Header list of 2do8.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 27-APR-06 2DO8
TITLE SOLUTION STRUCTURE OF UPF0301 PROTEIN HD_1794
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPF0301 PROTEIN HD_1794;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS DUCREYI;
SOURCE 3 ORGANISM_TAXID: 730;
SOURCE 4 GENE: ORDEREDLOCUSNAMES: HD_1794;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NESG, GFT NMR, STRUCTRAL GENOMICS, HDR14, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.ZHANG,G.LIU,R.SHASTRY,M.JIANG,K.CUNNINGHAM,L.C.MA,R.XIAO,T.R.ACTON,
AUTHOR 2 G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 3 09-MAR-22 2DO8 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DO8 1 VERSN
REVDAT 1 25-MAY-06 2DO8 0
JRNL AUTH Q.ZHANG,G.LIU,R.SHASTRY,M.JIANG,K.CUNNINGHAM,L.C.MA,R.XIAO,
JRNL AUTH 2 T.R.ACTON,G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL SOLUTION STRUCTURE OF UPF0301 PROTEIN HD_1794
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, CNS 1.1
REMARK 3 AUTHORS : GUNTERT, P. (DYANA),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DO8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025646.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50MM MES; 10MM DTT; 50MM
REMARK 210 ARGININE; 0.02% NAN3; 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : GFT (4,3)D HNNCABCA; GFT (4,3)D
REMARK 210 CABCA(CO)NHN; GFT (4,3)D
REMARK 210 HABCAB(CO)NHN; GFT (4,3)D HCCH;
REMARK 210 SIMULTANEOUS HETERONUCLEAR
REMARK 210 RESOLVED [1H,1H]-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1, NMRPIPE 2.3, XEASY
REMARK 210 1.3, UBNMR 1.0, AUTOSTRUCTURE
REMARK 210 2.0.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING GFT TECHNIQUES.
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: 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
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 PHE A 2 116.26 61.06
REMARK 500 1 ASN A 4 114.83 69.90
REMARK 500 1 THR A 13 82.38 58.35
REMARK 500 1 MET A 16 -74.61 -168.52
REMARK 500 1 ASP A 17 73.02 51.49
REMARK 500 1 ASP A 18 -49.70 75.64
REMARK 500 1 PHE A 21 -12.64 -176.94
REMARK 500 1 ARG A 23 123.74 71.50
REMARK 500 1 VAL A 25 140.60 73.55
REMARK 500 1 ILE A 26 -58.42 -135.19
REMARK 500 1 ASN A 42 103.59 63.97
REMARK 500 1 THR A 43 91.52 -161.34
REMARK 500 1 MET A 56 -91.69 -82.35
REMARK 500 1 ASP A 57 24.35 -146.76
REMARK 500 1 ALA A 61 -165.59 -111.34
REMARK 500 1 ARG A 64 -163.41 56.86
REMARK 500 1 THR A 67 -20.22 73.31
REMARK 500 1 ASP A 91 -147.89 59.68
REMARK 500 1 PHE A 94 102.60 167.59
REMARK 500 1 THR A 95 -55.05 -121.26
REMARK 500 1 HIS A 137 -9.19 74.83
REMARK 500 1 ASN A 155 -83.56 49.97
REMARK 500 1 THR A 161 88.46 38.39
REMARK 500 1 SER A 162 -37.24 76.29
REMARK 500 1 TYR A 163 93.61 68.23
REMARK 500 1 LEU A 164 -55.97 -173.60
REMARK 500 1 ASP A 165 143.27 175.47
REMARK 500 1 ILE A 176 73.94 55.62
REMARK 500 1 ILE A 179 166.47 68.77
REMARK 500 1 LEU A 180 62.51 63.01
REMARK 500 1 ALA A 181 -59.14 177.55
REMARK 500 1 ARG A 185 78.40 -108.47
REMARK 500 2 LEU A 5 -152.12 -130.00
REMARK 500 2 GLN A 6 119.25 67.98
REMARK 500 2 THR A 13 96.77 53.53
REMARK 500 2 ASP A 18 173.75 65.76
REMARK 500 2 GLU A 19 -39.70 70.99
REMARK 500 2 ARG A 23 86.62 64.16
REMARK 500 2 VAL A 25 100.47 68.24
REMARK 500 2 ILE A 26 -142.61 -129.67
REMARK 500 2 VAL A 39 68.03 -113.37
REMARK 500 2 ASN A 42 85.88 62.99
REMARK 500 2 THR A 43 123.11 -179.10
REMARK 500 2 ASP A 57 -150.47 -150.14
REMARK 500 2 ALA A 61 159.60 74.84
REMARK 500 2 LYS A 62 150.29 68.35
REMARK 500 2 MET A 71 165.89 63.06
REMARK 500 2 THR A 90 -169.30 -126.30
REMARK 500 2 HIS A 92 165.94 75.53
REMARK 500 2 GLU A 93 169.29 69.41
REMARK 500
REMARK 500 THIS ENTRY HAS 566 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HDR14 RELATED DB: TARGETDB
DBREF 2DO8 A 1 186 UNP Q7VKS7 Y1794_HAEDU 1 186
SEQADV 2DO8 LEU A 187 UNP Q7VKS7 CLONING ARTIFACT
SEQADV 2DO8 GLU A 188 UNP Q7VKS7 CLONING ARTIFACT
SEQRES 1 A 188 MET PHE GLY ASN LEU GLN GLY LYS PHE ILE ILE ALA THR
SEQRES 2 A 188 PRO GLU MET ASP ASP GLU TYR PHE ASP ARG THR VAL ILE
SEQRES 3 A 188 TYR ILE CYS GLU HIS ASN ASP ASN GLY THR ILE GLY VAL
SEQRES 4 A 188 ILE ILE ASN THR PRO THR ASP LEU SER VAL LEU GLU LEU
SEQRES 5 A 188 LEU THR ARG MET ASP PHE GLN MET ALA LYS PRO ARG ILE
SEQRES 6 A 188 TYR THR GLN ASP GLN MET VAL LEU ASN GLY GLY PRO VAL
SEQRES 7 A 188 ASN GLN ASP ARG GLY PHE ILE VAL HIS SER LYS THR ASP
SEQRES 8 A 188 HIS GLU PHE THR HIS SER TYR LYS VAL THR ASP ASP ILE
SEQRES 9 A 188 THR LEU THR THR SER GLY ASP VAL LEU ASP SER PHE GLY
SEQRES 10 A 188 THR GLN THR ALA PRO GLU LYS PHE ILE VAL CYS LEU GLY
SEQRES 11 A 188 CYS SER THR TRP LYS PRO HIS GLN LEU GLU GLN GLU ILE
SEQRES 12 A 188 ALA GLN ASN TYR TRP LEU LEU SER GLU ALA ASN ASN GLN
SEQRES 13 A 188 THR LEU PHE GLU THR SER TYR LEU ASP ARG TRP VAL GLU
SEQRES 14 A 188 ALA ASN GLU MET LEU GLY ILE SER GLY ILE LEU ALA PRO
SEQRES 15 A 188 ALA GLY ARG ALA LEU GLU
HELIX 1 1 VAL A 49 MET A 56 1 8
HELIX 2 2 PRO A 63 THR A 67 5 5
HELIX 3 3 GLY A 110 PHE A 116 1 7
HELIX 4 4 HIS A 137 GLN A 145 1 9
HELIX 5 5 ASN A 155 GLU A 160 1 6
HELIX 6 6 VAL A 168 MET A 173 1 6
SHEET 1 A 2 LYS A 8 ILE A 11 0
SHEET 2 A 2 LEU A 149 GLU A 152 -1 O LEU A 149 N ILE A 11
SHEET 1 B 5 TYR A 27 ASN A 32 0
SHEET 2 B 5 GLY A 35 VAL A 39 -1 O GLY A 35 N ASN A 32
SHEET 3 B 5 PHE A 125 TRP A 134 -1 O TRP A 134 N THR A 36
SHEET 4 B 5 MET A 71 ASN A 74 1 N LEU A 73 O LEU A 129
SHEET 5 B 5 PRO A 44 SER A 48 -1 N LEU A 47 O VAL A 72
SHEET 1 C 6 TYR A 27 ASN A 32 0
SHEET 2 C 6 GLY A 35 VAL A 39 -1 O GLY A 35 N ASN A 32
SHEET 3 C 6 PHE A 125 TRP A 134 -1 O TRP A 134 N THR A 36
SHEET 4 C 6 VAL A 78 HIS A 87 -1 N PHE A 84 O CYS A 128
SHEET 5 C 6 THR A 105 THR A 107 -1 O THR A 107 N ILE A 85
SHEET 6 C 6 SER A 97 LYS A 99 -1 N TYR A 98 O LEU A 106
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 - r 9 2 Bytes