Header list of 1eiw.pdb file
Complete list - b 16 2 Bytes
HEADER STRUCTURAL GENOMICS 29-FEB-00 1EIW
TITLE SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN MTH538 FROM
TITLE 2 METHANOBACTERIUM THERMOAUTOTROPHICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN MTH538;
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;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CHEY-LIKE FOLD, FLAVODOXIN-LIKE FOLD, (A/B)5 DOUBLY WOUND FOLD,
KEYWDS 2 PARALLEL BETA SHEET, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR J.R.CORT,C.H.ARROWSMITH,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (NESG)
REVDAT 5 16-FEB-22 1EIW 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1EIW 1 VERSN
REVDAT 3 06-SEP-05 1EIW 1 AUTHOR
REVDAT 2 25-JAN-05 1EIW 1 AUTHOR KEYWDS REMARK
REVDAT 1 06-SEP-00 1EIW 0
JRNL AUTH J.R.CORT,A.YEE,A.M.EDWARDS,C.H.ARROWSMITH,M.A.KENNEDY
JRNL TITL STRUCTURE-BASED FUNCTIONAL CLASSIFICATION OF HYPOTHETICAL
JRNL TITL 2 PROTEIN MTH538 FROM METHANOBACTERIUM THERMOAUTOTROPHICUM.
JRNL REF J.MOL.BIOL. V. 302 189 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10964569
JRNL DOI 10.1006/JMBI.2000.4052
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: 519 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 3 55 DIHEDRAL ANGLE CONSTRAINTS (PHI)
REMARK 3 28 HYDROGEN BONDS (2 CONSTRAINTS PER H-BOND)
REMARK 4
REMARK 4 1EIW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010618.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 150 MM SALT, 25 MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM MTH538 U-15N,13C; 25 MM
REMARK 210 PHOSPHATE BUFFER PH 7.4, 150 MM
REMARK 210 NACL, 90% H2O, 10% D2O, 5 MM DTT;
REMARK 210 2MM MTH538 U-15N,13C; 25 MM
REMARK 210 PHOSPHATE BUFFER PH 7.1, 150 MM
REMARK 210 NACL, 99% D2O, 5 MM DTT; 2MM
REMARK 210 MTH538 U-15N; 25 MM PHOSPHATE
REMARK 210 BUFFER PH 7.4, 150 MM NACL, 90%
REMARK 210 H2O, 10% D2O, 5 MM DTT; 2MM
REMARK 210 MTH538 U-15N; 25 MM PHOSPHATE
REMARK 210 BUFFER PH 7.1, 150 MM NACL, 99%
REMARK 210 D2O, 5 MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HMQC-J; 3D_13C,
REMARK 210 15N-SIMULTANEOUS NOESY; 1H-15N
REMARK 210 HSQC D2O EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 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
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY,STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH THE LOWEST 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 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 4 152.02 -46.89
REMARK 500 1 THR A 51 -58.20 -141.08
REMARK 500 1 ARG A 52 50.55 -117.28
REMARK 500 1 SER A 66 45.54 -143.94
REMARK 500 1 SER A 67 -3.59 78.21
REMARK 500 1 ARG A 74 154.57 -46.51
REMARK 500 1 GLU A 79 -143.24 -148.57
REMARK 500 1 LEU A 108 -71.20 -66.36
REMARK 500 1 ASP A 109 97.02 -57.83
REMARK 500 2 THR A 2 71.67 44.33
REMARK 500 2 GLU A 4 171.99 63.33
REMARK 500 2 THR A 10 -162.58 -57.35
REMARK 500 2 GLU A 13 39.25 -140.25
REMARK 500 2 ASP A 16 -74.25 -76.51
REMARK 500 2 LEU A 29 159.06 65.62
REMARK 500 2 ASP A 38 56.04 -158.45
REMARK 500 2 ARG A 52 57.24 -141.61
REMARK 500 2 ARG A 74 151.98 -43.14
REMARK 500 2 LEU A 78 -46.29 -167.30
REMARK 500 2 GLU A 79 -143.75 -128.86
REMARK 500 2 TRP A 95 57.95 -114.09
REMARK 500 3 GLU A 4 119.59 75.65
REMARK 500 3 GLU A 13 57.73 -141.75
REMARK 500 3 GLU A 30 59.60 -91.73
REMARK 500 3 ARG A 52 72.67 -114.11
REMARK 500 3 SER A 66 68.75 73.70
REMARK 500 3 SER A 67 -39.13 -154.06
REMARK 500 3 LEU A 78 90.10 61.29
REMARK 500 3 ASN A 80 82.91 56.34
REMARK 500 3 VAL A 88 13.81 -146.14
REMARK 500 4 ALA A 3 61.91 -165.30
REMARK 500 4 SER A 27 77.18 174.39
REMARK 500 4 LEU A 29 161.50 61.63
REMARK 500 4 ALA A 34 -169.61 -100.89
REMARK 500 4 ASP A 38 53.98 -147.21
REMARK 500 4 THR A 51 -39.02 -135.40
REMARK 500 4 LYS A 68 163.59 -47.44
REMARK 500 4 LEU A 78 -82.89 -133.00
REMARK 500 4 ASN A 80 -177.92 61.98
REMARK 500 4 TRP A 95 38.82 -88.74
REMARK 500 4 VAL A 110 84.22 43.91
REMARK 500 5 ALA A 3 -163.35 -101.36
REMARK 500 5 GLU A 4 123.17 74.75
REMARK 500 5 ARG A 18 -70.66 -77.04
REMARK 500 5 LEU A 29 131.93 62.75
REMARK 500 5 ALA A 34 -165.92 -116.63
REMARK 500 5 ARG A 52 47.95 -88.63
REMARK 500 5 SER A 66 -79.69 -112.58
REMARK 500 5 SER A 67 54.59 179.01
REMARK 500 5 GLU A 79 -143.62 -151.68
REMARK 500
REMARK 500 THIS ENTRY HAS 169 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 0.21 SIDE CHAIN
REMARK 500 1 ARG A 18 0.24 SIDE CHAIN
REMARK 500 1 ARG A 32 0.30 SIDE CHAIN
REMARK 500 1 ARG A 52 0.13 SIDE CHAIN
REMARK 500 1 ARG A 53 0.23 SIDE CHAIN
REMARK 500 1 ARG A 64 0.24 SIDE CHAIN
REMARK 500 1 ARG A 74 0.20 SIDE CHAIN
REMARK 500 1 ARG A 101 0.29 SIDE CHAIN
REMARK 500 2 ARG A 6 0.31 SIDE CHAIN
REMARK 500 2 ARG A 18 0.32 SIDE CHAIN
REMARK 500 2 ARG A 23 0.32 SIDE CHAIN
REMARK 500 2 ARG A 32 0.12 SIDE CHAIN
REMARK 500 2 ARG A 52 0.30 SIDE CHAIN
REMARK 500 2 ARG A 53 0.22 SIDE CHAIN
REMARK 500 2 ARG A 64 0.31 SIDE CHAIN
REMARK 500 2 ARG A 74 0.25 SIDE CHAIN
REMARK 500 2 ARG A 101 0.20 SIDE CHAIN
REMARK 500 3 ARG A 6 0.29 SIDE CHAIN
REMARK 500 3 ARG A 18 0.21 SIDE CHAIN
REMARK 500 3 ARG A 23 0.20 SIDE CHAIN
REMARK 500 3 ARG A 32 0.20 SIDE CHAIN
REMARK 500 3 ARG A 52 0.12 SIDE CHAIN
REMARK 500 3 ARG A 53 0.32 SIDE CHAIN
REMARK 500 3 ARG A 64 0.29 SIDE CHAIN
REMARK 500 3 ARG A 74 0.21 SIDE CHAIN
REMARK 500 3 ARG A 101 0.32 SIDE CHAIN
REMARK 500 4 ARG A 6 0.25 SIDE CHAIN
REMARK 500 4 ARG A 18 0.26 SIDE CHAIN
REMARK 500 4 ARG A 23 0.23 SIDE CHAIN
REMARK 500 4 ARG A 32 0.20 SIDE CHAIN
REMARK 500 4 ARG A 52 0.28 SIDE CHAIN
REMARK 500 4 ARG A 53 0.30 SIDE CHAIN
REMARK 500 4 ARG A 64 0.29 SIDE CHAIN
REMARK 500 4 ARG A 74 0.20 SIDE CHAIN
REMARK 500 4 ARG A 101 0.28 SIDE CHAIN
REMARK 500 5 ARG A 6 0.27 SIDE CHAIN
REMARK 500 5 ARG A 18 0.17 SIDE CHAIN
REMARK 500 5 ARG A 23 0.24 SIDE CHAIN
REMARK 500 5 ARG A 32 0.32 SIDE CHAIN
REMARK 500 5 ARG A 52 0.20 SIDE CHAIN
REMARK 500 5 ARG A 53 0.20 SIDE CHAIN
REMARK 500 5 ARG A 74 0.32 SIDE CHAIN
REMARK 500 5 ARG A 101 0.17 SIDE CHAIN
REMARK 500 6 ARG A 6 0.13 SIDE CHAIN
REMARK 500 6 ARG A 18 0.29 SIDE CHAIN
REMARK 500 6 ARG A 23 0.25 SIDE CHAIN
REMARK 500 6 ARG A 32 0.19 SIDE CHAIN
REMARK 500 6 ARG A 52 0.32 SIDE CHAIN
REMARK 500 6 ARG A 53 0.21 SIDE CHAIN
REMARK 500 6 ARG A 64 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 131 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TP1 RELATED DB: TARGETDB
DBREF 1EIW A 1 111 UNP O26638 P538_METTH 1 111
SEQADV 1EIW VAL A 1 UNP O26638 MET 1 CONFLICT
SEQRES 1 A 111 VAL THR ALA GLU ILE ARG LEU TYR ILE THR GLU GLY GLU
SEQRES 2 A 111 VAL GLU ASP TYR ARG VAL PHE LEU GLU ARG LEU GLU GLN
SEQRES 3 A 111 SER GLY LEU GLU TRP ARG PRO ALA THR PRO GLU ASP ALA
SEQRES 4 A 111 ASP ALA VAL ILE VAL LEU ALA GLY LEU TRP GLY THR ARG
SEQRES 5 A 111 ARG ASP GLU ILE LEU GLY ALA VAL ASP LEU ALA ARG LYS
SEQRES 6 A 111 SER SER LYS PRO ILE ILE THR VAL ARG PRO TYR GLY LEU
SEQRES 7 A 111 GLU ASN VAL PRO PRO GLU LEU GLU ALA VAL SER SER GLU
SEQRES 8 A 111 VAL VAL GLY TRP ASN PRO HIS CYS ILE ARG ASP ALA LEU
SEQRES 9 A 111 GLU ASP ALA LEU ASP VAL ILE
HELIX 1 1 VAL A 14 GLY A 28 1 15
HELIX 2 2 GLY A 47 TRP A 49 5 3
HELIX 3 3 ARG A 52 ARG A 64 1 13
HELIX 4 4 GLU A 84 SER A 89 1 6
HELIX 5 5 ASN A 96 ASP A 109 1 14
SHEET 1 A 5 TRP A 31 PRO A 33 0
SHEET 2 A 5 ILE A 5 ILE A 9 1 O ILE A 5 N ARG A 32
SHEET 3 A 5 ALA A 41 LEU A 45 1 N ALA A 41 O ARG A 6
SHEET 4 A 5 ILE A 70 VAL A 73 1 N ILE A 71 O VAL A 42
SHEET 5 A 5 GLU A 91 VAL A 93 1 O GLU A 91 N THR A 72
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