Header list of 1eij.pdb file
Complete list - b 16 2 Bytes
HEADER DNA BINDING PROTEIN 25-FEB-00 1EIJ
TITLE NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN MTH1615;
COMPND 3 CHAIN: A;
COMPND 4 OTHER_DETAILS: HOMOLOGOUS TO HUMAN APOPTOSIS PROTEIN TFAR19
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262
KEYWDS BETA-HELIX, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.CHRISTENDAT,V.BOOTH,M.GERNSTEIN,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 16-FEB-22 1EIJ 1 REMARK
REVDAT 4 24-FEB-09 1EIJ 1 VERSN
REVDAT 3 25-JAN-05 1EIJ 1 JRNL AUTHOR KEYWDS REMARK
REVDAT 2 29-AUG-01 1EIJ 1 HEADER KEYWDS REMARK
REVDAT 1 03-NOV-00 1EIJ 0
JRNL AUTH D.CHRISTENDAT,A.YEE,A.DHARAMSI,Y.KLUGER,A.SAVCHENKO,
JRNL AUTH 2 J.R.CORT,V.BOOTH,C.D.MACKERETH,V.SARIDAKIS,I.EKIEL,G.KOZLOV,
JRNL AUTH 3 K.L.MAXWELL,N.WU,L.P.MCINTOSH,K.GEHRING,M.A.KENNEDY,
JRNL AUTH 4 A.R.DAVIDSON,E.F.PAI,M.GERSTEIN,A.M.EDWARDS,C.H.ARROWSMITH
JRNL TITL STRUCTURAL PROTEOMICS OF AN ARCHAEON.
JRNL REF NAT.STRUCT.BIOL. V. 7 903 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11017201
JRNL DOI 10.1038/82823
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR ARIA
REMARK 3 AUTHORS : NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EIJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010609.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 300 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM MT1615-15N,13C, 10 MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C/15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR ARIA
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ARG A 73
REMARK 465 GLU A 74
REMARK 465 ILE A 75
REMARK 465 LYS A 76
REMARK 465 ILE A 77
REMARK 465 SER A 78
REMARK 465 ARG A 79
REMARK 465 LYS A 80
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 GLU A 40 H ILE A 44 1.55
REMARK 500 O ILE A 39 H LEU A 43 1.56
REMARK 500 O LEU A 64 H VAL A 68 1.59
REMARK 500 O THR A 57 H LEU A 61 1.60
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 ARG A 2 177.04 60.96
REMARK 500 1 GLN A 3 -64.88 69.06
REMARK 500 1 LEU A 5 96.31 -51.99
REMARK 500 1 GLU A 6 -88.50 48.51
REMARK 500 1 MET A 7 81.67 75.08
REMARK 500 1 LYS A 9 -61.89 -161.27
REMARK 500 1 ILE A 16 40.01 178.98
REMARK 500 1 THR A 31 -82.28 -86.83
REMARK 500 1 ARG A 51 -75.99 -156.07
REMARK 500 1 VAL A 52 27.59 -146.04
REMARK 500 2 ARG A 2 62.61 65.70
REMARK 500 2 GLN A 3 67.59 -115.24
REMARK 500 2 LYS A 9 -49.96 -157.67
REMARK 500 2 ILE A 16 55.93 177.90
REMARK 500 2 THR A 31 -82.29 -82.62
REMARK 500 2 MET A 49 -177.20 -52.74
REMARK 500 2 ARG A 51 -79.84 -113.37
REMARK 500 2 VAL A 52 44.88 -151.53
REMARK 500 3 GLN A 3 -71.39 -174.23
REMARK 500 3 GLN A 4 -73.90 177.54
REMARK 500 3 LEU A 5 78.77 -103.76
REMARK 500 3 GLU A 6 57.75 -101.26
REMARK 500 3 GLN A 8 99.44 59.37
REMARK 500 3 LYS A 9 -45.44 -162.96
REMARK 500 3 ILE A 16 50.43 178.97
REMARK 500 3 THR A 31 -84.30 -86.20
REMARK 500 3 LYS A 71 -40.69 -168.88
REMARK 500 4 GLN A 3 90.73 55.37
REMARK 500 4 MET A 7 -178.97 69.15
REMARK 500 4 LYS A 9 -69.99 -151.47
REMARK 500 4 ILE A 16 42.07 178.28
REMARK 500 4 THR A 31 -86.26 -95.17
REMARK 500 4 LYS A 71 -81.14 -124.45
REMARK 500 5 GLN A 3 -65.07 -161.80
REMARK 500 5 GLU A 6 50.37 -91.98
REMARK 500 5 MET A 7 164.45 70.68
REMARK 500 5 LYS A 9 -43.27 -150.89
REMARK 500 5 ILE A 16 41.44 -179.82
REMARK 500 5 THR A 31 -81.62 -112.51
REMARK 500 5 ARG A 51 -64.83 -167.20
REMARK 500 5 VAL A 52 28.71 -143.66
REMARK 500 6 ARG A 2 59.29 177.18
REMARK 500 6 GLN A 3 81.16 54.06
REMARK 500 6 GLU A 6 -164.56 -77.98
REMARK 500 6 LYS A 9 -68.51 -162.99
REMARK 500 6 ILE A 16 58.44 177.76
REMARK 500 7 LEU A 5 124.53 62.84
REMARK 500 7 LYS A 9 -54.07 -170.41
REMARK 500 7 ILE A 16 31.81 177.15
REMARK 500 7 THR A 31 -86.06 -95.69
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TT10 RELATED DB: TARGETDB
DBREF 1EIJ A 1 80 UNP O27652 DNBP_METTH 32 111
SEQRES 1 A 80 MET ARG GLN GLN LEU GLU MET GLN LYS LYS GLN ILE MET
SEQRES 2 A 80 MET GLN ILE LEU THR PRO GLU ALA ARG SER ARG LEU ALA
SEQRES 3 A 80 ASN LEU ARG LEU THR ARG PRO ASP PHE VAL GLU GLN ILE
SEQRES 4 A 80 GLU LEU GLN LEU ILE GLN LEU ALA GLN MET GLY ARG VAL
SEQRES 5 A 80 ARG SER LYS ILE THR ASP GLU GLN LEU LYS GLU LEU LEU
SEQRES 6 A 80 LYS ARG VAL ALA GLY LYS LYS ARG GLU ILE LYS ILE SER
SEQRES 7 A 80 ARG LYS
HELIX 1 1 LYS A 9 MET A 14 1 6
HELIX 2 2 THR A 18 ARG A 29 1 12
HELIX 3 3 ARG A 32 MET A 49 1 18
HELIX 4 4 THR A 57 ALA A 69 1 13
SHEET 1 A 2 ILE A 16 THR A 18 0
SHEET 2 A 2 LYS A 55 THR A 57 0
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