HEADER TRANSLATION 29-OCT-15 5EI3
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;
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_PLASMID: PET11D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 13 ORGANISM_TAXID: 32630;
SOURCE 14 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 29-NOV-17 5EI3 1 REMARK
REVDAT 2 14-SEP-16 5EI3 1 JRNL
REVDAT 1 07-SEP-16 5EI3 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. 1.71 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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.700
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 28089
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1411
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 40.0459 - 3.6832 1.00 2833 177 0.1529 0.1722
REMARK 3 2 3.6832 - 2.9238 1.00 2692 154 0.1577 0.1974
REMARK 3 3 2.9238 - 2.5543 1.00 2672 150 0.1671 0.1681
REMARK 3 4 2.5543 - 2.3208 1.00 2659 151 0.1709 0.1477
REMARK 3 5 2.3208 - 2.1544 1.00 2638 136 0.1611 0.2238
REMARK 3 6 2.1544 - 2.0274 1.00 2633 136 0.1684 0.1945
REMARK 3 7 2.0274 - 1.9259 1.00 2641 126 0.1735 0.1928
REMARK 3 8 1.9259 - 1.8420 1.00 2626 147 0.1742 0.1965
REMARK 3 9 1.8420 - 1.7711 1.00 2645 116 0.1801 0.2293
REMARK 3 10 1.7711 - 1.7100 1.00 2639 118 0.1988 0.2418
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.20
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 1794
REMARK 3 ANGLE : 0.946 2432
REMARK 3 CHIRALITY : 0.063 252
REMARK 3 PLANARITY : 0.005 305
REMARK 3 DIHEDRAL : 16.473 658
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 5EI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-APR-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 : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.85
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : PSI PILATUS 6M
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28165
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 62.595
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.34200
REMARK 200 R SYM FOR SHELL (I) : 0.34200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2V8W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
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, VAPOR DIFFUSION, HANGING
REMARK 280 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 19.29500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.59500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 19.29500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.59500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 511 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 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 654 O HOH A 696 1.86
REMARK 500 O HOH A 429 O HOH A 652 2.01
REMARK 500 O HOH B 710 O HOH B 720 2.01
REMARK 500 O HOH A 576 O HOH A 604 2.02
REMARK 500 NE2 GLN A 57 O HOH A 401 2.03
REMARK 500 O HOH A 683 O HOH B 735 2.05
REMARK 500 O HOH A 601 O HOH A 664 2.06
REMARK 500 O HOH A 671 O HOH A 706 2.07
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 TYR A 34 -13.25 -145.28
REMARK 500 ASP A 67 25.47 -144.41
REMARK 500 ASP A 143 -124.51 56.22
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 706 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 707 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 708 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A 709 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A 710 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B 744 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 745 DISTANCE = 6.10 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5O8 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V8W RELATED DB: PDB
REMARK 900 2V8W IS THE SAME PROTEIN WITH A DIFFERENT PEPTIDE AND LIGAND.
REMARK 900 RELATED ID: 5EHC RELATED DB: PDB
REMARK 900 5EHC IS ASSOCIATED WITH THIS DEPOSITION (SAME PRIMARY CITATION).
DBREF 5EI3 A 1 217 UNP P06730 IF4E_HUMAN 1 217
DBREF 5EI3 B 621 634 PDB 5EI3 5EI3 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 34
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 *355(H2 O)
HELIX 1 AA1 ASN A 30 TYR A 34 5 5
HELIX 2 AA2 TRP A 56 ALA A 58 5 3
HELIX 3 AA3 VAL A 69 ASN A 77 1 9
HELIX 4 AA4 LEU A 81 LEU A 85 5 5
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 LYS A 206 1 7
HELIX 10 AB1 ASP B 625 GLY B 631 1 7
SHEET 1 AA1 8 LEU A 60 THR A 68 0
SHEET 2 AA1 8 PRO A 38 PHE A 48 -1 N PHE A 47 O ARG A 61
SHEET 3 AA1 8 ASP A 90 LYS A 95 -1 O SER A 92 N TRP A 46
SHEET 4 AA1 8 VAL A 149 ASN A 155 -1 O VAL A 154 N TYR A 91
SHEET 5 AA1 8 LYS A 162 THR A 167 -1 O TRP A 166 N CYS A 150
SHEET 6 AA1 8 GLY A 111 THR A 116 -1 N ILE A 115 O ILE A 163
SHEET 7 AA1 8 ILE A 195 SER A 199 -1 O GLY A 196 N LEU A 114
SHEET 8 AA1 8 PHE A 215 VAL A 217 -1 O PHE A 215 N TYR A 197
SITE 1 AC1 15 TRP A 56 MET A 101 TRP A 102 GLU A 103
SITE 2 AC1 15 ARG A 112 TRP A 166 HIS A 200 THR A 203
SITE 3 AC1 15 ALA A 204 SO4 A 302 HOH A 421 HOH A 465
SITE 4 AC1 15 HOH A 525 HOH A 545 HOH A 583
SITE 1 AC2 8 ARG A 157 5O8 A 301 HOH A 420 HOH A 425
SITE 2 AC2 8 HOH A 436 HOH A 451 HOH A 525 HOH A 592
CRYST1 38.590 52.080 125.190 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 0.025913 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019201 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007988 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
