HEADER RNA BINDING PROTEIN 04-APR-18 5ZML
TITLE STAPLED-PEPTIDES TAILORED AGAINST INITIATION OF TRANSLATION
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: ACE-LYS-LYS-ARG-TYR-SER-ARG-MK8-GLN-LEU-LEU-MK8-PHE-ARG-
COMPND 8 ARG;
COMPND 9 CHAIN: B;
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEMB54;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS CAP DEPENDENT TRANSLATION, RNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.LAMA,A.LIBERATOR,Y.FROSI,J.NAKHLE,N.TSOMIA,T.BASHIR,D.P.LANE,
AUTHOR 2 C.J.BROWN,C.S.VERMA,S.AUVIN,J.YANO
REVDAT 2 03-APR-19 5ZML 1 JRNL
REVDAT 1 20-FEB-19 5ZML 0
JRNL AUTH D.LAMA,A.M.LIBERATORE,Y.FROSI,J.NAKHLE,N.TSOMAIA,T.BASHIR,
JRNL AUTH 2 D.P.LANE,C.J.BROWN,C.S.VERMA,S.AUVIN
JRNL TITL STRUCTURAL INSIGHTS REVEAL A RECOGNITION FEATURE FOR
JRNL TITL 2 TAILORING HYDROCARBON STAPLED-PEPTIDES AGAINST THE
JRNL TITL 3 EUKARYOTIC TRANSLATION INITIATION FACTOR 4E PROTEIN.
JRNL REF CHEM SCI V. 10 2489 2019
JRNL REFN ISSN 2041-6520
JRNL PMID 30881679
JRNL DOI 10.1039/C8SC03759K
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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) : 68.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 20343
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.300
REMARK 3 FREE R VALUE TEST SET COUNT : 2088
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1444
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 141
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1683
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.64000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : -2.10000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.133
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.822
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1744 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1589 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2357 ; 1.423 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3667 ; 0.938 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 201 ; 6.535 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;34.497 ;23.218
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 295 ;11.882 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;13.355 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 247 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1921 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 389 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 822 ; 1.585 ; 2.525
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 821 ; 1.574 ; 2.523
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1024 ; 2.548 ; 3.771
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1025 ; 2.547 ; 3.773
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 922 ; 1.798 ; 2.684
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 922 ; 1.796 ; 2.684
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1333 ; 2.906 ; 3.929
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2063 ; 4.666 ;29.406
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2064 ; 4.665 ;29.409
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5ZML COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1300007233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22468
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 68.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0500
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) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.170
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: 4BEA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40%(V/V) ETHYLENE GLYCOL, 20 %(W/V)
REMARK 280 PEG 8000, 0.3M SODIUM NITRATE, 0.3M AMMONIUM SULFATE, 100MM
REMARK 280 SODIUM HEPES/MOPS PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.41500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.41500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.14500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.80500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.14500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.80500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.41500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.14500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.80500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.41500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.14500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.80500
REMARK 290 SMTRY3 8 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: 2190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 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 A1152 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1169 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 ARG B 16
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 GLU A 27 CG CD OE1 OE2
REMARK 470 GLN A 57 CG CD OE1 NE2
REMARK 470 LYS A 159 CG CD CE NZ
REMARK 470 LYS A 206 CG CD CE NZ
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 ARG B 15 CG CD NE CZ NH1 NH2
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 CE MK8 B 8 CE MK8 B 12 1.34
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 -12.28 -144.75
REMARK 500 ILE A 63 -70.74 -85.86
REMARK 500 ASP A 67 21.55 -143.24
REMARK 500 ASP A 143 -129.27 62.86
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 NO3 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MK8 B 8 and MK8 B 12
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE CHAIN B IS A HYBRID SEQUENCE WHICH IS
REMARK 999 CORRESPONDS APPROXIMATELY TO SEQUENCE 609-624 OF EIF4G1 (Q04637).
REMARK 999 THE RESIDUESS B8 AND B12 ARE (S)-2-(4-PENTENYL) ALANINE AND FORM A
REMARK 999 ALIPHATIC HYDROCARBON STAPLE VIA A RING CLOSING METATHESIS REACTION.
DBREF 5ZML A 27 217 UNP P06730 IF4E_HUMAN 27 217
DBREF 5ZML B 1 16 PDB 5ZML 5ZML 1 16
SEQRES 1 A 191 GLU VAL ALA ASN PRO GLU HIS TYR ILE LYS HIS PRO LEU
SEQRES 2 A 191 GLN ASN ARG TRP ALA LEU TRP PHE PHE LYS ASN ASP LYS
SEQRES 3 A 191 SER LYS THR TRP GLN ALA ASN LEU ARG LEU ILE SER LYS
SEQRES 4 A 191 PHE ASP THR VAL GLU ASP PHE TRP ALA LEU TYR ASN HIS
SEQRES 5 A 191 ILE GLN LEU SER SER ASN LEU MET PRO GLY CYS ASP TYR
SEQRES 6 A 191 SER LEU PHE LYS ASP GLY ILE GLU PRO MET TRP GLU ASP
SEQRES 7 A 191 GLU LYS ASN LYS ARG GLY GLY ARG TRP LEU ILE THR LEU
SEQRES 8 A 191 ASN LYS GLN GLN ARG ARG SER ASP LEU ASP ARG PHE TRP
SEQRES 9 A 191 LEU GLU THR LEU LEU CYS LEU ILE GLY GLU SER PHE ASP
SEQRES 10 A 191 ASP TYR SER ASP ASP VAL CYS GLY ALA VAL VAL ASN VAL
SEQRES 11 A 191 ARG ALA LYS GLY ASP LYS ILE ALA ILE TRP THR THR GLU
SEQRES 12 A 191 CYS GLU ASN ARG GLU ALA VAL THR HIS ILE GLY ARG VAL
SEQRES 13 A 191 TYR LYS GLU ARG LEU GLY LEU PRO PRO LYS ILE VAL ILE
SEQRES 14 A 191 GLY TYR GLN SER HIS ALA ASP THR ALA THR LYS SER GLY
SEQRES 15 A 191 SER THR THR LYS ASN ARG PHE VAL VAL
SEQRES 1 B 16 ACE LYS LYS ARG TYR SER ARG MK8 GLN LEU LEU MK8 PHE
SEQRES 2 B 16 ARG ARG ARG
HET ACE B 1 3
HET MK8 B 8 9
HET MK8 B 12 9
HET NO3 A 901 4
HET EDO A 902 4
HET EDO A 903 4
HET EDO A 904 4
HETNAM ACE ACETYL GROUP
HETNAM MK8 2-METHYL-L-NORLEUCINE
HETNAM NO3 NITRATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ACE C2 H4 O
FORMUL 2 MK8 2(C7 H15 N O2)
FORMUL 3 NO3 N O3 1-
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 7 HOH *190(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 ILE A 79 1 11
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 GLU A 140 1 16
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 THR A 205 1 6
HELIX 10 AB1 SER B 6 PHE B 13 1 8
SHEET 1 AA1 8 LEU A 60 THR A 68 0
SHEET 2 AA1 8 PRO A 38 PHE A 48 -1 N LEU A 45 O ILE A 63
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 GLY A 196 SER A 199 -1 O GLY A 196 N LEU A 114
SHEET 8 AA1 8 PHE A 215 VAL A 216 -1 O PHE A 215 N TYR A 197
LINK C ACE B 1 N LYS B 2 1555 1555 1.34
LINK C ARG B 7 N MK8 B 8 1555 1555 1.35
LINK C MK8 B 8 N GLN B 9 1555 1555 1.30
LINK C LEU B 11 N MK8 B 12 1555 1555 1.35
LINK C MK8 B 12 N PHE B 13 1555 1555 1.29
SITE 1 AC1 7 LYS A 95 LYS A 106 ASP A 147 VAL A 149
SITE 2 AC1 7 CYS A 150 THR A 168 HOH A1038
SITE 1 AC2 6 PHE A 48 ASP A 90 SER A 92 PRO A 100
SITE 2 AC2 6 HOH A1009 HOH A1122
SITE 1 AC3 3 THR A 116 GLN A 121 HOH A1007
SITE 1 AC4 7 ARG A 122 ARG A 123 SER A 124 ASP A 125
SITE 2 AC4 7 LEU A 126 ASP A 127 ARG A 128
SITE 1 AC5 13 HIS A 178 ARG A 181 VAL A 182 GLU A 185
SITE 2 AC5 13 SER B 6 ARG B 7 GLN B 9 LEU B 10
SITE 3 AC5 13 LEU B 11 PHE B 13 ARG B 14 ARG B 15
SITE 4 AC5 13 HOH B 109
CRYST1 38.290 91.610 136.830 90.00 90.00 90.00 C 2 2 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 0.026116 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010916 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007308 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
