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PDBsum entry 4fpe

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Hydrolase/inhibitor PDB id
4fpe
Jmol
Contents
Protein chain
658 a.a.
Ligands
0H9
DMS ×2
Waters ×458
HEADER    HYDROLASE/INHIBITOR                     22-JUN-12   4FPE
TITLE     CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE
TITLE    2 IN COMPLEX WITH 2-[(4-METHOXYBENZYL)AMMONIO]ETHANESULFONATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE B;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: NEURAMINIDASE B;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE   3 ORGANISM_TAXID: 1313;
SOURCE   4 STRAIN: TIGR4;
SOURCE   5 GENE: NANB, SP_1687;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS    HYDROLASE, INTRAMOLECULAR TRANS-SIALIDASE, GLYCOSIDASE, DRUG DESIGN,
KEYWDS   2 NEURAMINIDASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.BREAR
REVDAT   2   14-NOV-12 4FPE    1       JRNL
REVDAT   1   31-OCT-12 4FPE    0
JRNL        AUTH   P.BREAR,J.TELFORD,G.L.TAYLOR,N.J.WESTWOOD
JRNL        TITL   SYNTHESIS AND STRUCTURAL CHARACTERISATION OF SELECTIVE
JRNL        TITL 2 NON-CARBOHYDRATE-BASED INHIBITORS OF BACTERIAL SIALIDASES.
JRNL        REF    CHEMBIOCHEM                   V.  13  2374 2012
JRNL        REFN                   ISSN 1439-4227
JRNL        PMID   23070966
JRNL        DOI    10.1002/CBIC.201200433
REMARK   2
REMARK   2 RESOLUTION.    2.18 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.18
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.11
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 38740
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191
REMARK   3   R VALUE            (WORKING SET) : 0.189
REMARK   3   FREE R VALUE                     : 0.236
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940
REMARK   3   FREE R VALUE TEST SET COUNT      : 1915
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 23.1100 -  5.2376    1.00     2817   142  0.2198 0.2379
REMARK   3     2  5.2376 -  4.1651    1.00     2688   125  0.1642 0.1630
REMARK   3     3  4.1651 -  3.6410    1.00     2663   143  0.1817 0.2314
REMARK   3     4  3.6410 -  3.3091    1.00     2629   137  0.1838 0.2296
REMARK   3     5  3.3091 -  3.0725    1.00     2663   129  0.1823 0.2309
REMARK   3     6  3.0725 -  2.8917    0.99     2604   144  0.1991 0.2536
REMARK   3     7  2.8917 -  2.7471    0.99     2562   147  0.2088 0.2383
REMARK   3     8  2.7471 -  2.6277    0.99     2602   146  0.2066 0.2699
REMARK   3     9  2.6277 -  2.5267    1.00     2608   133  0.1953 0.2729
REMARK   3    10  2.5267 -  2.4396    1.00     2595   134  0.1986 0.2658
REMARK   3    11  2.4396 -  2.3634    1.00     2626   122  0.1898 0.2874
REMARK   3    12  2.3634 -  2.2959    1.00     2565   145  0.1846 0.2572
REMARK   3    13  2.2959 -  2.2355    1.00     2597   145  0.1754 0.2453
REMARK   3    14  2.2355 -  2.1810    1.00     2606   123  0.1723 0.2691
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.86
REMARK   3   K_SOL              : 0.36
REMARK   3   B_SOL              : 39.53
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.870
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.34
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -3.15700
REMARK   3    B22 (A**2) : -4.78940
REMARK   3    B33 (A**2) : 7.94640
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           5334
REMARK   3   ANGLE     :  1.087           7213
REMARK   3   CHIRALITY :  0.079            785
REMARK   3   PLANARITY :  0.004            930
REMARK   3   DIHEDRAL  : 14.151           1963
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 4FPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-11
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
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 MICROMAX-007 HF
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 SATURN 944
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38884
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.180
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 4.600
REMARK 200  R MERGE                    (I) : 0.10300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.22
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.29800
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   (%): 47.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 0.1M IMIDAZOLE, PH 8.0,
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   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       38.11450
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.12400
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.24000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.12400
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.11450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.24000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A     1
REMARK 465     ASN A     2
REMARK 465     LYS A     3
REMARK 465     ARG A     4
REMARK 465     GLY A     5
REMARK 465     LEU A     6
REMARK 465     TYR A     7
REMARK 465     SER A     8
REMARK 465     LYS A     9
REMARK 465     LEU A    10
REMARK 465     GLY A    11
REMARK 465     ILE A    12
REMARK 465     SER A    13
REMARK 465     VAL A    14
REMARK 465     VAL A    15
REMARK 465     GLY A    16
REMARK 465     ILE A    17
REMARK 465     SER A    18
REMARK 465     LEU A    19
REMARK 465     LEU A    20
REMARK 465     MET A    21
REMARK 465     GLY A    22
REMARK 465     VAL A    23
REMARK 465     PRO A    24
REMARK 465     THR A    25
REMARK 465     LEU A    26
REMARK 465     ILE A    27
REMARK 465     HIS A    28
REMARK 465     ALA A    29
REMARK 465     ASN A    30
REMARK 465     GLU A    31
REMARK 465     LEU A    32
REMARK 465     ASN A    33
REMARK 465     TYR A    34
REMARK 465     GLY A    35
REMARK 465     GLN A    36
REMARK 465     LEU A    37
REMARK 465     SER A    38
REMARK 465     LYS A   697
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    ILE A 246       63.53     61.85
REMARK 500    SER A 271      138.17    179.37
REMARK 500    ASP A 327       96.20     65.82
REMARK 500    ASN A 353      145.38     63.59
REMARK 500    ALA A 355      100.77   -168.28
REMARK 500    ALA A 358        4.61     80.62
REMARK 500    ASN A 366       35.61     83.92
REMARK 500    ASN A 397        9.77     46.33
REMARK 500    ASN A 537       54.53     36.61
REMARK 500    SER A 615      140.16   -171.84
REMARK 500    ALA A 652     -122.00   -127.90
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 0H9 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VW0   RELATED DB: PDB
REMARK 900 RELATED ID: 2VW1   RELATED DB: PDB
REMARK 900 RELATED ID: 2VW2   RELATED DB: PDB
REMARK 900 RELATED ID: 4FOQ   RELATED DB: PDB
REMARK 900 RELATED ID: 4FOV   RELATED DB: PDB
REMARK 900 RELATED ID: 4FOW   RELATED DB: PDB
REMARK 900 RELATED ID: 4FOY   RELATED DB: PDB
REMARK 900 RELATED ID: 4FP2   RELATED DB: PDB
REMARK 900 RELATED ID: 4FP3   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPC   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPF   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPG   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPH   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPJ   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPK   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPL   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPO   RELATED DB: PDB
REMARK 900 RELATED ID: 4FPY   RELATED DB: PDB
REMARK 900 RELATED ID: 4FQ4   RELATED DB: PDB
DBREF  4FPE A    1   697  UNP    Q54727   NANB_STRPN       1    697
SEQRES   1 A  697  MET ASN LYS ARG GLY LEU TYR SER LYS LEU GLY ILE SER
SEQRES   2 A  697  VAL VAL GLY ILE SER LEU LEU MET GLY VAL PRO THR LEU
SEQRES   3 A  697  ILE HIS ALA ASN GLU LEU ASN TYR GLY GLN LEU SER ILE
SEQRES   4 A  697  SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN ASN
SEQRES   5 A  697  LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS LEU
SEQRES   6 A  697  SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS ALA
SEQRES   7 A  697  ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU SER
SEQRES   8 A  697  ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER ILE
SEQRES   9 A  697  PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE ARG
SEQRES  10 A  697  ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG PRO
SEQRES  11 A  697  ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL GLU
SEQRES  12 A  697  ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS THR
SEQRES  13 A  697  TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER GLU
SEQRES  14 A  697  THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN GLY
SEQRES  15 A  697  ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU GLY
SEQRES  16 A  697  LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU ILE
SEQRES  17 A  697  SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL SER
SEQRES  18 A  697  THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE GLN
SEQRES  19 A  697  SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE PRO
SEQRES  20 A  697  THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER SER
SEQRES  21 A  697  ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS SER
SEQRES  22 A  697  LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN GLY
SEQRES  23 A  697  LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE ASN
SEQRES  24 A  697  ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP ASN
SEQRES  25 A  697  LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER PHE
SEQRES  26 A  697  ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY LYS
SEQRES  27 A  697  THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE GLY
SEQRES  28 A  697  ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS GLU
SEQRES  29 A  697  ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN GLY
SEQRES  30 A  697  ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY VAL
SEQRES  31 A  697  VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR THR
SEQRES  32 A  697  ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS SER
SEQRES  33 A  697  LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER GLY
SEQRES  34 A  697  SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO MET
SEQRES  35 A  697  ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR PRO
SEQRES  36 A  697  THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG GLY
SEQRES  37 A  697  GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE LEU
SEQRES  38 A  697  GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY GLN
SEQRES  39 A  697  GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE ALA
SEQRES  40 A  697  THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER ASP
SEQRES  41 A  697  ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER ILE
SEQRES  42 A  697  PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL GLU
SEQRES  43 A  697  LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR THR
SEQRES  44 A  697  THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER GLY
SEQRES  45 A  697  GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE GLN
SEQRES  46 A  697  GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS TYR
SEQRES  47 A  697  SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU SER
SEQRES  48 A  697  THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN LEU
SEQRES  49 A  697  VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE ASP
SEQRES  50 A  697  TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER TYR GLY
SEQRES  51 A  697  TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS HIS
SEQRES  52 A  697  ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER ARG
SEQRES  53 A  697  ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE ASP
SEQRES  54 A  697  LEU GLU ILE ASN ASP LEU THR LYS
HET    0H9  A 701      16
HET    DMS  A 702       4
HET    DMS  A 703       4
HETNAM     0H9 2-[(4-METHOXYBENZYL)AMINO]ETHANESULFONIC ACID
HETNAM     DMS DIMETHYL SULFOXIDE
FORMUL   2  0H9    C10 H15 N O4 S
FORMUL   3  DMS    2(C2 H6 O S)
FORMUL   5  HOH   *458(H2 O)
HELIX    1   1 ILE A   57  LEU A   62  1                                   6
HELIX    2   2 ASP A   63  LEU A   65  5                                   3
HELIX    3   3 SER A  216  THR A  222  1                                   7
HELIX    4   4 GLU A  691  THR A  696  1                                   6
SHEET    1   A 6 PHE A  43  ASN A  51  0
SHEET    2   A 6 LYS A 202  PHE A 211 -1  O  ILE A 208   N  GLY A  45
SHEET    3   A 6 GLN A  70  LYS A  77 -1  N  VAL A  73   O  SER A 209
SHEET    4   A 6 ASN A 144  ASP A 151 -1  O  LEU A 146   N  MET A  74
SHEET    5   A 6 THR A 156  VAL A 161 -1  O  THR A 158   N  VAL A 149
SHEET    6   A 6 ILE A 164  THR A 170 -1  O  GLU A 169   N  TYR A 157
SHEET    1   B 6 ILE A  55  ASP A  56  0
SHEET    2   B 6 LYS A 185  LEU A 188 -1  O  LEU A 188   N  ILE A  55
SHEET    3   B 6 LEU A  84  SER A  91 -1  N  GLY A  89   O  THR A 187
SHEET    4   B 6 TYR A 101  ARG A 107 -1  O  PHE A 102   N  LEU A  90
SHEET    5   B 6 ILE A 112  ASP A 118 -1  O  ARG A 117   N  TYR A 101
SHEET    6   B 6 ILE A 123  ARG A 129 -1  O  ILE A 123   N  ASP A 118
SHEET    1   C 2 LYS A 136  HIS A 137  0
SHEET    2   C 2 GLN A 140  ALA A 141 -1  O  GLN A 140   N  HIS A 137
SHEET    1   D 2 VAL A 191  ARG A 193  0
SHEET    2   D 2 LYS A 196  HIS A 198 -1  O  HIS A 198   N  VAL A 191
SHEET    1   E 4 TYR A 243  THR A 251  0
SHEET    2   E 4 VAL A 257  ARG A 264 -1  O  LEU A 258   N  TYR A 250
SHEET    3   E 4 ILE A 275  SER A 282 -1  O  ASN A 276   N  ALA A 263
SHEET    4   E 4 ILE A 293  MET A 296 -1  O  ALA A 295   N  ILE A 277
SHEET    1   F 5 LYS A 475  LEU A 476  0
SHEET    2   F 5 TYR A 458  SER A 464 -1  N  MET A 461   O  LYS A 475
SHEET    3   F 5 THR A 339  MET A 346 -1  N  ALA A 343   O  ALA A 460
SHEET    4   F 5 SER A 324  GLU A 332 -1  N  SER A 324   O  MET A 346
SHEET    5   F 5 GLY A 493  GLN A 494  1  O  GLY A 493   N  SER A 328
SHEET    1   G 7 PHE A 362  GLU A 364  0
SHEET    2   G 7 TYR A 369  LYS A 375 -1  O  TYR A 370   N  LYS A 363
SHEET    3   G 7 TYR A 383  VAL A 385 -1  O  VAL A 385   N  LEU A 371
SHEET    4   G 7 VAL A 390  ASN A 393 -1  O  TYR A 392   N  THR A 384
SHEET    5   G 7 PRO A 399  ILE A 404 -1  O  TYR A 402   N  VAL A 391
SHEET    6   G 7 VAL A 410  GLU A 412 -1  O  LEU A 411   N  THR A 403
SHEET    7   G 7 LYS A 415  SER A 416 -1  O  LYS A 415   N  GLU A 412
SHEET    1   H 3 PHE A 362  GLU A 364  0
SHEET    2   H 3 TYR A 369  LYS A 375 -1  O  TYR A 370   N  LYS A 363
SHEET    3   H 3 PHE A 451  LYS A 452 -1  O  LYS A 452   N  LYS A 374
SHEET    1   I 2 THR A 418  ASP A 425  0
SHEET    2   I 2 ARG A 432  PRO A 441 -1  O  LYS A 438   N  GLN A 421
SHEET    1   J 3 TYR A 489  LEU A 490  0
SHEET    2   J 3 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489
SHEET    3   J 3 LEU A 496  ALA A 497 -1  N  LEU A 496   O  ILE A 505
SHEET    1   K 4 TYR A 489  LEU A 490  0
SHEET    2   K 4 LEU A 504  THR A 510 -1  O  TYR A 509   N  TYR A 489
SHEET    3   K 4 GLU A 513  SER A 519 -1  O  SER A 519   N  LEU A 504
SHEET    4   K 4 LYS A 527  SER A 532 -1  O  LYS A 527   N  ILE A 518
SHEET    1   L 4 ALA A 542  ARG A 548  0
SHEET    2   L 4 VAL A 551  PHE A 556 -1  O  PHE A 555   N  GLN A 543
SHEET    3   L 4 ALA A 564  SER A 568 -1  O  ALA A 564   N  PHE A 556
SHEET    4   L 4 SER A 579  TYR A 580 -1  O  SER A 579   N  TYR A 565
SHEET    1   M 4 SER A 594  LYS A 597  0
SHEET    2   M 4 ALA A 607  PRO A 613 -1  O  ILE A 609   N  ILE A 596
SHEET    3   M 4 GLY A 622  VAL A 629 -1  O  GLY A 627   N  VAL A 608
SHEET    4   M 4 ILE A 636  ASP A 643 -1  O  TYR A 642   N  LEU A 624
SHEET    1   N 3 SER A 654  GLU A 658  0
SHEET    2   N 3 ILE A 664  GLU A 669 -1  O  GLY A 665   N  THR A 657
SHEET    3   N 3 VAL A 685  LEU A 690 -1  O  LEU A 690   N  ILE A 664
CISPEP   1 SER A  271    LYS A  272          0        -0.60
CISPEP   2 ALA A  355    ASN A  356          0       -11.81
SITE     1 AC1 13 ARG A 245  ASP A 270  ILE A 326  ASP A 327
SITE     2 AC1 13 ASP A 344  MET A 346  TYR A 489  ARG A 557
SITE     3 AC1 13 ARG A 619  TYR A 653  TRP A 674  HOH A1077
SITE     4 AC1 13 HOH A1090
SITE     1 AC2  4 TYR A 250  THR A 251  GLN A 494  THR A 657
SITE     1 AC3  6 ARG A 129  VAL A 166  ARG A 310  HIS A 680
SITE     2 AC3  6 LEU A 681  SER A 682
CRYST1   76.229   82.480  116.248  90.00  90.00  90.00 P 21 21 21    4
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      0.013118  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012124  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008602        0.00000
      
PROCHECK
Go to PROCHECK summary
 References