Header list of 1z09.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSPORT PROTEIN 01-MAR-05 1Z09 TITLE SOLUTION STRUCTURE OF KM23 COMPND MOL_ID: 1; COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN 2A, CYTOPLASMIC; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: LC7 DYNEIN LIGHT CHAIN KM23; COMPND 5 SYNONYM: DYNEIN-ASSOCIATED PROTEIN KM23, BITHORAXOID-LIKE PROTEIN, COMPND 6 BLP, HSPC162; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: DNCL2A, BITH, DNLC2A; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS HOMODIMER, PROTEIN-PROTEIN COMPLEX, KM23, LC7, DYNEIN LIGHT CHAIN, KEYWDS 2 TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR U.ILANGOVAN,W.DING,K.MULDER,A.P.HINCK,J.ZUNIGA,J.A.TRBOVICH, AUTHOR 2 B.DEMELER,J.C.GROPPE REVDAT 4 02-MAR-22 1Z09 1 REMARK REVDAT 3 24-FEB-09 1Z09 1 VERSN REVDAT 2 06-SEP-05 1Z09 1 JRNL REVDAT 1 02-AUG-05 1Z09 0 JRNL AUTH U.ILANGOVAN,W.DING,Y.ZHONG,C.L.WILSON,J.C.GROPPE, JRNL AUTH 2 J.T.TRBOVICH,J.ZUNIGA,B.DEMELER,Q.TANG,G.GAO,K.M.MULDER, JRNL AUTH 3 A.P.HINCK JRNL TITL STRUCTURE AND DYNAMICS OF THE HOMODIMERIC DYNEIN LIGHT CHAIN JRNL TITL 2 KM23. JRNL REF J.MOL.BIOL. V. (2) 338 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 16083906 JRNL DOI 10.1016/J.JMB.2005.07.002 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, XPLOR-NIH 1.0.6 REMARK 3 AUTHORS : BRUKER (XWINNMR), CLORE, M. (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Z09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032134. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 315 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 0 M NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM 15N_KM23; 25 MM SODIUM REMARK 210 ACETATE; PH 6.0; 95 % H2O; 5 % REMARK 210 D2O; 1 MM 13C,15N_KM23; 25 MM REMARK 210 SODIUM ACETATE; PH 6.0; 95 % H2O; REMARK 210 5 % D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.2, NMRVIEW 5.0.4 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10 REMARK 210 REMARK 210 REMARK: FILTERED EXPERIMENTS WERE USED TO GET INTERMOLECULAR NOES 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 B 149 H VAL B 153 1.53 REMARK 500 O ALA A 53 H VAL A 57 1.54 REMARK 500 O LYS B 148 H THR B 152 1.55 REMARK 500 O LYS A 52 H THR A 56 1.55 REMARK 500 O TYR A 42 H MET A 46 1.56 REMARK 500 O TYR B 138 H MET B 142 1.56 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 SER A 13 -72.87 69.62 REMARK 500 1 GLN A 14 -34.58 -173.05 REMARK 500 1 LYS A 15 -19.74 174.14 REMARK 500 1 VAL A 17 93.82 18.25 REMARK 500 1 SER A 32 145.16 -172.23 REMARK 500 1 ASN A 36 -59.83 170.86 REMARK 500 1 ASP A 83 -148.69 -91.36 REMARK 500 1 LYS A 84 -100.03 -68.02 REMARK 500 1 SER B 109 -72.87 69.65 REMARK 500 1 GLN B 110 -34.70 -173.07 REMARK 500 1 LYS B 111 -19.58 174.20 REMARK 500 1 VAL B 113 93.96 18.23 REMARK 500 1 SER B 128 145.23 -172.17 REMARK 500 1 ASN B 132 -59.90 170.86 REMARK 500 1 ASP B 179 -148.69 -91.39 REMARK 500 1 LYS B 180 -99.91 -67.98 REMARK 500 2 SER A 13 98.25 44.47 REMARK 500 2 LYS A 15 -100.57 -49.26 REMARK 500 2 SER A 32 138.27 -171.00 REMARK 500 2 ASP A 35 137.22 89.85 REMARK 500 2 PHE A 68 147.02 -174.86 REMARK 500 2 ASN A 76 -176.41 -175.89 REMARK 500 2 ALA A 81 78.46 -158.79 REMARK 500 2 LYS A 84 -58.84 77.58 REMARK 500 2 ASP A 85 -45.92 -152.15 REMARK 500 2 ASN A 93 -175.81 -177.86 REMARK 500 2 PRO A 94 -162.94 -77.61 REMARK 500 2 THR A 95 -57.46 -155.84 REMARK 500 2 SER B 109 98.28 44.48 REMARK 500 2 LYS B 111 -100.52 -49.21 REMARK 500 2 SER B 128 138.30 -171.01 REMARK 500 2 ASP B 131 137.31 89.84 REMARK 500 2 PHE B 164 147.15 -174.82 REMARK 500 2 ASN B 172 -176.55 -175.94 REMARK 500 2 ALA B 177 78.45 -158.77 REMARK 500 2 LYS B 180 -58.87 77.69 REMARK 500 2 ASP B 181 -45.97 -152.13 REMARK 500 2 ASN B 189 -175.77 -177.76 REMARK 500 2 PRO B 190 -162.90 -77.64 REMARK 500 2 THR B 191 -57.50 -155.90 REMARK 500 3 SER A 13 -69.30 62.68 REMARK 500 3 GLN A 14 -4.84 76.10 REMARK 500 3 ILE A 30 -94.71 -121.15 REMARK 500 3 SER A 32 149.43 -173.07 REMARK 500 3 ASN A 36 -57.11 174.32 REMARK 500 3 ILE A 60 -75.65 -75.95 REMARK 500 3 LYS A 84 -95.41 33.44 REMARK 500 3 SER B 109 -69.35 62.75 REMARK 500 3 GLN B 110 -4.81 76.11 REMARK 500 3 ILE B 126 -94.68 -121.29 REMARK 500 REMARK 500 THIS ENTRY HAS 216 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 10 0.32 SIDE CHAIN REMARK 500 1 ARG A 54 0.17 SIDE CHAIN REMARK 500 1 ARG A 58 0.32 SIDE CHAIN REMARK 500 1 ARG A 70 0.27 SIDE CHAIN REMARK 500 1 ARG A 72 0.32 SIDE CHAIN REMARK 500 1 ARG B 106 0.32 SIDE CHAIN REMARK 500 1 ARG B 150 0.17 SIDE CHAIN REMARK 500 1 ARG B 154 0.32 SIDE CHAIN REMARK 500 1 ARG B 166 0.27 SIDE CHAIN REMARK 500 1 ARG B 168 0.32 SIDE CHAIN REMARK 500 2 ARG A 10 0.28 SIDE CHAIN REMARK 500 2 ARG A 54 0.10 SIDE CHAIN REMARK 500 2 ARG A 58 0.29 SIDE CHAIN REMARK 500 2 ARG A 70 0.32 SIDE CHAIN REMARK 500 2 ARG A 72 0.31 SIDE CHAIN REMARK 500 2 ARG B 106 0.28 SIDE CHAIN REMARK 500 2 ARG B 150 0.10 SIDE CHAIN REMARK 500 2 ARG B 154 0.29 SIDE CHAIN REMARK 500 2 ARG B 166 0.32 SIDE CHAIN REMARK 500 2 ARG B 168 0.31 SIDE CHAIN REMARK 500 3 ARG A 10 0.32 SIDE CHAIN REMARK 500 3 ARG A 54 0.23 SIDE CHAIN REMARK 500 3 ARG A 58 0.31 SIDE CHAIN REMARK 500 3 ARG A 70 0.27 SIDE CHAIN REMARK 500 3 ARG A 72 0.31 SIDE CHAIN REMARK 500 3 ARG B 106 0.32 SIDE CHAIN REMARK 500 3 ARG B 150 0.23 SIDE CHAIN REMARK 500 3 ARG B 154 0.31 SIDE CHAIN REMARK 500 3 ARG B 166 0.27 SIDE CHAIN REMARK 500 3 ARG B 168 0.31 SIDE CHAIN REMARK 500 4 ARG A 10 0.31 SIDE CHAIN REMARK 500 4 ARG A 54 0.23 SIDE CHAIN REMARK 500 4 ARG A 58 0.29 SIDE CHAIN REMARK 500 4 ARG A 70 0.18 SIDE CHAIN REMARK 500 4 ARG A 72 0.31 SIDE CHAIN REMARK 500 4 ARG B 106 0.31 SIDE CHAIN REMARK 500 4 ARG B 150 0.23 SIDE CHAIN REMARK 500 4 ARG B 154 0.29 SIDE CHAIN REMARK 500 4 ARG B 166 0.18 SIDE CHAIN REMARK 500 4 ARG B 168 0.30 SIDE CHAIN REMARK 500 5 ARG A 10 0.26 SIDE CHAIN REMARK 500 5 ARG A 54 0.22 SIDE CHAIN REMARK 500 5 ARG A 58 0.22 SIDE CHAIN REMARK 500 5 ARG A 70 0.28 SIDE CHAIN REMARK 500 5 ARG A 72 0.32 SIDE CHAIN REMARK 500 5 ARG B 106 0.26 SIDE CHAIN REMARK 500 5 ARG B 150 0.22 SIDE CHAIN REMARK 500 5 ARG B 154 0.22 SIDE CHAIN REMARK 500 5 ARG B 166 0.28 SIDE CHAIN REMARK 500 5 ARG B 168 0.32 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 100 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1Z09 A 1 96 UNP Q9NP97 DLC2A_HUMAN 1 96 DBREF 1Z09 B 97 192 UNP Q9NP97 DLC2A_HUMAN 1 96 SEQRES 1 A 96 MET ALA GLU VAL GLU GLU THR LEU LYS ARG LEU GLN SER SEQRES 2 A 96 GLN LYS GLY VAL GLN GLY ILE ILE VAL VAL ASN THR GLU SEQRES 3 A 96 GLY ILE PRO ILE LYS SER THR MET ASP ASN PRO THR THR SEQRES 4 A 96 THR GLN TYR ALA SER LEU MET HIS SER PHE ILE LEU LYS SEQRES 5 A 96 ALA ARG SER THR VAL ARG ASP ILE ASP PRO GLN ASN ASP SEQRES 6 A 96 LEU THR PHE LEU ARG ILE ARG SER LYS LYS ASN GLU ILE SEQRES 7 A 96 MET VAL ALA PRO ASP LYS ASP TYR PHE LEU ILE VAL ILE SEQRES 8 A 96 GLN ASN PRO THR GLU SEQRES 1 B 96 MET ALA GLU VAL GLU GLU THR LEU LYS ARG LEU GLN SER SEQRES 2 B 96 GLN LYS GLY VAL GLN GLY ILE ILE VAL VAL ASN THR GLU SEQRES 3 B 96 GLY ILE PRO ILE LYS SER THR MET ASP ASN PRO THR THR SEQRES 4 B 96 THR GLN TYR ALA SER LEU MET HIS SER PHE ILE LEU LYS SEQRES 5 B 96 ALA ARG SER THR VAL ARG ASP ILE ASP PRO GLN ASN ASP SEQRES 6 B 96 LEU THR PHE LEU ARG ILE ARG SER LYS LYS ASN GLU ILE SEQRES 7 B 96 MET VAL ALA PRO ASP LYS ASP TYR PHE LEU ILE VAL ILE SEQRES 8 B 96 GLN ASN PRO THR GLU HELIX 1 1 MET A 1 LEU A 11 1 11 HELIX 2 2 ASN A 36 ASP A 61 1 26 HELIX 3 3 MET B 97 LEU B 107 1 11 HELIX 4 4 ASN B 132 ASP B 157 1 26 SHEET 1 A10 PRO A 29 SER A 32 0 SHEET 2 A10 GLY A 19 ASN A 24 -1 N VAL A 22 O LYS A 31 SHEET 3 A10 TYR A 86 ILE A 91 -1 O PHE A 87 N VAL A 23 SHEET 4 A10 ILE A 78 PRO A 82 -1 N MET A 79 O VAL A 90 SHEET 5 A10 LEU A 69 ILE A 71 -1 N ILE A 71 O ILE A 78 SHEET 6 A10 LEU B 165 ILE B 167 -1 O ARG B 166 N ARG A 70 SHEET 7 A10 ILE B 174 PRO B 178 -1 O ILE B 174 N ILE B 167 SHEET 8 A10 TYR B 182 ILE B 187 -1 O VAL B 186 N MET B 175 SHEET 9 A10 GLY B 115 ASN B 120 -1 N VAL B 119 O PHE B 183 SHEET 10 A10 PRO B 125 SER B 128 -1 O LYS B 127 N VAL B 118 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