HEADER HYDROLASE/INHIBITOR 21-JUN-12 4FOV
TITLE CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE
TITLE 2 IN COMPLEX WITH 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NEURAMINIDASE B;
COMPND 5 EC: 3.2.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 GENE: NANB, SP_1687;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE, INTRAMOLECULAR TRANS-SIALIDASE, GLYCOSIDASE, DRUG DESIGN,
KEYWDS 2 NEURAMINIDASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BREAR
REVDAT 3 28-FEB-24 4FOV 1 REMARK
REVDAT 2 14-NOV-12 4FOV 1 JRNL
REVDAT 1 31-OCT-12 4FOV 0
JRNL AUTH P.BREAR,J.TELFORD,G.L.TAYLOR,N.J.WESTWOOD
JRNL TITL SYNTHESIS AND STRUCTURAL CHARACTERISATION OF SELECTIVE
JRNL TITL 2 NON-CARBOHYDRATE-BASED INHIBITORS OF BACTERIAL SIALIDASES.
JRNL REF CHEMBIOCHEM V. 13 2374 2012
JRNL REFN ISSN 1439-4227
JRNL PMID 23070966
JRNL DOI 10.1002/CBIC.201200433
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 33142
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950
REMARK 3 FREE R VALUE TEST SET COUNT : 1639
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 22.4330 - 5.2225 0.93 2647 133 0.2073 0.2144
REMARK 3 2 5.2225 - 4.1539 0.96 2629 124 0.1573 0.1784
REMARK 3 3 4.1539 - 3.6313 0.98 2649 138 0.1794 0.2292
REMARK 3 4 3.6313 - 3.3004 0.99 2648 137 0.1736 0.2144
REMARK 3 5 3.3004 - 3.0645 0.99 2660 132 0.1741 0.2347
REMARK 3 6 3.0645 - 2.8842 0.99 2626 159 0.1862 0.2478
REMARK 3 7 2.8842 - 2.7400 0.99 2612 137 0.1830 0.2639
REMARK 3 8 2.7400 - 2.6209 0.99 2624 150 0.1745 0.2495
REMARK 3 9 2.6209 - 2.5202 0.99 2631 138 0.1785 0.2462
REMARK 3 10 2.5202 - 2.4333 0.99 2591 138 0.1919 0.3041
REMARK 3 11 2.4333 - 2.3573 0.99 2632 117 0.1858 0.2820
REMARK 3 12 2.3573 - 2.2900 0.98 2554 136 0.1833 0.2706
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 42.59
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.28570
REMARK 3 B22 (A**2) : -5.29380
REMARK 3 B33 (A**2) : 8.57950
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 5342
REMARK 3 ANGLE : 1.065 7230
REMARK 3 CHIRALITY : 0.073 789
REMARK 3 PLANARITY : 0.004 933
REMARK 3 DIHEDRAL : 14.100 1971
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 4FOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000073169.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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 MICROMAX-007 HF
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33189
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.23900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 0.1M IMIDAZOLE, PH 8.0,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 38.13450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.40150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.27200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.40150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.13450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.27200
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 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 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 1
REMARK 465 ASN A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 GLY A 5
REMARK 465 LEU A 6
REMARK 465 TYR A 7
REMARK 465 SER A 8
REMARK 465 LYS A 9
REMARK 465 LEU A 10
REMARK 465 GLY A 11
REMARK 465 ILE A 12
REMARK 465 SER A 13
REMARK 465 VAL A 14
REMARK 465 VAL A 15
REMARK 465 GLY A 16
REMARK 465 ILE A 17
REMARK 465 SER A 18
REMARK 465 LEU A 19
REMARK 465 LEU A 20
REMARK 465 MET A 21
REMARK 465 GLY A 22
REMARK 465 VAL A 23
REMARK 465 PRO A 24
REMARK 465 THR A 25
REMARK 465 LEU A 26
REMARK 465 ILE A 27
REMARK 465 HIS A 28
REMARK 465 ALA A 29
REMARK 465 ASN A 30
REMARK 465 GLU A 31
REMARK 465 LEU A 32
REMARK 465 ASN A 33
REMARK 465 TYR A 34
REMARK 465 GLY A 35
REMARK 465 GLN A 36
REMARK 465 LEU A 37
REMARK 465 SER A 38
REMARK 465 LYS A 697
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 ASN A 51 62.82 -110.32
REMARK 500 ALA A 78 88.72 -160.10
REMARK 500 ASP A 108 3.16 -68.03
REMARK 500 ILE A 246 63.25 63.00
REMARK 500 SER A 273 -171.65 -178.89
REMARK 500 ASP A 327 92.59 60.40
REMARK 500 LYS A 484 42.48 -105.00
REMARK 500 PRO A 534 49.15 -83.06
REMARK 500 ASP A 549 108.07 -45.04
REMARK 500 SER A 615 132.36 -171.03
REMARK 500 ALA A 652 -122.99 -125.85
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 CXS A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VW0 RELATED DB: PDB
REMARK 900 RELATED ID: 2VW1 RELATED DB: PDB
REMARK 900 RELATED ID: 2VW2 RELATED DB: PDB
REMARK 900 RELATED ID: 4FOQ RELATED DB: PDB
REMARK 900 RELATED ID: 4FOW RELATED DB: PDB
REMARK 900 RELATED ID: 4FOY RELATED DB: PDB
REMARK 900 RELATED ID: 4FP2 RELATED DB: PDB
REMARK 900 RELATED ID: 4FP3 RELATED DB: PDB
REMARK 900 RELATED ID: 4FPC RELATED DB: PDB
REMARK 900 RELATED ID: 4FPE RELATED DB: PDB
REMARK 900 RELATED ID: 4FPF RELATED DB: PDB
REMARK 900 RELATED ID: 4FPG RELATED DB: PDB
REMARK 900 RELATED ID: 4FPH RELATED DB: PDB
REMARK 900 RELATED ID: 4FPJ RELATED DB: PDB
REMARK 900 RELATED ID: 4FPK RELATED DB: PDB
REMARK 900 RELATED ID: 4FPL RELATED DB: PDB
REMARK 900 RELATED ID: 4FPO RELATED DB: PDB
REMARK 900 RELATED ID: 4FPY RELATED DB: PDB
REMARK 900 RELATED ID: 4FQ4 RELATED DB: PDB
DBREF 4FOV A 1 697 UNP Q54727 NANB_STRPN 1 697
SEQRES 1 A 697 MET ASN LYS ARG GLY LEU TYR SER LYS LEU GLY ILE SER
SEQRES 2 A 697 VAL VAL GLY ILE SER LEU LEU MET GLY VAL PRO THR LEU
SEQRES 3 A 697 ILE HIS ALA ASN GLU LEU ASN TYR GLY GLN LEU SER ILE
SEQRES 4 A 697 SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN ASN
SEQRES 5 A 697 LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS LEU
SEQRES 6 A 697 SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS ALA
SEQRES 7 A 697 ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU SER
SEQRES 8 A 697 ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER ILE
SEQRES 9 A 697 PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE ARG
SEQRES 10 A 697 ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG PRO
SEQRES 11 A 697 ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL GLU
SEQRES 12 A 697 ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS THR
SEQRES 13 A 697 TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER GLU
SEQRES 14 A 697 THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN GLY
SEQRES 15 A 697 ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU GLY
SEQRES 16 A 697 LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU ILE
SEQRES 17 A 697 SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL SER
SEQRES 18 A 697 THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE GLN
SEQRES 19 A 697 SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE PRO
SEQRES 20 A 697 THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER SER
SEQRES 21 A 697 ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS SER
SEQRES 22 A 697 LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN GLY
SEQRES 23 A 697 LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE ASN
SEQRES 24 A 697 ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP ASN
SEQRES 25 A 697 LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER PHE
SEQRES 26 A 697 ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY LYS
SEQRES 27 A 697 THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE GLY
SEQRES 28 A 697 ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS GLU
SEQRES 29 A 697 ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN GLY
SEQRES 30 A 697 ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY VAL
SEQRES 31 A 697 VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR THR
SEQRES 32 A 697 ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS SER
SEQRES 33 A 697 LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER GLY
SEQRES 34 A 697 SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO MET
SEQRES 35 A 697 ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR PRO
SEQRES 36 A 697 THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG GLY
SEQRES 37 A 697 GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE LEU
SEQRES 38 A 697 GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY GLN
SEQRES 39 A 697 GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE ALA
SEQRES 40 A 697 THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER ASP
SEQRES 41 A 697 ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER ILE
SEQRES 42 A 697 PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL GLU
SEQRES 43 A 697 LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR THR
SEQRES 44 A 697 THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER GLY
SEQRES 45 A 697 GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE GLN
SEQRES 46 A 697 GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS TYR
SEQRES 47 A 697 SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU SER
SEQRES 48 A 697 THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN LEU
SEQRES 49 A 697 VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE ASP
SEQRES 50 A 697 TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER TYR GLY
SEQRES 51 A 697 TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS HIS
SEQRES 52 A 697 ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER ARG
SEQRES 53 A 697 ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE ASP
SEQRES 54 A 697 LEU GLU ILE ASN ASP LEU THR LYS
HET CXS A 701 14
HET DMS A 702 4
HET DMS A 703 4
HETNAM CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 CXS C9 H19 N O3 S
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 HOH *503(H2 O)
HELIX 1 1 ILE A 57 LEU A 62 1 6
HELIX 2 2 ASP A 63 LEU A 65 5 3
HELIX 3 3 SER A 216 SER A 221 1 6
HELIX 4 4 GLU A 691 THR A 696 1 6
SHEET 1 A 6 PHE A 43 ASN A 51 0
SHEET 2 A 6 LYS A 202 PHE A 211 -1 O ILE A 208 N GLY A 45
SHEET 3 A 6 GLN A 70 LYS A 77 -1 N LYS A 75 O GLU A 207
SHEET 4 A 6 ASN A 144 ASP A 151 -1 O LEU A 146 N MET A 74
SHEET 5 A 6 THR A 156 VAL A 161 -1 O THR A 158 N VAL A 149
SHEET 6 A 6 ILE A 164 THR A 170 -1 O GLU A 169 N TYR A 157
SHEET 1 B 6 ILE A 55 ASP A 56 0
SHEET 2 B 6 LYS A 185 LEU A 188 -1 O LEU A 188 N ILE A 55
SHEET 3 B 6 LEU A 84 SER A 91 -1 N GLY A 89 O THR A 187
SHEET 4 B 6 TYR A 101 ARG A 107 -1 O PHE A 102 N LEU A 90
SHEET 5 B 6 ILE A 112 ASP A 118 -1 O GLY A 113 N PHE A 105
SHEET 6 B 6 ILE A 123 ARG A 129 -1 O TYR A 125 N ILE A 116
SHEET 1 C 2 LYS A 136 HIS A 137 0
SHEET 2 C 2 GLN A 140 ALA A 141 -1 O GLN A 140 N HIS A 137
SHEET 1 D 2 VAL A 191 ARG A 193 0
SHEET 2 D 2 LYS A 196 HIS A 198 -1 O HIS A 198 N VAL A 191
SHEET 1 E 3 TYR A 243 ARG A 245 0
SHEET 2 E 3 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 E 3 TYR A 250 THR A 251 -1 N TYR A 250 O LEU A 258
SHEET 1 F 4 TYR A 243 ARG A 245 0
SHEET 2 F 4 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 F 4 ILE A 275 SER A 282 -1 O ASN A 276 N ALA A 263
SHEET 4 F 4 ILE A 293 MET A 296 -1 O ILE A 293 N THR A 279
SHEET 1 G 5 LYS A 475 LEU A 476 0
SHEET 2 G 5 TYR A 458 SER A 464 -1 N MET A 461 O LYS A 475
SHEET 3 G 5 THR A 339 MET A 346 -1 N LEU A 341 O THR A 462
SHEET 4 G 5 SER A 324 GLU A 332 -1 N VAL A 331 O ILE A 340
SHEET 5 G 5 GLY A 493 GLN A 494 1 O GLY A 493 N SER A 328
SHEET 1 H 7 PHE A 362 ILE A 365 0
SHEET 2 H 7 HIS A 368 LYS A 375 -1 O TYR A 370 N LYS A 363
SHEET 3 H 7 TYR A 383 VAL A 385 -1 O VAL A 385 N LEU A 371
SHEET 4 H 7 VAL A 390 ASN A 393 -1 O TYR A 392 N THR A 384
SHEET 5 H 7 PRO A 399 ILE A 404 -1 O TYR A 402 N VAL A 391
SHEET 6 H 7 VAL A 410 GLU A 412 -1 O LEU A 411 N THR A 403
SHEET 7 H 7 LYS A 415 SER A 416 -1 O LYS A 415 N GLU A 412
SHEET 1 I 3 PHE A 362 ILE A 365 0
SHEET 2 I 3 HIS A 368 LYS A 375 -1 O TYR A 370 N LYS A 363
SHEET 3 I 3 PHE A 451 LYS A 452 -1 O LYS A 452 N LYS A 374
SHEET 1 J 2 THR A 418 ASP A 425 0
SHEET 2 J 2 ARG A 432 PRO A 441 -1 O VAL A 440 N VAL A 419
SHEET 1 K 5 TYR A 489 LEU A 490 0
SHEET 2 K 5 THR A 508 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 K 5 GLU A 513 SER A 519 -1 O THR A 515 N THR A 508
SHEET 4 K 5 LEU A 504 PHE A 506 -1 N LEU A 504 O SER A 519
SHEET 5 K 5 LEU A 496 ALA A 497 -1 N LEU A 496 O ILE A 505
SHEET 1 L 4 TYR A 489 LEU A 490 0
SHEET 2 L 4 THR A 508 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 L 4 GLU A 513 SER A 519 -1 O THR A 515 N THR A 508
SHEET 4 L 4 LYS A 527 SER A 532 -1 O LYS A 527 N ILE A 518
SHEET 1 M 4 ALA A 542 ARG A 548 0
SHEET 2 M 4 VAL A 551 PHE A 556 -1 O PHE A 555 N GLN A 543
SHEET 3 M 4 ALA A 564 SER A 568 -1 O ALA A 564 N PHE A 556
SHEET 4 M 4 SER A 579 TYR A 580 -1 O SER A 579 N TYR A 565
SHEET 1 N 4 SER A 594 LYS A 597 0
SHEET 2 N 4 ALA A 607 PRO A 613 -1 O SER A 611 N SER A 594
SHEET 3 N 4 GLY A 622 VAL A 629 -1 O GLY A 627 N VAL A 608
SHEET 4 N 4 ILE A 636 ASP A 643 -1 O TYR A 642 N LEU A 624
SHEET 1 O 3 SER A 654 GLU A 658 0
SHEET 2 O 3 ILE A 664 GLU A 669 -1 O GLY A 665 N THR A 657
SHEET 3 O 3 VAL A 685 LEU A 690 -1 O LEU A 690 N ILE A 664
CISPEP 1 SER A 271 LYS A 272 0 4.08
SITE 1 AC1 14 ARG A 245 ASP A 270 ILE A 326 ASP A 327
SITE 2 AC1 14 MET A 346 ASN A 352 TYR A 509 GLU A 541
SITE 3 AC1 14 ARG A 557 ARG A 619 TYR A 653 TRP A 674
SITE 4 AC1 14 HOH A 923 HOH A1015
SITE 1 AC2 4 TYR A 250 THR A 251 GLN A 494 THR A 657
SITE 1 AC3 5 ARG A 129 VAL A 166 HIS A 680 LEU A 681
SITE 2 AC3 5 SER A 682
CRYST1 76.269 82.544 116.803 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 0.013111 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012115 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008561 0.00000
(ATOM LINES ARE NOT SHOWN.)
END