HEADER RNA BINDING PROTEIN 19-MAR-02 1L8B
TITLE COCRYSTAL STRUCTURE OF THE MESSENGER RNA 5' CAP-BINDING PROTEIN
TITLE 2 (EIF4E) BOUND TO 7-METHYLGPPPG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4E;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 28-217;
COMPND 5 SYNONYM: EIF-4E, EIF4E, MRNA CAP-BINDING PROTEIN, EIF-4F 25 KDA
COMPND 6 SUBUNIT;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3B
KEYWDS EUKARYOTIC INITIATION FACTOR 4E, EIF4E, CAP, 7-METHYLGPPPG, RNA
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.NIEDZWIECKA,J.MARCOTRIGIANO,J.STEPINSKI,M.JANKOWSKA-ANYSZKA,
AUTHOR 2 A.WYSLOUCH-CIESZYNSKA,M.DADLEZ,A.-C.GINGRAS,P.MAK,E.DARZYNKIEWICZ,
AUTHOR 3 N.SONENBERG
REVDAT 5 14-FEB-24 1L8B 1 REMARK
REVDAT 4 03-FEB-21 1L8B 1 JRNL REMARK
REVDAT 3 24-FEB-09 1L8B 1 VERSN
REVDAT 2 01-APR-03 1L8B 1 JRNL
REVDAT 1 12-JUN-02 1L8B 0
JRNL AUTH A.NIEDZWIECKA,J.MARCOTRIGIANO,J.STEPINSKI,
JRNL AUTH 2 M.JANKOWSKA-ANYSZKA,A.WYSLOUCH-CIESZYNSKA,M.DADLEZ,
JRNL AUTH 3 A.C.GINGRAS,P.MAK,E.DARZYNKIEWICZ,N.SONENBERG,S.K.BURLEY,
JRNL AUTH 4 R.STOLARSKI
JRNL TITL BIOPHYSICAL STUDIES OF EIF4E CAP-BINDING PROTEIN:
JRNL TITL 2 RECOGNITION OF MRNA 5' CAP STRUCTURE AND SYNTHETIC FRAGMENTS
JRNL TITL 3 OF EIF4G AND 4E-BP1 PROTEINS.
JRNL REF J.MOL.BIOL. V. 319 615 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12054859
JRNL DOI 10.1016/S0022-2836(02)00328-5
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 35866
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3608
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 41
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 186
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.240
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L8B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015731.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : PRINCETON 2K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38968
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 35.06000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.92000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.92000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.06000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.96000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 VAL A 28
REMARK 465 ALA A 29
REMARK 465 ASN A 30
REMARK 465 PRO A 31
REMARK 465 GLU A 32
REMARK 465 HIS A 33
REMARK 465 TYR A 34
REMARK 465 ILE A 35
REMARK 465 SER A 207
REMARK 465 GLY A 208
REMARK 465 SER A 209
REMARK 465 THR A 210
REMARK 465 THR A 211
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 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 GLU B 105 CG CD OE1 OE2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 GLN B 120 CG CD OE1 NE2
REMARK 470 ARG B 123 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 206 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 LYS A 52 -45.57 91.77
REMARK 500 ASP A 67 23.55 -146.29
REMARK 500 ASP A 143 -110.92 39.07
REMARK 500 PRO A 191 -4.06 -43.15
REMARK 500 THR A 205 55.15 -107.20
REMARK 500 ASP B 67 21.08 -142.93
REMARK 500 ASP B 125 -33.68 -134.71
REMARK 500 ASP B 143 -117.33 44.71
REMARK 500 CYS B 170 1.49 -69.88
REMARK 500 PRO B 191 -35.72 -23.83
REMARK 500 VAL B 194 115.59 36.33
REMARK 500 LYS B 206 -159.21 48.71
REMARK 500 SER B 207 37.62 -177.30
REMARK 500 SER B 209 -92.85 61.29
REMARK 500 LYS B 212 -176.79 -68.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE (MGP) IS
REMARK 600 ACTUALLY BOUND TO ANOTHER GUANOSINE-5'-MONOPHOSPHATE,
REMARK 600 WHICH IS MISSING IN THE ELECTRON DENSITY.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGP A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGP B 2000
DBREF 1L8B A 28 217 UNP P63073 IF4E_MOUSE 28 217
DBREF 1L8B B 28 217 UNP P63073 IF4E_MOUSE 28 217
SEQRES 1 A 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 A 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 A 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 A 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 A 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 A 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 A 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 A 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 A 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 A 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 A 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 A 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 A 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 A 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 A 190 THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 B 190 VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU GLN
SEQRES 2 B 190 ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS SER
SEQRES 3 B 190 LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS PHE
SEQRES 4 B 190 ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS ILE
SEQRES 5 B 190 GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR SER
SEQRES 6 B 190 LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP GLU
SEQRES 7 B 190 LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU ASN
SEQRES 8 B 190 LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP LEU
SEQRES 9 B 190 GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP ASP
SEQRES 10 B 190 TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL ARG
SEQRES 11 B 190 ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU CYS
SEQRES 12 B 190 GLU ASN ARG ASP ALA VAL THR HIS ILE GLY ARG VAL TYR
SEQRES 13 B 190 LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE GLY
SEQRES 14 B 190 TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY SER
SEQRES 15 B 190 THR THR LYS ASN ARG PHE VAL VAL
HET MGP A1000 33
HET MGP B2000 33
HETNAM MGP 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE
FORMUL 3 MGP 2(C11 H19 N5 O14 P3 1+)
FORMUL 5 HOH *186(H2 O)
HELIX 1 1 TRP A 56 ALA A 58 5 3
HELIX 2 2 VAL A 69 ASN A 77 1 9
HELIX 3 3 LEU A 81 LEU A 85 5 5
HELIX 4 4 GLN A 120 ARG A 122 5 3
HELIX 5 5 ASP A 125 GLY A 139 1 15
HELIX 6 6 PHE A 142 ASP A 147 5 6
HELIX 7 7 ASN A 172 GLY A 188 1 17
HELIX 8 8 HIS A 200 THR A 205 1 6
HELIX 9 9 ASN B 30 ILE B 35 5 6
HELIX 10 10 TRP B 56 ALA B 58 5 3
HELIX 11 11 VAL B 69 ASN B 77 1 9
HELIX 12 12 LEU B 81 LEU B 85 5 5
HELIX 13 13 GLN B 120 ASP B 125 1 6
HELIX 14 14 ASP B 125 GLY B 139 1 15
HELIX 15 15 PHE B 142 ASP B 147 5 6
HELIX 16 16 ASN B 172 GLY B 188 1 17
HELIX 17 17 HIS B 200 LYS B 206 1 7
SHEET 1 A 8 LEU A 60 THR A 68 0
SHEET 2 A 8 PRO A 38 LYS A 49 -1 N LEU A 45 O SER A 64
SHEET 3 A 8 CYS A 89 LYS A 95 -1 O SER A 92 N TRP A 46
SHEET 4 A 8 VAL A 149 VAL A 156 -1 O VAL A 156 N CYS A 89
SHEET 5 A 8 GLY A 160 THR A 167 -1 O LYS A 162 N ASN A 155
SHEET 6 A 8 GLY A 111 ASN A 118 -1 N LEU A 117 O ASP A 161
SHEET 7 A 8 ILE A 195 SER A 199 -1 O GLN A 198 N ARG A 112
SHEET 8 A 8 PHE A 215 VAL A 217 -1 O VAL A 217 N ILE A 195
SHEET 1 B 8 LEU B 60 THR B 68 0
SHEET 2 B 8 PRO B 38 PHE B 48 -1 N TRP B 43 O PHE B 66
SHEET 3 B 8 ASP B 90 LYS B 95 -1 O SER B 92 N TRP B 46
SHEET 4 B 8 VAL B 149 ASN B 155 -1 O VAL B 154 N TYR B 91
SHEET 5 B 8 LYS B 162 THR B 167 -1 O LYS B 162 N ASN B 155
SHEET 6 B 8 GLY B 111 THR B 116 -1 N ILE B 115 O ILE B 163
SHEET 7 B 8 ILE B 195 SER B 199 -1 O GLN B 198 N ARG B 112
SHEET 8 B 8 PHE B 215 VAL B 217 -1 O PHE B 215 N TYR B 197
SITE 1 AC1 15 TRP A 56 MET A 101 TRP A 102 GLU A 103
SITE 2 AC1 15 ARG A 157 LYS A 162 LYS A 206 HOH A1021
SITE 3 AC1 15 HOH A1029 HOH A1044 HOH A1054 HOH A1070
SITE 4 AC1 15 HOH A1073 HOH A1096 THR B 205
SITE 1 AC2 13 TRP B 56 MET B 101 TRP B 102 GLU B 103
SITE 2 AC2 13 ARG B 157 LYS B 162 HOH B2013 HOH B2026
SITE 3 AC2 13 HOH B2039 HOH B2060 HOH B2070 HOH B2081
SITE 4 AC2 13 HOH B2085
CRYST1 70.120 75.920 77.840 90.00 90.00 90.00 P 21 21 21 8
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 0.014261 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012847 0.00000
(ATOM LINES ARE NOT SHOWN.)
END