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PDBsum entry 4ks1

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Hydrolase/hydrolase inhibitor PDB id
4ks1
Jmol
Contents
Protein chain
389 a.a.
Ligands
2H8
NAG
Metals
_CA
Waters ×277
HEADER    HYDROLASE/HYDROLASE INHIBITOR           17-MAY-13   4KS1
TITLE     INFLUENZA NEURAMINIDASE IN COMPLEX WITH ANTIVIRAL COMPOUND (3S,4R,5R)-
TITLE    2 4-(ACETYLAMINO)-3-AMINO-5-(PENTAN-3-YLOXY)CYCLOHEX-1-ENE-1-CARBOXYLIC
TITLE    3 ACID
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 81-470;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 ORGANISM_COMMON: INFLUENZA VIRUS;
SOURCE   4 ORGANISM_TAXID: 385580;
SOURCE   5 STRAIN: A/DUCK/UKRAINE/1/1963 H3N8;
SOURCE   6 GENE: NA;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    SIALIDASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.S.KERRY,R.J.M.RUSSELL
REVDAT   1   30-OCT-13 4KS1    0
JRNL        AUTH   P.S.KERRY,S.MOHAN,R.J.RUSSELL,N.BANCE,M.NIIKURA,B.M.PINTO
JRNL        TITL   STRUCTURAL BASIS FOR A CLASS OF NANOMOLAR INFLUENZA A
JRNL        TITL 2 NEURAMINIDASE INHIBITORS.
JRNL        REF    SCI REP                       V.   3  2871 2013
JRNL        REFN                   ESSN 2045-2322
JRNL        PMID   24129600
JRNL        DOI    10.1038/SREP02871
REMARK   2
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.20
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.08
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3
REMARK   3   NUMBER OF REFLECTIONS             : 17888
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155
REMARK   3   R VALUE            (WORKING SET) : 0.153
REMARK   3   FREE R VALUE                     : 0.201
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110
REMARK   3   FREE R VALUE TEST SET COUNT      : 914
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 22.0775 -  4.2004    1.00     2643   130  0.1443 0.1709
REMARK   3     2  4.2004 -  3.3377    1.00     2625   113  0.1305 0.1493
REMARK   3     3  3.3377 -  2.9169    1.00     2589   150  0.1455 0.2203
REMARK   3     4  2.9169 -  2.6507    1.00     2543   157  0.1619 0.2236
REMARK   3     5  2.6507 -  2.4609    0.99     2570   148  0.1793 0.2219
REMARK   3     6  2.4609 -  2.3160    0.88     2278   115  0.1874 0.2474
REMARK   3     7  2.3160 -  2.2001    0.67     1726   101  0.1997 0.2717
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              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.650
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.008           3136
REMARK   3   ANGLE     :  1.088           4244
REMARK   3   CHIRALITY :  0.232            455
REMARK   3   PLANARITY :  0.004            549
REMARK   3   DIHEDRAL  : 12.896           1130
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 4KS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB079722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
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) : 1.54
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 : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17922
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
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) : 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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2HT5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% 2-METHYL-2,4-PENTANEDIOL, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       45.12650
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.12650
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       47.05800
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.12650
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.12650
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       47.05800
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       45.12650
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       45.12650
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       47.05800
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       45.12650
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       45.12650
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       47.05800
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: 13660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 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 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 A 625  LIES ON A SPECIAL POSITION.
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   471
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   ND2  ASN A   146     C1   NAG A   503              1.79
REMARK 500   O    LYS A   470     O    HOH A   839              1.80
REMARK 500   O3   NAG A   503     O    HOH A   874              1.84
REMARK 500   OD1  ASP A   450     O    HOH A   828              1.88
REMARK 500   ND2  ASN A   146     O1   NAG A   503              1.88
REMARK 500   OE1  GLU A   389     O    HOH A   797              1.92
REMARK 500   NZ   LYS A   415     O    HOH A   831              1.94
REMARK 500   OE1  GLU A   452     O    HOH A   864              2.05
REMARK 500   O    HOH A   669     O    HOH A   760              2.06
REMARK 500   NH1  ARG A   248     O    HOH A   806              2.09
REMARK 500   C3   NAG A   503     O    HOH A   874              2.14
REMARK 500   O    HOH A   777     O    HOH A   789              2.14
REMARK 500   O    HOH A   673     O    HOH A   810              2.18
REMARK 500   C2   NAG A   503     O    HOH A   874              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NZ   LYS A   430     O    HOH A   663     6445     2.16
REMARK 500   O    HOH A   842     O    HOH A   848     3555     2.16
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    ARG A 111      -40.42   -130.56
REMARK 500    LYS A 200       49.62   -156.40
REMARK 500    ASP A 221       79.94   -152.39
REMARK 500    THR A 225     -159.76   -145.25
REMARK 500    ALA A 250     -163.63   -119.21
REMARK 500    PHE A 270       55.25   -161.48
REMARK 500    ASN A 283      114.29   -160.00
REMARK 500    CYS A 291     -162.24   -123.09
REMARK 500    TRP A 295      -75.86    -98.97
REMARK 500    TYR A 347     -166.62     59.51
REMARK 500    THR A 386       35.95    -72.23
REMARK 500    SER A 404     -132.88   -117.78
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 A 833        DISTANCE =  6.51 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                              CA A 501  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 347   O
REMARK 620 2 ASP A 293   O    92.7
REMARK 620 3 ASP A 324   OD1 110.2  86.3
REMARK 620 4 GLY A 297   O   157.1  91.8  92.5
REMARK 620 5 HOH A 651   O    72.7 164.9 102.1 100.3
REMARK 620 6 HOH A 742   O    72.4  84.8 170.8  85.7  87.1
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2H8 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KS2   RELATED DB: PDB
REMARK 900 RELATED ID: 4KS3   RELATED DB: PDB
REMARK 900 RELATED ID: 4KS4   RELATED DB: PDB
REMARK 900 RELATED ID: 4KS5   RELATED DB: PDB
DBREF  4KS1 A   83   471  UNP    Q0A480   Q0A480_I63A3    81    470
SEQRES   1 A  390  THR TYR MET ASN ASN THR GLU ALA ILE CYS ASP VAL LYS
SEQRES   2 A  390  GLY PHE ALA PRO PHE SER LYS ASP ASN GLY ILE ARG ILE
SEQRES   3 A  390  GLY SER ARG GLY HIS ILE PHE VAL ILE ARG GLU PRO PHE
SEQRES   4 A  390  VAL SER CYS SER PRO ILE GLU CYS ARG THR PHE PHE LEU
SEQRES   5 A  390  THR GLN GLY SER LEU LEU ASN ASP LYS HIS SER ASN GLY
SEQRES   6 A  390  THR VAL LYS ASP ARG SER PRO PHE ARG THR LEU MET SER
SEQRES   7 A  390  VAL LYS VAL GLY GLN SER PRO ASN VAL TYR GLN ALA ARG
SEQRES   8 A  390  PHE GLU ALA VAL ALA TRP SER ALA THR ALA CYS HIS ASP
SEQRES   9 A  390  GLY LYS LYS TRP MET THR VAL GLY VAL THR GLY PRO ASP
SEQRES  10 A  390  SER LYS ALA VAL ALA VAL ILE HIS TYR GLY GLY VAL PRO
SEQRES  11 A  390  THR ASP VAL ILE ASN SER TRP ALA GLY ASP ILE LEU ARG
SEQRES  12 A  390  THR GLN GLU SER SER CYS THR CYS ILE GLN GLY ASP CYS
SEQRES  13 A  390  TYR TRP VAL MET THR ASP GLY PRO ALA ASN ARG GLN ALA
SEQRES  14 A  390  GLN TYR ARG ILE TYR LYS ALA ASN GLN GLY ARG ILE ILE
SEQRES  15 A  390  GLY GLN ALA ASP ILE SER PHE ASN GLY GLY HIS ILE GLU
SEQRES  16 A  390  GLU CYS SER CYS TYR PRO ASN ASP GLY LYS VAL GLU CYS
SEQRES  17 A  390  VAL CYS ARG ASP ASN TRP THR GLY THR ASN ARG PRO VAL
SEQRES  18 A  390  LEU VAL ILE SER PRO ASP LEU SER TYR ARG VAL GLY TYR
SEQRES  19 A  390  LEU CYS ALA GLY ILE PRO SER ASP THR PRO ARG GLY GLU
SEQRES  20 A  390  ASP ALA GLN PHE THR GLY SER CYS THR SER PRO MET GLY
SEQRES  21 A  390  ASN GLN GLY TYR GLY VAL LYS GLY PHE GLY PHE ARG GLN
SEQRES  22 A  390  GLY THR ASP VAL TRP MET GLY ARG THR ILE SER ARG THR
SEQRES  23 A  390  SER ARG SER GLY PHE GLU ILE LEU ARG ILE LYS ASN GLY
SEQRES  24 A  390  TRP THR GLN THR SER LYS GLU GLN VAL ARG LYS GLN VAL
SEQRES  25 A  390  VAL VAL ASP ASN LEU ASN TRP SER GLY TYR SER GLY SER
SEQRES  26 A  390  PHE THR LEU PRO VAL GLU LEU SER GLY LYS ASP CYS LEU
SEQRES  27 A  390  VAL PRO CYS PHE TRP VAL GLU MET ILE ARG GLY LYS PRO
SEQRES  28 A  390  GLU GLU LYS THR ILE TRP THR SER SER SER SER ILE VAL
SEQRES  29 A  390  MET CYS GLY VAL ASP TYR GLU ILE ALA ASP TRP SER TRP
SEQRES  30 A  390  HIS ASP GLY ALA ILE LEU PRO PHE ASP ILE ASP LYS MET
HET     CA  A 501       1
HET    2H8  A 502      20
HET    NAG  A 503      15
HETNAM      CA CALCIUM ION
HETNAM     2H8 (3S,4R,5R)-4-(ACETYLAMINO)-3-AMINO-5-(PENTAN-3-YLOXY)
HETNAM   2 2H8  CYCLOHEX-1-ENE-1-CARBOXYLIC ACID
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   2   CA    CA 2+
FORMUL   3  2H8    C14 H24 N2 O4
FORMUL   4  NAG    C8 H15 N O6
FORMUL   5  HOH   *277(H2 O)
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 GLU A  329  PHE A  332  5                                   5
HELIX    4   4 PRO A  412A GLY A  414  1                                   6
HELIX    5   5 PHE A  466  LYS A  470  5                                   5
SHEET    1   A 4 GLY A  96  LYS A 102  0
SHEET    2   A 4 THR A 439  VAL A 449 -1  O  VAL A 445   N  PHE A 100
SHEET    3   A 4 VAL A 419  GLY A 429 -1  N  PRO A 420   O  GLY A 448
SHEET    4   A 4 SER A 407  LEU A 412 -1  N  PHE A 410   O  CYS A 421
SHEET    1   B 4 PHE A 115  CYS A 124  0
SHEET    2   B 4 CYS A 129  LEU A 139 -1  O  PHE A 132   N  PHE A 121
SHEET    3   B 4 THR A 157  LYS A 162 -1  O  THR A 157   N  THR A 135
SHEET    4   B 4 ARG A 172  VAL A 176 -1  O  ALA A 175   N  LEU A 158
SHEET    1   C 4 SER A 179  HIS A 184  0
SHEET    2   C 4 TRP A 189  THR A 195 -1  O  MET A 190   N  CYS A 183
SHEET    3   C 4 VAL A 202  TYR A 207 -1  O  HIS A 206   N  THR A 191
SHEET    4   C 4 VAL A 210  ASN A 216 -1  O  THR A 212   N  ILE A 205
SHEET    1   D 3 ARG A 224  THR A 225  0
SHEET    2   D 3 ASP A 236  ASP A 243 -1  O  THR A 242   N  ARG A 224
SHEET    3   D 3 THR A 231  ILE A 233 -1  N  THR A 231   O  TYR A 238
SHEET    1   E 4 ARG A 224  THR A 225  0
SHEET    2   E 4 ASP A 236  ASP A 243 -1  O  THR A 242   N  ARG A 224
SHEET    3   E 4 GLN A 251  ASN A 258 -1  O  ALA A 257   N  CYS A 237
SHEET    4   E 4 ARG A 261  ASP A 267 -1  O  GLY A 264   N  LYS A 256
SHEET    1   F 4 GLU A 276  ASN A 283  0
SHEET    2   F 4 LYS A 286  ARG A 292 -1  O  ARG A 292   N  GLU A 276
SHEET    3   F 4 PRO A 301  ILE A 305 -1  O  ILE A 305   N  VAL A 287
SHEET    4   F 4 TYR A 312  TYR A 316 -1  O  GLY A 315   N  VAL A 302
SHEET    1   G 4 GLY A 353  GLN A 356  0
SHEET    2   G 4 ASP A 359  ARG A 364 -1  O  ASP A 359   N  GLN A 356
SHEET    3   G 4 SER A 372  ILE A 379 -1  O  ILE A 379   N  VAL A 360
SHEET    4   G 4 GLN A 390  TRP A 403 -1  O  VAL A 398   N  PHE A 374
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.03
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.04
SSBOND   3 CYS A  183    CYS A  230                          1555   1555  2.03
SSBOND   4 CYS A  232    CYS A  237                          1555   1555  2.01
SSBOND   5 CYS A  278    CYS A  291                          1555   1555  2.03
SSBOND   6 CYS A  280    CYS A  289                          1555   1555  2.03
SSBOND   7 CYS A  318    CYS A  337                          1555   1555  2.03
SSBOND   8 CYS A  421    CYS A  447                          1555   1555  2.02
LINK         O   TYR A 347                CA    CA A 501     1555   1555  2.29
LINK         O   ASP A 293                CA    CA A 501     1555   1555  2.29
LINK         OD1 ASP A 324                CA    CA A 501     1555   1555  2.39
LINK         O   GLY A 297                CA    CA A 501     1555   1555  2.39
LINK        CA    CA A 501                 O   HOH A 651     1555   1555  2.46
LINK        CA    CA A 501                 O   HOH A 742     1555   1555  2.58
CISPEP   1 THR A  325    PRO A  326          0         9.06
CISPEP   2 LYS A  430    PRO A  431          0         6.06
CISPEP   3 LEU A  464    PRO A  465          0         1.67
SITE     1 AC1  6 ASP A 293  GLY A 297  ASP A 324  TYR A 347
SITE     2 AC1  6 HOH A 651  HOH A 742
SITE     1 AC2 16 ARG A 118  GLU A 119  ASP A 151  ARG A 152
SITE     2 AC2 16 ARG A 224  GLU A 276  GLU A 277  ARG A 292
SITE     3 AC2 16 TYR A 347  ARG A 371  TYR A 406  HOH A 745
SITE     4 AC2 16 HOH A 758  HOH A 779  HOH A 782  HOH A 791
SITE     1 AC3  2 ASN A 146  HOH A 874
CRYST1   90.253   90.253   94.116  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      0.011080  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011080  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010625        0.00000
      
PROCHECK
Go to PROCHECK summary
 References