HEADER TRANSLATION 09-AUG-15 5ABU
TITLE COMPLEX OF D. MELANOGASTER EIF4E WITH THE 4E-BINDING PROTEIN MEXTLI
TITLE 2 AND CAP ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 69-248;
COMPND 5 SYNONYM: EIF-4E, EIF4E, EIF-4F 25 KDA SUBUNIT, MRNA CAP-BINDING PROT
COMPND 6 PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 4E-BINDING PROTEIN MEXTLI;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 577-640;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETMCN (PNYC);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 13 ORGANISM_COMMON: FRUIT FLY;
SOURCE 14 ORGANISM_TAXID: 7227;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 18 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR: PETMCN (PNEA)
KEYWDS TRANSLATION, GENE REGULATION, CAP BINDING PROTEIN, 4E BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PETER,O.WEICHENRIEDER
REVDAT 3 10-JAN-24 5ABU 1 REMARK
REVDAT 2 23-SEP-15 5ABU 1 JRNL
REVDAT 1 02-SEP-15 5ABU 0
JRNL AUTH D.PETER,R.WEBER,C.KOENE,M.-Y.CHUNG,L.EBERTSCH,V.TRUFFAULT,
JRNL AUTH 2 O.WEICHENRIEDER,C.IGREJA,E.IZAURRALDE
JRNL TITL MEXTLI PROTEINS USE BOTH CANONICAL BIPARTITE AND NOVEL
JRNL TITL 2 TRIPARTITE BINDING MODES TO FORM EIF4E COMPLEXES THAT
JRNL TITL 3 DISPLAY DIFFERENTIAL SENSITIVITY TO 4E-BP REGULATION
JRNL REF GENES DEV. V. 29 1835 2015
JRNL REFN ISSN 0890-9369
JRNL PMID 26294658
JRNL DOI 10.1101/GAD.269068.115
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 13971
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 739
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 40.8888 - 3.6929 0.99 2755 164 0.1775 0.2077
REMARK 3 2 3.6929 - 2.9314 1.00 2658 147 0.1965 0.2406
REMARK 3 3 2.9314 - 2.5609 1.00 2614 152 0.2043 0.2794
REMARK 3 4 2.5609 - 2.3268 1.00 2624 132 0.2234 0.2686
REMARK 3 5 2.3268 - 2.1600 0.99 2581 144 0.2308 0.2989
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.70
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 : 0.002 2015
REMARK 3 ANGLE : 0.603 2745
REMARK 3 CHIRALITY : 0.025 293
REMARK 3 PLANARITY : 0.002 370
REMARK 3 DIHEDRAL : 10.574 761
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: HYDROGENS WERE REFINED IN THE RIDING
REMARK 3 POSITIONS. SIDECHAINS OF THE FOLLOWING RESIDUES WERE TRUNCATED
REMARK 3 AT CB ATOMS. CHAIN A, RESIDUES 67, 68, 150, 190, 237, 243. THE
REMARK 3 FOLLOWING RESIDUES WERE MODELED AS DOUBLE CONFORMATIONS. CHAIN A,
REMARK 3 RESIDUES 73, 215. THE FOLLOWING RESIDUES ARE DISORDERED. CHAIN
REMARK 3 A, RESIDUES 151 TO 153, 238 TO 241. CHAIN B, RESIDUES 636 TO
REMARK 3 640. RESTRAINTS FOR THE GTG LIGAND WERE GENERATED WITH GRADE.
REMARK 4
REMARK 4 5ABU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1290063848.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00002
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14107
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 48.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.56000
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4UE8 CHAIN A
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MMT (MALIC ACID:MES:TRIS),
REMARK 280 PH=4.0, 23% PEG1500, PH 4.0
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 22.44000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.54000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.54000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.44000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.20000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.8 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 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 65
REMARK 465 PRO A 66
REMARK 465 ASN A 151
REMARK 465 LYS A 152
REMARK 465 SER A 153
REMARK 465 GLN A 238
REMARK 465 GLY A 239
REMARK 465 SER A 240
REMARK 465 ASN A 241
REMARK 465 GLY B 571
REMARK 465 PRO B 572
REMARK 465 HIS B 573
REMARK 465 MET B 574
REMARK 465 LEU B 575
REMARK 465 GLU B 576
REMARK 465 SER B 577
REMARK 465 THR B 636
REMARK 465 ALA B 637
REMARK 465 ALA B 638
REMARK 465 LYS B 639
REMARK 465 ARG B 640
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 67 CG ND1 CD2 CE1 NE2
REMARK 470 MET A 68 CG SD CE
REMARK 470 LEU A 150 CG CD1 CD2
REMARK 470 LYS A 190 CG CD CE NZ
REMARK 470 LYS A 237 CG CD CE NZ
REMARK 470 LYS A 243 CG CD CE NZ
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 100 23.63 -150.04
REMARK 500 ALA B 609 63.31 -151.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTG A 1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1636
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5ABV RELATED DB: PDB
REMARK 900 COMPLEX OF D. MELANOGASTER EIF4E WITH THE 4E-BINDING PROTEIN MEXTLI
REMARK 900 RELATED ID: 5ABX RELATED DB: PDB
REMARK 900 COMPLEX OF C. ELEGANS EIF4E-3 WITH THE 4E-BINDING PROTEIN MEXTLI
REMARK 900 AND CAP ANALOG
REMARK 900 RELATED ID: 5ABY RELATED DB: PDB
REMARK 900 COMPLEX OF C. ELEGANS EIF4E-3 WITH THE 4E-BINDING PROTEIN MEXTLI
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NUMBERING OF CHAIN A CORRESPONDS TO UNP P48598-2. COMPARED
REMARK 999 TO UNP P48598, SEQUENCE NUMBERS ARE SHIFTED BY -11
REMARK 999 RESIDUES. THE FIRST FOUR RESIDUES OF CHAIN A REMAIN FROM
REMARK 999 THE EXPRESSION TAG.
REMARK 999 THE FIRST SIX RESIDUES OF CHAIN B REMAIN FROM THE
REMARK 999 EXPRESSION TAG.
DBREF 5ABU A 69 248 UNP P48598 IF4E_DROME 69 248
DBREF 5ABU B 577 640 UNP Q9VR35 Q9VR35_DROME 577 640
SEQADV 5ABU GLY A 65 UNP P48598 EXPRESSION TAG
SEQADV 5ABU PRO A 66 UNP P48598 EXPRESSION TAG
SEQADV 5ABU HIS A 67 UNP P48598 EXPRESSION TAG
SEQADV 5ABU MET A 68 UNP P48598 EXPRESSION TAG
SEQADV 5ABU GLY B 571 UNP Q9VR35 EXPRESSION TAG
SEQADV 5ABU PRO B 572 UNP Q9VR35 EXPRESSION TAG
SEQADV 5ABU HIS B 573 UNP Q9VR35 EXPRESSION TAG
SEQADV 5ABU MET B 574 UNP Q9VR35 EXPRESSION TAG
SEQADV 5ABU LEU B 575 UNP Q9VR35 EXPRESSION TAG
SEQADV 5ABU GLU B 576 UNP Q9VR35 EXPRESSION TAG
SEQRES 1 A 184 GLY PRO HIS MET LYS HIS PRO LEU MET ASN VAL TRP THR
SEQRES 2 A 184 LEU TRP TYR LEU GLU ASN ASP ARG SER LYS SER TRP GLU
SEQRES 3 A 184 ASP MET GLN ASN GLU ILE THR SER PHE ASP THR VAL GLU
SEQRES 4 A 184 ASP PHE TRP SER LEU TYR ASN HIS ILE LYS PRO PRO SER
SEQRES 5 A 184 GLU ILE LYS LEU GLY SER ASP TYR SER LEU PHE LYS LYS
SEQRES 6 A 184 ASN ILE ARG PRO MET TRP GLU ASP ALA ALA ASN LYS GLN
SEQRES 7 A 184 GLY GLY ARG TRP VAL ILE THR LEU ASN LYS SER SER LYS
SEQRES 8 A 184 THR ASP LEU ASP ASN LEU TRP LEU ASP VAL LEU LEU CYS
SEQRES 9 A 184 LEU ILE GLY GLU ALA PHE ASP HIS SER ASP GLN ILE CYS
SEQRES 10 A 184 GLY ALA VAL ILE ASN ILE ARG GLY LYS SER ASN LYS ILE
SEQRES 11 A 184 SER ILE TRP THR ALA ASP GLY ASN ASN GLU GLU ALA ALA
SEQRES 12 A 184 LEU GLU ILE GLY HIS LYS LEU ARG ASP ALA LEU ARG LEU
SEQRES 13 A 184 GLY ARG ASN ASN SER LEU GLN TYR GLN LEU HIS LYS ASP
SEQRES 14 A 184 THR MET VAL LYS GLN GLY SER ASN VAL LYS SER ILE TYR
SEQRES 15 A 184 THR LEU
SEQRES 1 B 70 GLY PRO HIS MET LEU GLU SER ARG VAL SER TYR ASP ILE
SEQRES 2 B 70 GLU HIS LEU LEU TYR TYR SER MET SER PRO HIS SER TRP
SEQRES 3 B 70 THR LEU PRO THR ASP TRP GLN LYS MET GLN GLU THR ALA
SEQRES 4 B 70 PRO SER ILE LEU ARG ASN LYS ASP LEU GLN ASP GLU SER
SEQRES 5 B 70 GLN ARG PHE ASP GLY ASP LYS TYR LEU ALA SER ILE LYS
SEQRES 6 B 70 THR ALA ALA LYS ARG
HET GTG A1249 82
HET CL B1636 1
HETNAM GTG 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE
HETNAM CL CHLORIDE ION
HETSYN GTG MRNA CAP ANALOG N7-METHYL GPPPG
FORMUL 3 GTG C21 H30 N10 O18 P3 1+
FORMUL 4 CL CL 1-
FORMUL 5 HOH *81(H2 O)
HELIX 1 1 TRP A 89 MET A 92 1 4
HELIX 2 2 VAL A 102 HIS A 111 1 10
HELIX 3 3 LYS A 155 ILE A 170 1 16
HELIX 4 4 GLU A 204 ALA A 217 1 14
HELIX 5 5 HIS A 231 VAL A 236 1 6
HELIX 6 6 ILE B 583 SER B 590 1 8
HELIX 7 7 TRP B 602 THR B 608 1 7
HELIX 8 8 GLY B 627 SER B 633 1 7
SHEET 1 AA 8 GLN A 93 THR A 101 0
SHEET 2 AA 8 PRO A 71 LEU A 81 -1 N LEU A 72 O ASP A 100
SHEET 3 AA 8 ASP A 123 LYS A 128 -1 O ASP A 123 N LEU A 81
SHEET 4 AA 8 ILE A 180 ILE A 187 -1 O CYS A 181 N LYS A 128
SHEET 5 AA 8 ASN A 192 THR A 198 -1 O LYS A 193 N ASN A 186
SHEET 6 AA 8 GLY A 144 THR A 149 -1 O GLY A 144 N THR A 198
SHEET 7 AA 8 GLN A 227 LEU A 230 -1 O GLN A 227 N VAL A 147
SHEET 8 AA 8 TYR A 246 THR A 247 -1 O TYR A 246 N TYR A 228
SITE 1 AC1 15 TRP A 89 MET A 92 GLY A 121 MET A 134
SITE 2 AC1 15 TRP A 135 GLU A 136 ARG A 188 LYS A 193
SITE 3 AC1 15 HOH A2041 HOH A2057 HOH A2058 GLU B 584
SITE 4 AC1 15 HIS B 585 TYR B 588 HOH B2006
SITE 1 AC2 1 HIS B 585
CRYST1 44.880 56.400 99.080 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 0.022282 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010093 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
