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PDBsum entry 2xcy

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2xcy
Jmol
Contents
Protein chains
386 a.a.
Ligands
GOL
Metals
_CL ×2
Waters ×1049
HEADER    HYDROLASE                               27-APR-10   2XCY
TITLE     CRYSTAL STRUCTURE OF ASPERGILLUS FUMIGATUS SIALIDASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: EXTRACELLULAR SIALIDASE/NEURAMINIDASE, PUTATIVE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: RESIDUES 21-406;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE   3 ORGANISM_TAXID: 5085;
SOURCE   4 ATCC: ATCC 13073;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS    HYDROLASE, GLYCOSIDASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.C.TELFORD,J.YEUNG,G.XU,A.BENNET,M.M.MOORE,G.L.TAYLOR
REVDAT   3   21-SEP-11 2XCY    1       JRNL   REMARK VERSN
REVDAT   2   02-FEB-11 2XCY    1       JRNL   REMARK
REVDAT   1   12-MAY-10 2XCY    0
JRNL        AUTH   J.C.TELFORD,J.H.YEUNG,G.XU,M.J.KIEFEL,A.G.WATTS,
JRNL        AUTH 2 S.HADER,J.CHAN,A.J.BENNET,M.M.MOORE,G.L.TAYLOR
JRNL        TITL   THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE:
JRNL        TITL 2 STRUCTURAL AND MECHANISTIC INSIGHTS.
JRNL        REF    J.BIOL.CHEM.                  V. 286 10783 2011
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   21247893
JRNL        DOI    10.1074/JBC.M110.207043
REMARK   2
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.40
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.48
REMARK   3   NUMBER OF REFLECTIONS             : 56944
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.15528
REMARK   3   R VALUE            (WORKING SET) : 0.15322
REMARK   3   FREE R VALUE                     : 0.19406
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 3022
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.837
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.884
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3071
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.48
REMARK   3   BIN R VALUE           (WORKING SET) : 0.217
REMARK   3   BIN FREE R VALUE SET COUNT          : 150
REMARK   3   BIN FREE R VALUE                    : 0.276
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5940
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 8
REMARK   3   SOLVENT ATOMS            : 1049
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 12.2
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.755
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00
REMARK   3    B22 (A**2) : 0.00
REMARK   3    B33 (A**2) : 0.00
REMARK   3    B12 (A**2) : 0.00
REMARK   3    B13 (A**2) : 0.00
REMARK   3    B23 (A**2) : 0.00
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.149
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.069
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.230
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6094 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8275 ; 1.134 ; 1.941
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   774 ; 6.284 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   287 ;28.941 ;22.892
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   943 ;12.814 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;15.166 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   864 ; 0.072 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4796 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3811 ; 0.433 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6101 ; 0.808 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2283 ; 1.368 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2171 ; 2.206 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2XCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-10.
REMARK 100 THE PDBE ID CODE IS EBI-43745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-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 MIRCOMAX 007HF
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 : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59980
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.84
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.40
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.2
REMARK 200  DATA REDUNDANCY                : 3.1
REMARK 200  R MERGE                    (I) : 0.06
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.60
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.0
REMARK 200  R MERGE FOR SHELL          (I) : 0.20
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.20
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.09500
REMARK 290   SMTRY3   2  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 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     ILE B     1
REMARK 465     ASN B     2
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    ASN A   359     O    HOH A  2533              2.17
REMARK 500   O    HOH A  2002     O    HOH B  2386              2.15
REMARK 500   O    HOH A  2266     O    HOH A  2551              2.10
REMARK 500   O    HOH B  2197     O    HOH B  2254              1.77
REMARK 500   O    HOH B  2304     O    HOH B  2317              2.16
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   O    HOH B  2254     O    HOH B  2320     1657     2.19
REMARK 500   O    HOH B  2461     O    HOH A  2492     1747     2.08
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    ILE A  40       64.89     65.66
REMARK 500    ALA A 181      -86.07   -110.07
REMARK 500    ASN A 215       46.48   -145.81
REMARK 500    ALA A 275       69.78     63.58
REMARK 500    ILE B  40       66.71     66.52
REMARK 500    ASN B  81       19.01     58.86
REMARK 500    ALA B  99       32.03    -92.86
REMARK 500    ALA B 181      -84.18   -105.50
REMARK 500    ASN B 215       42.39   -142.78
REMARK 500    ALA B 275       64.52     65.30
REMARK 500    THR B 300      -32.73   -131.43
REMARK 500    ARG B 303       32.90    -99.39
REMARK 500    ASP B 346       30.43    -95.01
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  CL A1387
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1387
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1388
DBREF  2XCY A    1   386  UNP    Q4WQS0   Q4WQS0_ASPFU    21    406
DBREF  2XCY B    1   386  UNP    Q4WQS0   Q4WQS0_ASPFU    21    406
SEQRES   1 A  386  ILE ASN ASP PRO ALA LYS SER ALA ALA PRO TYR HIS ASP
SEQRES   2 A  386  GLU PHE PRO LEU PHE ARG SER ALA ASN MSE ALA SER PRO
SEQRES   3 A  386  ASP LYS LEU SER THR GLY ILE GLY PHE HIS SER PHE ARG
SEQRES   4 A  386  ILE PRO ALA VAL VAL ARG THR THR THR GLY ARG ILE LEU
SEQRES   5 A  386  ALA PHE ALA GLU GLY ARG ARG HIS THR ASN GLN ASP PHE
SEQRES   6 A  386  GLY ASP ILE ASN LEU VAL TYR LYS ARG THR LYS THR THR
SEQRES   7 A  386  ALA ASN ASN GLY ALA SER PRO SER ASP TRP GLU PRO LEU
SEQRES   8 A  386  ARG GLU VAL VAL GLY SER GLY ALA GLY THR TRP GLY ASN
SEQRES   9 A  386  PRO THR PRO VAL VAL ASP ASP ASP ASN THR ILE TYR LEU
SEQRES  10 A  386  PHE LEU SER TRP ASN GLY ALA THR TYR SER GLN ASN GLY
SEQRES  11 A  386  LYS ASP VAL LEU PRO ASP GLY THR VAL THR LYS LYS ILE
SEQRES  12 A  386  ASP SER THR TRP GLU GLY ARG ARG HIS LEU TYR LEU THR
SEQRES  13 A  386  GLU SER ARG ASP ASP GLY ASN THR TRP SER LYS PRO VAL
SEQRES  14 A  386  ASP LEU THR LYS GLU LEU THR PRO ASP GLY TRP ALA TRP
SEQRES  15 A  386  ASP ALA VAL GLY PRO GLY ASN GLY ILE ARG LEU THR THR
SEQRES  16 A  386  GLY GLU LEU VAL ILE PRO ALA MSE GLY ARG ASN ILE ILE
SEQRES  17 A  386  GLY ARG GLY ALA PRO GLY ASN ARG THR TRP SER VAL GLN
SEQRES  18 A  386  ARG LEU SER GLY ALA GLY ALA GLU GLY THR ILE VAL GLN
SEQRES  19 A  386  THR PRO ASP GLY LYS LEU TYR ARG ASN ASP ARG PRO SER
SEQRES  20 A  386  GLN LYS GLY TYR ARG MSE VAL ALA ARG GLY THR LEU GLU
SEQRES  21 A  386  GLY PHE GLY ALA PHE ALA PRO ASP ALA GLY LEU PRO ASP
SEQRES  22 A  386  PRO ALA CYS GLN GLY SER VAL LEU ARG TYR ASN SER ASP
SEQRES  23 A  386  ALA PRO ALA ARG THR ILE PHE LEU ASN SER ALA SER GLY
SEQRES  24 A  386  THR SER ARG ARG ALA MSE ARG VAL ARG ILE SER TYR ASP
SEQRES  25 A  386  ALA ASP ALA LYS LYS PHE ASN TYR GLY ARG LYS LEU GLU
SEQRES  26 A  386  ASP ALA LYS VAL SER GLY ALA GLY HIS GLU GLY GLY TYR
SEQRES  27 A  386  SER SER MSE THR LYS THR GLY ASP TYR LYS ILE GLY ALA
SEQRES  28 A  386  LEU VAL GLU SER ASP PHE PHE ASN ASP GLY THR GLY LYS
SEQRES  29 A  386  ASN SER TYR ARG ALA ILE ILE TRP ARG ARG PHE ASN LEU
SEQRES  30 A  386  SER TRP ILE LEU ASN GLY PRO ASN ASN
SEQRES   1 B  386  ILE ASN ASP PRO ALA LYS SER ALA ALA PRO TYR HIS ASP
SEQRES   2 B  386  GLU PHE PRO LEU PHE ARG SER ALA ASN MSE ALA SER PRO
SEQRES   3 B  386  ASP LYS LEU SER THR GLY ILE GLY PHE HIS SER PHE ARG
SEQRES   4 B  386  ILE PRO ALA VAL VAL ARG THR THR THR GLY ARG ILE LEU
SEQRES   5 B  386  ALA PHE ALA GLU GLY ARG ARG HIS THR ASN GLN ASP PHE
SEQRES   6 B  386  GLY ASP ILE ASN LEU VAL TYR LYS ARG THR LYS THR THR
SEQRES   7 B  386  ALA ASN ASN GLY ALA SER PRO SER ASP TRP GLU PRO LEU
SEQRES   8 B  386  ARG GLU VAL VAL GLY SER GLY ALA GLY THR TRP GLY ASN
SEQRES   9 B  386  PRO THR PRO VAL VAL ASP ASP ASP ASN THR ILE TYR LEU
SEQRES  10 B  386  PHE LEU SER TRP ASN GLY ALA THR TYR SER GLN ASN GLY
SEQRES  11 B  386  LYS ASP VAL LEU PRO ASP GLY THR VAL THR LYS LYS ILE
SEQRES  12 B  386  ASP SER THR TRP GLU GLY ARG ARG HIS LEU TYR LEU THR
SEQRES  13 B  386  GLU SER ARG ASP ASP GLY ASN THR TRP SER LYS PRO VAL
SEQRES  14 B  386  ASP LEU THR LYS GLU LEU THR PRO ASP GLY TRP ALA TRP
SEQRES  15 B  386  ASP ALA VAL GLY PRO GLY ASN GLY ILE ARG LEU THR THR
SEQRES  16 B  386  GLY GLU LEU VAL ILE PRO ALA MSE GLY ARG ASN ILE ILE
SEQRES  17 B  386  GLY ARG GLY ALA PRO GLY ASN ARG THR TRP SER VAL GLN
SEQRES  18 B  386  ARG LEU SER GLY ALA GLY ALA GLU GLY THR ILE VAL GLN
SEQRES  19 B  386  THR PRO ASP GLY LYS LEU TYR ARG ASN ASP ARG PRO SER
SEQRES  20 B  386  GLN LYS GLY TYR ARG MSE VAL ALA ARG GLY THR LEU GLU
SEQRES  21 B  386  GLY PHE GLY ALA PHE ALA PRO ASP ALA GLY LEU PRO ASP
SEQRES  22 B  386  PRO ALA CYS GLN GLY SER VAL LEU ARG TYR ASN SER ASP
SEQRES  23 B  386  ALA PRO ALA ARG THR ILE PHE LEU ASN SER ALA SER GLY
SEQRES  24 B  386  THR SER ARG ARG ALA MSE ARG VAL ARG ILE SER TYR ASP
SEQRES  25 B  386  ALA ASP ALA LYS LYS PHE ASN TYR GLY ARG LYS LEU GLU
SEQRES  26 B  386  ASP ALA LYS VAL SER GLY ALA GLY HIS GLU GLY GLY TYR
SEQRES  27 B  386  SER SER MSE THR LYS THR GLY ASP TYR LYS ILE GLY ALA
SEQRES  28 B  386  LEU VAL GLU SER ASP PHE PHE ASN ASP GLY THR GLY LYS
SEQRES  29 B  386  ASN SER TYR ARG ALA ILE ILE TRP ARG ARG PHE ASN LEU
SEQRES  30 B  386  SER TRP ILE LEU ASN GLY PRO ASN ASN
MODRES 2XCY MSE A   23  MET  SELENOMETHIONINE
MODRES 2XCY MSE A  203  MET  SELENOMETHIONINE
MODRES 2XCY MSE A  253  MET  SELENOMETHIONINE
MODRES 2XCY MSE A  305  MET  SELENOMETHIONINE
MODRES 2XCY MSE A  341  MET  SELENOMETHIONINE
MODRES 2XCY MSE B   23  MET  SELENOMETHIONINE
MODRES 2XCY MSE B  203  MET  SELENOMETHIONINE
MODRES 2XCY MSE B  253  MET  SELENOMETHIONINE
MODRES 2XCY MSE B  305  MET  SELENOMETHIONINE
MODRES 2XCY MSE B  341  MET  SELENOMETHIONINE
HET    MSE  A  23       8
HET    MSE  A 203       8
HET    MSE  A 253       8
HET    MSE  A 305       8
HET    MSE  A 341       8
HET     CL  A1387       1
HET    MSE  B  23       8
HET    MSE  B 203       8
HET    MSE  B 253       8
HET    MSE  B 305       8
HET    MSE  B 341       8
HET     CL  B1387       1
HET    GOL  A1388       6
HETNAM     GOL GLYCEROL
HETNAM      CL CHLORIDE ION
HETNAM     MSE SELENOMETHIONINE
FORMUL   3  GOL    C3 H8 O3
FORMUL   4   CL    2(CL 1-)
FORMUL   5  MSE    10(C5 H11 N O2 SE)
FORMUL   6  HOH   *1049(H2 O)
HELIX    1   1 ASP A    3  ALA A    8  5                                   6
HELIX    2   2 SER A   84  ASP A   87  5                                   4
HELIX    3   3 LEU A  171  THR A  176  1                                   6
HELIX    4   4 GLU A  325  LYS A  328  5                                   4
HELIX    5   5 ASN A  376  ASN A  382  1                                   7
HELIX    6   6 ASP B    3  ALA B    8  5                                   6
HELIX    7   7 SER B   84  ASP B   87  5                                   4
HELIX    8   8 LEU B  171  THR B  176  1                                   6
HELIX    9   9 GLU B  325  LYS B  328  5                                   4
HELIX   10  10 ASN B  376  ASN B  382  1                                   7
SHEET    1  AA 4 HIS A  12  PHE A  18  0
SHEET    2  AA 4 ARG A 368  PHE A 375 -1  O  ILE A 370   N  LEU A  17
SHEET    3  AA 4 ILE A 349  ASP A 356 -1  O  ILE A 349   N  PHE A 375
SHEET    4  AA 4 HIS A 334  LYS A 343 -1  O  HIS A 334   N  ASP A 356
SHEET    1  AB 4 SER A  37  ARG A  45  0
SHEET    2  AB 4 ILE A  51  ARG A  58 -1  O  LEU A  52   N  VAL A  44
SHEET    3  AB 4 ILE A  68  ARG A  74 -1  O  ASN A  69   N  GLY A  57
SHEET    4  AB 4 ARG A  92  VAL A  95 -1  O  ARG A  92   N  TYR A  72
SHEET    1  AC 4 THR A 101  VAL A 109  0
SHEET    2  AC 4 ILE A 115  ASN A 122 -1  O  TYR A 116   N  VAL A 108
SHEET    3  AC 4 HIS A 152  SER A 158 -1  O  HIS A 152   N  TRP A 121
SHEET    4  AC 4 VAL A 169  ASP A 170 -1  O  VAL A 169   N  LEU A 155
SHEET    1  AD 2 TYR A 126  SER A 127  0
SHEET    2  AD 2 LYS A 141  LYS A 142  1  O  LYS A 141   N  SER A 127
SHEET    1  AE 4 ILE A 191  ARG A 192  0
SHEET    2  AE 4 LEU A 198  ALA A 202 -1  O  VAL A 199   N  ILE A 191
SHEET    3  AE 4 ARG A 205  ALA A 212 -1  O  ARG A 205   N  ALA A 202
SHEET    4  AE 4 ASN A 215  ARG A 222 -1  O  ASN A 215   N  ALA A 212
SHEET    1  AF 4 ILE A 232  GLN A 234  0
SHEET    2  AF 4 LEU A 240  ASP A 244 -1  O  TYR A 241   N  VAL A 233
SHEET    3  AF 4 GLY A 250  THR A 258 -1  O  MSE A 253   N  ASP A 244
SHEET    4  AF 4 GLY A 261  PHE A 262  1  O  GLY A 261   N  THR A 258
SHEET    1  AG 4 ILE A 232  GLN A 234  0
SHEET    2  AG 4 LEU A 240  ASP A 244 -1  O  TYR A 241   N  VAL A 233
SHEET    3  AG 4 GLY A 250  THR A 258 -1  O  MSE A 253   N  ASP A 244
SHEET    4  AG 4 ALA A 266  ASP A 273 -1  O  ALA A 266   N  VAL A 254
SHEET    1  AH 2 GLY A 261  PHE A 262  0
SHEET    2  AH 2 GLY A 250  THR A 258  1  O  THR A 258   N  GLY A 261
SHEET    1  AI 4 SER A 279  ASN A 284  0
SHEET    2  AI 4 ARG A 290  SER A 296 -1  O  ARG A 290   N  TYR A 283
SHEET    3  AI 4 MSE A 305  SER A 310 -1  O  ARG A 306   N  ASN A 295
SHEET    4  AI 4 ARG A 322  LYS A 323 -1  O  ARG A 322   N  VAL A 307
SHEET    1  BA 4 HIS B  12  PHE B  18  0
SHEET    2  BA 4 ARG B 368  PHE B 375 -1  O  ILE B 370   N  LEU B  17
SHEET    3  BA 4 ILE B 349  ASP B 356 -1  O  ILE B 349   N  PHE B 375
SHEET    4  BA 4 HIS B 334  LYS B 343 -1  O  HIS B 334   N  ASP B 356
SHEET    1  BB 4 SER B  37  ARG B  45  0
SHEET    2  BB 4 ILE B  51  ARG B  58 -1  O  LEU B  52   N  VAL B  44
SHEET    3  BB 4 ILE B  68  ARG B  74 -1  O  ASN B  69   N  GLY B  57
SHEET    4  BB 4 ARG B  92  VAL B  95 -1  O  ARG B  92   N  TYR B  72
SHEET    1  BC 4 GLY B 100  VAL B 109  0
SHEET    2  BC 4 ILE B 115  GLY B 123 -1  O  TYR B 116   N  VAL B 108
SHEET    3  BC 4 HIS B 152  SER B 158 -1  O  HIS B 152   N  TRP B 121
SHEET    4  BC 4 VAL B 169  ASP B 170 -1  O  VAL B 169   N  LEU B 155
SHEET    1  BD 2 TYR B 126  SER B 127  0
SHEET    2  BD 2 LYS B 141  LYS B 142  1  O  LYS B 141   N  SER B 127
SHEET    1  BE 4 ILE B 191  ARG B 192  0
SHEET    2  BE 4 LEU B 198  ALA B 202 -1  O  VAL B 199   N  ILE B 191
SHEET    3  BE 4 ARG B 205  ARG B 210 -1  O  ARG B 205   N  ALA B 202
SHEET    4  BE 4 THR B 217  ARG B 222 -1  O  THR B 217   N  ARG B 210
SHEET    1  BF 4 GLY B 230  GLN B 234  0
SHEET    2  BF 4 LEU B 240  ASP B 244 -1  O  TYR B 241   N  VAL B 233
SHEET    3  BF 4 GLY B 250  THR B 258 -1  O  MSE B 253   N  ASP B 244
SHEET    4  BF 4 GLY B 261  PHE B 262  1  O  GLY B 261   N  THR B 258
SHEET    1  BG 4 GLY B 230  GLN B 234  0
SHEET    2  BG 4 LEU B 240  ASP B 244 -1  O  TYR B 241   N  VAL B 233
SHEET    3  BG 4 GLY B 250  THR B 258 -1  O  MSE B 253   N  ASP B 244
SHEET    4  BG 4 ALA B 266  ASP B 273 -1  O  ALA B 266   N  VAL B 254
SHEET    1  BH 2 GLY B 261  PHE B 262  0
SHEET    2  BH 2 GLY B 250  THR B 258  1  O  THR B 258   N  GLY B 261
SHEET    1  BI 4 SER B 279  ASN B 284  0
SHEET    2  BI 4 ARG B 290  SER B 296 -1  O  ARG B 290   N  TYR B 283
SHEET    3  BI 4 MSE B 305  SER B 310 -1  O  ARG B 306   N  ASN B 295
SHEET    4  BI 4 ARG B 322  LYS B 323 -1  O  ARG B 322   N  VAL B 307
LINK         C   ASN A  22                 N   MSE A  23     1555   1555  1.33
LINK         C   MSE A  23                 N   ALA A  24     1555   1555  1.33
LINK         C   ALA A 202                 N   MSE A 203     1555   1555  1.33
LINK         C   MSE A 203                 N   GLY A 204     1555   1555  1.33
LINK         C   ARG A 252                 N   MSE A 253     1555   1555  1.33
LINK         C   MSE A 253                 N   VAL A 254     1555   1555  1.33
LINK         C   ALA A 304                 N   MSE A 305     1555   1555  1.33
LINK         C   MSE A 305                 N   ARG A 306     1555   1555  1.33
LINK         C   SER A 340                 N   MSE A 341     1555   1555  1.33
LINK         C   MSE A 341                 N   THR A 342     1555   1555  1.33
LINK         C   ASN B  22                 N   MSE B  23     1555   1555  1.33
LINK         C   MSE B  23                 N   ALA B  24     1555   1555  1.33
LINK         C   ALA B 202                 N   MSE B 203     1555   1555  1.33
LINK         C   MSE B 203                 N   GLY B 204     1555   1555  1.34
LINK         C   ARG B 252                 N   MSE B 253     1555   1555  1.33
LINK         C   MSE B 253                 N   VAL B 254     1555   1555  1.34
LINK         C   ALA B 304                 N   MSE B 305     1555   1555  1.34
LINK         C   MSE B 305                 N   ARG B 306     1555   1555  1.33
LINK         C   SER B 340                 N   MSE B 341     1555   1555  1.33
LINK         C   MSE B 341                 N   THR B 342     1555   1555  1.33
CISPEP   1 GLY A  186    PRO A  187          0         4.38
CISPEP   2 ALA A  287    PRO A  288          0        -5.46
CISPEP   3 GLY B  186    PRO B  187          0         2.96
CISPEP   4 ALA B  287    PRO B  288          0        -6.79
SITE     1 AC1  5 ARG A 245  ARG A 302  TYR A 338  HOH A2150
SITE     2 AC1  5 HOH A2515
SITE     1 AC2  4 ARG B 245  ARG B 302  TYR B 338  HOH B2446
SITE     1 AC3  6 ASP A 112  ASN A 113  THR A 114  ARG A 159
SITE     2 AC3  6 HOH A2562  HOH A2563
CRYST1   75.890   58.190   94.700  90.00 100.01  90.00 P 1 21 1      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      0.013177  0.000000  0.002326        0.00000
SCALE2      0.000000  0.017185  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010723        0.00000
      
PROCHECK
Go to PROCHECK summary
 References