spacer
spacer

PDBsum entry 2w20

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2w20
Jmol
Contents
Protein chains
470 a.a.
Ligands
MES ×2
GOL ×3
Metals
_CL ×3
Waters ×1025
HEADER    HYDROLASE                               21-OCT-08   2W20
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF THE NATIVE NANA
TITLE    2 SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 321-791;
COMPND   5 SYNONYM: NEURAMINIDASE A, NANA SIALIDASE;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE   3 ORGANISM_TAXID: 171101;
SOURCE   4 STRAIN: R6;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS    SECRETED, CELL WALL, HYDROLASE, SIALIDASE, GLYCOSIDASE,
KEYWDS   2 NEURAMINIDASE, PEPTIDOGLYCAN-ANCHOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.XU,P.W.ANDREW,G.L.TAYLOR
REVDAT   2   10-NOV-09 2W20    1       REMARK
REVDAT   1   23-DEC-08 2W20    0
JRNL        AUTH   G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS
JRNL        TITL 2 PNEUMONIAE SIALIDASE NANA.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  64   772 2008
JRNL        REFN                   ISSN 1744-3091
JRNL        PMID   18765901
JRNL        DOI    10.1107/S1744309108024044
REMARK   2
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)
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) : 1.49
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.23
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7
REMARK   3   NUMBER OF REFLECTIONS             : 159301
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.201
REMARK   3   R VALUE            (WORKING SET) : 0.200
REMARK   3   FREE R VALUE                     : 0.225
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 8003
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 40.2411 -  4.6338    0.88     4899   235  0.1801 0.1815
REMARK   3     2  4.6338 -  3.6788    0.94     4991   261  0.1602 0.1778
REMARK   3     3  3.6788 -  3.2140    0.96     5049   270  0.1735 0.1950
REMARK   3     4  3.2140 -  2.9202    0.96     5019   279  0.1878 0.2126
REMARK   3     5  2.9202 -  2.7109    0.97     5067   294  0.1971 0.2355
REMARK   3     6  2.7109 -  2.5511    0.98     5060   256  0.2015 0.2253
REMARK   3     7  2.5511 -  2.4234    0.98     5093   270  0.1966 0.2055
REMARK   3     8  2.4234 -  2.3179    0.98     5059   276  0.1986 0.2409
REMARK   3     9  2.3179 -  2.2287    0.98     5055   277  0.1976 0.2144
REMARK   3    10  2.2287 -  2.1518    0.99     5035   273  0.1915 0.2150
REMARK   3    11  2.1518 -  2.0845    0.99     5112   299  0.1935 0.2095
REMARK   3    12  2.0845 -  2.0249    0.99     5086   262  0.1910 0.2290
REMARK   3    13  2.0249 -  1.9716    0.99     5073   270  0.1990 0.2439
REMARK   3    14  1.9716 -  1.9235    0.99     5160   256  0.1974 0.2232
REMARK   3    15  1.9235 -  1.8798    1.00     5074   281  0.1920 0.2134
REMARK   3    16  1.8798 -  1.8398    1.00     5195   244  0.2007 0.2489
REMARK   3    17  1.8398 -  1.8030    1.00     5064   274  0.2065 0.2343
REMARK   3    18  1.8030 -  1.7690    1.00     5143   256  0.2022 0.2475
REMARK   3    19  1.7690 -  1.7374    1.00     5078   272  0.2160 0.2649
REMARK   3    20  1.7374 -  1.7079    0.99     5120   276  0.2140 0.2659
REMARK   3    21  1.7079 -  1.6804    0.99     5016   281  0.2105 0.2496
REMARK   3    22  1.6804 -  1.6545    0.99     5112   263  0.2071 0.2284
REMARK   3    23  1.6545 -  1.6302    0.99     4977   264  0.2200 0.2953
REMARK   3    24  1.6302 -  1.6072    0.98     5067   281  0.2225 0.2551
REMARK   3    25  1.6072 -  1.5855    0.99     5038   260  0.2305 0.2766
REMARK   3    26  1.5855 -  1.5649    0.98     5060   262  0.2430 0.2652
REMARK   3    27  1.5649 -  1.5453    0.98     5004   251  0.2422 0.2605
REMARK   3    28  1.5453 -  1.5267    0.99     5002   252  0.2471 0.2609
REMARK   3    29  1.5267 -  1.5090    0.97     5003   249  0.2475 0.2620
REMARK   3    30  1.5090 -  1.4920    0.90     4587   259  0.2624 0.2845
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              : 0.40
REMARK   3   B_SOL              : 45.55
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.870
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 14.85
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.81280
REMARK   3    B22 (A**2) : -1.01710
REMARK   3    B33 (A**2) : -1.79570
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      :  0.000           7630
REMARK   3   ANGLE     :  1.220          10302
REMARK   3   CHIRALITY :  0.110           1083
REMARK   3   PLANARITY :  0.000           1343
REMARK   3   DIHEDRAL  : 17.270           2825
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 2W20 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-08.
REMARK 100 THE PDBE ID CODE IS EBI-37899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ESRF
REMARK 200  BEAMLINE                       : ID14-2
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
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 159417
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.49
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0
REMARK 200  DATA REDUNDANCY                : 3.9
REMARK 200  R MERGE                    (I) : 0.07
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.00
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   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG4K, 0.1 M MES PH6.0
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       23.60000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      109.10000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.30000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      109.10000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.60000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.30000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 350
REMARK 350 BIOMOLECULE:  2
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: B
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     LYS A   791
REMARK 465     ALA B   321
REMARK 465     LYS B   791
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 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 348       71.12     71.52
REMARK 500    HIS A 369      176.07    178.88
REMARK 500    ASP A 372       46.42    -80.00
REMARK 500    ASP A 417      103.99     71.41
REMARK 500    ARG A 476     -149.64   -112.49
REMARK 500    LYS A 564      -87.70    -89.99
REMARK 500    HIS A 597     -124.38     41.63
REMARK 500    THR A 646     -119.10   -123.09
REMARK 500    TYR A 695       68.28     73.46
REMARK 500    LYS A 720     -158.49   -103.73
REMARK 500    GLU A 733       50.36    -92.13
REMARK 500    ALA A 751     -116.16   -132.84
REMARK 500    ASN B 339     -169.34    -79.78
REMARK 500    ILE B 348       68.92     70.25
REMARK 500    HIS B 369      176.81    179.12
REMARK 500    ASP B 372       45.13    -76.15
REMARK 500    ASP B 417      103.00     71.14
REMARK 500    ARG B 476     -152.13   -117.04
REMARK 500    ASP B 533     -156.11   -128.66
REMARK 500    LYS B 564      -86.15    -89.66
REMARK 500    HIS B 597     -126.33     44.67
REMARK 500    THR B 646     -117.83   -120.39
REMARK 500    TYR B 695       70.33     71.33
REMARK 500    LYS B 720     -152.53   -107.00
REMARK 500    GLU B 733     -120.25     30.10
REMARK 500    ALA B 751     -120.88   -133.86
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 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B1791
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1793
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1793
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1794
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1795
DBREF  2W20 A  321   791  UNP    P62576   NANA_STRR6     321    791
DBREF  2W20 B  321   791  UNP    P62576   NANA_STRR6     321    791
SEQRES   1 A  471  ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU SER GLY
SEQRES   2 A  471  ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS SER TYR
SEQRES   3 A  471  ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY THR LEU
SEQRES   4 A  471  ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER SER ASP
SEQRES   5 A  471  TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER GLU ASP
SEQRES   6 A  471  ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE THR ASN
SEQRES   7 A  471  LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER ILE GLY
SEQRES   8 A  471  SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN ASP PRO
SEQRES   9 A  471  GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET PHE PRO
SEQRES  10 A  471  GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN LYS GLU
SEQRES  11 A  471  GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR GLN ILE
SEQRES  12 A  471  LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR ILE ARG
SEQRES  13 A  471  GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS ALA THR
SEQRES  14 A  471  ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO ALA TYR
SEQRES  15 A  471  SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN LEU LEU
SEQRES  16 A  471  GLY ASN ILE TYR PHE THR THR ASN LYS THR SER PRO PHE
SEQRES  17 A  471  ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER TYR SER
SEQRES  18 A  471  ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN ASP ILE
SEQRES  19 A  471  THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE LEU GLY
SEQRES  20 A  471  VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN GLY PRO
SEQRES  21 A  471  HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR THR ASN
SEQRES  22 A  471  ASN VAL SER HIS LEU ASN GLY SER GLN SER SER ARG ILE
SEQRES  23 A  471  ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS ALA GLY
SEQRES  24 A  471  GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY GLN LYS
SEQRES  25 A  471  ILE HIS SER SER THR MET ASN ASN ARG ARG ALA GLN ASN
SEQRES  26 A  471  THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY ASP VAL
SEQRES  27 A  471  LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU GLN VAL
SEQRES  28 A  471  ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU LYS ASP
SEQRES  29 A  471  ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR VAL GLN
SEQRES  30 A  471  MET SER ALA ILE HIS THR MET HIS GLU GLY LYS GLU TYR
SEQRES  31 A  471  ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG GLU ASN
SEQRES  32 A  471  GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN GLY GLU
SEQRES  33 A  471  LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS GLY GLU
SEQRES  34 A  471  PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN GLY GLU
SEQRES  35 A  471  TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY GLN ASN
SEQRES  36 A  471  ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP ASP PHE
SEQRES  37 A  471  LEU SER LYS
SEQRES   1 B  471  ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU SER GLY
SEQRES   2 B  471  ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS SER TYR
SEQRES   3 B  471  ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY THR LEU
SEQRES   4 B  471  ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER SER ASP
SEQRES   5 B  471  TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER GLU ASP
SEQRES   6 B  471  ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE THR ASN
SEQRES   7 B  471  LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER ILE GLY
SEQRES   8 B  471  SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN ASP PRO
SEQRES   9 B  471  GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET PHE PRO
SEQRES  10 B  471  GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN LYS GLU
SEQRES  11 B  471  GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR GLN ILE
SEQRES  12 B  471  LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR ILE ARG
SEQRES  13 B  471  GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS ALA THR
SEQRES  14 B  471  ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO ALA TYR
SEQRES  15 B  471  SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN LEU LEU
SEQRES  16 B  471  GLY ASN ILE TYR PHE THR THR ASN LYS THR SER PRO PHE
SEQRES  17 B  471  ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER TYR SER
SEQRES  18 B  471  ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN ASP ILE
SEQRES  19 B  471  THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE LEU GLY
SEQRES  20 B  471  VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN GLY PRO
SEQRES  21 B  471  HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR THR ASN
SEQRES  22 B  471  ASN VAL SER HIS LEU ASN GLY SER GLN SER SER ARG ILE
SEQRES  23 B  471  ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS ALA GLY
SEQRES  24 B  471  GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY GLN LYS
SEQRES  25 B  471  ILE HIS SER SER THR MET ASN ASN ARG ARG ALA GLN ASN
SEQRES  26 B  471  THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY ASP VAL
SEQRES  27 B  471  LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU GLN VAL
SEQRES  28 B  471  ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU LYS ASP
SEQRES  29 B  471  ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR VAL GLN
SEQRES  30 B  471  MET SER ALA ILE HIS THR MET HIS GLU GLY LYS GLU TYR
SEQRES  31 B  471  ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG GLU ASN
SEQRES  32 B  471  GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN GLY GLU
SEQRES  33 B  471  LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS GLY GLU
SEQRES  34 B  471  PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN GLY GLU
SEQRES  35 B  471  TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY GLN ASN
SEQRES  36 B  471  ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP ASP PHE
SEQRES  37 B  471  LEU SER LYS
HET    MES  A1791      12
HET    MES  B1791      12
HET     CL  B1792       1
HET     CL  A1792       1
HET     CL  A1793       1
HET    GOL  B1793       6
HET    GOL  A1794       6
HET    GOL  A1795       6
HETNAM     GOL GLYCEROL
HETNAM      CL CHLORIDE ION
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL   3  GOL    3(C3 H8 O3)
FORMUL   4   CL    3(CL 1-)
FORMUL   5  MES    2(C6 H13 N O4 S)
FORMUL   6  HOH   *1025(H2 O1)
HELIX    1   1 ASP A  407  GLY A  411  5                                   5
HELIX    2   2 LYS A  440  MET A  445  5                                   6
HELIX    3   3 LYS A  499  SER A  503  5                                   5
HELIX    4   4 ILE A  554  LYS A  559  1                                   6
HELIX    5   5 SER A  596  SER A  601  1                                   6
HELIX    6   6 ASN A  640  GLN A  644  5                                   5
HELIX    7   7 TRP A  786  SER A  790  1                                   5
HELIX    8   8 ASP B  407  GLY B  411  5                                   5
HELIX    9   9 LYS B  440  MET B  445  5                                   6
HELIX   10  10 LYS B  499  SER B  503  5                                   5
HELIX   11  11 ILE B  554  LYS B  559  1                                   6
HELIX   12  12 SER B  596  SER B  601  1                                   6
HELIX   13  13 ASN B  640  GLN B  644  5                                   5
HELIX   14  14 TRP B  786  SER B  790  1                                   5
SHEET    1  AA 4 THR A 327  PHE A 330  0
SHEET    2  AA 4 THR A 778  ASN A 785 -1  O  LEU A 779   N  ILE A 329
SHEET    3  AA 4 GLU A 762  HIS A 769 -1  O  TYR A 763   N  PHE A 784
SHEET    4  AA 4 ASN A 753  GLY A 759 -1  O  SER A 754   N  LEU A 766
SHEET    1  AB 4 SER A 345  LYS A 353  0
SHEET    2  AB 4 LEU A 359  ARG A 366 -1  O  ILE A 360   N  LEU A 352
SHEET    3  AB 4 ILE A 376  SER A 383 -1  O  GLY A 377   N  GLU A 365
SHEET    4  AB 4 VAL A 394  THR A 397 -1  O  VAL A 394   N  ILE A 380
SHEET    1  AC 5 GLN A 552  ASP A 553  0
SHEET    2  AC 5 TYR A 535  SER A 541 -1  O  MET A 538   N  GLN A 552
SHEET    3  AC 5 ILE A 429  PHE A 436 -1  O  ILE A 429   N  SER A 541
SHEET    4  AC 5 VAL A 414  GLN A 422 -1  O  VAL A 414   N  PHE A 436
SHEET    5  AC 5 GLY A 571  THR A 572  1  O  GLY A 571   N  LEU A 420
SHEET    1  AD 7 TYR A 453  ILE A 456  0
SHEET    2  AD 7 LYS A 459  ARG A 466 -1  O  LYS A 459   N  ILE A 456
SHEET    3  AD 7 TYR A 473  ILE A 475 -1  O  TYR A 473   N  LEU A 464
SHEET    4  AD 7 THR A 480  TYR A 482 -1  O  TYR A 482   N  THR A 474
SHEET    5  AD 7 ALA A 488  VAL A 493 -1  N  THR A 489   O  VAL A 481
SHEET    6  AD 7 ASP A 507  LYS A 510 -1  O  TYR A 509   N  ARG A 492
SHEET    7  AD 7 GLN A 513  ASN A 517 -1  O  GLN A 513   N  LYS A 510
SHEET    1  AE 3 TYR A 453  ILE A 456  0
SHEET    2  AE 3 LYS A 459  ARG A 466 -1  O  LYS A 459   N  ILE A 456
SHEET    3  AE 3 PHE A 528  ARG A 529 -1  O  ARG A 529   N  TYR A 465
SHEET    1  AF 3 LEU A 566  VAL A 568  0
SHEET    2  AF 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3  AF 3 ILE A 574  VAL A 575 -1  O  ILE A 574   N  LEU A 586
SHEET    1  AG 4 LEU A 566  VAL A 568  0
SHEET    2  AG 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3  AG 4 SER A 603  SER A 609 -1  O  SER A 603   N  THR A 591
SHEET    4  AG 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608
SHEET    1  AH 2 ARG A 626  VAL A 628  0
SHEET    2  AH 2 GLN A 631  ILE A 633 -1  O  GLN A 631   N  VAL A 628
SHEET    1  AI 4 SER A 648  GLN A 652  0
SHEET    2  AI 4 VAL A 658  MET A 662 -1  O  LYS A 659   N  VAL A 651
SHEET    3  AI 4 ASP A 668  SER A 674 -1  O  GLN A 670   N  MET A 662
SHEET    4  AI 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671
SHEET    1  AJ 4 SER A 699  HIS A 705  0
SHEET    2  AJ 4 LYS A 708  ALA A 716 -1  O  LYS A 708   N  HIS A 705
SHEET    3  AJ 4 GLU A 722  VAL A 731 -1  O  MET A 725   N  ASN A 715
SHEET    4  AJ 4 LEU A 737  GLU A 749 -1  O  THR A 738   N  ARG A 730
SHEET    1  BA 4 THR B 327  PHE B 330  0
SHEET    2  BA 4 THR B 778  ASN B 785 -1  O  LEU B 779   N  ILE B 329
SHEET    3  BA 4 GLU B 762  HIS B 769 -1  O  TYR B 763   N  PHE B 784
SHEET    4  BA 4 ASN B 753  GLY B 759 -1  O  SER B 754   N  LEU B 766
SHEET    1  BB 4 SER B 345  LYS B 353  0
SHEET    2  BB 4 LEU B 359  ARG B 366 -1  O  ILE B 360   N  LEU B 352
SHEET    3  BB 4 ILE B 376  SER B 383 -1  O  GLY B 377   N  GLU B 365
SHEET    4  BB 4 VAL B 394  THR B 397 -1  O  VAL B 394   N  ILE B 380
SHEET    1  BC 5 GLN B 552  ASP B 553  0
SHEET    2  BC 5 TYR B 535  SER B 541 -1  O  MET B 538   N  GLN B 552
SHEET    3  BC 5 ILE B 429  PHE B 436 -1  O  ILE B 429   N  SER B 541
SHEET    4  BC 5 VAL B 414  GLN B 422 -1  O  VAL B 414   N  PHE B 436
SHEET    5  BC 5 GLY B 571  THR B 572  1  O  GLY B 571   N  LEU B 420
SHEET    1  BD 7 TYR B 453  ILE B 456  0
SHEET    2  BD 7 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456
SHEET    3  BD 7 TYR B 473  ILE B 475 -1  O  TYR B 473   N  LEU B 464
SHEET    4  BD 7 THR B 480  TYR B 482 -1  O  TYR B 482   N  THR B 474
SHEET    5  BD 7 ALA B 488  VAL B 493 -1  N  THR B 489   O  VAL B 481
SHEET    6  BD 7 ASP B 507  LYS B 510 -1  O  TYR B 509   N  ARG B 492
SHEET    7  BD 7 GLN B 513  ASN B 517 -1  O  GLN B 513   N  LYS B 510
SHEET    1  BE 3 TYR B 453  ILE B 456  0
SHEET    2  BE 3 LYS B 459  ARG B 466 -1  O  LYS B 459   N  ILE B 456
SHEET    3  BE 3 PHE B 528  ARG B 529 -1  O  ARG B 529   N  TYR B 465
SHEET    1  BF 7 LEU B 566  VAL B 568  0
SHEET    2  BF 7 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567
SHEET    3  BF 7 ILE B 574  VAL B 575 -1  O  ILE B 574   N  LEU B 586
SHEET    4  BF 7 ILE B 585  THR B 591 -1  O  LEU B 586   N  ILE B 574
SHEET    5  BF 7 HIS B 617  ALA B 618
SHEET    6  BF 7 SER B 603  SER B 609 -1  O  TYR B 608   N  HIS B 617
SHEET    7  BF 7 ILE B 585  THR B 591 -1  O  ILE B 585   N  SER B 609
SHEET    1  BG 2 ARG B 626  VAL B 628  0
SHEET    2  BG 2 GLN B 631  ILE B 633 -1  O  GLN B 631   N  VAL B 628
SHEET    1  BH 4 SER B 648  GLN B 652  0
SHEET    2  BH 4 VAL B 658  MET B 662 -1  O  LYS B 659   N  VAL B 651
SHEET    3  BH 4 ASP B 668  SER B 674 -1  O  GLN B 670   N  MET B 662
SHEET    4  BH 4 LYS B 686  LYS B 692 -1  O  LYS B 686   N  VAL B 671
SHEET    1  BI 4 SER B 699  HIS B 705  0
SHEET    2  BI 4 LYS B 708  ALA B 716 -1  O  LYS B 708   N  HIS B 705
SHEET    3  BI 4 GLU B 722  VAL B 731 -1  O  MET B 725   N  ASN B 715
SHEET    4  BI 4 LEU B 737  GLU B 749 -1  O  THR B 738   N  ARG B 730
CISPEP   1 GLY A  718    PRO A  719          0         6.25
CISPEP   2 ASN A  734    GLY A  735          0         0.36
CISPEP   3 ALA A  776    TYR A  777          0       -12.76
CISPEP   4 GLY B  718    PRO B  719          0         5.75
CISPEP   5 ALA B  776    TYR B  777          0        -6.02
SITE     1 AC1 10 TYR A 465  ARG A 466  GLU A 467  GLY A 468
SITE     2 AC1 10 GLU A 469  ARG A 529  HOH A2559  HOH A2560
SITE     3 AC1 10 ASN B 625  LYS B 632
SITE     1 AC2 12 ASN A 625  LYS A 632  GLU B 450  TYR B 465
SITE     2 AC2 12 ARG B 466  GLU B 467  GLY B 468  GLU B 469
SITE     3 AC2 12 LYS B 470  ARG B 529  GOL B1793  HOH B2465
SITE     1 AC3  4 ASN B 517  LYS B 524  THR B 525  SER B 526
SITE     1 AC4  5 GLY A 516  ASN A 517  LYS A 524  THR A 525
SITE     2 AC4  5 SER A 526
SITE     1 AC5  4 VAL A 628  GLN A 631  HOH A2396  HOH A2403
SITE     1 AC6  6 GLN A 627  LYS A 632  LYS A 683  GLU B 469
SITE     2 AC6  6 LYS B 470  MES B1791
SITE     1 AC7  7 ASP A 385  ASN A 386  GLU A 762  LYS A 783
SITE     2 AC7  7 HOH A2057  ASP B 490  LYS B 510
SITE     1 AC8  6 SER A 371  TRP A 373  SER A 409  ILE A 410
SITE     2 AC8  6 GLU A 425  HIS A 612
CRYST1   47.200   96.600  218.200  90.00  90.00  90.00 P 21 21 21    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      0.021186  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010352  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004583        0.00000
      
PROCHECK
Go to PROCHECK summary
 References