HEADER TRANSLATION 30-OCT-15 5EIR
TITLE CO-CRYSTAL STRUCTURE OF EIF4E WITH NUCLEOTIDE MIMETIC INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EIF4E,EIF-4F 25 KDA SUBUNIT,MRNA CAP-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: EIF4E BINDING SEQUENCE;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EIF4E, EIF4EL1, EIF4F;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: COMMERCIAL SYNTHESIS
KEYWDS COMPLEX, INHIBITOR, TRANSLATION, EIF4E
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.NOWICKI,M.D.WALKINSHAW,P.M.FISCHER
REVDAT 3 10-JAN-24 5EIR 1 REMARK
REVDAT 2 14-SEP-16 5EIR 1 JRNL
REVDAT 1 07-SEP-16 5EIR 0
JRNL AUTH F.SOUKARIEH,M.W.NOWICKI,A.BASTIDE,T.POYRY,C.JONES,K.DUDEK,
JRNL AUTH 2 G.PATWARDHAN,F.MEULLENET,N.J.OLDHAM,M.D.WALKINSHAW,
JRNL AUTH 3 A.E.WILLIS,P.M.FISCHER
JRNL TITL DESIGN OF NUCLEOTIDE-MIMETIC AND NON-NUCLEOTIDE INHIBITORS
JRNL TITL 2 OF THE TRANSLATION INITIATION FACTOR EIF4E: SYNTHESIS,
JRNL TITL 3 STRUCTURAL AND FUNCTIONAL CHARACTERISATION.
JRNL REF EUR.J.MED.CHEM. V. 124 200 2016
JRNL REFN ISSN 0223-5234
JRNL PMID 27592390
JRNL DOI 10.1016/J.EJMECH.2016.08.047
REMARK 2
REMARK 2 RESOLUTION. 2.69 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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.290
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 6738
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 310
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 48.0365 - 3.3891 0.92 3269 176 0.2300 0.2443
REMARK 3 2 3.3891 - 2.6901 0.92 3159 134 0.2769 0.3327
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.14
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 : 0.009 1809
REMARK 3 ANGLE : 1.245 2463
REMARK 3 CHIRALITY : 0.060 253
REMARK 3 PLANARITY : 0.007 304
REMARK 3 DIHEDRAL : 19.619 658
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 5EIR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9173
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : PILATUS 6M
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6814
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 123.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.35900
REMARK 200 R SYM FOR SHELL (I) : 0.35900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 2V8Y CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-31% PEG 8000, 1???3% (NH4)2SO4, 100
REMARK 280 MM HEPES, PH 7.5, 1 ROUND OF SEEDING. CRYSTALS REPLACED IN TO
REMARK 280 ABOVE CONDITIONS WITHOUT (NH4)2SO4 PRIOR TO FREEZING., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 19.12500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.83500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 19.12500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 61.83500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 A 404 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 VAL A 4
REMARK 465 GLU A 5
REMARK 465 PRO A 6
REMARK 465 GLU A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 PRO A 10
REMARK 465 THR A 11
REMARK 465 PRO A 12
REMARK 465 ASN A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 THR A 16
REMARK 465 THR A 17
REMARK 465 GLU A 18
REMARK 465 GLU A 19
REMARK 465 GLU A 20
REMARK 465 LYS A 21
REMARK 465 THR A 22
REMARK 465 GLU A 23
REMARK 465 SER A 24
REMARK 465 ASN A 25
REMARK 465 GLN A 26
REMARK 465 GLU A 27
REMARK 465 LYS A 206
REMARK 465 SER A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
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 402 O HOH A 431 1.99
REMARK 500 CB ALA A 204 FAI 5O8 A 301 2.05
REMARK 500 CB ALA A 204 FAG 5O8 A 301 2.11
REMARK 500
REMARK 500 REMARK: NULL
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 MET A 101 O - C - N ANGL. DEV. = -9.8 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 143 -135.68 57.46
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 residues 5O8 A 301 and SO4 A
REMARK 800 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 5O8 A 301 and SO4 A
REMARK 800 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V8W RELATED DB: PDB
REMARK 900 RELATED ID: 2W97 RELATED DB: PDB
DBREF 5EIR A 1 217 UNP P06730 IF4E_HUMAN 1 217
DBREF 5EIR B 621 634 PDB 5EIR 5EIR 621 634
SEQRES 1 A 217 MET ALA THR VAL GLU PRO GLU THR THR PRO THR PRO ASN
SEQRES 2 A 217 PRO PRO THR THR GLU GLU GLU LYS THR GLU SER ASN GLN
SEQRES 3 A 217 GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU
SEQRES 4 A 217 GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS
SEQRES 5 A 217 SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS
SEQRES 6 A 217 PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS
SEQRES 7 A 217 ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR
SEQRES 8 A 217 SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP
SEQRES 9 A 217 GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU
SEQRES 10 A 217 ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP
SEQRES 11 A 217 LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP
SEQRES 12 A 217 ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL
SEQRES 13 A 217 ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU
SEQRES 14 A 217 CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL
SEQRES 15 A 217 TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE
SEQRES 16 A 217 GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY
SEQRES 17 A 217 SER THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 B 14 LYS LYS ARG TYR ASP ARG GLU PHE LEU LEU GLY PHE GLN
SEQRES 2 B 14 PHE
HET 5O8 A 301 68
HET SO4 A 302 5
HETNAM 5O8 ~{N}-[[(2~{R},3~{S},4~{R},5~{R})-5-[2-AZANYL-6-
HETNAM 2 5O8 OXIDANYLIDENE-7-(PHENYLMETHYL)-1~{H}-PURIN-7-IUM-9-
HETNAM 3 5O8 YL]-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL]-1,1,1-
HETNAM 4 5O8 TRIS(FLUORANYL)METHANESULFONAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 5O8 C18 H20 F3 N6 O6 S 1+
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *32(H2 O)
HELIX 1 AA1 ASN A 30 TYR A 34 5 5
HELIX 2 AA2 THR A 55 ASN A 59 1 5
HELIX 3 AA3 VAL A 69 ASN A 77 1 9
HELIX 4 AA4 ASP A 104 ARG A 109 1 6
HELIX 5 AA5 GLN A 120 ASP A 125 1 6
HELIX 6 AA6 ASP A 125 GLY A 139 1 15
HELIX 7 AA7 PHE A 142 ASP A 147 5 6
HELIX 8 AA8 ASN A 172 GLY A 188 1 17
HELIX 9 AA9 HIS A 200 ALA A 204 1 5
HELIX 10 AB1 ASP B 625 LEU B 630 1 6
HELIX 11 AB2 GLY B 631 GLN B 633 5 3
SHEET 1 AA1 8 LEU A 60 THR A 68 0
SHEET 2 AA1 8 PRO A 38 PHE A 48 -1 N TRP A 43 O PHE A 66
SHEET 3 AA1 8 CYS A 89 LYS A 95 -1 O PHE A 94 N ALA A 44
SHEET 4 AA1 8 VAL A 149 VAL A 156 -1 O ALA A 152 N LEU A 93
SHEET 5 AA1 8 LYS A 162 THR A 167 -1 O LYS A 162 N ASN A 155
SHEET 6 AA1 8 GLY A 111 THR A 116 -1 N GLY A 111 O THR A 167
SHEET 7 AA1 8 ILE A 195 SER A 199 -1 O GLN A 198 N ARG A 112
SHEET 8 AA1 8 PHE A 215 VAL A 217 -1 O PHE A 215 N TYR A 197
SSBOND 1 5O8 A 301 SO4 A 302 1555 1555 2.01
LINK CBGA5O8 A 301 O3 SO4 A 302 1555 1555 1.21
LINK CBGA5O8 A 301 O4 SO4 A 302 1555 1555 1.45
SITE 1 AC1 12 TRP A 56 MET A 101 TRP A 102 GLU A 103
SITE 2 AC1 12 ARG A 112 ARG A 157 TRP A 166 HIS A 200
SITE 3 AC1 12 THR A 203 ALA A 204 HOH A 413 HOH A 416
SITE 1 AC2 12 TRP A 56 MET A 101 TRP A 102 GLU A 103
SITE 2 AC2 12 ARG A 112 ARG A 157 TRP A 166 HIS A 200
SITE 3 AC2 12 THR A 203 ALA A 204 HOH A 413 HOH A 416
CRYST1 38.250 52.120 123.670 90.00 90.00 90.00 P 21 2 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 0.026144 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008086 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
