HEADER HYDROLASE 15-NOV-05 2F25
TITLE CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2 E111Q MUTANT
TITLE 2 IN COMPLEX WITH DANA INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NEU2, CYTOSOLIC SIALIDASE, N-ACETYL-ALPHA-
COMPND 5 NEURAMINIDASE 2;
COMPND 6 EC: 3.2.1.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS SIALIDASE, NEURAMINIDASE, GANGLIOSIDE, DRUG DESIGN,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.G.CHAVAS,R.KATO,P.FUSI,C.TRINGALI,B.VENERANDO,
AUTHOR 2 G.TETTAMANTI,E.MONTI,S.WAKATSUKI
REVDAT 2 24-FEB-09 2F25 1 VERSN
REVDAT 1 21-NOV-06 2F25 0
JRNL AUTH L.M.G.CHAVAS,R.KATO,P.FUSI,C.TRINGALI,B.VENERANDO,
JRNL AUTH 2 G.TETTAMANTI,E.MONTI,S.WAKATSUKI
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN SIALIDASE NEU2
JRNL TITL 2 E111Q MUTANT IN COMPLEX WITH DANA INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.06
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) (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 60460
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 SET) : 0.192
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3201
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 : 5850
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.11200
REMARK 3 B22 (A**2) : -4.06000
REMARK 3 B33 (A**2) : 1.94800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.99100
REMARK 3 B23 (A**2) : 0.00000
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) : 1.405
REMARK 3 BOND ANGLES (DEGREES) : 0.01
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 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 67.63
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : DANA_HEPES_REP.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F25 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB035358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JAN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63661
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 79.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1SNT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2-METHYL-2,4-PENTANEDIOL, GUANIDINE
REMARK 280 HYDROCHLORIDE, 2-DEOXY-2,3-DEHYDRO-N-ACETYLNEURAMINIC ACID, PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
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 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 1.000000 0.000000 0.000000 78.68500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.82000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.68500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.82000
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 300 REMARK: THE BIOLOGICAL UNIT IS A MONOMER. THERE ARE 2 BIOLOGICAL
REMARK 300 UNITS IN THE ASYMMETRIC UNIT (CHAIN A AND CHAIN B)
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 B1196 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 SER A 284
REMARK 465 GLY A 285
REMARK 465 PRO A 286
REMARK 465 GLY A 287
REMARK 465 LEU A 378
REMARK 465 PRO A 379
REMARK 465 GLN A 380
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 THR B 226
REMARK 465 GLY B 227
REMARK 465 GLU B 228
REMARK 465 SER B 284
REMARK 465 GLY B 285
REMARK 465 PRO B 286
REMARK 465 GLY B 287
REMARK 465 LEU B 378
REMARK 465 PRO B 379
REMARK 465 GLN B 380
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 22 72.74 61.03
REMARK 500 GLU A 50 -73.90 -135.45
REMARK 500 ALA A 213 52.25 -60.60
REMARK 500 ASP A 215 93.19 -68.23
REMARK 500 LEU A 217 -137.13 -114.62
REMARK 500 ASP A 306 73.95 55.99
REMARK 500 ALA A 333 -114.36 -131.26
REMARK 500 ILE B 22 72.57 64.23
REMARK 500 GLU B 50 -75.49 -136.62
REMARK 500 THR B 156 169.46 178.75
REMARK 500 CYS B 164 -163.69 -102.21
REMARK 500 LEU B 217 -136.03 -113.17
REMARK 500 ASP B 306 74.94 60.09
REMARK 500 ARG B 314 55.15 -140.81
REMARK 500 ALA B 317 105.30 -46.47
REMARK 500 ALA B 333 -118.29 -134.30
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 DAN A 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1004
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1005
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SNT RELATED DB: PDB
REMARK 900 HUMAN NEU2 APO-FORM
REMARK 900 RELATED ID: 1SO7 RELATED DB: PDB
REMARK 900 HUMAN NEU2 SUGAR-INDUCED FORM
REMARK 900 RELATED ID: 1VCU RELATED DB: PDB
REMARK 900 HUMAN NEU2-DANA COMPLEX
REMARK 900 RELATED ID: 2F0Z RELATED DB: PDB
REMARK 900 RELATED ID: 2F10 RELATED DB: PDB
REMARK 900 RELATED ID: 2F11 RELATED DB: PDB
REMARK 900 RELATED ID: 2F12 RELATED DB: PDB
REMARK 900 RELATED ID: 2F13 RELATED DB: PDB
REMARK 900 RELATED ID: 2F24 RELATED DB: PDB
REMARK 900 RELATED ID: 2F26 RELATED DB: PDB
REMARK 900 RELATED ID: 2F27 RELATED DB: PDB
REMARK 900 RELATED ID: 2F28 RELATED DB: PDB
REMARK 900 RELATED ID: 2F29 RELATED DB: PDB
DBREF 2F25 A 1 380 UNP Q9Y3R4 NEUR2_HUMAN 1 380
DBREF 2F25 B 1 380 UNP Q9Y3R4 NEUR2_HUMAN 1 380
SEQADV 2F25 GLY A -1 UNP Q9Y3R4 CLONING ARTIFACT
SEQADV 2F25 SER A 0 UNP Q9Y3R4 CLONING ARTIFACT
SEQADV 2F25 GLN A 111 UNP Q9Y3R4 GLU 111 ENGINEERED
SEQADV 2F25 GLY B -1 UNP Q9Y3R4 CLONING ARTIFACT
SEQADV 2F25 SER B 0 UNP Q9Y3R4 CLONING ARTIFACT
SEQADV 2F25 GLN B 111 UNP Q9Y3R4 GLU 111 ENGINEERED
SEQRES 1 A 382 GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER
SEQRES 2 A 382 VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA
SEQRES 3 A 382 LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE
SEQRES 4 A 382 ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU
SEQRES 5 A 382 LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR
SEQRES 6 A 382 HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN
SEQRES 7 A 382 ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO
SEQRES 8 A 382 LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE
SEQRES 9 A 382 ILE ALA ILE PRO GLY GLN VAL THR GLN GLN GLN GLN LEU
SEQRES 10 A 382 GLN THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR
SEQRES 11 A 382 SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP
SEQRES 12 A 382 LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP
SEQRES 13 A 382 SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU
SEQRES 14 A 382 ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA
SEQRES 15 A 382 TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER
SEQRES 16 A 382 ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP
SEQRES 17 A 382 ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS
SEQRES 18 A 382 GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL
SEQRES 19 A 382 THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN
SEQRES 20 A 382 ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER
SEQRES 21 A 382 GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY
SEQRES 22 A 382 CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER
SEQRES 23 A 382 GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS
SEQRES 24 A 382 PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR
SEQRES 25 A 382 LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU
SEQRES 26 A 382 PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP
SEQRES 27 A 382 LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU
SEQRES 28 A 382 PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE
SEQRES 29 A 382 VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA
SEQRES 30 A 382 GLU TYR LEU PRO GLN
SEQRES 1 B 382 GLY SER MET ALA SER LEU PRO VAL LEU GLN LYS GLU SER
SEQRES 2 B 382 VAL PHE GLN SER GLY ALA HIS ALA TYR ARG ILE PRO ALA
SEQRES 3 B 382 LEU LEU TYR LEU PRO GLY GLN GLN SER LEU LEU ALA PHE
SEQRES 4 B 382 ALA GLU GLN ARG ALA SER LYS LYS ASP GLU HIS ALA GLU
SEQRES 5 B 382 LEU ILE VAL LEU ARG ARG GLY ASP TYR ASP ALA PRO THR
SEQRES 6 B 382 HIS GLN VAL GLN TRP GLN ALA GLN GLU VAL VAL ALA GLN
SEQRES 7 B 382 ALA ARG LEU ASP GLY HIS ARG SER MET ASN PRO CYS PRO
SEQRES 8 B 382 LEU TYR ASP ALA GLN THR GLY THR LEU PHE LEU PHE PHE
SEQRES 9 B 382 ILE ALA ILE PRO GLY GLN VAL THR GLN GLN GLN GLN LEU
SEQRES 10 B 382 GLN THR ARG ALA ASN VAL THR ARG LEU CYS GLN VAL THR
SEQRES 11 B 382 SER THR ASP HIS GLY ARG THR TRP SER SER PRO ARG ASP
SEQRES 12 B 382 LEU THR ASP ALA ALA ILE GLY PRO ALA TYR ARG GLU TRP
SEQRES 13 B 382 SER THR PHE ALA VAL GLY PRO GLY HIS CYS LEU GLN LEU
SEQRES 14 B 382 ASN ASP ARG ALA ARG SER LEU VAL VAL PRO ALA TYR ALA
SEQRES 15 B 382 TYR ARG LYS LEU HIS PRO ILE GLN ARG PRO ILE PRO SER
SEQRES 16 B 382 ALA PHE CYS PHE LEU SER HIS ASP HIS GLY ARG THR TRP
SEQRES 17 B 382 ALA ARG GLY HIS PHE VAL ALA GLN ASP THR LEU GLU CYS
SEQRES 18 B 382 GLN VAL ALA GLU VAL GLU THR GLY GLU GLN ARG VAL VAL
SEQRES 19 B 382 THR LEU ASN ALA ARG SER HIS LEU ARG ALA ARG VAL GLN
SEQRES 20 B 382 ALA GLN SER THR ASN ASP GLY LEU ASP PHE GLN GLU SER
SEQRES 21 B 382 GLN LEU VAL LYS LYS LEU VAL GLU PRO PRO PRO GLN GLY
SEQRES 22 B 382 CYS GLN GLY SER VAL ILE SER PHE PRO SER PRO ARG SER
SEQRES 23 B 382 GLY PRO GLY SER PRO ALA GLN TRP LEU LEU TYR THR HIS
SEQRES 24 B 382 PRO THR HIS SER TRP GLN ARG ALA ASP LEU GLY ALA TYR
SEQRES 25 B 382 LEU ASN PRO ARG PRO PRO ALA PRO GLU ALA TRP SER GLU
SEQRES 26 B 382 PRO VAL LEU LEU ALA LYS GLY SER CYS ALA TYR SER ASP
SEQRES 27 B 382 LEU GLN SER MET GLY THR GLY PRO ASP GLY SER PRO LEU
SEQRES 28 B 382 PHE GLY CYS LEU TYR GLU ALA ASN ASP TYR GLU GLU ILE
SEQRES 29 B 382 VAL PHE LEU MET PHE THR LEU LYS GLN ALA PHE PRO ALA
SEQRES 30 B 382 GLU TYR LEU PRO GLN
HET DAN A1001 20
HET DAN B1002 20
HET EPE A1003 15
HET EPE B1004 15
HET EPE A1005 15
HET EPE B1006 15
HETNAM DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 3 DAN 2(C11 H17 N O8)
FORMUL 5 EPE 4(C8 H18 N2 O4 S)
FORMUL 9 HOH *460(H2 O)
HELIX 1 1 LYS A 45 GLU A 47 5 3
HELIX 2 2 THR A 110 ARG A 118 1 9
HELIX 3 3 LEU A 142 ILE A 147 1 6
HELIX 4 4 GLY A 148 ARG A 152 5 5
HELIX 5 5 ALA A 317 TRP A 321 5 5
HELIX 6 6 LEU A 369 PHE A 373 1 5
HELIX 7 7 PRO A 374 TYR A 377 5 4
HELIX 8 8 LYS B 45 GLU B 47 5 3
HELIX 9 9 THR B 110 ARG B 118 1 9
HELIX 10 10 LEU B 142 ILE B 147 1 6
HELIX 11 11 GLY B 148 ARG B 152 5 5
HELIX 12 12 ALA B 317 TRP B 321 5 5
HELIX 13 13 LEU B 369 PHE B 373 1 5
HELIX 14 14 PRO B 374 TYR B 377 5 4
SHEET 1 A 7 GLN A 8 GLN A 14 0
SHEET 2 A 7 GLU A 361 THR A 368 -1 O PHE A 364 N GLU A 10
SHEET 3 A 7 PRO A 348 ALA A 356 -1 N PHE A 350 O PHE A 367
SHEET 4 A 7 VAL A 325 THR A 342 -1 N MET A 340 O LEU A 349
SHEET 5 A 7 ALA A 305 ASN A 312 -1 N ASP A 306 O GLY A 330
SHEET 6 A 7 GLN A 291 PRO A 298 -1 N TYR A 295 O TYR A 310
SHEET 7 A 7 SER A 275 PRO A 280 -1 N ILE A 277 O LEU A 294
SHEET 1 B 4 ALA A 19 LEU A 28 0
SHEET 2 B 4 SER A 33 ARG A 41 -1 O SER A 33 N LEU A 28
SHEET 3 B 4 ALA A 49 ASP A 60 -1 O LEU A 51 N GLN A 40
SHEET 4 B 4 GLN A 65 TRP A 68 -1 O GLN A 65 N ASP A 60
SHEET 1 C 4 ALA A 19 LEU A 28 0
SHEET 2 C 4 SER A 33 ARG A 41 -1 O SER A 33 N LEU A 28
SHEET 3 C 4 ALA A 49 ASP A 60 -1 O LEU A 51 N GLN A 40
SHEET 4 C 4 GLU A 72 VAL A 73 -1 O GLU A 72 N LEU A 54
SHEET 1 D 4 HIS A 82 ASP A 92 0
SHEET 2 D 4 THR A 97 PRO A 106 -1 O PHE A 99 N LEU A 90
SHEET 3 D 4 ARG A 123 SER A 129 -1 O CYS A 125 N PHE A 102
SHEET 4 D 4 ARG A 140 ASP A 141 -1 O ARG A 140 N GLN A 126
SHEET 1 E 3 TRP A 154 VAL A 159 0
SHEET 2 E 3 LEU A 174 ARG A 182 -1 O TYR A 181 N THR A 156
SHEET 3 E 3 LEU A 165 GLN A 166 -1 N LEU A 165 O VAL A 175
SHEET 1 F 4 TRP A 154 VAL A 159 0
SHEET 2 F 4 LEU A 174 ARG A 182 -1 O TYR A 181 N THR A 156
SHEET 3 F 4 ILE A 191 SER A 199 -1 O PHE A 197 N VAL A 176
SHEET 4 F 4 ALA A 207 ARG A 208 -1 O ALA A 207 N LEU A 198
SHEET 1 G 4 CYS A 219 GLU A 225 0
SHEET 2 G 4 ARG A 230 ALA A 236 -1 O VAL A 231 N VAL A 224
SHEET 3 G 4 ALA A 242 SER A 248 -1 O VAL A 244 N ALA A 236
SHEET 4 G 4 GLN A 256 VAL A 265 -1 O GLN A 256 N GLN A 247
SHEET 1 H 7 GLN B 8 GLN B 14 0
SHEET 2 H 7 GLU B 361 THR B 368 -1 O PHE B 364 N GLU B 10
SHEET 3 H 7 PRO B 348 ALA B 356 -1 N CYS B 352 O LEU B 365
SHEET 4 H 7 VAL B 325 THR B 342 -1 N MET B 340 O LEU B 349
SHEET 5 H 7 ALA B 305 ASN B 312 -1 N ASP B 306 O GLY B 330
SHEET 6 H 7 GLN B 291 PRO B 298 -1 N TYR B 295 O TYR B 310
SHEET 7 H 7 SER B 275 PRO B 280 -1 N PHE B 279 O TRP B 292
SHEET 1 I 4 ALA B 19 LEU B 28 0
SHEET 2 I 4 SER B 33 ARG B 41 -1 O ARG B 41 N ALA B 19
SHEET 3 I 4 ALA B 49 ASP B 60 -1 O GLY B 57 N LEU B 34
SHEET 4 I 4 GLN B 65 TRP B 68 -1 O GLN B 65 N ASP B 60
SHEET 1 J 4 ALA B 19 LEU B 28 0
SHEET 2 J 4 SER B 33 ARG B 41 -1 O ARG B 41 N ALA B 19
SHEET 3 J 4 ALA B 49 ASP B 60 -1 O GLY B 57 N LEU B 34
SHEET 4 J 4 GLU B 72 VAL B 73 -1 O GLU B 72 N LEU B 54
SHEET 1 K 4 HIS B 82 TYR B 91 0
SHEET 2 K 4 LEU B 98 PRO B 106 -1 O PHE B 99 N LEU B 90
SHEET 3 K 4 ARG B 123 SER B 129 -1 O CYS B 125 N PHE B 102
SHEET 4 K 4 ARG B 140 ASP B 141 -1 O ARG B 140 N GLN B 126
SHEET 1 L 3 TRP B 154 VAL B 159 0
SHEET 2 L 3 LEU B 174 ARG B 182 -1 O TYR B 181 N SER B 155
SHEET 3 L 3 LEU B 165 GLN B 166 -1 N LEU B 165 O VAL B 175
SHEET 1 M 4 TRP B 154 VAL B 159 0
SHEET 2 M 4 LEU B 174 ARG B 182 -1 O TYR B 181 N SER B 155
SHEET 3 M 4 ILE B 191 SER B 199 -1 O PHE B 195 N ALA B 178
SHEET 4 M 4 ALA B 207 ARG B 208 -1 O ALA B 207 N LEU B 198
SHEET 1 N 4 CYS B 219 VAL B 224 0
SHEET 2 N 4 VAL B 231 ALA B 236 -1 O VAL B 231 N VAL B 224
SHEET 3 N 4 ALA B 242 SER B 248 -1 O VAL B 244 N ALA B 236
SHEET 4 N 4 GLU B 257 VAL B 265 -1 O VAL B 261 N ARG B 243
CISPEP 1 GLY A 160 PRO A 161 0 0.28
CISPEP 2 PRO A 268 PRO A 269 0 -0.07
CISPEP 3 PRO A 315 PRO A 316 0 0.17
CISPEP 4 GLY B 160 PRO B 161 0 0.39
CISPEP 5 PRO B 268 PRO B 269 0 -0.04
CISPEP 6 PRO B 315 PRO B 316 0 -0.04
SITE 1 AC1 15 ARG A 21 ASP A 46 GLN A 111 TYR A 179
SITE 2 AC1 15 TYR A 181 GLU A 218 ARG A 237 ARG A 304
SITE 3 AC1 15 TYR A 334 EPE A1005 HOH A1019 HOH A1031
SITE 4 AC1 15 HOH A1033 HOH A1132 HOH A1193
SITE 1 AC2 17 ARG B 21 ARG B 41 ASP B 46 MET B 85
SITE 2 AC2 17 GLN B 111 TYR B 179 TYR B 181 GLU B 218
SITE 3 AC2 17 ARG B 237 GLN B 270 ARG B 304 TYR B 334
SITE 4 AC2 17 HOH B1047 HOH B1056 HOH B1061 HOH B1107
SITE 5 AC2 17 HOH B1115
SITE 1 AC3 15 SER A 11 VAL A 12 PHE A 13 GLN A 14
SITE 2 AC3 15 GLY A 16 ALA A 17 HIS A 18 TYR A 20
SITE 3 AC3 15 ARG A 55 HOH A1006 HOH A1016 HOH A1126
SITE 4 AC3 15 HOH A1166 VAL B 6 LEU B 7
SITE 1 AC4 12 VAL A 6 LEU A 7 HOH A1034 SER B 11
SITE 2 AC4 12 VAL B 12 PHE B 13 GLN B 14 GLY B 16
SITE 3 AC4 12 ALA B 17 HIS B 18 TYR B 20 HOH B1007
SITE 1 AC5 13 ARG A 21 ARG A 41 LYS A 44 ASP A 46
SITE 2 AC5 13 ARG A 237 PRO A 269 GLN A 270 ARG A 304
SITE 3 AC5 13 TYR A 359 DAN A1001 HOH A1033 HOH A1046
SITE 4 AC5 13 HOH A1077
SITE 1 AC6 10 ARG B 21 ARG B 41 LYS B 44 ASP B 46
SITE 2 AC6 10 PRO B 269 GLN B 270 TYR B 359 HOH B1047
SITE 3 AC6 10 HOH B1063 HOH B1096
CRYST1 157.370 73.640 78.950 90.00 90.31 90.00 C 1 2 1 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 0.006354 0.000000 0.000034 0.00000
SCALE2 0.000000 0.013580 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012666 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
