Header list of 1wlo.pdb file
Complete list - r 25 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-JUN-04 1WLO
TITLE SOLUTION STRUCTURE OF THE HYPOTHETICAL PROTEIN FROM THERMUS
TITLE 2 THERMOPHILUS HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUFE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HYPOTHETICAL PROTEIN TTC0409;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 2 (RSGI)
REVDAT 3 13-JUL-11 1WLO 1 VERSN
REVDAT 2 24-FEB-09 1WLO 1 VERSN
REVDAT 1 12-JUL-05 1WLO 0
JRNL AUTH F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE HYPOTHETICAL PROTEIN FROM THERMUS
JRNL TITL 2 THERMOPHILUS HB8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 1.0.7
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB023714.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 170MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.72MM PROTEIN U-15N, 13C; 20MM
REMARK 210 PHOSPHATE BUFFER NA; 150MM NACL;
REMARK 210 0.02% NAN3; 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 20020425,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.902,
REMARK 210 CYANA 1.0.7
REMARK 210 METHOD USED : 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 LOWEST
REMARK 210 ENERGY, TARGET FUNCTION
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: 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 LEU A 116 H GLU A 120 1.48
REMARK 500 O ASP A 56 H ARG A 63 1.52
REMARK 500 O PRO A 4 H GLN A 8 1.53
REMARK 500 O LEU A 86 H GLU A 89 1.53
REMARK 500 O GLY A 80 H GLU A 84 1.57
REMARK 500 O PRO A 17 H ARG A 21 1.58
REMARK 500 O LEU A 123 H GLN A 127 1.59
REMARK 500 O LEU A 107 H PHE A 110 1.59
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 LYS A 5 -38.45 -38.30
REMARK 500 1 ARG A 21 -39.52 -39.99
REMARK 500 1 LYS A 31 41.98 -100.03
REMARK 500 1 VAL A 39 142.17 -39.90
REMARK 500 1 LEU A 86 -44.38 -154.48
REMARK 500 1 GLU A 87 108.19 -49.91
REMARK 500 1 GLU A 89 -179.03 -62.65
REMARK 500 1 TYR A 105 -109.77 -165.12
REMARK 500 1 THR A 112 164.87 54.28
REMARK 500 1 ALA A 121 -33.90 -38.73
REMARK 500 1 ARG A 131 -38.49 -35.39
REMARK 500 2 VAL A 2 140.71 65.16
REMARK 500 2 LYS A 5 -31.56 -38.06
REMARK 500 2 ARG A 21 -31.55 -38.19
REMARK 500 2 VAL A 39 141.95 -39.98
REMARK 500 2 ASP A 70 -28.80 -39.29
REMARK 500 2 LEU A 86 -44.92 -155.81
REMARK 500 2 GLU A 89 -176.12 -65.91
REMARK 500 2 ARG A 103 119.98 -36.90
REMARK 500 2 TYR A 105 -85.07 -38.07
REMARK 500 2 THR A 112 158.59 -38.87
REMARK 500 3 LYS A 5 -32.55 -37.63
REMARK 500 3 VAL A 32 101.29 -41.28
REMARK 500 3 GLN A 48 -59.05 79.32
REMARK 500 3 HIS A 54 113.64 -164.62
REMARK 500 3 ASP A 70 -29.22 -39.19
REMARK 500 3 LEU A 86 -45.20 -155.77
REMARK 500 3 GLU A 89 -167.54 -68.44
REMARK 500 3 TYR A 105 -45.82 -173.08
REMARK 500 3 THR A 112 162.67 -41.04
REMARK 500 3 LEU A 114 -63.55 -91.97
REMARK 500 3 LEU A 124 -35.35 -39.98
REMARK 500 4 VAL A 2 141.58 67.21
REMARK 500 4 LYS A 7 -33.54 -39.48
REMARK 500 4 LYS A 31 30.33 -96.13
REMARK 500 4 GLN A 48 -71.84 -64.58
REMARK 500 4 LEU A 86 -43.79 -154.99
REMARK 500 4 TYR A 105 -45.56 -178.47
REMARK 500 4 PHE A 110 -63.71 -91.33
REMARK 500 5 ARG A 21 -31.74 -38.81
REMARK 500 5 GLU A 84 -36.69 -35.81
REMARK 500 5 LEU A 86 -45.68 -156.27
REMARK 500 5 GLU A 89 -173.44 -68.65
REMARK 500 5 TYR A 105 -46.51 -175.60
REMARK 500 5 ARG A 117 -30.59 -38.78
REMARK 500 5 ALA A 122 -70.31 -39.97
REMARK 500 5 ARG A 131 -33.52 -35.62
REMARK 500 6 VAL A 2 161.37 54.43
REMARK 500 6 LYS A 5 -35.24 -38.99
REMARK 500 6 LYS A 31 39.96 -95.87
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003001586.1 RELATED DB: TARGETDB
DBREF 1WLO A 1 136 UNP Q5SK87 Q5SK87_THET8 1 136
SEQRES 1 A 136 MET VAL PRO PRO LYS LEU LYS GLN ALA LEU GLU LEU PHE
SEQRES 2 A 136 LYS SER LEU PRO LYS GLU LEU ARG SER GLN VAL LEU LEU
SEQRES 3 A 136 GLU TYR ALA ALA LYS VAL PRO PRO PRO PRO PRO GLY VAL
SEQRES 4 A 136 GLU LEU GLU ARG VAL HIS GLU CYS GLN THR PRO PHE PHE
SEQRES 5 A 136 VAL HIS ALA ASP VAL GLU GLY GLY LYS VAL ARG LEU TYR
SEQRES 6 A 136 PHE HIS VAL PRO ASP GLU ALA PRO THR VAL LYS ALA PHE
SEQRES 7 A 136 ALA GLY LEU LEU ARG GLU GLY LEU GLU GLY GLU SER PRO
SEQRES 8 A 136 GLU ALA VAL LEU GLU VAL PRO PRO GLY PHE TYR ARG GLY
SEQRES 9 A 136 TYR GLY LEU GLU GLU PHE PHE THR PRO LEU ARG LEU ARG
SEQRES 10 A 136 GLY LEU GLU ALA ALA LEU LEU ARG LEU GLN ALA GLN VAL
SEQRES 11 A 136 ARG LYS ALA LEU THR SER
HELIX 1 1 PRO A 3 LEU A 16 1 14
HELIX 2 2 PRO A 17 LYS A 31 1 15
HELIX 3 3 ALA A 72 GLY A 85 1 14
HELIX 4 4 LEU A 107 THR A 112 1 6
HELIX 5 5 THR A 112 THR A 135 1 24
SHEET 1 A 3 GLU A 42 ARG A 43 0
SHEET 2 A 3 PHE A 52 GLU A 58 -1 O VAL A 53 N GLU A 42
SHEET 3 A 3 LYS A 61 HIS A 67 -1 O ARG A 63 N ASP A 56
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 25 2 Bytes