Header list of 1ix5.pdb file
Complete list - v 10 2 Bytes
HEADER ISOMERASE 12-JUN-02 1IX5 TITLE SOLUTION STRUCTURE OF THE METHANOCOCCUS THERMOLITHOTROPHICUS FKBP COMPND MOL_ID: 1; COMPND 2 MOLECULE: FKBP; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; COMPND 5 EC: 5.2.1.8; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOCOCCUS THERMOLITHOTROPHICUS; SOURCE 3 ORGANISM_TAXID: 2186; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYSS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-11D KEYWDS FKBP FOLD, PPIASE, ISOMERASE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR R.SUZUKI,K.NAGATA,M.KAWAKAMI,N.NEMOTO,M.FURUTANI,K.ADACHI,T.MARUYAMA, AUTHOR 2 M.TANOKURA REVDAT 3 10-NOV-21 1IX5 1 REMARK SEQADV REVDAT 2 24-FEB-09 1IX5 1 VERSN REVDAT 1 10-JUN-03 1IX5 0 JRNL AUTH R.SUZUKI,K.NAGATA,F.YUMOTO,M.KAWAKAMI,N.NEMOTO,M.FURUTANI, JRNL AUTH 2 K.ADACHI,T.MARUYAMA,M.TANOKURA JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN ARCHAEAL FKBP JRNL TITL 2 WITH A DUAL FUNCTION OF PEPTIDYL PROLYL CIS-TRANS ISOMERASE JRNL TITL 3 AND CHAPERONE-LIKE ACTIVITIES JRNL REF J.MOL.BIOL. V. 328 1149 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12729748 JRNL DOI 10.1016/S0022-2836(03)00379-6 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 5.3B, DYANA 1.5 REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1IX5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-JUN-02. REMARK 100 THE DEPOSITION ID IS D_1000005365. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER K REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 5.5MM FKBP U-15N,13C; 50MM REMARK 210 PHOSPHATE BUFFER K; 90% H2O, 10% REMARK 210 D2O; 5.5MM FKBP U-15N,13C; 50MM REMARK 210 PHOSPHATE BUFFER K; 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; REMARK 210 HNCOHB REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.6, SPARKY 3.106, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 HD1 HIS A 136 H LEU A 138 0.74 REMARK 500 H MET A 4 HA GLU A 69 1.22 REMARK 500 HG1 THR A 126 H GLU A 129 1.28 REMARK 500 HH21 ARG A 97 HD2 PRO A 107 1.28 REMARK 500 HB3 LEU A 91 H ASN A 135 1.32 REMARK 500 HE22 GLN A 93 HB2 PHE A 134 1.34 REMARK 500 O LYS A 10 H VAL A 153 1.46 REMARK 500 ND1 HIS A 136 H LEU A 138 1.46 REMARK 500 O LEU A 19 H GLY A 22 1.46 REMARK 500 O THR A 121 H ASP A 133 1.48 REMARK 500 HD1 HIS A 136 N LEU A 138 1.55 REMARK 500 O THR A 126 H GLU A 129 1.59 REMARK 500 OD2 ASP A 133 HD22 ASN A 135 1.60 REMARK 500 O ARG A 97 H LYS A 101 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 LYS A 7 77.05 -61.23 REMARK 500 1 GLU A 20 1.69 -55.19 REMARK 500 1 TYR A 39 -16.37 -45.59 REMARK 500 1 ALA A 40 174.75 71.96 REMARK 500 1 PRO A 41 -80.79 -72.38 REMARK 500 1 ARG A 43 152.99 -41.89 REMARK 500 1 GLU A 54 -8.60 -151.90 REMARK 500 1 GLN A 56 -78.56 -44.41 REMARK 500 1 GLU A 69 -173.44 -69.20 REMARK 500 1 ALA A 80 -10.66 -49.59 REMARK 500 1 ALA A 83 -93.81 -72.46 REMARK 500 1 ASN A 86 -164.84 46.72 REMARK 500 1 ALA A 99 -16.39 -45.87 REMARK 500 1 GLU A 102 43.77 -90.99 REMARK 500 1 ALA A 103 127.89 -174.94 REMARK 500 1 ASP A 104 -9.28 -49.01 REMARK 500 1 PHE A 105 -14.85 -47.04 REMARK 500 1 GLU A 106 99.85 -4.32 REMARK 500 1 GLU A 109 66.98 -65.81 REMARK 500 1 VAL A 112 73.94 -156.23 REMARK 500 1 GLU A 116 -11.09 166.29 REMARK 500 1 THR A 121 95.54 -62.55 REMARK 500 1 ILE A 122 89.98 -68.98 REMARK 500 1 ASP A 127 0.06 -52.12 REMARK 500 1 ASN A 135 -118.04 55.98 REMARK 500 1 ILE A 147 175.09 -53.31 REMARK 500 1 LYS A 148 96.64 -177.59 REMARK 500 1 VAL A 153 -143.95 -142.28 REMARK 500 2 LYS A 7 70.18 -63.44 REMARK 500 2 ASP A 14 -160.18 -114.55 REMARK 500 2 LYS A 18 -162.75 -123.92 REMARK 500 2 GLU A 20 0.97 -55.02 REMARK 500 2 GLU A 31 -70.78 -52.54 REMARK 500 2 ILE A 38 16.75 -141.85 REMARK 500 2 TYR A 39 -13.25 -47.62 REMARK 500 2 ALA A 40 151.55 71.27 REMARK 500 2 PRO A 41 -82.60 -72.50 REMARK 500 2 VAL A 52 -10.26 -49.08 REMARK 500 2 ASP A 67 55.58 -98.74 REMARK 500 2 VAL A 70 96.63 -68.62 REMARK 500 2 LYS A 82 41.45 -105.67 REMARK 500 2 ALA A 83 -34.27 -159.57 REMARK 500 2 TYR A 84 8.60 -158.89 REMARK 500 2 ASN A 86 167.38 -47.82 REMARK 500 2 MET A 90 11.86 -69.48 REMARK 500 2 ALA A 99 -6.99 -50.56 REMARK 500 2 ALA A 103 -137.51 -100.61 REMARK 500 2 ASP A 104 18.15 -145.72 REMARK 500 2 PHE A 105 -144.07 -133.13 REMARK 500 2 GLU A 106 126.65 -171.21 REMARK 500 REMARK 500 THIS ENTRY HAS 279 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4668 RELATED DB: BMRB REMARK 900 4668 CONTAINS CHEMICAL SHIFTS DBREF 1IX5 A 4 154 UNP O52980 FKBP_METTL 4 154 SEQADV 1IX5 MET A 4 UNP O52980 LEU 4 ENGINEERED MUTATION SEQRES 1 A 151 MET VAL ASP LYS GLY VAL LYS ILE LYS VAL ASP TYR ILE SEQRES 2 A 151 GLY LYS LEU GLU SER GLY ASP VAL PHE ASP THR SER ILE SEQRES 3 A 151 GLU GLU VAL ALA LYS GLU ALA GLY ILE TYR ALA PRO ASP SEQRES 4 A 151 ARG GLU TYR GLU PRO LEU GLU PHE VAL VAL GLY GLU GLY SEQRES 5 A 151 GLN LEU ILE GLN GLY PHE GLU GLU ALA VAL LEU ASP MET SEQRES 6 A 151 GLU VAL GLY ASP GLU LYS THR VAL LYS ILE PRO ALA GLU SEQRES 7 A 151 LYS ALA TYR GLY ASN ARG ASN GLU MET LEU ILE GLN LYS SEQRES 8 A 151 ILE PRO ARG ASP ALA PHE LYS GLU ALA ASP PHE GLU PRO SEQRES 9 A 151 GLU GLU GLY MET VAL ILE LEU ALA GLU GLY ILE PRO ALA SEQRES 10 A 151 THR ILE THR GLU VAL THR ASP ASN GLU VAL THR LEU ASP SEQRES 11 A 151 PHE ASN HIS GLU LEU ALA GLY LYS ASP LEU VAL PHE THR SEQRES 12 A 151 ILE LYS ILE ILE GLU VAL VAL GLU HELIX 1 1 ILE A 29 GLY A 37 1 9 HELIX 2 2 ILE A 58 ASP A 67 1 10 HELIX 3 3 ARG A 97 GLU A 102 1 6 SHEET 1 A 2 LYS A 10 VAL A 13 0 SHEET 2 A 2 LEU A 48 VAL A 51 -1 O PHE A 50 N ILE A 11 SHEET 1 B 2 ILE A 16 GLY A 17 0 SHEET 2 B 2 ASP A 26 THR A 27 -1 O ASP A 26 N GLY A 17 SHEET 1 C 2 THR A 75 ILE A 78 0 SHEET 2 C 2 LEU A 143 THR A 146 -1 O LEU A 143 N ILE A 78 SHEET 1 D 4 ILE A 95 PRO A 96 0 SHEET 2 D 4 GLU A 129 ASP A 133 -1 O VAL A 130 N ILE A 95 SHEET 3 D 4 PRO A 119 THR A 126 -1 N THR A 121 O ASP A 133 SHEET 4 D 4 MET A 111 LEU A 114 -1 N ILE A 113 O ALA A 120 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 - v 10 2 Bytes