A 765   CD    ARG A 765   NE     -0.106
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 243   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    ARG A 243   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    LYS A 247   CD  -  CE  -  NZ  ANGL. DEV. =  21.9 DEGREES
REMARK 500    THR A 265   N   -  CA  -  CB  ANGL. DEV. =  11.7 DEGREES
REMARK 500    TYR A 296   CB  -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    TYR A 296   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    GLU A 309   CG  -  CD  -  OE1 ANGL. DEV. =  15.6 DEGREES
REMARK 500    ASP A 377   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A 398   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ARG A 406   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A 440   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES
REMARK 500    ARG A 549   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 549   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    GLU A 574   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES
REMARK 500    ARG A 611   CD  -  NE  -  CZ  ANGL. DEV. =  11.8 DEGREES
REMARK 500    ARG A 611   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 611   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    TYR A 661   CG  -  CD2 -  CE2 ANGL. DEV. =   5.0 DEGREES
REMARK 500    TYR A 661   CZ  -  CE2 -  CD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    LYS A 662   N   -  CA  -  CB  ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG A 667   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP A 690   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES
REMARK 500    ASN A 712   OD1 -  CG  -  ND2 ANGL. DEV. =  22.7 DEGREES
REMARK 500    ASN A 712   CB  -  CG  -  OD1 ANGL. DEV. = -17.4 DEGREES
REMARK 500    MET A 717   CG  -  SD  -  CE  ANGL. DEV. = -10.6 DEGREES
REMARK 500    HIS A 723   CE1 -  NE2 -  CD2 ANGL. DEV. =   4.2 DEGREES
REMARK 500    ARG A 765   CD  -  NE  -  CZ  ANGL. DEV. =  15.7 DEGREES
REMARK 500    ARG A 765   NE  -  CZ  -  NH1 ANGL. DEV. = -12.8 DEGREES
REMARK 500    ARG A 765   NE  -  CZ  -  NH2 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ARG A 812   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    VAL A 251      -53.61   -133.88
REMARK 500    GLU A 310       -0.46     67.92
REMARK 500    ASP A 321       71.79   -155.23
REMARK 500    ASN A 338       -1.27     79.54
REMARK 500    ARG A 354       19.27     58.88
REMARK 500    ASP A 364       38.88   -140.76
REMARK 500    SER A 528      156.87     78.97
REMARK 500    ASP A 533     -162.22   -162.61
REMARK 500    HIS A 624       33.11     70.31
REMARK 500    HIS A 628       -2.12     71.39
REMARK 500    VAL A 704       66.33     33.84
REMARK 500    ASP A 711     -131.69     57.62
REMARK 500    SER A 740     -133.53     56.23
REMARK 500    SER A 806      -16.84   -146.99
REMARK 500    SER A 808       75.38     57.00
REMARK 500    SER A 878       -8.84     78.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 GLN A  330     ASP A  331                  -32.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    ARG A 243         0.14    SIDE CHAIN
REMARK 500    ARG A 569         0.12    SIDE CHAIN
REMARK 500    ARG A 765         0.14    SIDE CHAIN
REMARK 500    ARG A 865         0.08    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A2214        DISTANCE =  5.51 ANGSTROMS
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                              NA A   7  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 322   O
REMARK 620 2 TYR A 324   O    83.7
REMARK 620 3 HIS A 743   O   118.1  93.8
REMARK 620 4 SER A 745   O   137.0  85.9 104.1
REMARK 620 5 ASP A 746   OD2  88.5 150.5 114.8  80.7
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLB A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 7
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V0E   RELATED DB: PDB
REMARK 900 RELATED ID: 1V0F   RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE DEPOSITORS STATE THAT RESIDUE 628 IS HIS AND THAT UNIPROT IS
REMARK 999 INCORRECT AT THIS POSITION.
DBREF  3JU4 A  246   910  UNP    Q04830   ENAN_BPK1F     246    910
SEQADV 3JU4 VAL A  241  UNP  Q04830              EXPRESSION TAG
SEQADV 3JU4 PRO A  242  UNP  Q04830              EXPRESSION TAG
SEQADV 3JU4 ARG A  243  UNP  Q04830              EXPRESSION TAG
SEQADV 3JU4 GLY A  244  UNP  Q04830              EXPRESSION TAG
SEQADV 3JU4 SER A  245  UNP  Q04830              EXPRESSION TAG
SEQADV 3JU4 HIS A  628  UNP  Q04830    ARG   628 SEE REMARK 999
SEQRES   1 A  670  VAL PRO ARG GLY SER ALA LYS GLY ASP GLY VAL THR ASP
SEQRES   2 A  670  ASP THR ALA ALA LEU THR SER ALA LEU ASN ASP THR PRO
SEQRES   3 A  670  VAL GLY GLN LYS ILE ASN GLY ASN GLY LYS THR TYR LYS
SEQRES   4 A  670  VAL THR SER LEU PRO ASP ILE SER ARG PHE ILE ASN THR
SEQRES   5 A  670  ARG PHE VAL TYR GLU ARG ILE PRO GLY GLN PRO LEU TYR
SEQRES   6 A  670  TYR ALA SER GLU GLU PHE VAL GLN GLY GLU LEU PHE LYS
SEQRES   7 A  670  ILE THR ASP THR PRO TYR TYR ASN ALA TRP PRO GLN ASP
SEQRES   8 A  670  LYS ALA PHE VAL TYR GLU ASN VAL ILE TYR ALA PRO TYR
SEQRES   9 A  670  MET GLY SER ASP ARG HIS GLY VAL SER ARG LEU HIS VAL
SEQRES  10 A  670  SER TRP VAL LYS SER GLY ASP ASP GLY GLN THR TRP SER
SEQRES  11 A  670  THR PRO GLU TRP LEU THR ASP LEU HIS PRO ASP TYR PRO
SEQRES  12 A  670  THR VAL ASN TYR HIS CYS MET SER MET GLY VAL CYS ARG
SEQRES  13 A  670  ASN ARG LEU PHE ALA MET ILE GLU THR ARG THR LEU ALA
SEQRES  14 A  670  LYS ASN ALA LEU THR ASN CYS ALA LEU TRP ASP ARG PRO
SEQRES  15 A  670  MET SER ARG SER LEU HIS LEU THR GLY GLY ILE THR LYS
SEQRES  16 A  670  ALA ALA ASN GLN ARG TYR ALA THR ILE HIS VAL PRO ASP
SEQRES  17 A  670  HIS GLY LEU PHE VAL GLY ASP PHE VAL ASN PHE SER ASN
SEQRES  18 A  670  SER ALA VAL THR GLY VAL SER GLY ASP MET THR VAL ALA
SEQRES  19 A  670  THR VAL ILE ASP LYS ASP ASN PHE THR VAL LEU THR PRO
SEQRES  20 A  670  ASN GLN GLN THR SER ASP LEU ASN ASN ALA GLY LYS ASN
SEQRES  21 A  670  TRP HIS MET GLY THR SER PHE HIS LYS SER PRO TRP ARG
SEQRES  22 A  670  LYS THR ASP LEU GLY LEU ILE PRO SER VAL THR GLU VAL
SEQRES  23 A  670  HIS SER PHE ALA THR ILE ASP ASN ASN GLY PHE ALA MET
SEQRES  24 A  670  GLY TYR HIS GLN GLY ASP VAL ALA PRO ARG GLU VAL GLY
SEQRES  25 A  670  LEU PHE TYR PHE PRO ASP ALA PHE ASN SER PRO SER ASN
SEQRES  26 A  670  TYR VAL ARG ARG GLN ILE PRO SER GLU TYR GLU PRO ASP
SEQRES  27 A  670  ALA SER GLU PRO CYS ILE LYS TYR TYR ASP GLY VAL LEU
SEQRES  28 A  670  TYR LEU ILE THR ARG GLY THR ARG GLY ASP ARG LEU GLY
SEQRES  29 A  670  SER SER LEU HIS ARG SER ARG ASP ILE GLY GLN THR TRP
SEQRES  30 A  670  GLU SER LEU ARG PHE PRO HIS ASN VAL HIS HIS THR THR
SEQRES  31 A  670  LEU PRO PHE ALA LYS VAL GLY ASP ASP LEU ILE MET PHE
SEQRES  32 A  670  GLY SER GLU ARG ALA GLU ASN GLU TRP GLU ALA GLY ALA
SEQRES  33 A  670  PRO ASP ASP ARG TYR LYS ALA SER TYR PRO ARG THR PHE
SEQRES  34 A  670  TYR ALA ARG LEU ASN VAL ASN ASN TRP ASN ALA ASP ASP
SEQRES  35 A  670  ILE GLU TRP VAL ASN ILE THR ASP GLN ILE TYR GLN GLY
SEQRES  36 A  670  GLY ILE VAL ASN SER GLY VAL GLY VAL GLY SER VAL VAL
SEQRES  37 A  670  VAL LYS ASP ASN TYR ILE TYR TYR MET PHE GLY GLY GLU
SEQRES  38 A  670  ASP HIS PHE ASN PRO TRP THR TYR GLY ASP ASN SER ALA
SEQRES  39 A  670  LYS ASP PRO PHE LYS SER ASP GLY HIS PRO SER ASP LEU
SEQRES  40 A  670  TYR CYS TYR LYS MET LYS ILE GLY PRO ASP ASN ARG VAL
SEQRES  41 A  670  SER ARG ASP PHE ARG TYR GLY ALA VAL PRO ASN ARG ALA
SEQRES  42 A  670  VAL PRO VAL PHE PHE ASP THR ASN GLY VAL ARG THR VAL
SEQRES  43 A  670  PRO ALA PRO MET GLU PHE THR GLY ASP LEU GLY LEU GLY
SEQRES  44 A  670  HIS VAL THR ILE ARG ALA SER THR SER SER ASN ILE ARG
SEQRES  45 A  670  SER GLU VAL LEU MET GLU GLY GLU TYR GLY PHE ILE GLY
SEQRES  46 A  670  LYS SER ILE PRO THR ASP ASN PRO ALA GLY GLN ARG ILE
SEQRES  47 A  670  ILE PHE CYS GLY GLY GLU GLY THR SER SER THR THR GLY
SEQRES  48 A  670  ALA GLN ILE THR LEU TYR GLY ALA ASN ASN THR ASP SER
SEQRES  49 A  670  ARG ARG ILE VAL TYR ASN GLY ASP GLU HIS LEU PHE GLN
SEQRES  50 A  670  SER ALA ASP VAL LYS PRO TYR ASN ASP ASN VAL THR ALA
SEQRES  51 A  670  LEU GLY GLY PRO SER ASN ARG PHE THR THR ALA TYR LEU
SEQRES  52 A  670  GLY SER ASN PRO ILE VAL THR
HET    SLB  A   1      21
HET     CL  A   2       1
HET     CL  A   3       1
HET     CL  A   4       1
HET     CL  A   5       1
HET     CL  A   6       1
HET     NA  A   7       1
HETNAM     SLB 5-N-ACETYL-BETA-D-NEURAMINIC ACID
HETNAM      CL CHLORIDE ION
HETNAM      NA SODIUM ION
HETSYN     SLB BETA-SIALIC ACID
FORMUL   2  SLB    C11 H19 N O9
FORMUL   3   CL    5(CL 1-)
FORMUL   8   NA    NA 1+
FORMUL   9  HOH   *1616(H2 O)
HELIX    1   1 ASP A  254  THR A  265  1                                  12
HELIX    2   2 ASP A  285  SER A  287  5                                   3
HELIX    3   3 PRO A  572  GLU A  576  5                                   5
HELIX    4   4 ASN A  832  GLY A  835  5                                   4
HELIX    5   5 SER A  847  GLY A  851  5                                   5
SHEET    1   A 8 ASP A 249  ASP A 253  0
SHEET    2   A 8 THR A 277  LYS A 279  1  O  THR A 277   N  GLY A 250
SHEET    3   A 8 ARG A 293  TYR A 296  1  O  ARG A 293   N  TYR A 278
SHEET    4   A 8 LEU A 304  ALA A 307 -1  O  TYR A 306   N  PHE A 294
SHEET    5   A 8 VAL A 686  ASP A 690  1  O  ASN A 687   N  TYR A 305
SHEET    6   A 8 ARG A 667  ASN A 674 -1  N  TYR A 670   O  VAL A 686
SHEET    7   A 8 ASP A 639  SER A 645 -1  N  LEU A 640   O  LEU A 673
SHEET    8   A 8 PHE A 633  VAL A 636 -1  N  ALA A 634   O  ILE A 641
SHEET    1   B 2 ILE A 271  ASN A 272  0
SHEET    2   B 2 PHE A 289  ILE A 290  1  O  ILE A 290   N  ILE A 271
SHEET    1   C 4 GLY A 314  LYS A 318  0
SHEET    2   C 4 ASP A 746  LYS A 753 -1  O  LYS A 751   N  GLU A 315
SHEET    3   C 4 TYR A 713  GLY A 720 -1  N  PHE A 718   O  TYR A 748
SHEET    4   C 4 GLY A 703  LYS A 710 -1  N  SER A 706   O  MET A 717
SHEET    1   D 3 TYR A 325  ALA A 327  0
SHEET    2   D 3 VAL A 339  SER A 347 -1  O  SER A 347   N  TYR A 325
SHEET    3   D 3 PHE A 334  TYR A 336 -1  N  PHE A 334   O  TYR A 341
SHEET    1   E 4 TYR A 325  ALA A 327  0
SHEET    2   E 4 VAL A 339  SER A 347 -1  O  SER A 347   N  TYR A 325
SHEET    3   E 4 HIS A 356  SER A 362 -1  O  VAL A 360   N  ALA A 342
SHEET    4   E 4 GLU A 373  TRP A 374 -1  O  GLU A 373   N  TRP A 359
SHEET    1   F 3 VAL A 385  HIS A 388  0
SHEET    2   F 3 ARG A 398  THR A 407 -1  O  GLU A 404   N  HIS A 388
SHEET    3   F 3 MET A 392  CYS A 395 -1  N  GLY A 393   O  PHE A 400
SHEET    1   G 4 VAL A 385  HIS A 388  0
SHEET    2   G 4 ARG A 398  THR A 407 -1  O  GLU A 404   N  HIS A 388
SHEET    3   G 4 LEU A 413  PRO A 422 -1  O  THR A 414   N  THR A 405
SHEET    4   G 4 ARG A 513  ASP A 516 -1  O  ARG A 513   N  ASP A 420
SHEET    1   H 4 SER A 426  THR A 430  0
SHEET    2   H 4 ASN A 500  THR A 505 -1  O  MET A 503   N  LEU A 427
SHEET    3   H 4 PHE A 456  SER A 460 -1  N  ASN A 458   O  GLY A 504
SHEET    4   H 4 GLY A 469  THR A 472 -1  O  MET A 471   N  VAL A 457
SHEET    1   I 5 THR A 475  ASP A 478  0
SHEET    2   I 5 ASN A 481  LEU A 485 -1  O  THR A 483   N  THR A 475
SHEET    3   I 5 TYR A 441  HIS A 445 -1  N  ILE A 444   O  PHE A 482
SHEET    4   I 5 ILE A 433  LYS A 435 -1  N  THR A 434   O  THR A 443
SHEET    5   I 5 LEU A 494  ASN A 495 -1  O  LEU A 494   N  LYS A 435
SHEET    1   J 4 GLU A 525  THR A 531  0
SHEET    2   J 4 PHE A 537  GLN A 543 -1  O  ALA A 538   N  ALA A 530
SHEET    3   J 4 GLU A 550  PHE A 556 -1  O  PHE A 556   N  PHE A 537
SHEET    4   J 4 VAL A 567  GLN A 570 -1  O  ARG A 569   N  LEU A 553
SHEET    1   K 4 ALA A 579  TYR A 587  0
SHEET    2   K 4 VAL A 590  GLY A 597 -1  O  TYR A 592   N  LYS A 585
SHEET    3   K 4 SER A 606  SER A 610 -1  O  SER A 610   N  LEU A 591
SHEET    4   K 4 GLU A 618  ARG A 621 -1  O  LEU A 620   N  LEU A 607
SHEET    1   L 2 PHE A 777  PHE A 778  0
SHEET    2   L 2 ARG A 784  THR A 785 -1  O  THR A 785   N  PHE A 777
SHEET    1   M 3 ARG A 837  CYS A 841  0
SHEET    2   M 3 GLN A 853  TYR A 857 -1  O  ILE A 854   N  PHE A 840
SHEET    3   M 3 ILE A 867  ASN A 870 -1  O  ASN A 870   N  GLN A 853
LINK         O   THR A 322                NA    NA A   7     1555   1555  2.44
LINK         O   TYR A 324                NA    NA A   7     1555   1555  2.53
LINK         O   HIS A 743                NA    NA A   7     1555   1555  2.46
LINK         O   SER A 745                NA    NA A   7     1555   1555  2.54
LINK         OD2 ASP A 746                NA    NA A   7     1555   1555  2.79
CISPEP   1 TYR A  382    PRO A  383          0         6.53
CISPEP   2 ALA A  547    PRO A  548          0        -3.55
SITE     1 AC1 17 HOH A  28  HOH A  47  HOH A 104  HOH A 147
SITE     2 AC1 17 TYR A 821  ARG A 837  ILE A 839  THR A 846
SITE     3 AC1 17 SER A 848  GLN A 853  ASN A 870  HOH A1238
SITE     4 AC1 17 HOH A1260  HOH A1508  HOH A1664  HOH A1830
SITE     5 AC1 17 HOH A2252
SITE     1 AC2  5 ARG A 596  GLY A 597  THR A 598  HIS A 628
SITE     2 AC2  5 HOH A2254
SITE     1 AC3  7 ALA A 327  TRP A 328  PRO A 329  GLY A 701
SITE     2 AC3  7 GLY A 703  VAL A 704  GLY A 719
SITE     1 AC4  7 ARG A 596  GLY A 597  SER A 605  VAL A 626
SITE     2 AC4  7 HIS A 627  HIS A 628  THR A 629
SITE     1 AC5  7 GLY A 799  HIS A 800  ILE A 803  ARG A 804
SITE     2 AC5  7 SER A 806  SER A 813  GLU A 814
SITE     1 AC6  6 GLU A 525  HIS A 527  TYR A 541  HIS A 542
SITE     2 AC6  6 GLU A 581  PRO A 582
SITE     1 AC7  7 THR A 322  TYR A 324  ASN A 326  HIS A 743
SITE     2 AC7  7 SER A 745  ASP A 746  ARG A 772
CRYST1  119.040  119.040  175.690  90.00  90.00 120.00 H 3           9
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      0.008401  0.004850  0.000000        0.00000
SCALE2      0.000000  0.009700  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005692        0.00000
      
PROCHECK
Go to PROCHECK summary
 References