HEADER HYDROLASE 05-JAN-15 4XHB
TITLE CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM STREPTOCOCCUS PNEUMONIAE
TITLE 2 IN COMPLEX WITH PENTANEDIOL AND CHES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 39-696;
COMPND 5 SYNONYM: NEURAMINIDASE B;
COMPND 6 EC: 3.2.1.18;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE SEROTYPE 4 (STRAIN
SOURCE 3 ATCC BAA-334 / TIGR4);
SOURCE 4 ORGANISM_TAXID: 170187;
SOURCE 5 STRAIN: ATCC BAA-334 / TIGR4;
SOURCE 6 GENE: NANB, SP_1687;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS HYDROLASE, INTRAMOLECULAR TRANS-SIALIDASE, GLYCOSIDASE, DRUG DESIGN,
KEYWDS 2 NEURAMINIDASE, ALLOSTERIC INHIBITOR, SERENDIPITOUS ALLOSTERIC SITES,
KEYWDS 3 CRYSTALLIZATION ARTEFACTS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BREAR
REVDAT 2 10-JAN-24 4XHB 1 REMARK
REVDAT 1 27-JAN-16 4XHB 0
JRNL AUTH G.W.ROGERS,P.BREAR,L.YANG,A.S.CHEN,J.B.O.MITCHELL,
JRNL AUTH 2 G.L.TAYLOR,N.J.WESTWOOD
JRNL TITL THE HUNT FOR SERENDIPITOUS ALLOSTERIC SITES: DISCOVERY OF A
JRNL TITL 2 NOVEL ALLOSTERIC INHIBITOR OF THE BACTERIAL SIALIDASE NANB
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 55149
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 2699
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 9.9807 - 4.8302 0.81 2592 135 0.1610 0.1690
REMARK 3 2 4.8302 - 3.9090 0.85 2668 131 0.1327 0.1529
REMARK 3 3 3.9090 - 3.4380 0.87 2671 134 0.1372 0.1565
REMARK 3 4 3.4380 - 3.1343 0.87 2672 129 0.1432 0.1705
REMARK 3 5 3.1343 - 2.9157 0.89 2709 150 0.1542 0.1813
REMARK 3 6 2.9157 - 2.7476 0.91 2732 153 0.1588 0.1798
REMARK 3 7 2.7476 - 2.6125 0.91 2765 151 0.1590 0.2082
REMARK 3 8 2.6125 - 2.5007 0.92 2773 135 0.1634 0.1934
REMARK 3 9 2.5007 - 2.4058 0.92 2806 151 0.1594 0.2278
REMARK 3 10 2.4058 - 2.3239 0.93 2810 129 0.1583 0.2249
REMARK 3 11 2.3239 - 2.2521 0.93 2761 164 0.1536 0.1886
REMARK 3 12 2.2521 - 2.1884 0.93 2826 135 0.1532 0.2492
REMARK 3 13 2.1884 - 2.1313 0.93 2808 142 0.1526 0.2203
REMARK 3 14 2.1313 - 2.0798 0.93 2794 149 0.1462 0.1932
REMARK 3 15 2.0798 - 2.0329 0.94 2811 153 0.1478 0.2016
REMARK 3 16 2.0329 - 1.9900 0.94 2847 122 0.1451 0.2094
REMARK 3 17 1.9900 - 1.9505 0.94 2787 154 0.1461 0.1960
REMARK 3 18 1.9505 - 1.9140 0.94 2799 146 0.1432 0.2185
REMARK 3 19 1.9140 - 1.8800 0.94 2819 136 0.1593 0.2138
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.590
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.81
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.00
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 : 0.007 5347
REMARK 3 ANGLE : 1.096 7239
REMARK 3 CHIRALITY : 0.079 790
REMARK 3 PLANARITY : 0.004 932
REMARK 3 DIHEDRAL : 13.162 1973
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 4XHB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-11
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) : 1.5418
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55181
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
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 (%) : 91.0
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.18800
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: 2VW0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
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 38.24700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.59650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.29250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.59650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.24700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.29250
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 TOTAL BURIED SURFACE AREA: 530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 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 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 HOH A 1279 O HOH A 1420 2.18
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 ASN A 51 60.55 -117.97
REMARK 500 ILE A 246 63.41 64.36
REMARK 500 SER A 273 -167.10 -171.34
REMARK 500 ASP A 327 89.33 68.80
REMARK 500 PRO A 534 38.48 -85.30
REMARK 500 ALA A 540 59.99 -90.62
REMARK 500 ASP A 645 -166.66 -160.80
REMARK 500 ALA A 652 -118.02 -123.02
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 17Y A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NHE A 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XE9 RELATED DB: PDB
DBREF 4XHB A 39 696 UNP Q54727 NANB_STRPN 39 696
SEQADV 4XHB GLY A 643 UNP Q54727 ASP 643 ENGINEERED MUTATION
SEQRES 1 A 658 ILE SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU ASN
SEQRES 2 A 658 ASN LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP LYS
SEQRES 3 A 658 LEU SER GLY GLU SER GLN THR VAL VAL MET LYS PHE LYS
SEQRES 4 A 658 ALA ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY LEU
SEQRES 5 A 658 SER ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE SER
SEQRES 6 A 658 ILE PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU ILE
SEQRES 7 A 658 ARG ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER ARG
SEQRES 8 A 658 PRO ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA VAL
SEQRES 9 A 658 GLU ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP LYS
SEQRES 10 A 658 THR TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE SER
SEQRES 11 A 658 GLU THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE ASN
SEQRES 12 A 658 GLY ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG GLU
SEQRES 13 A 658 GLY LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP GLU
SEQRES 14 A 658 ILE SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU VAL
SEQRES 15 A 658 SER THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE PHE
SEQRES 16 A 658 GLN SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG ILE
SEQRES 17 A 658 PRO THR LEU TYR THR LEU SER SER GLY ARG VAL LEU SER
SEQRES 18 A 658 SER ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER LYS
SEQRES 19 A 658 SER LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP ASN
SEQRES 20 A 658 GLY LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS PHE
SEQRES 21 A 658 ASN ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG ASP
SEQRES 22 A 658 ASN LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA SER
SEQRES 23 A 658 PHE ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER GLY
SEQRES 24 A 658 LYS THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY ILE
SEQRES 25 A 658 GLY ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE LYS
SEQRES 26 A 658 GLU ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS ASN
SEQRES 27 A 658 GLY ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN GLY
SEQRES 28 A 658 VAL VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN TYR
SEQRES 29 A 658 THR ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY LYS
SEQRES 30 A 658 SER LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP SER
SEQRES 31 A 658 GLY SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL PRO
SEQRES 32 A 658 MET ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL THR
SEQRES 33 A 658 PRO THR ASN TYR ILE ALA MET THR THR SER GLN ASN ARG
SEQRES 34 A 658 GLY GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO PHE
SEQRES 35 A 658 LEU GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO GLY
SEQRES 36 A 658 GLN GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE PHE
SEQRES 37 A 658 ALA THR TYR THR SER GLY GLU LEU THR TYR LEU ILE SER
SEQRES 38 A 658 ASP ASP SER GLY GLN THR TRP LYS LYS SER SER ALA SER
SEQRES 39 A 658 ILE PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET VAL
SEQRES 40 A 658 GLU LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG THR
SEQRES 41 A 658 THR THR GLY LYS ILE ALA TYR MET THR SER ARG ASP SER
SEQRES 42 A 658 GLY GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY ILE
SEQRES 43 A 658 GLN GLN THR SER TYR GLY THR GLN VAL SER ALA ILE LYS
SEQRES 44 A 658 TYR SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE LEU
SEQRES 45 A 658 SER THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY GLN
SEQRES 46 A 658 LEU VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER ILE
SEQRES 47 A 658 ASP TRP LYS TYR HIS TYR GLY ILE ASP LEU PRO SER TYR
SEQRES 48 A 658 GLY TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN HIS
SEQRES 49 A 658 HIS ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP SER
SEQRES 50 A 658 ARG ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR ILE
SEQRES 51 A 658 ASP LEU GLU ILE ASN ASP LEU THR
HET 17Y A 701 7
HET NHE A 702 13
HETNAM 17Y (1R,2S)-CYCLOPENTANE-1,2-DIOL
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL 2 17Y C5 H10 O2
FORMUL 3 NHE C8 H17 N O3 S
FORMUL 4 HOH *675(H2 O)
HELIX 1 AA1 ILE A 57 LEU A 62 1 6
HELIX 2 AA2 ASP A 63 LEU A 65 5 3
HELIX 3 AA3 PRO A 176 ILE A 180 5 5
HELIX 4 AA4 SER A 216 ILE A 223 1 8
HELIX 5 AA5 GLU A 691 THR A 696 1 6
SHEET 1 AA1 6 PHE A 43 ASN A 51 0
SHEET 2 AA1 6 LYS A 202 PHE A 211 -1 O ILE A 205 N TYR A 48
SHEET 3 AA1 6 GLN A 70 LYS A 77 -1 N LYS A 75 O GLU A 207
SHEET 4 AA1 6 ASN A 144 ASP A 151 -1 O LEU A 146 N MET A 74
SHEET 5 AA1 6 THR A 156 VAL A 161 -1 O THR A 158 N VAL A 149
SHEET 6 AA1 6 ILE A 164 THR A 170 -1 O VAL A 166 N MET A 159
SHEET 1 AA2 6 ILE A 55 ASP A 56 0
SHEET 2 AA2 6 LYS A 185 LEU A 188 -1 O LEU A 188 N ILE A 55
SHEET 3 AA2 6 LEU A 84 SER A 91 -1 N GLY A 89 O THR A 187
SHEET 4 AA2 6 TYR A 101 ARG A 107 -1 O PHE A 102 N LEU A 90
SHEET 5 AA2 6 ILE A 112 ASP A 118 -1 O ARG A 117 N TYR A 101
SHEET 6 AA2 6 ILE A 123 ARG A 129 -1 O TYR A 125 N ILE A 116
SHEET 1 AA3 2 LYS A 136 HIS A 137 0
SHEET 2 AA3 2 GLN A 140 ALA A 141 -1 O GLN A 140 N HIS A 137
SHEET 1 AA4 2 VAL A 191 ARG A 193 0
SHEET 2 AA4 2 LYS A 196 HIS A 198 -1 O HIS A 198 N VAL A 191
SHEET 1 AA5 3 TYR A 243 ARG A 245 0
SHEET 2 AA5 3 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 AA5 3 TYR A 250 THR A 251 -1 N TYR A 250 O LEU A 258
SHEET 1 AA6 4 TYR A 243 ARG A 245 0
SHEET 2 AA6 4 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 AA6 4 ILE A 275 SER A 282 -1 O ASN A 276 N ALA A 263
SHEET 4 AA6 4 ILE A 293 MET A 296 -1 O ALA A 295 N ILE A 277
SHEET 1 AA7 5 LYS A 475 LEU A 476 0
SHEET 2 AA7 5 TYR A 458 SER A 464 -1 N MET A 461 O LYS A 475
SHEET 3 AA7 5 THR A 339 MET A 346 -1 N ALA A 343 O ALA A 460
SHEET 4 AA7 5 SER A 324 GLU A 332 -1 N SER A 324 O MET A 346
SHEET 5 AA7 5 GLY A 493 GLN A 494 1 O GLY A 493 N ILE A 330
SHEET 1 AA8 7 PHE A 362 GLU A 364 0
SHEET 2 AA8 7 TYR A 369 LYS A 375 -1 O TYR A 370 N LYS A 363
SHEET 3 AA8 7 TYR A 383 VAL A 385 -1 O TYR A 383 N LEU A 373
SHEET 4 AA8 7 VAL A 390 ASN A 393 -1 O TYR A 392 N THR A 384
SHEET 5 AA8 7 LYS A 398 ILE A 404 -1 O LYS A 398 N ASN A 393
SHEET 6 AA8 7 VAL A 410 GLU A 412 -1 O LEU A 411 N THR A 403
SHEET 7 AA8 7 LYS A 415 SER A 416 -1 O LYS A 415 N GLU A 412
SHEET 1 AA9 3 PHE A 362 GLU A 364 0
SHEET 2 AA9 3 TYR A 369 LYS A 375 -1 O TYR A 370 N LYS A 363
SHEET 3 AA9 3 PHE A 451 LYS A 452 -1 O LYS A 452 N LYS A 374
SHEET 1 AB1 2 THR A 418 ASP A 425 0
SHEET 2 AB1 2 ARG A 432 PRO A 441 -1 O LYS A 438 N GLN A 421
SHEET 1 AB2 3 TYR A 489 LEU A 490 0
SHEET 2 AB2 3 LEU A 504 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 AB2 3 LEU A 496 ALA A 497 -1 N LEU A 496 O ILE A 505
SHEET 1 AB3 4 TYR A 489 LEU A 490 0
SHEET 2 AB3 4 LEU A 504 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 AB3 4 GLU A 513 SER A 519 -1 O LEU A 517 N PHE A 506
SHEET 4 AB3 4 LYS A 527 SER A 532 -1 O LYS A 527 N ILE A 518
SHEET 1 AB4 4 ALA A 542 ARG A 548 0
SHEET 2 AB4 4 VAL A 551 PHE A 556 -1 O ARG A 553 N VAL A 545
SHEET 3 AB4 4 ALA A 564 SER A 568 -1 O ALA A 564 N PHE A 556
SHEET 4 AB4 4 SER A 579 TYR A 580 -1 O SER A 579 N TYR A 565
SHEET 1 AB5 4 SER A 594 ILE A 602 0
SHEET 2 AB5 4 LYS A 605 PRO A 613 -1 O SER A 611 N SER A 594
SHEET 3 AB5 4 GLY A 622 VAL A 629 -1 O GLY A 627 N VAL A 608
SHEET 4 AB5 4 ILE A 636 GLY A 643 -1 O TYR A 642 N LEU A 624
SHEET 1 AB6 3 SER A 654 GLU A 658 0
SHEET 2 AB6 3 ILE A 664 GLU A 669 -1 O GLY A 665 N THR A 657
SHEET 3 AB6 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 1.40
SITE 1 AC1 5 THR A 251 GLN A 494 THR A 657 HOH A 984
SITE 2 AC1 5 HOH A1056
SITE 1 AC2 12 ARG A 245 ASP A 270 ASP A 327 ASN A 352
SITE 2 AC2 12 TYR A 509 ARG A 557 ARG A 619 TYR A 653
SITE 3 AC2 12 TRP A 674 HOH A1095 HOH A1249 HOH A1263
CRYST1 76.494 82.585 117.193 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 0.013073 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012109 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008533 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
