HEADER TRANSLATION 21-AUG-03 1Q8K
TITLE SOLUTION STRUCTURE OF ALPHA SUBUNIT OF HUMAN EIF2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EUKARYOTIC TRANSLATION INITIATION FACTOR 2 ALPHA SUBUNIT,
COMPND 5 EIF-2-ALPHA, EIF- 2ALPHA, EIF-2A;
COMPND 6 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: EIF2S1 OR EIF2A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSLATION, TRANSLATION INITIATION, EUKARYOTIC TRANSLATION
KEYWDS 2 INITIATION FACTOR 2
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR T.ITO,A.MARINTCHEV,G.WAGNER
REVDAT 4 27-OCT-21 1Q8K 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1Q8K 1 VERSN
REVDAT 2 05-OCT-04 1Q8K 1 JRNL
REVDAT 1 07-SEP-04 1Q8K 0
JRNL AUTH T.ITO,A.MARINTCHEV,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF HUMAN INITIATION FACTOR EIF2ALPHA
JRNL TITL 2 REVEALS HOMOLOGY TO THE ELONGATION FACTOR EEF1B.
JRNL REF STRUCTURE V. 12 1693 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15341733
JRNL DOI 10.1016/J.STR.2004.07.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NIH-XPLOR1 2.1
REMARK 3 AUTHORS : JONES,ZOU,COWAN,KJELDGAARD
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Q8K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020051.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 1.1
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : VARIAN INOVA; BRUKER DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NIH-XPLOR1 2.1
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 51
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 LEU A 303
REMARK 465 GLU A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
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
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 SER A 4 -67.67 -102.03
REMARK 500 1 CYS A 5 156.80 -46.58
REMARK 500 1 ARG A 6 -46.51 -168.49
REMARK 500 1 TYR A 8 28.32 179.64
REMARK 500 1 GLN A 9 26.30 46.14
REMARK 500 1 HIS A 10 107.05 67.75
REMARK 500 1 LYS A 11 78.06 -175.93
REMARK 500 1 PRO A 13 -162.95 -72.30
REMARK 500 1 GLU A 16 32.26 -179.69
REMARK 500 1 VAL A 23 151.72 -45.60
REMARK 500 1 ARG A 24 -64.89 -131.29
REMARK 500 1 LEU A 36 110.39 55.95
REMARK 500 1 GLU A 37 40.26 -74.94
REMARK 500 1 TYR A 38 -57.87 -148.49
REMARK 500 1 ASN A 40 -92.31 -155.02
REMARK 500 1 ILE A 41 -151.88 173.12
REMARK 500 1 GLU A 42 -159.04 -81.92
REMARK 500 1 ARG A 52 -179.03 -57.73
REMARK 500 1 ARG A 53 -159.99 55.19
REMARK 500 1 ARG A 56 -62.55 -120.22
REMARK 500 1 SER A 57 26.90 -164.72
REMARK 500 1 ILE A 58 37.49 34.75
REMARK 500 1 ILE A 64 81.35 30.28
REMARK 500 1 ARG A 74 131.56 -176.67
REMARK 500 1 LYS A 79 -36.64 -166.33
REMARK 500 1 ARG A 88 74.76 64.58
REMARK 500 1 GLU A 119 67.15 65.44
REMARK 500 1 ASP A 123 -80.55 59.55
REMARK 500 1 THR A 133 -72.89 -149.96
REMARK 500 1 ASP A 158 72.42 -118.10
REMARK 500 1 LEU A 183 -70.00 -118.31
REMARK 500 1 PRO A 185 -167.34 -74.27
REMARK 500 1 ALA A 187 147.82 58.22
REMARK 500 1 TYR A 199 101.78 -49.78
REMARK 500 1 SER A 218 -163.42 -60.88
REMARK 500 1 PRO A 231 -74.96 -72.63
REMARK 500 1 PRO A 232 49.83 -78.76
REMARK 500 1 THR A 238 -176.82 -176.98
REMARK 500 1 LEU A 241 175.11 -53.45
REMARK 500 1 GLU A 242 130.95 70.17
REMARK 500 1 ARG A 265 64.47 61.04
REMARK 500 1 MET A 272 16.21 -145.70
REMARK 500 1 GLU A 273 176.53 51.15
REMARK 500 1 GLN A 288 -74.68 -86.12
REMARK 500 1 MET A 289 -158.83 56.03
REMARK 500 1 GLU A 290 91.05 53.52
REMARK 500 1 GLU A 298 57.87 -112.63
REMARK 500 2 CYS A 5 118.51 62.32
REMARK 500 2 GLN A 9 5.65 -67.29
REMARK 500 2 HIS A 10 96.00 70.11
REMARK 500
REMARK 500 THIS ENTRY HAS 587 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 6 0.26 SIDE CHAIN
REMARK 500 1 ARG A 24 0.27 SIDE CHAIN
REMARK 500 1 ARG A 52 0.15 SIDE CHAIN
REMARK 500 1 ARG A 53 0.19 SIDE CHAIN
REMARK 500 1 ARG A 54 0.25 SIDE CHAIN
REMARK 500 1 ARG A 56 0.17 SIDE CHAIN
REMARK 500 1 ARG A 63 0.32 SIDE CHAIN
REMARK 500 1 ARG A 66 0.28 SIDE CHAIN
REMARK 500 1 ARG A 74 0.16 SIDE CHAIN
REMARK 500 1 ARG A 87 0.29 SIDE CHAIN
REMARK 500 1 ARG A 88 0.32 SIDE CHAIN
REMARK 500 1 ARG A 112 0.31 SIDE CHAIN
REMARK 500 1 ARG A 132 0.29 SIDE CHAIN
REMARK 500 1 ARG A 143 0.18 SIDE CHAIN
REMARK 500 1 ARG A 172 0.14 SIDE CHAIN
REMARK 500 1 ARG A 181 0.23 SIDE CHAIN
REMARK 500 1 ARG A 182 0.23 SIDE CHAIN
REMARK 500 1 ARG A 191 0.26 SIDE CHAIN
REMARK 500 1 ARG A 212 0.30 SIDE CHAIN
REMARK 500 1 ARG A 233 0.11 SIDE CHAIN
REMARK 500 1 ARG A 243 0.28 SIDE CHAIN
REMARK 500 1 ARG A 265 0.23 SIDE CHAIN
REMARK 500 1 ARG A 287 0.14 SIDE CHAIN
REMARK 500 1 ARG A 291 0.27 SIDE CHAIN
REMARK 500 1 ARG A 294 0.21 SIDE CHAIN
REMARK 500 2 ARG A 6 0.22 SIDE CHAIN
REMARK 500 2 ARG A 24 0.23 SIDE CHAIN
REMARK 500 2 ARG A 52 0.10 SIDE CHAIN
REMARK 500 2 ARG A 53 0.17 SIDE CHAIN
REMARK 500 2 ARG A 54 0.18 SIDE CHAIN
REMARK 500 2 ARG A 56 0.29 SIDE CHAIN
REMARK 500 2 ARG A 63 0.23 SIDE CHAIN
REMARK 500 2 ARG A 66 0.22 SIDE CHAIN
REMARK 500 2 ARG A 74 0.17 SIDE CHAIN
REMARK 500 2 ARG A 87 0.30 SIDE CHAIN
REMARK 500 2 ARG A 88 0.13 SIDE CHAIN
REMARK 500 2 ARG A 112 0.32 SIDE CHAIN
REMARK 500 2 ARG A 132 0.16 SIDE CHAIN
REMARK 500 2 ARG A 172 0.26 SIDE CHAIN
REMARK 500 2 ARG A 181 0.29 SIDE CHAIN
REMARK 500 2 ARG A 182 0.28 SIDE CHAIN
REMARK 500 2 ARG A 191 0.31 SIDE CHAIN
REMARK 500 2 ARG A 212 0.20 SIDE CHAIN
REMARK 500 2 ARG A 233 0.28 SIDE CHAIN
REMARK 500 2 ARG A 243 0.18 SIDE CHAIN
REMARK 500 2 ARG A 287 0.31 SIDE CHAIN
REMARK 500 2 ARG A 291 0.21 SIDE CHAIN
REMARK 500 2 ARG A 294 0.26 SIDE CHAIN
REMARK 500 3 ARG A 6 0.32 SIDE CHAIN
REMARK 500 3 ARG A 24 0.11 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 360 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Q8K A 4 302 UNP P05198 IF2A_HUMAN 4 302
SEQADV 1Q8K MET A 3 UNP P05198 CLONING ARTIFACT
SEQADV 1Q8K GLN A 27 UNP P05198 ALA 27 ENGINEERED MUTATION
SEQADV 1Q8K HIS A 46 UNP P05198 LEU 46 ENGINEERED MUTATION
SEQADV 1Q8K LYS A 71 UNP P05198 VAL 71 ENGINEERED MUTATION
SEQADV 1Q8K LEU A 303 UNP P05198 CLONING ARTIFACT
SEQADV 1Q8K GLU A 304 UNP P05198 CLONING ARTIFACT
SEQADV 1Q8K HIS A 305 UNP P05198 EXPRESSION TAG
SEQADV 1Q8K HIS A 306 UNP P05198 EXPRESSION TAG
SEQADV 1Q8K HIS A 307 UNP P05198 EXPRESSION TAG
SEQADV 1Q8K HIS A 308 UNP P05198 EXPRESSION TAG
SEQADV 1Q8K HIS A 309 UNP P05198 EXPRESSION TAG
SEQADV 1Q8K HIS A 310 UNP P05198 EXPRESSION TAG
SEQRES 1 A 308 MET SER CYS ARG PHE TYR GLN HIS LYS PHE PRO GLU VAL
SEQRES 2 A 308 GLU ASP VAL VAL MET VAL ASN VAL ARG SER ILE GLN GLU
SEQRES 3 A 308 MET GLY ALA TYR VAL SER LEU LEU GLU TYR ASN ASN ILE
SEQRES 4 A 308 GLU GLY MET ILE HIS LEU SER GLU LEU SER ARG ARG ARG
SEQRES 5 A 308 ILE ARG SER ILE ASN LYS LEU ILE ARG ILE GLY ARG ASN
SEQRES 6 A 308 GLU CYS VAL LYS VAL ILE ARG VAL ASP LYS GLU LYS GLY
SEQRES 7 A 308 TYR ILE ASP LEU SER LYS ARG ARG VAL SER PRO GLU GLU
SEQRES 8 A 308 ALA ILE LYS CYS GLU ASP LYS PHE THR LYS SER LYS THR
SEQRES 9 A 308 VAL TYR SER ILE LEU ARG HIS VAL ALA GLU VAL LEU GLU
SEQRES 10 A 308 TYR THR LYS ASP GLU GLN LEU GLU SER LEU PHE GLN ARG
SEQRES 11 A 308 THR ALA TRP VAL PHE ASP ASP LYS TYR LYS ARG PRO GLY
SEQRES 12 A 308 TYR GLY ALA TYR ASP ALA PHE LYS HIS ALA VAL SER ASP
SEQRES 13 A 308 PRO SER ILE LEU ASP SER LEU ASP LEU ASN GLU ASP GLU
SEQRES 14 A 308 ARG GLU VAL LEU ILE ASN ASN ILE ASN ARG ARG LEU THR
SEQRES 15 A 308 PRO GLN ALA VAL LYS ILE ARG ALA ASP ILE GLU VAL ALA
SEQRES 16 A 308 CYS TYR GLY TYR GLU GLY ILE ASP ALA VAL LYS GLU ALA
SEQRES 17 A 308 LEU ARG ALA GLY LEU ASN CYS SER THR GLU ASN MET PRO
SEQRES 18 A 308 ILE LYS ILE ASN LEU ILE ALA PRO PRO ARG TYR VAL MET
SEQRES 19 A 308 THR THR THR THR LEU GLU ARG THR GLU GLY LEU SER VAL
SEQRES 20 A 308 LEU SER GLN ALA MET ALA VAL ILE LYS GLU LYS ILE GLU
SEQRES 21 A 308 GLU LYS ARG GLY VAL PHE ASN VAL GLN MET GLU PRO LYS
SEQRES 22 A 308 VAL VAL THR ASP THR ASP GLU THR GLU LEU ALA ARG GLN
SEQRES 23 A 308 MET GLU ARG LEU GLU ARG GLU ASN ALA GLU VAL ASP GLY
SEQRES 24 A 308 ASP LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 LEU A 47 LEU A 50 5 4
HELIX 2 3 PRO A 91 LEU A 118 1 28
HELIX 3 4 ASP A 123 GLN A 131 1 9
HELIX 4 5 ALA A 134 TYR A 141 1 8
HELIX 5 6 TYR A 146 HIS A 154 1 9
HELIX 6 8 GLU A 169 LEU A 183 1 15
HELIX 7 9 ILE A 204 ASN A 216 1 13
HELIX 8 10 ARG A 243 GLU A 262 1 20
HELIX 9 11 ASP A 281 GLN A 288 1 8
SHEET 1 A 6 VAL A 18 ILE A 26 0
SHEET 2 A 6 ALA A 31 LEU A 35 -1 O TYR A 32 N SER A 25
SHEET 3 A 6 ILE A 41 ILE A 45 -1 O ILE A 45 N ALA A 31
SHEET 4 A 6 TYR A 81 SER A 85 1 O ILE A 82 N MET A 44
SHEET 5 A 6 ASN A 67 ASP A 76 -1 N LYS A 71 O SER A 85
SHEET 6 A 6 VAL A 18 ILE A 26 -1 N VAL A 21 O GLU A 68
SHEET 1 B 5 ILE A 224 ALA A 230 0
SHEET 2 B 5 ARG A 233 THR A 240 -1 O THR A 237 N LYS A 225
SHEET 3 B 5 VAL A 188 ALA A 197 -1 N ILE A 190 O THR A 238
SHEET 4 B 5 VAL A 267 VAL A 270 -1 O VAL A 267 N ALA A 197
SHEET 5 B 5 LYS A 275 VAL A 277 1 O LYS A 275 N ARG A 191
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
(ATOM LINES ARE NOT SHOWN.)
END