Header list of 1xdx.pdb file
Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN 08-SEP-04 1XDX TITLE SOLUTION STRUCTURE OF THE TCTEX1 LIGHT CHAIN FROM CHLAMYDOMONAS INNER TITLE 2 DYNEIN ARM I1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: TCTEX1 LIGHT CHAIN PROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII; SOURCE 3 ORGANISM_TAXID: 3055; SOURCE 4 GENE: AF039437; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21 CELLS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23D; SOURCE 10 OTHER_DETAILS: FLAGELLA INNER DYNEIN ARM I1 KEYWDS CHLAMYDOMONAS FLAGELLA, TCTEX1 DIMER, NMR SOLUTION STRUCTURE, KEYWDS 2 CONTRACTILE PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR H.WU,M.W.MACIEJEWSKI,S.TAKEBE,S.M.KING REVDAT 3 02-MAR-22 1XDX 1 REMARK REVDAT 2 24-FEB-09 1XDX 1 VERSN REVDAT 1 01-MAR-05 1XDX 0 JRNL AUTH H.WU,M.W.MACIEJEWSKI,S.TAKEBE,S.M.KING JRNL TITL SOLUTION STRUCTURE OF THE TCTEX1 DIMER REVEALS A MECHANISM JRNL TITL 2 FOR DYNEIN-CARGO INTERACTIONS JRNL REF STRUCTURE V. 13 213 2005 JRNL REFN ISSN 0969-2126 JRNL PMID 15698565 JRNL DOI 10.1016/J.STR.2004.11.013 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.851 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XDX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-04. REMARK 100 THE DEPOSITION ID IS D_1000030251. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : ~0.7 MM TCTEX1 PROTEIN; U REMARK 210 -15N,13C; 20 MM NA PHOSPHATE; PH REMARK 210 6.7; 100MM NACL; 20MM DTT; 90% REMARK 210 H2O, 10% D2O; ~0.7 MM TCTEX1 REMARK 210 PROTEIN; U-15N,13C; 20 MM NA REMARK 210 PHOSPHATE; PH 6.7; 100MM NACL; REMARK 210 20MM DTT; >99% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.1, XEASY 1.4, CYANA REMARK 210 1.1 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 90 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH REMARK 210 THE LEAST RESTRAINT VIOLATIONS 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 ALA A 81 H CYS B 68 0.46 REMARK 500 H CYS A 68 O ALA B 81 0.46 REMARK 500 H SER A 83 O VAL B 66 0.58 REMARK 500 O VAL A 66 H SER B 83 0.58 REMARK 500 O CYS A 68 H ALA B 81 0.60 REMARK 500 H ALA A 81 O CYS B 68 0.61 REMARK 500 HA THR A 67 HA ALA B 82 0.69 REMARK 500 HA ALA A 82 HA THR B 67 0.69 REMARK 500 HD23 LEU A 78 HD23 LEU B 78 0.94 REMARK 500 H ILE A 70 O HIS B 79 1.15 REMARK 500 O HIS A 79 H ILE B 70 1.15 REMARK 500 HB2 SER A 83 HB3 LEU B 48 1.16 REMARK 500 HB3 LEU A 48 HB2 SER B 83 1.16 REMARK 500 HD21 LEU A 78 HD21 LEU B 78 1.17 REMARK 500 HB2 ALA A 82 HG1 THR B 67 1.21 REMARK 500 HG1 THR A 67 HB2 ALA B 82 1.21 REMARK 500 HE1 TRP A 85 OH TYR B 64 1.21 REMARK 500 OH TYR A 64 HE1 TRP B 85 1.21 REMARK 500 HG22 THR A 80 HG13 ILE B 69 1.22 REMARK 500 HG13 ILE A 69 HG22 THR B 80 1.22 REMARK 500 HA ILE A 69 HA THR B 80 1.26 REMARK 500 HA THR A 80 HA ILE B 69 1.26 REMARK 500 OD1 ASP A 87 HZ2 LYS B 63 1.30 REMARK 500 HZ2 LYS A 63 OD1 ASP B 87 1.30 REMARK 500 HD1 TRP A 85 HE1 TYR B 64 1.31 REMARK 500 HE1 TYR A 64 HD1 TRP B 85 1.31 REMARK 500 HG12 ILE A 70 HB3 HIS B 79 1.31 REMARK 500 HB3 HIS A 79 HG12 ILE B 70 1.32 REMARK 500 OD2 ASP A 87 HZ3 LYS B 63 1.38 REMARK 500 HZ3 LYS A 63 OD2 ASP B 87 1.38 REMARK 500 CD2 LEU A 78 HD23 LEU B 78 1.39 REMARK 500 HD23 LEU A 78 CD2 LEU B 78 1.39 REMARK 500 O ALA A 81 N CYS B 68 1.39 REMARK 500 N CYS A 68 O ALA B 81 1.39 REMARK 500 O CYS A 68 N ALA B 81 1.39 REMARK 500 N ALA A 81 O CYS B 68 1.40 REMARK 500 N SER A 83 O VAL B 66 1.43 REMARK 500 O VAL A 66 N SER B 83 1.43 REMARK 500 CG ASP A 87 HZ3 LYS B 63 1.43 REMARK 500 HZ3 LYS A 63 CG ASP B 87 1.43 REMARK 500 HH TYR A 64 CZ2 TRP B 85 1.45 REMARK 500 CZ2 TRP A 85 HH TYR B 64 1.45 REMARK 500 OG1 THR A 67 HB2 ALA B 82 1.49 REMARK 500 HB2 ALA A 82 OG1 THR B 67 1.49 REMARK 500 O SER A 83 H VAL B 66 1.49 REMARK 500 H VAL A 66 O SER B 83 1.49 REMARK 500 HB2 HIS A 79 CG1 ILE B 70 1.50 REMARK 500 CG1 ILE A 70 HB2 HIS B 79 1.50 REMARK 500 NE1 TRP A 85 OH TYR B 64 1.51 REMARK 500 OH TYR A 64 NE1 TRP B 85 1.51 REMARK 500 REMARK 500 THIS ENTRY HAS 666 CLOSE CONTACTS 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 GLU A 2 -70.48 -123.08 REMARK 500 1 ALA A 12 -169.50 44.56 REMARK 500 1 LYS A 60 110.55 -178.48 REMARK 500 1 PRO A 61 -159.17 -66.64 REMARK 500 1 PHE A 62 -67.96 -97.83 REMARK 500 1 LYS A 73 -168.67 59.84 REMARK 500 1 TRP A 85 -161.32 -75.51 REMARK 500 1 ASP A 87 89.84 176.86 REMARK 500 1 SER A 93 96.38 45.12 REMARK 500 1 ASN A 100 -60.91 -125.32 REMARK 500 1 LYS A 101 -44.71 -135.27 REMARK 500 1 SER A 102 -47.36 -150.18 REMARK 500 1 GLU B 2 -70.47 -123.04 REMARK 500 1 ALA B 12 -169.48 44.45 REMARK 500 1 LYS B 60 110.53 -178.56 REMARK 500 1 PRO B 61 -159.17 -66.66 REMARK 500 1 PHE B 62 -68.06 -97.78 REMARK 500 1 LYS B 73 -168.65 59.91 REMARK 500 1 TRP B 85 -161.33 -75.61 REMARK 500 1 ASP B 87 89.75 176.84 REMARK 500 1 SER B 93 96.41 45.12 REMARK 500 1 ASN B 100 -60.90 -125.32 REMARK 500 1 LYS B 101 -44.67 -135.34 REMARK 500 1 SER B 102 -47.48 -150.19 REMARK 500 2 ALA A 7 88.97 62.31 REMARK 500 2 GLU A 9 69.73 -113.13 REMARK 500 2 ALA A 12 156.17 58.46 REMARK 500 2 PHE A 13 17.66 -143.06 REMARK 500 2 GLN A 33 -91.65 -142.80 REMARK 500 2 ASN A 59 93.45 48.27 REMARK 500 2 LYS A 60 103.69 -177.08 REMARK 500 2 PRO A 61 -75.97 -84.99 REMARK 500 2 PHE A 62 -69.77 -141.60 REMARK 500 2 LYS A 73 -177.87 61.36 REMARK 500 2 TRP A 85 -166.68 -75.80 REMARK 500 2 ASP A 87 103.87 177.38 REMARK 500 2 THR A 90 65.28 -105.24 REMARK 500 2 ASN A 100 -76.89 -120.73 REMARK 500 2 SER A 102 -47.40 -152.61 REMARK 500 2 ALA B 7 88.98 62.29 REMARK 500 2 GLU B 9 69.75 -113.18 REMARK 500 2 ALA B 12 156.13 58.51 REMARK 500 2 PHE B 13 17.79 -142.98 REMARK 500 2 GLN B 33 -91.51 -142.86 REMARK 500 2 ASN B 59 93.40 48.37 REMARK 500 2 LYS B 60 103.79 -177.13 REMARK 500 2 PRO B 61 -75.95 -84.94 REMARK 500 2 PHE B 62 -69.76 -141.61 REMARK 500 2 LYS B 73 -177.74 61.28 REMARK 500 2 TRP B 85 -166.74 -75.87 REMARK 500 REMARK 500 THIS ENTRY HAS 469 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1XDX A 1 114 UNP O64980 O64980_CHLRE 1 114 DBREF 1XDX B 1 114 UNP O64980 O64980_CHLRE 1 114 SEQRES 1 A 114 MET GLU GLY VAL ASP PRO ALA VAL GLU GLU ALA ALA PHE SEQRES 2 A 114 VAL ALA ASP ASP VAL SER ASN ILE ILE LYS GLU SER ILE SEQRES 3 A 114 ASP ALA VAL LEU GLN ASN GLN GLN TYR SER GLU ALA LYS SEQRES 4 A 114 VAL SER GLN TRP THR SER SER CYS LEU GLU HIS CYS ILE SEQRES 5 A 114 LYS ARG LEU THR ALA LEU ASN LYS PRO PHE LYS TYR VAL SEQRES 6 A 114 VAL THR CYS ILE ILE MET GLN LYS ASN GLY ALA GLY LEU SEQRES 7 A 114 HIS THR ALA ALA SER CYS TRP TRP ASP SER THR THR ASP SEQRES 8 A 114 GLY SER ARG THR VAL ARG TRP GLU ASN LYS SER MET TYR SEQRES 9 A 114 CYS ILE CYS THR VAL PHE GLY LEU ALA ILE SEQRES 1 B 114 MET GLU GLY VAL ASP PRO ALA VAL GLU GLU ALA ALA PHE SEQRES 2 B 114 VAL ALA ASP ASP VAL SER ASN ILE ILE LYS GLU SER ILE SEQRES 3 B 114 ASP ALA VAL LEU GLN ASN GLN GLN TYR SER GLU ALA LYS SEQRES 4 B 114 VAL SER GLN TRP THR SER SER CYS LEU GLU HIS CYS ILE SEQRES 5 B 114 LYS ARG LEU THR ALA LEU ASN LYS PRO PHE LYS TYR VAL SEQRES 6 B 114 VAL THR CYS ILE ILE MET GLN LYS ASN GLY ALA GLY LEU SEQRES 7 B 114 HIS THR ALA ALA SER CYS TRP TRP ASP SER THR THR ASP SEQRES 8 B 114 GLY SER ARG THR VAL ARG TRP GLU ASN LYS SER MET TYR SEQRES 9 B 114 CYS ILE CYS THR VAL PHE GLY LEU ALA ILE HELIX 1 1 ALA A 15 ASN A 32 1 18 HELIX 2 2 SER A 36 ASN A 59 1 24 HELIX 3 3 ALA B 15 ASN B 32 1 18 HELIX 4 4 SER B 36 ASN B 59 1 24 SHEET 1 A 4 ARG A 94 GLU A 99 0 SHEET 2 A 4 TYR A 104 LEU A 112 -1 O CYS A 105 N TRP A 98 SHEET 3 A 4 LYS A 63 MET A 71 -1 N THR A 67 O THR A 108 SHEET 4 A 4 HIS B 79 CYS B 84 -1 O SER B 83 N VAL A 66 SHEET 1 B 4 HIS A 79 CYS A 84 0 SHEET 2 B 4 LYS B 63 MET B 71 -1 O CYS B 68 N ALA A 81 SHEET 3 B 4 TYR B 104 LEU B 112 -1 O THR B 108 N THR B 67 SHEET 4 B 4 ARG B 94 GLU B 99 -1 N TRP B 98 O CYS B 105 CISPEP 1 LYS A 60 PRO A 61 1 0.05 CISPEP 2 LYS B 60 PRO B 61 1 0.06 CISPEP 3 LYS A 60 PRO A 61 2 0.17 CISPEP 4 LYS B 60 PRO B 61 2 0.11 CISPEP 5 LYS A 60 PRO A 61 3 0.09 CISPEP 6 LYS B 60 PRO B 61 3 0.15 CISPEP 7 LYS A 60 PRO A 61 4 -0.21 CISPEP 8 LYS B 60 PRO B 61 4 -0.09 CISPEP 9 LYS A 60 PRO A 61 5 0.46 CISPEP 10 LYS B 60 PRO B 61 5 0.35 CISPEP 11 LYS A 60 PRO A 61 6 0.02 CISPEP 12 LYS B 60 PRO B 61 6 0.06 CISPEP 13 LYS A 60 PRO A 61 7 0.07 CISPEP 14 LYS B 60 PRO B 61 7 0.05 CISPEP 15 LYS A 60 PRO A 61 8 0.25 CISPEP 16 LYS B 60 PRO B 61 8 0.30 CISPEP 17 LYS A 60 PRO A 61 9 -0.09 CISPEP 18 LYS B 60 PRO B 61 9 -0.11 CISPEP 19 LYS A 60 PRO A 61 10 -0.14 CISPEP 20 LYS B 60 PRO B 61 10 -0.17 CISPEP 21 LYS A 60 PRO A 61 11 0.05 CISPEP 22 LYS B 60 PRO B 61 11 0.03 CISPEP 23 LYS A 60 PRO A 61 12 0.14 CISPEP 24 LYS B 60 PRO B 61 12 0.05 CISPEP 25 LYS A 60 PRO A 61 13 -0.17 CISPEP 26 LYS B 60 PRO B 61 13 -0.05 CISPEP 27 LYS A 60 PRO A 61 14 -0.14 CISPEP 28 LYS B 60 PRO B 61 14 -0.22 CISPEP 29 LYS A 60 PRO A 61 15 0.07 CISPEP 30 LYS B 60 PRO B 61 15 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 2 2 Bytes