Header list of 2g2k.pdb file
Complete list - v 10 2 Bytes
HEADER TRANSLATION 16-FEB-06 2G2K
TITLE NMR STRUCTURE OF AN N-TERMINAL FRAGMENT OF THE EUKARYOTIC INITIATION
TITLE 2 FACTOR 5 (EIF5)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL FRAGMENT, RESIDUES 1-170;
COMPND 5 SYNONYM: EIF-5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EIF5, EIF125 FOLD, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR M.R.CONTE,G.KELLY,J.BABON,D.SANFELICE,S.J.SMERDON,C.G.PROUD
REVDAT 3 10-NOV-21 2G2K 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2G2K 1 VERSN
REVDAT 1 13-JUN-06 2G2K 0
JRNL AUTH M.R.CONTE,G.KELLY,J.BABON,D.SANFELICE,J.YOUELL,S.J.SMERDON,
JRNL AUTH 2 C.G.PROUD
JRNL TITL STRUCTURE OF THE EUKARYOTIC INITIATION FACTOR (EIF) 5
JRNL TITL 2 REVEALS A FOLD COMMON TO SEVERAL TRANSLATION FACTORS
JRNL REF BIOCHEMISTRY V. 45 4550 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16584190
JRNL DOI 10.1021/BI052387U
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2G2K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036608.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : NO ADDED SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM U-15N, 13C; 20MM SODIUM
REMARK 210 ACETATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE LATEST
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 1-18
REMARK 465 RES C SSSEQI
REMARK 465 GLU A 157
REMARK 465 LYS A 158
REMARK 465 GLU A 159
REMARK 465 LYS A 160
REMARK 465 LYS A 161
REMARK 465 ASN A 162
REMARK 465 ARG A 163
REMARK 465 LYS A 164
REMARK 465 GLY A 165
REMARK 465 LYS A 166
REMARK 465 ASP A 167
REMARK 465 LYS A 168
REMARK 465 GLU A 169
REMARK 465 ASN A 170
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 ILE A 118 H LEU A 131 1.49
REMARK 500 O THR A 34 H VAL A 76 1.58
REMARK 500 O ASN A 120 H GLY A 129 1.58
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 MET A 10 -30.71 176.80
REMARK 500 1 PHE A 13 78.99 57.80
REMARK 500 1 ARG A 15 -31.24 -178.59
REMARK 500 1 ILE A 32 105.14 168.46
REMARK 500 1 ASN A 47 -142.28 175.43
REMARK 500 1 PRO A 50 48.83 -74.58
REMARK 500 1 GLN A 64 -119.16 -105.40
REMARK 500 1 GLU A 101 -29.37 175.81
REMARK 500 1 ASN A 104 -63.06 -164.96
REMARK 500 1 LYS A 123 43.45 -84.34
REMARK 500 1 ALA A 124 -33.71 -130.82
REMARK 500 1 TYR A 127 -64.65 -10.97
REMARK 500 1 ARG A 128 92.81 24.36
REMARK 500 1 ASP A 132 -65.40 -176.81
REMARK 500 1 THR A 133 -54.46 71.59
REMARK 500 1 HIS A 134 -178.11 -177.93
REMARK 500 1 HIS A 135 86.70 -52.63
REMARK 500 1 LEU A 137 -19.17 -42.72
REMARK 500 1 SER A 149 -153.31 -151.03
REMARK 500 1 THR A 153 94.70 -65.52
REMARK 500 1 LYS A 155 -28.86 178.01
REMARK 500 2 VAL A 9 122.18 58.80
REMARK 500 2 MET A 10 131.74 66.61
REMARK 500 2 PHE A 13 72.30 46.47
REMARK 500 2 ARG A 15 22.92 -158.29
REMARK 500 2 PRO A 19 -155.83 -74.80
REMARK 500 2 ARG A 20 -67.72 -106.68
REMARK 500 2 ASN A 47 -58.34 66.73
REMARK 500 2 GLN A 64 -120.13 -112.27
REMARK 500 2 LEU A 98 90.57 33.51
REMARK 500 2 GLU A 101 -36.73 -159.22
REMARK 500 2 CYS A 102 62.62 175.01
REMARK 500 2 ASN A 104 -56.12 -29.09
REMARK 500 2 ARG A 128 92.44 29.48
REMARK 500 2 ASP A 132 -78.21 -107.25
REMARK 500 2 THR A 133 -139.45 69.87
REMARK 500 2 HIS A 135 94.82 -42.72
REMARK 500 2 ASN A 144 167.14 63.18
REMARK 500 2 GLU A 147 23.69 -150.21
REMARK 500 2 SER A 149 -59.75 66.97
REMARK 500 2 LYS A 155 -170.46 52.77
REMARK 500 3 VAL A 9 -94.91 -42.61
REMARK 500 3 MET A 10 -179.27 65.48
REMARK 500 3 PHE A 13 -68.16 -172.17
REMARK 500 3 TYR A 14 80.69 178.02
REMARK 500 3 PRO A 19 -155.83 -74.96
REMARK 500 3 ARG A 20 20.43 -149.13
REMARK 500 3 ILE A 32 88.14 -153.67
REMARK 500 3 ASN A 47 -64.55 65.43
REMARK 500 3 GLN A 64 -119.07 -107.95
REMARK 500
REMARK 500 THIS ENTRY HAS 378 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 7 0.31 SIDE CHAIN
REMARK 500 1 ARG A 15 0.31 SIDE CHAIN
REMARK 500 1 ARG A 20 0.29 SIDE CHAIN
REMARK 500 1 ARG A 48 0.26 SIDE CHAIN
REMARK 500 1 ARG A 73 0.31 SIDE CHAIN
REMARK 500 1 ARG A 128 0.12 SIDE CHAIN
REMARK 500 2 ARG A 7 0.28 SIDE CHAIN
REMARK 500 2 ARG A 15 0.20 SIDE CHAIN
REMARK 500 2 ARG A 20 0.08 SIDE CHAIN
REMARK 500 2 ARG A 48 0.18 SIDE CHAIN
REMARK 500 2 ARG A 73 0.08 SIDE CHAIN
REMARK 500 2 ARG A 128 0.22 SIDE CHAIN
REMARK 500 3 ARG A 7 0.22 SIDE CHAIN
REMARK 500 3 ARG A 15 0.08 SIDE CHAIN
REMARK 500 3 ARG A 20 0.21 SIDE CHAIN
REMARK 500 3 ARG A 48 0.23 SIDE CHAIN
REMARK 500 3 ARG A 73 0.28 SIDE CHAIN
REMARK 500 3 ARG A 128 0.27 SIDE CHAIN
REMARK 500 4 ARG A 7 0.15 SIDE CHAIN
REMARK 500 4 ARG A 15 0.28 SIDE CHAIN
REMARK 500 4 ARG A 20 0.21 SIDE CHAIN
REMARK 500 4 ARG A 48 0.32 SIDE CHAIN
REMARK 500 4 ARG A 73 0.29 SIDE CHAIN
REMARK 500 4 ARG A 128 0.15 SIDE CHAIN
REMARK 500 5 ARG A 7 0.08 SIDE CHAIN
REMARK 500 5 ARG A 15 0.27 SIDE CHAIN
REMARK 500 5 ARG A 20 0.29 SIDE CHAIN
REMARK 500 5 ARG A 48 0.32 SIDE CHAIN
REMARK 500 5 ARG A 73 0.26 SIDE CHAIN
REMARK 500 5 ARG A 128 0.29 SIDE CHAIN
REMARK 500 6 ARG A 7 0.17 SIDE CHAIN
REMARK 500 6 ARG A 15 0.31 SIDE CHAIN
REMARK 500 6 ARG A 20 0.13 SIDE CHAIN
REMARK 500 6 ARG A 48 0.29 SIDE CHAIN
REMARK 500 6 ARG A 73 0.32 SIDE CHAIN
REMARK 500 6 ARG A 128 0.30 SIDE CHAIN
REMARK 500 7 ARG A 7 0.19 SIDE CHAIN
REMARK 500 7 ARG A 15 0.28 SIDE CHAIN
REMARK 500 7 ARG A 20 0.24 SIDE CHAIN
REMARK 500 7 ARG A 48 0.17 SIDE CHAIN
REMARK 500 7 ARG A 128 0.31 SIDE CHAIN
REMARK 500 8 ARG A 7 0.21 SIDE CHAIN
REMARK 500 8 ARG A 15 0.29 SIDE CHAIN
REMARK 500 8 ARG A 20 0.21 SIDE CHAIN
REMARK 500 8 ARG A 48 0.32 SIDE CHAIN
REMARK 500 8 ARG A 73 0.21 SIDE CHAIN
REMARK 500 8 ARG A 128 0.32 SIDE CHAIN
REMARK 500 9 ARG A 7 0.22 SIDE CHAIN
REMARK 500 9 ARG A 15 0.11 SIDE CHAIN
REMARK 500 9 ARG A 20 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 106 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6944 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENT
DBREF 2G2K A 2 170 UNP P55010 IF5_HUMAN 2 170
SEQADV 2G2K LEU A 1 UNP P55010 CLONING ARTIFACT
SEQADV 2G2K MET A 10 UNP P55010 SER 10 ENGINEERED MUTATION
SEQRES 1 A 170 LEU SER VAL ASN VAL ASN ARG SER VAL MET ASP GLN PHE
SEQRES 2 A 170 TYR ARG TYR LYS MET PRO ARG LEU ILE ALA LYS VAL GLU
SEQRES 3 A 170 GLY LYS GLY ASN GLY ILE LYS THR VAL ILE VAL ASN MET
SEQRES 4 A 170 VAL ASP VAL ALA LYS ALA LEU ASN ARG PRO PRO THR TYR
SEQRES 5 A 170 PRO THR LYS TYR PHE GLY CYS GLU LEU GLY ALA GLN THR
SEQRES 6 A 170 GLN PHE ASP VAL LYS ASN ASP ARG TYR ILE VAL ASN GLY
SEQRES 7 A 170 SER HIS GLU ALA ASN LYS LEU GLN ASP MET LEU ASP GLY
SEQRES 8 A 170 PHE ILE LYS LYS PHE VAL LEU CYS PRO GLU CYS GLU ASN
SEQRES 9 A 170 PRO GLU THR ASP LEU HIS VAL ASN PRO LYS LYS GLN THR
SEQRES 10 A 170 ILE GLY ASN SER CYS LYS ALA CYS GLY TYR ARG GLY MET
SEQRES 11 A 170 LEU ASP THR HIS HIS LYS LEU CYS THR PHE ILE LEU LYS
SEQRES 12 A 170 ASN PRO PRO GLU ASN SER ASP SER GLY THR GLY LYS LYS
SEQRES 13 A 170 GLU LYS GLU LYS LYS ASN ARG LYS GLY LYS ASP LYS GLU
SEQRES 14 A 170 ASN
HELIX 1 1 ASN A 38 ASN A 47 1 10
HELIX 2 2 PRO A 53 LEU A 61 1 9
HELIX 3 3 GLU A 81 LEU A 98 1 18
HELIX 4 4 LYS A 136 LYS A 143 1 8
SHEET 1 A 4 LYS A 24 GLU A 26 0
SHEET 2 A 4 LYS A 33 VAL A 35 -1 O VAL A 35 N LYS A 24
SHEET 3 A 4 TYR A 74 ASN A 77 -1 O VAL A 76 N THR A 34
SHEET 4 A 4 GLN A 66 PHE A 67 -1 N GLN A 66 O ILE A 75
SHEET 1 B 2 THR A 107 ASN A 112 0
SHEET 2 B 2 THR A 117 CYS A 122 -1 O SER A 121 N ASP A 108
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 - v 10 2 Bytes