Header list of 2d9f.pdb file
Complete list - r 9 2 Bytes
HEADER ISOMERASE 09-DEC-05 2D9F
TITLE SOLUTION STRUCTURE OF RUH-047, AN FKBP DOMAIN FROM HUMAN CDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FK506-BINDING PROTEIN 8 VARIANT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 8-129;
COMPND 5 SYNONYM: FK506-BINDING DOMAIN, FKBP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P040614-07;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FKBP, FK506 BINDING PROTEIN, RAPAMYCIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.Z.M.RUHUL MOMEN,H.HIROTA,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D9F 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D9F 1 VERSN
REVDAT 1 09-JUN-06 2D9F 0
JRNL AUTH A.Z.M.RUHUL MOMEN,H.HIROTA,S.KOSHIBA,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RUH-047, AN FKBP DOMAIN FROM HUMAN
JRNL TITL 2 CDNA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025150.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.01MM DOMAIN U-15N, 13C; 20MM D
REMARK 210 -TRIS-HCL (PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 90%H2O,
REMARK 210 10%D2O
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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.04,
REMARK 210 KUJIRA 0.9295
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 : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 TRP A 10 161.20 -40.68
REMARK 500 1 LEU A 18 -71.02 -60.08
REMARK 500 1 PRO A 34 -170.09 -69.76
REMARK 500 1 GLU A 59 73.51 -112.39
REMARK 500 1 PRO A 78 2.95 -69.76
REMARK 500 1 CYS A 95 -71.22 -77.19
REMARK 500 1 PRO A 98 2.81 -69.78
REMARK 500 1 ARG A 102 -69.79 -107.14
REMARK 500 1 HIS A 109 26.40 48.43
REMARK 500 1 ALA A 111 159.44 -46.56
REMARK 500 1 LYS A 119 -61.03 -93.74
REMARK 500 1 MET A 129 51.71 34.76
REMARK 500 2 GLU A 8 40.30 -107.61
REMARK 500 2 ARG A 33 139.84 -37.78
REMARK 500 2 PRO A 34 -170.20 -69.75
REMARK 500 2 PRO A 78 3.13 -69.78
REMARK 500 2 ARG A 102 -65.01 -105.59
REMARK 500 2 HIS A 109 27.49 43.52
REMARK 500 2 ALA A 111 160.50 -48.39
REMARK 500 2 SER A 130 173.40 -53.34
REMARK 500 3 SER A 2 107.06 -41.76
REMARK 500 3 LEU A 18 -70.27 -62.00
REMARK 500 3 SER A 32 136.27 -171.71
REMARK 500 3 ARG A 33 137.42 -39.22
REMARK 500 3 PRO A 34 -164.04 -69.73
REMARK 500 3 GLU A 59 74.06 -110.17
REMARK 500 3 PRO A 78 4.28 -69.76
REMARK 500 3 SER A 92 -36.38 -36.71
REMARK 500 3 CYS A 95 -72.54 -78.82
REMARK 500 3 SER A 103 105.38 -160.13
REMARK 500 3 HIS A 109 25.24 45.45
REMARK 500 3 ALA A 111 159.09 -46.66
REMARK 500 3 GLU A 128 77.50 -65.29
REMARK 500 4 LEU A 18 -70.16 -64.79
REMARK 500 4 SER A 31 170.19 -57.88
REMARK 500 4 PRO A 34 -172.89 -69.80
REMARK 500 4 PRO A 78 4.90 -69.79
REMARK 500 4 CYS A 95 -73.42 -78.94
REMARK 500 4 PRO A 98 2.77 -69.73
REMARK 500 4 ARG A 102 -65.02 -105.79
REMARK 500 4 ALA A 111 160.34 -43.06
REMARK 500 4 LEU A 127 96.18 -57.46
REMARK 500 4 SER A 133 163.13 -43.52
REMARK 500 5 SER A 2 165.79 -48.79
REMARK 500 5 GLU A 8 31.83 -93.73
REMARK 500 5 SER A 31 170.91 -52.40
REMARK 500 5 PRO A 34 -165.17 -69.75
REMARK 500 5 PRO A 78 3.25 -69.76
REMARK 500 5 CYS A 95 -71.42 -74.46
REMARK 500 5 PRO A 98 1.33 -69.80
REMARK 500
REMARK 500 THIS ENTRY HAS 207 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001001573.1 RELATED DB: TARGETDB
DBREF 2D9F A 8 129 GB 62897235 BAD96558 50 171
SEQADV 2D9F GLY A 1 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 2 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 3 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F GLY A 4 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 5 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 6 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F GLY A 7 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 130 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F GLY A 131 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F PRO A 132 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 133 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F SER A 134 GB 62897235 CLONING ARTIFACT
SEQADV 2D9F GLY A 135 GB 62897235 CLONING ARTIFACT
SEQRES 1 A 135 GLY SER SER GLY SER SER GLY GLU GLU TRP LEU ASP ILE
SEQRES 2 A 135 LEU GLY ASN GLY LEU LEU ARG LYS LYS THR LEU VAL PRO
SEQRES 3 A 135 GLY PRO PRO GLY SER SER ARG PRO VAL LYS GLY GLN VAL
SEQRES 4 A 135 VAL THR VAL HIS LEU GLN THR SER LEU GLU ASN GLY THR
SEQRES 5 A 135 ARG VAL GLN GLU GLU PRO GLU LEU VAL PHE THR LEU GLY
SEQRES 6 A 135 ASP CYS ASP VAL ILE GLN ALA LEU ASP LEU SER VAL PRO
SEQRES 7 A 135 LEU MET ASP VAL GLY GLU THR ALA MET VAL THR ALA ASP
SEQRES 8 A 135 SER LYS TYR CYS TYR GLY PRO GLN GLY SER ARG SER PRO
SEQRES 9 A 135 TYR ILE PRO PRO HIS ALA ALA LEU CYS LEU GLU VAL THR
SEQRES 10 A 135 LEU LYS THR ALA VAL ASP ARG PRO ASP LEU GLU MET SER
SEQRES 11 A 135 GLY PRO SER SER GLY
HELIX 1 1 SER A 76 MET A 80 5 5
HELIX 2 2 ASP A 91 TYR A 96 1 6
SHEET 1 A 6 LEU A 11 ASP A 12 0
SHEET 2 A 6 ARG A 20 VAL A 25 -1 O LYS A 21 N LEU A 11
SHEET 3 A 6 THR A 85 ALA A 90 -1 O MET A 87 N LYS A 22
SHEET 4 A 6 LEU A 112 VAL A 122 -1 O LEU A 114 N VAL A 88
SHEET 5 A 6 VAL A 39 LEU A 48 -1 N SER A 47 O CYS A 113
SHEET 6 A 6 ARG A 53 THR A 63 -1 O LEU A 60 N VAL A 42
CISPEP 1 SER A 103 PRO A 104 1 -0.01
CISPEP 2 SER A 103 PRO A 104 2 0.01
CISPEP 3 SER A 103 PRO A 104 3 -0.06
CISPEP 4 SER A 103 PRO A 104 4 -0.03
CISPEP 5 SER A 103 PRO A 104 5 -0.04
CISPEP 6 SER A 103 PRO A 104 6 0.00
CISPEP 7 SER A 103 PRO A 104 7 -0.12
CISPEP 8 SER A 103 PRO A 104 8 -0.04
CISPEP 9 SER A 103 PRO A 104 9 -0.10
CISPEP 10 SER A 103 PRO A 104 10 0.03
CISPEP 11 SER A 103 PRO A 104 11 -0.05
CISPEP 12 SER A 103 PRO A 104 12 0.04
CISPEP 13 SER A 103 PRO A 104 13 -0.03
CISPEP 14 SER A 103 PRO A 104 14 -0.06
CISPEP 15 SER A 103 PRO A 104 15 -0.04
CISPEP 16 SER A 103 PRO A 104 16 -0.06
CISPEP 17 SER A 103 PRO A 104 17 -0.01
CISPEP 18 SER A 103 PRO A 104 18 0.05
CISPEP 19 SER A 103 PRO A 104 19 -0.02
CISPEP 20 SER A 103 PRO A 104 20 -0.08
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