Header list of 1eo1.pdb file
Complete list - b 16 2 Bytes
HEADER STRUCTURAL GENOMICS 21-MAR-00 1EO1
TITLE SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN MTH1175 FROM
TITLE 2 METHANOBACTERIUM THERMOAUTOTROPHICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN MTH1175;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS MIXED A/B PROTEIN, MIXED BETA SHEET, STRAND ORDER 321456, STRANDS 2
KEYWDS 2 AND 6 ANTIPARALLEL TO REST., STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.CORT,C.H.ARROWSMITH,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (NESG)
REVDAT 5 16-FEB-22 1EO1 1 REMARK
REVDAT 4 24-FEB-09 1EO1 1 VERSN
REVDAT 3 06-SEP-05 1EO1 1 AUTHOR
REVDAT 2 25-JAN-05 1EO1 1 AUTHOR KEYWDS REMARK
REVDAT 1 20-DEC-00 1EO1 0
JRNL AUTH J.R.CORT,A.YEE,A.M.EDWARDS,C.H.ARROWSMITH,M.A.KENNEDY
JRNL TITL NMR STRUCTURE DETERMINATION AND STRUCTURE-BASED FUNCTIONAL
JRNL TITL 2 CHARACTERIZATION OF CONSERVED HYPOTHETICAL PROTEIN MTH1175
JRNL TITL 3 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM
JRNL REF J.STRUCT.FUNCT.GENOM. V. 1 15 2000
JRNL REFN ISSN 1345-711X
JRNL PMID 12836677
JRNL DOI 10.1023/A:1011348803324
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 436 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 40 DIHEDRAL ANGLE CONSTRAINTS (PHI), 58 HYDROGEN BONDS (2
REMARK 3 CONSTRAINTS PER H-BOND)
REMARK 4
REMARK 4 1EO1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010752.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 150 MM SALT, 25 MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM MTH1175 U-15N,13C; 25 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.5, 150 MM
REMARK 210 NACL, 90% H2O, 10% D2O; 2 MM
REMARK 210 MTH1175 U-15N; 25 MM PHOSPHATE
REMARK 210 BUFFER, PH* 6.1, 150 MM NACL, 99%
REMARK 210 D2O; 2 MM MTH1175 U-15N; 25 MM
REMARK 210 PHOSPHATE BUFFER, PH 6.5, 150 MM
REMARK 210 NACL, 90% H2O, 10% D2O; 2 MM
REMARK 210 MTH1175 U-15N; 25 MM PHOSPHATE
REMARK 210 BUFFER, PH* 6.1, 150 MM NACL, 99%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C,
REMARK 210 15N-SIMULTANEOUS NOESY; 1H-15N
REMARK 210 HSQC D2O EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, VNMR, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
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: 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 7 -98.09 52.73
REMARK 500 1 SER A 8 15.36 59.05
REMARK 500 1 ASP A 11 -89.17 -131.19
REMARK 500 1 LEU A 12 26.33 -158.99
REMARK 500 1 SER A 17 -95.91 51.60
REMARK 500 1 ARG A 18 -77.93 -158.35
REMARK 500 1 ALA A 23 106.63 -48.16
REMARK 500 1 PRO A 24 42.23 -80.74
REMARK 500 1 TYR A 25 69.53 -159.83
REMARK 500 1 LYS A 32 -72.08 -117.58
REMARK 500 1 LYS A 33 58.84 -110.58
REMARK 500 1 PRO A 45 -78.71 -78.34
REMARK 500 1 SER A 48 66.06 -118.23
REMARK 500 1 ALA A 49 -52.44 -179.79
REMARK 500 1 SER A 50 170.74 -55.23
REMARK 500 1 ALA A 53 -150.28 -136.16
REMARK 500 1 VAL A 66 92.06 -48.09
REMARK 500 1 THR A 95 -67.30 -164.38
REMARK 500 1 SER A 96 157.21 171.71
REMARK 500 1 LEU A 109 176.80 -56.34
REMARK 500 1 ARG A 119 88.68 49.33
REMARK 500 2 THR A 10 -45.05 -148.73
REMARK 500 2 ASP A 11 -55.29 -154.47
REMARK 500 2 SER A 17 -163.56 44.36
REMARK 500 2 PRO A 24 46.65 -80.50
REMARK 500 2 TYR A 25 70.01 -158.51
REMARK 500 2 LYS A 32 -91.30 -87.99
REMARK 500 2 SER A 38 128.20 176.25
REMARK 500 2 PRO A 45 -167.01 -78.08
REMARK 500 2 SER A 48 57.28 -140.49
REMARK 500 2 ALA A 49 61.33 -103.27
REMARK 500 2 VAL A 66 97.50 -68.61
REMARK 500 2 SER A 73 151.06 -49.22
REMARK 500 2 PRO A 74 -72.48 -78.29
REMARK 500 2 THR A 95 -32.98 -142.13
REMARK 500 2 LEU A 109 -152.03 178.04
REMARK 500 2 ARG A 113 -45.47 -134.26
REMARK 500 2 PRO A 115 -168.61 -77.93
REMARK 500 3 SER A 7 -141.38 46.32
REMARK 500 3 THR A 10 -90.65 49.01
REMARK 500 3 ASP A 11 -150.61 173.15
REMARK 500 3 GLU A 15 -114.20 -72.75
REMARK 500 3 SER A 17 -150.26 47.06
REMARK 500 3 ARG A 18 12.95 -144.55
REMARK 500 3 TYR A 25 70.92 -160.41
REMARK 500 3 LYS A 32 -79.76 -81.99
REMARK 500 3 GLU A 37 20.11 -145.65
REMARK 500 3 SER A 38 129.66 -179.21
REMARK 500 3 SER A 46 36.67 74.60
REMARK 500 3 SER A 50 58.93 -100.91
REMARK 500
REMARK 500 THIS ENTRY HAS 367 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 18 0.32 SIDE CHAIN
REMARK 500 1 ARG A 22 0.16 SIDE CHAIN
REMARK 500 1 ARG A 56 0.25 SIDE CHAIN
REMARK 500 1 ARG A 91 0.31 SIDE CHAIN
REMARK 500 1 ARG A 113 0.20 SIDE CHAIN
REMARK 500 1 ARG A 119 0.30 SIDE CHAIN
REMARK 500 1 ARG A 121 0.30 SIDE CHAIN
REMARK 500 1 ARG A 122 0.23 SIDE CHAIN
REMARK 500 1 ARG A 123 0.31 SIDE CHAIN
REMARK 500 1 ARG A 124 0.26 SIDE CHAIN
REMARK 500 2 ARG A 18 0.31 SIDE CHAIN
REMARK 500 2 ARG A 56 0.28 SIDE CHAIN
REMARK 500 2 ARG A 91 0.28 SIDE CHAIN
REMARK 500 2 ARG A 113 0.18 SIDE CHAIN
REMARK 500 2 ARG A 119 0.31 SIDE CHAIN
REMARK 500 2 ARG A 121 0.32 SIDE CHAIN
REMARK 500 2 ARG A 122 0.30 SIDE CHAIN
REMARK 500 2 ARG A 123 0.08 SIDE CHAIN
REMARK 500 2 ARG A 124 0.30 SIDE CHAIN
REMARK 500 3 ARG A 18 0.31 SIDE CHAIN
REMARK 500 3 ARG A 22 0.11 SIDE CHAIN
REMARK 500 3 ARG A 56 0.09 SIDE CHAIN
REMARK 500 3 ARG A 91 0.13 SIDE CHAIN
REMARK 500 3 ARG A 113 0.23 SIDE CHAIN
REMARK 500 3 ARG A 119 0.30 SIDE CHAIN
REMARK 500 3 ARG A 121 0.27 SIDE CHAIN
REMARK 500 3 ARG A 122 0.22 SIDE CHAIN
REMARK 500 3 ARG A 123 0.29 SIDE CHAIN
REMARK 500 3 ARG A 124 0.15 SIDE CHAIN
REMARK 500 4 ARG A 22 0.30 SIDE CHAIN
REMARK 500 4 ARG A 56 0.23 SIDE CHAIN
REMARK 500 4 ARG A 91 0.32 SIDE CHAIN
REMARK 500 4 ARG A 113 0.31 SIDE CHAIN
REMARK 500 4 ARG A 119 0.31 SIDE CHAIN
REMARK 500 4 ARG A 121 0.31 SIDE CHAIN
REMARK 500 4 ARG A 122 0.18 SIDE CHAIN
REMARK 500 4 ARG A 123 0.28 SIDE CHAIN
REMARK 500 4 ARG A 124 0.29 SIDE CHAIN
REMARK 500 5 ARG A 18 0.27 SIDE CHAIN
REMARK 500 5 ARG A 22 0.27 SIDE CHAIN
REMARK 500 5 ARG A 56 0.29 SIDE CHAIN
REMARK 500 5 ARG A 113 0.20 SIDE CHAIN
REMARK 500 5 ARG A 119 0.32 SIDE CHAIN
REMARK 500 5 ARG A 121 0.27 SIDE CHAIN
REMARK 500 5 ARG A 122 0.28 SIDE CHAIN
REMARK 500 5 ARG A 123 0.29 SIDE CHAIN
REMARK 500 5 ARG A 124 0.28 SIDE CHAIN
REMARK 500 6 ARG A 18 0.20 SIDE CHAIN
REMARK 500 6 ARG A 22 0.23 SIDE CHAIN
REMARK 500 6 ARG A 56 0.16 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 191 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EIW RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN MTH538 FROM
REMARK 900 METHANOBACTERIUM THERMOAUTOTROPHICUM
REMARK 900 RELATED ID: TP2 RELATED DB: TARGETDB
DBREF 1EO1 A 1 124 UNP O27243 O27243_METTH 1 124
SEQRES 1 A 124 MET LYS ILE ALA ILE ALA SER SER GLY THR ASP LEU GLY
SEQRES 2 A 124 SER GLU VAL SER ARG PHE PHE GLY ARG ALA PRO TYR PHE
SEQRES 3 A 124 MET ILE VAL GLU MET LYS LYS GLY ASN ILE GLU SER SER
SEQRES 4 A 124 GLU VAL ILE GLU ASN PRO SER ALA SER ALA SER GLY GLY
SEQRES 5 A 124 ALA GLY ILE ARG THR ALA GLN ILE ILE ALA ASN ASN GLY
SEQRES 6 A 124 VAL LYS ALA VAL ILE ALA SER SER PRO GLY PRO ASN ALA
SEQRES 7 A 124 PHE GLU VAL LEU ASN GLU LEU GLY ILE LYS ILE TYR ARG
SEQRES 8 A 124 ALA THR GLY THR SER VAL GLU GLU ASN LEU LYS LEU PHE
SEQRES 9 A 124 THR GLU GLY ASN LEU GLU GLU ILE ARG SER PRO GLY SER
SEQRES 10 A 124 GLY ARG GLY ARG ARG ARG ARG
HELIX 1 1 ARG A 56 ASN A 64 1 9
HELIX 2 2 GLY A 75 GLY A 86 1 12
HELIX 3 3 SER A 96 GLU A 106 1 11
SHEET 1 A 6 ILE A 36 ILE A 42 0
SHEET 2 A 6 PHE A 26 MET A 31 -1 O PHE A 26 N ILE A 42
SHEET 3 A 6 LYS A 2 ILE A 5 -1 N ILE A 3 O VAL A 29
SHEET 4 A 6 ALA A 68 ALA A 71 1 N ALA A 68 O LYS A 2
SHEET 5 A 6 LYS A 88 ARG A 91 1 O LYS A 88 N VAL A 69
SHEET 6 A 6 GLU A 111 ILE A 112 -1 O ILE A 112 N ILE A 89
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