Header list of 1d7q.pdb file
Complete list - b 16 2 Bytes
HEADER GENE REGULATION 19-OCT-99 1D7Q
TITLE HUMAN TRANSLATION INITIATION FACTOR EIF1A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (N-TERMINAL HISTIDINE TAG);
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TRANSLATION INITIATION FACTOR 1A;
COMPND 7 CHAIN: A;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: HISTIDINE TAG IS ENGINEERED INTO THE VECTOR THAT IS
SOURCE 4 EXPRESSED WITH THE PROTEIN;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PQE31
KEYWDS OB-FOLD, BETA-BARREL, RNA-BINDING PROTEIN, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.L.BATTISTE,T.V.PESTOVA,C.U.T.HELLEN,G.WAGNER
REVDAT 5 16-FEB-22 1D7Q 1 REMARK
REVDAT 4 24-FEB-09 1D7Q 1 VERSN
REVDAT 3 01-APR-03 1D7Q 1 JRNL
REVDAT 2 05-MAY-00 1D7Q 1 REMARK ATOM
REVDAT 1 17-MAR-00 1D7Q 0
JRNL AUTH J.L.BATTISTE,T.V.PESTOVA,C.U.HELLEN,G.WAGNER
JRNL TITL THE EIF1A SOLUTION STRUCTURE REVEALS A LARGE RNA-BINDING
JRNL TITL 2 SURFACE IMPORTANT FOR SCANNING FUNCTION.
JRNL REF MOL.CELL V. 5 109 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 10678173
JRNL DOI 10.1016/S1097-2765(00)80407-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.V.PESTOVA,S.I.BORUKHOV,C.U.T.HELLEN
REMARK 1 TITL EUKARYOTIC RIBOSOMES REQUIRE INITIATION FACTORS 1 AND 1A TO
REMARK 1 TITL 2 LOCATE INITIATION CODONS
REMARK 1 REF NATURE V. 394 854 1998
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/29703
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 3.851
REMARK 3 AUTHORS : VARIAN (VNMR), A.T. BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 CALCULATIONS WERE RESTRAINED WITH THE FOLLOWING NMR DATA. NOE
REMARK 3 DISTANCE
REMARK 3 RESTRAINTS INTRA-RESIDUE 607 INTER-RESIDUE SEQUENTIAL (IJ=1) 266
REMARK 3 INTER-RESIDUE
REMARK 3 MEDIUM (IJ <= 4) 105 INTER-RESIDUE LONG (IJ > 4) 342 HYDROGENS
REMARK 3 BONDS: PROTEIN
REMARK 3 BACKBONE 40 DIHEDRAL ANGLES: PHI 65 PSI 65 NO NOE VIOLATIONS >0.3
REMARK 3 A IN FINAL
REMARK 3 STRUCTURES. RMS DEVIATIONS OF THE ENSEMBLE SUPERPOSITION TO THE
REMARK 3 AVERAGE
REMARK 3 STRUCTURE ARE: BACKBONE 39-131 0.57 A SECONDARY STRUCTURE 0.23 A
REMARK 3 HEAVY ATOMS
REMARK 3 39-131 1.17 A SECONDARY STRUCTURE 0.72 A BOND LENGTHS 0.0016 A
REMARK 3 BOND ANGLES
REMARK 3 0.345 DEGREE IMPROPER ANGLES 0.259 DEGREE. NOTE THAT RESIDUES 1-38
REMARK 3 AND 132-143 HAD NO LONG
REMARK 3 RANGE NOES AND ARE DISORDERED IN THE CALCULATED STRUCTURES.
REMARK 4
REMARK 4 1D7Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009868.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298
REMARK 210 PH : 7.5; 7.5; 7.5; 7.5
REMARK 210 IONIC STRENGTH : 500MM; 500MM; 500MM; 500MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8MM U-13C,15N EIF1A, 10MM
REMARK 210 PHOSPHATE BUFFER, PH 7.5, 500MM
REMARK 210 NACL, 1MM DTT, 0.1MM EDTA; 0.5MM
REMARK 210 U-15N EIF1A, 10MM PHOSPHATE
REMARK 210 BUFFER, PH 7.5, 500MM NACL, 1MM
REMARK 210 DTT, 0.1MM EDTA; 1.2MM EIF1A,
REMARK 210 10MM PHOSPHATE BUFFER, PH 7.5,
REMARK 210 500MM NACL, 1MM DTT, 0.1MM EDTA;
REMARK 210 0.4MM 15N-LYSINE EIF1A, 10MM
REMARK 210 PHOSPHATE BUFFER, PH 7.5, 500MM
REMARK 210 NACL, 1MM DTT, 0.1MM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, XEASY 1.2, X-PLOR
REMARK 210 3.851, TALOS 1.0
REMARK 210 METHOD USED : STRUCTURES WERE CALCULATED USING
REMARK 210 SIMULATED ANNEALING/MOLECULAR
REMARK 210 DYNAMICS FROM AN EXTENDED
REMARK 210 CONFORMATION WITH RANDOM PHI/PSI
REMARK 210 ANGLES.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE PROTEIN WAS ASSIGNED FROM THE TRIPLE RESONANCE EXPERIMENTS
REMARK 210 HNCA, HN(CO)CA,
REMARK 210 HNCO, HN(CA)CO, CBCA(CO)NH, HBHA(CBCACO)NH, H(CCCO)NH, (H)C(CCO)NH,
REMARK 210 AND HCCH-
REMARK 210 TOCSY. VAL AND LEU METHYL GROUPS WERE STEREOSPECIFICALLY ASSIGNED
REMARK 210 FROM
REMARK 210 ANALYSIS OF MULTIPLET COUPLINGS IN AN HSQC OF 10% 13C-LABELED
REMARK 210 PROTEIN.
REMARK 210 BACKBONE DIHEDRAL ANGLES WERE ESTIMATED USING THE PROGRAM TALOS
REMARK 210 AND BACKBONE
REMARK 210 HETERONUCLEAR CHEMICAL SHIFTS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 C MET B 14 N PRO A 15 1.35
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 B 4 -75.34 -170.15
REMARK 500 1 HIS B 5 78.01 -166.03
REMARK 500 1 HIS B 6 -70.74 68.29
REMARK 500 1 HIS B 7 109.18 -163.67
REMARK 500 1 HIS B 10 85.00 59.28
REMARK 500 1 ASN A 17 93.83 60.22
REMARK 500 1 LYS A 20 -67.08 -152.12
REMARK 500 1 LYS A 23 36.12 -159.57
REMARK 500 1 ARG A 25 -65.58 69.41
REMARK 500 1 ARG A 26 128.56 64.27
REMARK 500 1 ASN A 32 97.26 61.63
REMARK 500 1 SER A 34 32.63 -159.36
REMARK 500 1 LYS A 36 132.17 -177.57
REMARK 500 1 GLU A 38 87.02 -158.76
REMARK 500 1 LEU A 55 -155.83 -103.79
REMARK 500 1 ASN A 57 -43.81 -159.76
REMARK 500 1 SER A 87 68.62 -151.08
REMARK 500 1 ARG A 95 -8.08 82.03
REMARK 500 1 ASP A 99 -175.61 82.99
REMARK 500 1 ASN A 100 -60.93 69.62
REMARK 500 1 GLU A 130 145.24 63.13
REMARK 500 1 THR A 131 -46.71 -148.80
REMARK 500 1 ASP A 132 145.52 63.13
REMARK 500 1 THR A 133 76.81 -67.76
REMARK 500 1 PHE A 134 118.99 61.91
REMARK 500 1 PRO A 136 174.67 -51.11
REMARK 500 1 ASP A 138 -83.19 61.52
REMARK 500 1 ASP A 139 71.25 47.30
REMARK 500 1 GLU A 141 140.30 63.58
REMARK 500 1 PHE A 144 -80.53 62.73
REMARK 500 1 ILE A 147 82.94 65.35
REMARK 500 1 ASP A 149 -69.06 68.50
REMARK 500 1 ASP A 151 -67.09 68.41
REMARK 500 1 GLU A 152 154.88 64.79
REMARK 500 1 ASP A 153 -65.74 69.48
REMARK 500 2 HIS B 8 -36.75 -177.87
REMARK 500 2 HIS B 9 100.40 -47.90
REMARK 500 2 ASP B 12 75.64 67.99
REMARK 500 2 LYS A 16 102.00 61.69
REMARK 500 2 LYS A 20 53.66 -154.07
REMARK 500 2 ASN A 24 152.39 62.56
REMARK 500 2 ARG A 25 43.80 -95.55
REMARK 500 2 ARG A 27 -76.51 65.61
REMARK 500 2 LYS A 29 -51.19 -158.96
REMARK 500 2 ASN A 30 -67.22 68.91
REMARK 500 2 GLU A 31 128.48 64.37
REMARK 500 2 ASN A 32 123.80 62.37
REMARK 500 2 GLU A 33 59.60 -108.11
REMARK 500 2 SER A 34 29.34 -141.42
REMARK 500 2 GLU A 38 78.52 -118.91
REMARK 500
REMARK 500 THIS ENTRY HAS 532 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1D7Q A 15 157 UNP P47813 IF1AX_HUMAN 1 143
DBREF 1D7Q B 1 14 PDB 1D7Q 1D7Q 1 14
SEQRES 1 B 14 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP PRO
SEQRES 2 B 14 MET
SEQRES 1 A 143 PRO LYS ASN LYS GLY LYS GLY GLY LYS ASN ARG ARG ARG
SEQRES 2 A 143 GLY LYS ASN GLU ASN GLU SER GLU LYS ARG GLU LEU VAL
SEQRES 3 A 143 PHE LYS GLU ASP GLY GLN GLU TYR ALA GLN VAL ILE LYS
SEQRES 4 A 143 MET LEU GLY ASN GLY ARG LEU GLU ALA MET CYS PHE ASP
SEQRES 5 A 143 GLY VAL LYS ARG LEU CYS HIS ILE ARG GLY LYS LEU ARG
SEQRES 6 A 143 LYS LYS VAL TRP ILE ASN THR SER ASP ILE ILE LEU VAL
SEQRES 7 A 143 GLY LEU ARG ASP TYR GLN ASP ASN LYS ALA ASP VAL ILE
SEQRES 8 A 143 LEU LYS TYR ASN ALA ASP GLU ALA ARG SER LEU LYS ALA
SEQRES 9 A 143 TYR GLY GLU LEU PRO GLU HIS ALA LYS ILE ASN GLU THR
SEQRES 10 A 143 ASP THR PHE GLY PRO GLY ASP ASP ASP GLU ILE GLN PHE
SEQRES 11 A 143 ASP ASP ILE GLY ASP ASP ASP GLU ASP ILE ASP ASP ILE
HELIX 1 1 GLY A 76 LYS A 81 5 6
HELIX 2 2 GLU A 112 GLY A 120 1 9
SHEET 1 A 5 VAL A 68 HIS A 73 0
SHEET 2 A 5 ARG A 59 CYS A 64 -1 N LEU A 60 O CYS A 72
SHEET 3 A 5 GLN A 46 MET A 54 -1 O GLN A 50 N MET A 63
SHEET 4 A 5 ILE A 89 GLY A 93 -1 O ILE A 90 N ALA A 49
SHEET 5 A 5 ASP A 103 TYR A 108 -1 O ASP A 103 N GLY A 93
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