spacer
spacer

PDBsum entry 3o9k

Go to PDB code: 
Top Page protein ligands links
Hydrolase PDB id
3o9k
Jmol
Contents
Protein chain
387 a.a.
Ligands
ETT
HEADER    HYDROLASE                               04-AUG-10   3O9K
TITLE     INFLUENZA NA IN COMPLEX WITH COMPOUND 6
CAVEAT     3O9K    PEPTIDE LINK ERROR BETWEEN A 445/446
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 81-467;
COMPND   5 EC: 3.2.1.18
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS (A/DUCK/UKRAINE/1/1963(H3N8)
SOURCE   3 );
SOURCE   4 ORGANISM_TAXID: 385580;
SOURCE   5 STRAIN: A/DUCK/UKRAINE/1/1963 H3N8
KEYWDS    GLYCOSIDASE, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.J.RUSSELL,P.S.KERRY
REVDAT   1   15-DEC-10 3O9K    0
JRNL        AUTH   S.RUDRAWAR,J.C.DYASON,M.A.RAMEIX-WELTI,F.J.ROSE,P.S.KERRY,
JRNL        AUTH 2 R.J.RUSSELL,S.VAN DER WERF,R.J.THOMSON,N.NAFFAKH,
JRNL        AUTH 3 M.VON ITZSTEIN
JRNL        TITL   NOVEL SIALIC ACID DERIVATIVES LOCK OPEN THE 150-LOOP OF AN
JRNL        TITL 2 INFLUENZA A VIRUS GROUP-1 SIALIDASE.
JRNL        REF    NAT COMMUN                    V.   1   113 2010
JRNL        REFN                   ESSN 2041-1723
JRNL        PMID   21081911
JRNL        DOI    10.1038/NCOMMS1114
REMARK   2
REMARK   2 RESOLUTION.    2.49 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.51
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.2
REMARK   3   NUMBER OF REFLECTIONS             : 13808
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224
REMARK   3   R VALUE            (WORKING SET) : 0.220
REMARK   3   FREE R VALUE                     : 0.296
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050
REMARK   3   FREE R VALUE TEST SET COUNT      : 697
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 21.5067 -  4.2567    0.99     2882   146  0.1792 0.2143
REMARK   3     2  4.2567 -  3.3830    0.97     2780   147  0.1929 0.2815
REMARK   3     3  3.3830 -  2.9566    0.96     2771   142  0.2500 0.3345
REMARK   3     4  2.9566 -  2.6868    0.94     2670   158  0.2676 0.3604
REMARK   3     5  2.6868 -  2.4945    0.70     2008   104  0.2962 0.4269
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              : 0.34
REMARK   3   B_SOL              : 23.34
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.640
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) : -18.18000
REMARK   3    B22 (A**2) : -18.18000
REMARK   3    B33 (A**2) : 36.36010
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : -0.00000
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      :  0.008           3108
REMARK   3   ANGLE     :  1.225           4195
REMARK   3   CHIRALITY :  0.076            451
REMARK   3   PLANARITY :  0.006            538
REMARK   3   DIHEDRAL  : 16.191           1133
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3O9K COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-10.
REMARK 100 THE RCSB ID CODE IS RCSB060836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-FEB-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13808
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.494
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 60.7
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   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% MPD, PH 7, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -Y,X,Z
REMARK 290       4555   Y,-X,Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  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       45.24550
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.24550
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       53.88900
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.24550
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.24550
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.88900
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       45.24550
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       45.24550
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       53.88900
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       45.24550
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       45.24550
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       53.88900
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    GLY A    96     O    GLY A   458              2.14
REMARK 500   O    THR A   333     N    PHE A   337              2.16
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    TYR A 170   CB    TYR A 170   CG      0.588
REMARK 500    GLN A 172   N     GLN A 172   CA      0.134
REMARK 500    GLN A 172   CB    GLN A 172   CG      0.244
REMARK 500    SER A 308   CA    SER A 308   CB      0.096
REMARK 500    PRO A 310   CD    PRO A 310   N       0.159
REMARK 500    THR A 333   CB    THR A 333   CG2     0.408
REMARK 500    PHE A 337   CB    PHE A 337   CG      0.694
REMARK 500    SER A 341   C     CYS A 342   N       0.159
REMARK 500    PRO A 345   C     MET A 346   N       0.252
REMARK 500    ARG A 397   CB    ARG A 397   CG      0.379
REMARK 500    ILE A 396   C     ARG A 397   N       0.207
REMARK 500    LYS A 399   CB    LYS A 399   CG      0.589
REMARK 500    LEU A 421   CB    LEU A 421   CG     -0.251
REMARK 500    GLU A 443   CA    GLU A 443   CB      0.143
REMARK 500    LYS A 445   CB    LYS A 445   CG      0.730
REMARK 500    LYS A 445   C     THR A 446   N      -0.257
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    TYR A 170   CA  -  CB  -  CG  ANGL. DEV. = -21.8 DEGREES
REMARK 500    TYR A 170   CB  -  CG  -  CD2 ANGL. DEV. =   8.5 DEGREES
REMARK 500    TYR A 170   CB  -  CG  -  CD1 ANGL. DEV. =  -9.4 DEGREES
REMARK 500    SER A 308   CB  -  CA  -  C   ANGL. DEV. =  25.4 DEGREES
REMARK 500    PRO A 310   CA  -  N   -  CD  ANGL. DEV. = -14.1 DEGREES
REMARK 500    PRO A 310   N   -  CA  -  CB  ANGL. DEV. =   8.7 DEGREES
REMARK 500    PRO A 310   N   -  CD  -  CG  ANGL. DEV. =  12.4 DEGREES
REMARK 500    THR A 333   OG1 -  CB  -  CG2 ANGL. DEV. = -17.5 DEGREES
REMARK 500    THR A 333   CA  -  CB  -  CG2 ANGL. DEV. = -21.3 DEGREES
REMARK 500    GLN A 334   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    PHE A 337   CA  -  CB  -  CG  ANGL. DEV. = -23.6 DEGREES
REMARK 500    PHE A 337   CB  -  CG  -  CD2 ANGL. DEV. = -12.2 DEGREES
REMARK 500    PHE A 337   CB  -  CG  -  CD1 ANGL. DEV. =  11.9 DEGREES
REMARK 500    GLN A 334   O   -  C   -  N   ANGL. DEV. = -10.5 DEGREES
REMARK 500    ARG A 397   N   -  CA  -  CB  ANGL. DEV. =  15.3 DEGREES
REMARK 500    LYS A 399   CA  -  CB  -  CG  ANGL. DEV. = -14.5 DEGREES
REMARK 500    LEU A 421   CB  -  CG  -  CD2 ANGL. DEV. = -17.5 DEGREES
REMARK 500    GLU A 420   O   -  C   -  N   ANGL. DEV. = -12.7 DEGREES
REMARK 500    LEU A 421   C   -  N   -  CA  ANGL. DEV. =  16.4 DEGREES
REMARK 500    GLU A 443   CB  -  CA  -  C   ANGL. DEV. =  14.5 DEGREES
REMARK 500    GLU A 442   O   -  C   -  N   ANGL. DEV. =  -9.9 DEGREES
REMARK 500    LYS A 445   CA  -  CB  -  CG  ANGL. DEV. = -15.8 DEGREES
REMARK 500    LYS A 445   CA  -  C   -  N   ANGL. DEV. =  16.0 DEGREES
REMARK 500    LYS A 445   O   -  C   -  N   ANGL. DEV. = -14.8 DEGREES
REMARK 500    THR A 446   C   -  N   -  CA  ANGL. DEV. =  20.2 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    ASN A  87       55.01   -108.66
REMARK 500    ASN A 146      -19.92    -41.42
REMARK 500    ARG A 152       56.49    -94.75
REMARK 500    LYS A 202       61.68   -155.87
REMARK 500    ILE A 224       71.45     43.27
REMARK 500    ASN A 249     -107.03    -83.12
REMARK 500    ARG A 250     -172.37    -30.43
REMARK 500    ALA A 252     -163.13   -127.28
REMARK 500    PHE A 272       56.95   -163.38
REMARK 500    ASN A 285      125.53   -170.82
REMARK 500    CYS A 293     -158.13   -107.90
REMARK 500    TRP A 297      -63.56    -99.94
REMARK 500    GLN A 334       12.73    -48.38
REMARK 500    GLN A 350      135.00    -25.42
REMARK 500    TYR A 352      173.12     68.63
REMARK 500    THR A 391       34.19    -77.10
REMARK 500    SER A 409     -144.11   -122.08
REMARK 500    LYS A 425     -177.89    -65.11
REMARK 500    GLU A 442        8.11    -68.73
REMARK 500    VAL A 459      135.30     73.65
REMARK 500    ASP A 460       34.37    -97.13
REMARK 500    ASP A 477      -25.90    -37.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    GLN A 172        -11.35
REMARK 500    GLN A 334        -12.78
REMARK 500    GLU A 420         10.22
REMARK 500    GLU A 442        -14.26
REMARK 500    LYS A 445        -18.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ARG A 397        21.4      L          L   OUTSIDE RANGE
REMARK 500    GLU A 443        20.0      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETT A 1
DBREF  3O9K A   83   478  UNP    Q07599   NRAM_I63A3      81    467
SEQADV 3O9K ASN A  296  UNP  Q07599    GLY   293 CONFLICT
SEQRES   1 A  387  THR TYR MET ASN ASN THR GLU ALA ILE CYS ASP ALA LYS
SEQRES   2 A  387  GLY PHE ALA PRO PHE SER LYS ASP ASN GLY ILE ARG ILE
SEQRES   3 A  387  GLY SER ARG GLY HIS ILE PHE VAL ILE ARG GLU PRO PHE
SEQRES   4 A  387  VAL SER CYS SER PRO ILE GLU CYS ARG THR PHE PHE LEU
SEQRES   5 A  387  THR GLN GLY SER LEU LEU ASN ASP LYS HIS SER ASN GLY
SEQRES   6 A  387  THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER
SEQRES   7 A  387  VAL GLU VAL GLY GLN SER PRO ASN VAL TYR GLN ALA ARG
SEQRES   8 A  387  PHE GLU ALA VAL ALA TRP SER ALA THR ALA CYS HIS ASP
SEQRES   9 A  387  GLY LYS LYS TRP MET THR VAL GLY VAL THR GLY PRO ASP
SEQRES  10 A  387  SER LYS ALA VAL ALA VAL ILE HIS TYR GLY GLY VAL PRO
SEQRES  11 A  387  THR ASP VAL VAL ASN SER TRP ALA GLY ASP ILE LEU ARG
SEQRES  12 A  387  THR GLN GLU SER SER CYS THR CYS ILE GLN GLY ASP CYS
SEQRES  13 A  387  TYR TRP VAL MET THR ASP GLY PRO ALA ASN ARG GLN ALA
SEQRES  14 A  387  GLN TYR ARG ILE TYR LYS ALA ASN GLN GLY ARG ILE ILE
SEQRES  15 A  387  GLY GLN THR ASP ILE SER PHE ASN GLY GLY HIS ILE GLU
SEQRES  16 A  387  GLU CYS SER CYS TYR PRO ASN ASP GLY LYS VAL GLU CYS
SEQRES  17 A  387  VAL CYS ARG ASP ASN TRP THR GLY THR ASN ARG PRO VAL
SEQRES  18 A  387  LEU VAL ILE SER PRO ASP LEU SER TYR ARG VAL GLY TYR
SEQRES  19 A  387  LEU CYS ALA GLY ILE PRO SER ASP THR PRO ARG GLY GLU
SEQRES  20 A  387  ASP THR GLN PHE THR GLY SER CYS THR SER PRO MET GLY
SEQRES  21 A  387  ASN GLN GLY TYR GLY VAL LYS GLY PHE GLY PHE ARG GLN
SEQRES  22 A  387  GLY THR ASP VAL TRP MET GLY ARG THR ILE SER ARG THR
SEQRES  23 A  387  SER ARG SER GLY PHE GLU ILE LEU ARG ILE LYS ASN GLY
SEQRES  24 A  387  TRP THR GLN THR SER LYS GLU GLN ILE ARG LYS GLN VAL
SEQRES  25 A  387  VAL VAL ASP ASN LEU ASN TRP SER GLY TYR SER GLY SER
SEQRES  26 A  387  PHE THR LEU PRO VAL GLU LEU SER GLY LYS ASP CYS LEU
SEQRES  27 A  387  VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY LYS PRO
SEQRES  28 A  387  GLU GLU LYS THR ILE TRP THR SER SER SER SER ILE VAL
SEQRES  29 A  387  MET CYS GLY VAL ASP TYR GLU VAL ALA ASP TRP SER TRP
SEQRES  30 A  387  HIS ASP GLY ALA ILE LEU PRO PHE ASP ILE
HET    ETT  A   1      30
HETNAM     ETT 5-(ACETYLAMINO)-2,6-ANHYDRO-3,5-DIDEOXY-3-[(2E)-3-(4-
HETNAM   2 ETT  METHYLPHENYL)PROP-2-EN-1-YL]-D-GLYCERO-D-GALACTO-NON-
HETNAM   3 ETT  2-ENONIC ACID
FORMUL   2  ETT    C21 H27 N O8
HELIX    1   1 ASN A  104  GLY A  109  1                                   6
HELIX    2   2 ASP A  142  ASN A  146  5                                   5
HELIX    3   3 PRO A  199  LYS A  202  5                                   4
HELIX    4   4 PRO A  418  GLY A  424  1                                   6
SHEET    1   A 4 ALA A  98  LYS A 102  0
SHEET    2   A 4 THR A 449  CYS A 457 -1  O  VAL A 455   N  PHE A 100
SHEET    3   A 4 VAL A 429  GLY A 439 -1  N  MET A 436   O  SER A 452
SHEET    4   A 4 SER A 412  LEU A 417 -1  N  PHE A 415   O  CYS A 431
SHEET    1   B 3 PHE A 115  ARG A 118  0
SHEET    2   B 3 CYS A 129  LEU A 139 -1  O  LEU A 134   N  ARG A 118
SHEET    3   B 3 VAL A 122  CYS A 124 -1  N  SER A 123   O  ARG A 130
SHEET    1   C 4 PHE A 115  ARG A 118  0
SHEET    2   C 4 CYS A 129  LEU A 139 -1  O  LEU A 134   N  ARG A 118
SHEET    3   C 4 THR A 157  GLU A 162 -1  O  VAL A 161   N  THR A 131
SHEET    4   C 4 ARG A 174  VAL A 178 -1  O  ALA A 177   N  LEU A 158
SHEET    1   D 4 SER A 181  HIS A 186  0
SHEET    2   D 4 TRP A 191  THR A 197 -1  O  MET A 192   N  CYS A 185
SHEET    3   D 4 VAL A 204  TYR A 209 -1  O  HIS A 208   N  THR A 193
SHEET    4   D 4 PRO A 213  ASN A 218 -1  O  VAL A 217   N  ALA A 205
SHEET    1   E 3 ARG A 226  THR A 227  0
SHEET    2   E 3 ASP A 238  ASP A 245 -1  O  THR A 244   N  ARG A 226
SHEET    3   E 3 THR A 233  ILE A 235 -1  N  THR A 233   O  TYR A 240
SHEET    1   F 4 ARG A 226  THR A 227  0
SHEET    2   F 4 ASP A 238  ASP A 245 -1  O  THR A 244   N  ARG A 226
SHEET    3   F 4 GLN A 253  ASN A 260 -1  O  ALA A 259   N  CYS A 239
SHEET    4   F 4 ARG A 263  ASP A 269 -1  O  ARG A 263   N  ASN A 260
SHEET    1   G 4 SER A 281  ASN A 285  0
SHEET    2   G 4 LYS A 288  VAL A 292 -1  O  VAL A 292   N  SER A 281
SHEET    3   G 4 PRO A 303  ILE A 307 -1  O  ILE A 307   N  VAL A 289
SHEET    4   G 4 TYR A 314  TYR A 318 -1  O  GLY A 317   N  VAL A 304
SHEET    1   H 4 GLY A 358  GLN A 361  0
SHEET    2   H 4 ASP A 364  THR A 370 -1  O  ASP A 364   N  GLN A 361
SHEET    3   H 4 SER A 377  ILE A 384 -1  O  LEU A 382   N  MET A 367
SHEET    4   H 4 GLN A 395  TRP A 408 -1  O  ASN A 407   N  GLY A 378
SSBOND   1 CYS A   92    CYS A  427                          1555   1555  2.03
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.05
SSBOND   3 CYS A  185    CYS A  232                          1555   1555  2.03
SSBOND   4 CYS A  234    CYS A  239                          1555   1555  2.04
SSBOND   5 CYS A  280    CYS A  293                          1555   1555  2.04
SSBOND   6 CYS A  282    CYS A  291                          1555   1555  2.05
SSBOND   7 CYS A  320    CYS A  342                          1555   1555  2.04
SSBOND   8 CYS A  431    CYS A  457                          1555   1555  2.04
CISPEP   1 THR A  327    PRO A  328          0         4.47
CISPEP   2 LYS A  440    PRO A  441          0         6.20
CISPEP   3 LEU A  474    PRO A  475          0        -2.08
SITE     1 AC1 11 ARG A 118  ASP A 151  ARG A 152  TRP A 180
SITE     2 AC1 11 ALA A 248  GLU A 278  GLU A 279  ARG A 294
SITE     3 AC1 11 TYR A 352  ARG A 376  TYR A 411
CRYST1   90.491   90.491  107.778  90.00  90.00  90.00 I 4           8
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      0.011051  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011051  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009278        0.00000
      
PROCHECK
Go to PROCHECK summary
 References