HEADER GLYCOSIDASE 23-APR-96 1DIM
TITLE SIALIDASE FROM SALMONELLA TYPHIMURIUM COMPLEXED WITH EPANA INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.18;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 99287;
SOURCE 4 STRAIN: LT2;
SOURCE 5 VARIANT: TA263, PROTOTROPH;
SOURCE 6 GENE: NANH;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACTERIAL;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSX62;
SOURCE 11 EXPRESSION_SYSTEM_GENE: NANH;
SOURCE 12 OTHER_DETAILS: RESIDUE MET 1 WAS EXCISED BY ESCHERICHIA COLI
KEYWDS GLYCOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.F.GARMAN,S.C.CRENNELL,E.R.VIMR,W.G.LAVER,G.L.TAYLOR
REVDAT 3 13-JUL-11 1DIM 1 VERSN
REVDAT 2 24-FEB-09 1DIM 1 VERSN
REVDAT 1 07-DEC-96 1DIM 0
JRNL AUTH S.J.CRENNELL,E.F.GARMAN,C.PHILIPPON,A.VASELLA,W.G.LAVER,
JRNL AUTH 2 E.R.VIMR,G.L.TAYLOR
JRNL TITL THE STRUCTURES OF SALMONELLA TYPHIMURIUM LT2 NEURAMINIDASE
JRNL TITL 2 AND ITS COMPLEXES WITH THREE INHIBITORS AT HIGH RESOLUTION.
JRNL REF J.MOL.BIOL. V. 259 264 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8656428
JRNL DOI 10.1006/JMBI.1996.0318
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.J.CRENNELL,E.F.GARMAN,W.G.LAVER,E.R.VIMR,G.L.TAYLOR
REMARK 1 TITL CRYSTAL STRUCTURE OF A BACTERIAL SIALIDASE (FROM SALMONELLA
REMARK 1 TITL 2 TYPHIMURIUM LT2) SHOWS THE SAME FOLD AS AN INFLUENZA VIRUS
REMARK 1 TITL 3 NEURAMINIDASE
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 90 9852 1993
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.TAYLOR,E.VIMR,E.GARMAN,G.LAVER
REMARK 1 TITL PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 2 CRYSTALLOGRAPHIC STUDY OF NEURAMINIDASE FROM VIBRIO CHOLERAE
REMARK 1 TITL 3 AND SALMONELLA TYPHIMURIUM LT2
REMARK 1 REF J.MOL.BIOL. V. 226 1287 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.WALLIMANN,A.VASELLA
REMARK 1 TITL PHOSPHONIC-ACID ANALOGUES OF THE N-ACETYL-2-DEOXYNEURAMINIC
REMARK 1 TITL 2 ACIDS: SYNTHESIS AND INHIBITION OF VIBRIO CHOLERAE SIALIDASE
REMARK 1 REF HELV.CHIM.ACTA V. 73 1359 1990
REMARK 1 REFN ISSN 0018-019X
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 42613
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2954
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 219
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.42
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.79
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : STNA_EPANA.PAR
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : STNA_EPANA.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-92
REMARK 200 TEMPERATURE (KELVIN) : 289
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12091
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.07800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE MAP
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 2SIM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 23.70000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.85000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.85000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.70000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.15000
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 37 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 251 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 251 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 VAL A 280 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 VAL A 358 CB - CA - C ANGL. DEV. = -14.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 100 69.87 60.41
REMARK 500 ASN A 122 -50.18 -131.46
REMARK 500 VAL A 178 126.10 83.33
REMARK 500 SER A 208 -151.79 -169.10
REMARK 500 PHE A 228 -128.56 53.07
REMARK 500 SER A 230 -36.58 52.10
REMARK 500 ASN A 238 -126.21 63.56
REMARK 500 ARG A 276 -158.48 59.07
REMARK 500 HIS A 278 -26.39 72.74
REMARK 500 ARG A 309 60.79 38.57
REMARK 500 VAL A 351 -103.80 54.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 SER A 230 23.4 L L OUTSIDE RANGE
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 801 DISTANCE = 6.93 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 K A 690 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 62 OD2
REMARK 620 2 EQP A 1 O2P 89.0
REMARK 620 3 EQP A 1 O6 86.2 61.5
REMARK 620 4 EQP A 1 O7 79.4 121.8 61.0
REMARK 620 5 HOH A 691 O 52.2 141.2 111.5 59.8
REMARK 620 6 HOH A 692 O 154.9 66.6 76.9 107.5 152.1
REMARK 620 7 HOH A 697 O 112.4 156.1 127.8 74.6 60.7 92.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ACT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 690
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EQP A 1
DBREF 1DIM A 2 382 UNP P29768 NANH_SALTY 1 381
SEQADV 1DIM ASP A 329 UNP P29768 ALA 328 CONFLICT
SEQRES 1 A 381 THR VAL GLU LYS SER VAL VAL PHE LYS ALA GLU GLY GLU
SEQRES 2 A 381 HIS PHE THR ASP GLN LYS GLY ASN THR ILE VAL GLY SER
SEQRES 3 A 381 GLY SER GLY GLY THR THR LYS TYR PHE ARG ILE PRO ALA
SEQRES 4 A 381 MET CYS THR THR SER LYS GLY THR ILE VAL VAL PHE ALA
SEQRES 5 A 381 ASP ALA ARG HIS ASN THR ALA SER ASP GLN SER PHE ILE
SEQRES 6 A 381 ASP THR ALA ALA ALA ARG SER THR ASP GLY GLY LYS THR
SEQRES 7 A 381 TRP ASN LYS LYS ILE ALA ILE TYR ASN ASP ARG VAL ASN
SEQRES 8 A 381 SER LYS LEU SER ARG VAL MET ASP PRO THR CYS ILE VAL
SEQRES 9 A 381 ALA ASN ILE GLN GLY ARG GLU THR ILE LEU VAL MET VAL
SEQRES 10 A 381 GLY LYS TRP ASN ASN ASN ASP LYS THR TRP GLY ALA TYR
SEQRES 11 A 381 ARG ASP LYS ALA PRO ASP THR ASP TRP ASP LEU VAL LEU
SEQRES 12 A 381 TYR LYS SER THR ASP ASP GLY VAL THR PHE SER LYS VAL
SEQRES 13 A 381 GLU THR ASN ILE HIS ASP ILE VAL THR LYS ASN GLY THR
SEQRES 14 A 381 ILE SER ALA MET LEU GLY GLY VAL GLY SER GLY LEU GLN
SEQRES 15 A 381 LEU ASN ASP GLY LYS LEU VAL PHE PRO VAL GLN MET VAL
SEQRES 16 A 381 ARG THR LYS ASN ILE THR THR VAL LEU ASN THR SER PHE
SEQRES 17 A 381 ILE TYR SER THR ASP GLY ILE THR TRP SER LEU PRO SER
SEQRES 18 A 381 GLY TYR CYS GLU GLY PHE GLY SER GLU ASN ASN ILE ILE
SEQRES 19 A 381 GLU PHE ASN ALA SER LEU VAL ASN ASN ILE ARG ASN SER
SEQRES 20 A 381 GLY LEU ARG ARG SER PHE GLU THR LYS ASP PHE GLY LYS
SEQRES 21 A 381 THR TRP THR GLU PHE PRO PRO MET ASP LYS LYS VAL ASP
SEQRES 22 A 381 ASN ARG ASN HIS GLY VAL GLN GLY SER THR ILE THR ILE
SEQRES 23 A 381 PRO SER GLY ASN LYS LEU VAL ALA ALA HIS SER SER ALA
SEQRES 24 A 381 GLN ASN LYS ASN ASN ASP TYR THR ARG SER ASP ILE SER
SEQRES 25 A 381 LEU TYR ALA HIS ASN LEU TYR SER GLY GLU VAL LYS LEU
SEQRES 26 A 381 ILE ASP ASP PHE TYR PRO LYS VAL GLY ASN ALA SER GLY
SEQRES 27 A 381 ALA GLY TYR SER CYS LEU SER TYR ARG LYS ASN VAL ASP
SEQRES 28 A 381 LYS GLU THR LEU TYR VAL VAL TYR GLU ALA ASN GLY SER
SEQRES 29 A 381 ILE GLU PHE GLN ASP LEU SER ARG HIS LEU PRO VAL ILE
SEQRES 30 A 381 LYS SER TYR ASN
HET K A 690 1
HET EQP A 1 21
HETNAM K POTASSIUM ION
HETNAM EQP (4-ACETAMIDO-2,4-DIDEOXY-D-GLYCERO-ALPHA-D-GALACTO-1-
HETNAM 2 EQP OCTOPYRANOSYL)PHOSPHONIC ACID
FORMUL 2 K K 1+
FORMUL 3 EQP C10 H20 N O9 P
FORMUL 4 HOH *219(H2 O)
HELIX 1 1 SER A 29 GLY A 31 5 3
HELIX 2 2 TRP A 128 ALA A 130 5 3
HELIX 3 3 ILE A 161 ASN A 168 1 8
HELIX 4 4 SER A 372 SER A 380 5 9
SHEET 1 A 4 TYR A 35 ARG A 37 0
SHEET 2 A 4 ILE A 49 ARG A 56 -1 N ARG A 56 O TYR A 35
SHEET 3 A 4 ILE A 66 SER A 73 -1 N SER A 73 O ILE A 49
SHEET 4 A 4 ASN A 81 ILE A 86 -1 N ILE A 86 O THR A 68
SHEET 1 B 2 ALA A 40 THR A 43 0
SHEET 2 B 2 ILE A 49 PHE A 52 -1 N PHE A 52 O ALA A 40
SHEET 1 C 3 ARG A 97 MET A 99 0
SHEET 2 C 3 ILE A 114 TRP A 121 -1 N TRP A 121 O ARG A 97
SHEET 3 C 3 ASP A 141 SER A 147 -1 N SER A 147 O ILE A 114
SHEET 1 D 2 THR A 102 ILE A 108 0
SHEET 2 D 2 ARG A 111 MET A 117 -1 N MET A 117 O THR A 102
SHEET 1 E 4 TRP A 218 LEU A 220 0
SHEET 2 E 4 LEU A 205 SER A 212 -1 N TYR A 211 O SER A 219
SHEET 3 E 4 LEU A 189 ARG A 197 -1 N MET A 195 O ASN A 206
SHEET 4 E 4 ILE A 171 GLY A 176 -1 N LEU A 175 O GLN A 194
SHEET 1 F 2 ASN A 232 PHE A 237 0
SHEET 2 F 2 SER A 240 ILE A 245 -1 N ASN A 244 O ASN A 233
SHEET 1 G 4 SER A 283 SER A 289 0
SHEET 2 G 4 LYS A 292 ALA A 300 -1 N SER A 298 O SER A 283
SHEET 3 G 4 ILE A 312 HIS A 317 -1 N HIS A 317 O ALA A 295
SHEET 4 G 4 VAL A 324 ASP A 328 -1 N ASP A 328 O LEU A 314
SHEET 1 H 4 SER A 343 ASN A 350 0
SHEET 2 H 4 LYS A 353 ALA A 362 -1 N VAL A 359 O CYS A 344
SHEET 3 H 4 SER A 365 ASP A 370 -1 N GLN A 369 O VAL A 358
SHEET 4 H 4 LYS A 5 PHE A 9 -1 N PHE A 9 O ILE A 366
SSBOND 1 CYS A 42 CYS A 103 1555 1555 2.05
LINK K K A 690 OD2 ASP A 62 1555 1555 2.77
LINK K K A 690 O2P EQP A 1 1555 1555 2.91
LINK K K A 690 O6 EQP A 1 1555 1555 2.83
LINK K K A 690 O7 EQP A 1 1555 1555 2.77
LINK K K A 690 O HOH A 691 1555 1555 3.38
LINK K K A 690 O HOH A 692 1555 1555 3.33
LINK K K A 690 O HOH A 697 1555 1555 2.90
CISPEP 1 ALA A 135 PRO A 136 0 -0.20
SITE 1 ACT 13 ARG A 37 ARG A 56 ASP A 62 MET A 99
SITE 2 ACT 13 ASP A 100 TRP A 121 TRP A 128 LEU A 175
SITE 3 ACT 13 GLU A 231 ARG A 246 ARG A 309 TYR A 342
SITE 4 ACT 13 GLU A 361
SITE 1 AC1 3 EQP A 1 ASP A 62 HOH A 697
SITE 1 AC2 20 ARG A 37 ILE A 38 ARG A 56 ASP A 62
SITE 2 AC2 20 ASP A 100 THR A 127 TRP A 128 LEU A 175
SITE 3 AC2 20 ARG A 246 ARG A 309 TYR A 342 HOH A 664
SITE 4 AC2 20 HOH A 688 HOH A 689 K A 690 HOH A 692
SITE 5 AC2 20 HOH A 693 HOH A 694 HOH A 695 HOH A 696
CRYST1 47.400 82.300 91.700 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 0.021097 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010905 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
