Header list of 1ap8.pdb file
Complete list - b 16 2 Bytes
HEADER RNA CAP 25-JUL-97 1AP8
TITLE TRANSLATION INITIATION FACTOR EIF4E IN COMPLEX WITH M7GDP, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATION INITIATION FACTOR EIF4E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 CELL_LINE: BL21 (DE3);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS RNA CAP, TRANSLATION INITIATION FACTOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.MATSUO,H.LI,A.M.MCGUIRE,M.FLETCHER,A.C.GINGRAS,N.SONENBERG,G.WAGNER
REVDAT 3 16-FEB-22 1AP8 1 REMARK
REVDAT 2 24-FEB-09 1AP8 1 VERSN
REVDAT 1 28-JAN-98 1AP8 0
JRNL AUTH H.MATSUO,H.LI,A.M.MCGUIRE,C.M.FLETCHER,A.C.GINGRAS,
JRNL AUTH 2 N.SONENBERG,G.WAGNER
JRNL TITL STRUCTURE OF TRANSLATION FACTOR EIF4E BOUND TO M7GDP AND
JRNL TITL 2 INTERACTION WITH 4E-BINDING PROTEIN.
JRNL REF NAT.STRUCT.BIOL. V. 4 717 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9302999
JRNL DOI 10.1038/NSB0997-717
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AP8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171088.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY (1H; 13C; 15N); HCCHTOCSY;
REMARK 210 CT-HNCA; CT-HN(CO)CA; HNCACB;
REMARK 210 HN(CO)CACB; HNCACO-D; HNCO;
REMARK 210 HN(COCA)NH; HN(CA)HA; HN(COCA)HA;
REMARK 210 HCC (CO)NNH
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS750; UNITY500;
REMARK 210 UNITYPLUS500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO VIOLATION ABOVE 0.5 ANGSTROMS
REMARK 210 AND 5 DEGREE DIHEDRAL ANGLE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 GLU A 103 H GLU A 107 1.39
REMARK 500 O GLN A 184 H LYS A 187 1.45
REMARK 500 H LYS A 114 O PHE A 197 1.46
REMARK 500 HD21 ASN A 150 O THR A 167 1.50
REMARK 500 O ILE A 78 H ILE A 81 1.50
REMARK 500 H LEU A 39 O GLN A 69 1.56
REMARK 500 O GLU A 83 H HIS A 85 1.58
REMARK 500 O SER A 57 H ASP A 60 1.59
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 1 GLU A 5 -179.03 -57.68
REMARK 500 1 LYS A 8 130.84 64.01
REMARK 500 1 GLU A 11 49.93 -154.64
REMARK 500 1 ASP A 18 165.23 55.09
REMARK 500 1 LEU A 27 89.87 -172.48
REMARK 500 1 SER A 30 65.94 -158.78
REMARK 500 1 ALA A 31 -76.17 -49.85
REMARK 500 1 HIS A 32 -153.39 49.75
REMARK 500 1 ASP A 34 -86.62 -104.07
REMARK 500 1 VAL A 35 13.37 57.60
REMARK 500 1 HIS A 37 -60.06 167.43
REMARK 500 1 LEU A 39 -101.98 -93.99
REMARK 500 1 ASN A 40 24.84 -169.22
REMARK 500 1 LYS A 49 -65.72 -103.99
REMARK 500 1 PRO A 50 -160.47 -73.57
REMARK 500 1 ALA A 51 24.15 -165.72
REMARK 500 1 ASP A 53 -29.45 -38.31
REMARK 500 1 GLU A 56 -107.07 -97.33
REMARK 500 1 SER A 57 129.35 -170.23
REMARK 500 1 LEU A 61 -63.30 -95.06
REMARK 500 1 LEU A 62 122.10 -37.90
REMARK 500 1 VAL A 65 -135.60 -151.00
REMARK 500 1 THR A 66 112.49 -13.40
REMARK 500 1 ILE A 81 50.06 33.81
REMARK 500 1 PRO A 84 55.05 -69.01
REMARK 500 1 PRO A 88 41.82 -78.26
REMARK 500 1 LEU A 89 -157.79 36.22
REMARK 500 1 LYS A 90 24.88 45.50
REMARK 500 1 ASP A 92 93.99 -161.44
REMARK 500 1 PHE A 96 -178.57 175.75
REMARK 500 1 ARG A 97 -21.25 163.37
REMARK 500 1 ASN A 98 -71.18 -33.24
REMARK 500 1 VAL A 100 -132.74 -130.04
REMARK 500 1 ARG A 101 23.08 119.69
REMARK 500 1 GLU A 103 167.85 157.83
REMARK 500 1 TRP A 104 -18.02 -49.17
REMARK 500 1 LYS A 111 39.74 91.87
REMARK 500 1 ALA A 124 -10.82 75.64
REMARK 500 1 ASP A 125 40.83 -151.77
REMARK 500 1 GLU A 140 32.54 35.57
REMARK 500 1 THR A 141 29.60 40.85
REMARK 500 1 ASP A 143 158.50 62.97
REMARK 500 1 ASP A 145 -44.19 176.77
REMARK 500 1 LYS A 158 106.61 -45.56
REMARK 500 1 SER A 169 -0.76 151.11
REMARK 500 1 GLU A 170 -18.60 -41.15
REMARK 500 1 ASP A 171 139.67 91.21
REMARK 500 1 THR A 189 -28.29 173.71
REMARK 500 1 ASP A 190 -34.47 -39.01
REMARK 500 1 ASP A 191 33.60 -179.09
REMARK 500
REMARK 500 THIS ENTRY HAS 1128 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 63 0.29 SIDE CHAIN
REMARK 500 1 ARG A 97 0.21 SIDE CHAIN
REMARK 500 1 ARG A 101 0.12 SIDE CHAIN
REMARK 500 1 ARG A 120 0.18 SIDE CHAIN
REMARK 500 1 ARG A 132 0.29 SIDE CHAIN
REMARK 500 1 ARG A 177 0.25 SIDE CHAIN
REMARK 500 1 ARG A 205 0.17 SIDE CHAIN
REMARK 500 2 ARG A 63 0.11 SIDE CHAIN
REMARK 500 2 ARG A 97 0.31 SIDE CHAIN
REMARK 500 2 ARG A 101 0.31 SIDE CHAIN
REMARK 500 2 ARG A 120 0.32 SIDE CHAIN
REMARK 500 2 ARG A 132 0.24 SIDE CHAIN
REMARK 500 2 ARG A 157 0.20 SIDE CHAIN
REMARK 500 2 ARG A 177 0.17 SIDE CHAIN
REMARK 500 2 ARG A 205 0.32 SIDE CHAIN
REMARK 500 3 ARG A 63 0.18 SIDE CHAIN
REMARK 500 3 ARG A 97 0.29 SIDE CHAIN
REMARK 500 3 ARG A 101 0.31 SIDE CHAIN
REMARK 500 3 ARG A 120 0.25 SIDE CHAIN
REMARK 500 3 ARG A 132 0.15 SIDE CHAIN
REMARK 500 3 ARG A 177 0.23 SIDE CHAIN
REMARK 500 3 ARG A 205 0.09 SIDE CHAIN
REMARK 500 4 ARG A 63 0.17 SIDE CHAIN
REMARK 500 4 ARG A 97 0.19 SIDE CHAIN
REMARK 500 4 ARG A 101 0.31 SIDE CHAIN
REMARK 500 4 ARG A 120 0.28 SIDE CHAIN
REMARK 500 4 ARG A 132 0.24 SIDE CHAIN
REMARK 500 4 ARG A 157 0.32 SIDE CHAIN
REMARK 500 4 ARG A 177 0.32 SIDE CHAIN
REMARK 500 4 ARG A 205 0.26 SIDE CHAIN
REMARK 500 5 ARG A 63 0.16 SIDE CHAIN
REMARK 500 5 ARG A 97 0.26 SIDE CHAIN
REMARK 500 5 ARG A 101 0.29 SIDE CHAIN
REMARK 500 5 ARG A 120 0.14 SIDE CHAIN
REMARK 500 5 ARG A 132 0.32 SIDE CHAIN
REMARK 500 5 ARG A 157 0.19 SIDE CHAIN
REMARK 500 5 ARG A 205 0.32 SIDE CHAIN
REMARK 500 6 ARG A 63 0.28 SIDE CHAIN
REMARK 500 6 ARG A 97 0.21 SIDE CHAIN
REMARK 500 6 ARG A 132 0.13 SIDE CHAIN
REMARK 500 6 ARG A 157 0.14 SIDE CHAIN
REMARK 500 6 ARG A 177 0.28 SIDE CHAIN
REMARK 500 6 ARG A 205 0.17 SIDE CHAIN
REMARK 500 7 ARG A 63 0.16 SIDE CHAIN
REMARK 500 7 ARG A 97 0.31 SIDE CHAIN
REMARK 500 7 ARG A 101 0.30 SIDE CHAIN
REMARK 500 7 ARG A 120 0.30 SIDE CHAIN
REMARK 500 7 ARG A 132 0.32 SIDE CHAIN
REMARK 500 7 ARG A 157 0.18 SIDE CHAIN
REMARK 500 7 ARG A 177 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 145 PLANE DEVIATIONS.
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 M7G A 214
DBREF 1AP8 A 1 213 UNP P07260 IF4E_YEAST 1 213
SEQRES 1 A 213 MET SER VAL GLU GLU VAL SER LYS LYS PHE GLU GLU ASN
SEQRES 2 A 213 VAL SER VAL ASP ASP THR THR ALA THR PRO LYS THR VAL
SEQRES 3 A 213 LEU SER ASP SER ALA HIS PHE ASP VAL LYS HIS PRO LEU
SEQRES 4 A 213 ASN THR LYS TRP THR LEU TRP TYR THR LYS PRO ALA VAL
SEQRES 5 A 213 ASP LYS SER GLU SER TRP SER ASP LEU LEU ARG PRO VAL
SEQRES 6 A 213 THR SER PHE GLN THR VAL GLU GLU PHE TRP ALA ILE ILE
SEQRES 7 A 213 GLN ASN ILE PRO GLU PRO HIS GLU LEU PRO LEU LYS SER
SEQRES 8 A 213 ASP TYR HIS VAL PHE ARG ASN ASP VAL ARG PRO GLU TRP
SEQRES 9 A 213 GLU ASP GLU ALA ASN ALA LYS GLY GLY LYS TRP SER PHE
SEQRES 10 A 213 GLN LEU ARG GLY LYS GLY ALA ASP ILE ASP GLU LEU TRP
SEQRES 11 A 213 LEU ARG THR LEU LEU ALA VAL ILE GLY GLU THR ILE ASP
SEQRES 12 A 213 GLU ASP ASP SER GLN ILE ASN GLY VAL VAL LEU SER ILE
SEQRES 13 A 213 ARG LYS GLY GLY ASN LYS PHE ALA LEU TRP THR LYS SER
SEQRES 14 A 213 GLU ASP LYS GLU PRO LEU LEU ARG ILE GLY GLY LYS PHE
SEQRES 15 A 213 LYS GLN VAL LEU LYS LEU THR ASP ASP GLY HIS LEU GLU
SEQRES 16 A 213 PHE PHE PRO HIS SER SER ALA ASN GLY ARG HIS PRO GLN
SEQRES 17 A 213 PRO SER ILE THR LEU
HET M7G A 214 44
HETNAM M7G 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE
FORMUL 2 M7G C11 H19 N5 O11 P2
HELIX 1 H1 TRP A 58 ASP A 60 1 3
HELIX 2 H2 VAL A 71 ASN A 80 1 10
HELIX 3 H3 ASP A 106 ALA A 110 1 5
HELIX 4 H4 ILE A 126 ILE A 138 1 13
HELIX 5 H5 GLU A 173 VAL A 185 1 13
HELIX 6 H6 HIS A 199 ALA A 202 1 4
SHEET 1 S1 8 LEU A 62 GLN A 69 0
SHEET 2 S1 8 LEU A 39 THR A 48 -1
SHEET 3 S1 8 SER A 91 PHE A 96 -1
SHEET 4 S1 8 GLY A 151 ARG A 157 -1
SHEET 5 S1 8 ASN A 161 THR A 167 -1
SHEET 6 S1 8 GLY A 113 LEU A 119 -1
SHEET 7 S1 8 LEU A 194 PHE A 197 -1
SHEET 8 S1 8 ILE A 211 LEU A 213 -1
SITE 1 AC1 7 TRP A 58 ASP A 92 GLU A 103 TRP A 104
SITE 2 AC1 7 GLU A 105 ILE A 156 ARG A 157
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 16 2 Bytes