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Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN 01-DEC-04 1Y4O TITLE SOLUTION STRUCTURE OF A MOUSE CYTOPLASMIC ROADBLOCK/LC7 DYNEIN LIGHT TITLE 2 CHAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN 2A, CYTOPLASMIC; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: DNCL2A; SOURCE 6 EXPRESSION_SYSTEM: CELL-FREE SYNTHESIS; SOURCE 7 OTHER_DETAILS: WHEAT GERM CELL-FREE, IN VITRO EXPRESSION KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI, CENTER FOR KEYWDS 2 EUKARYOTIC STRUCTURAL GENOMICS, CESG, DYNEIN LIGHT CHAIN, KEYWDS 3 CONTRACTILE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.SONG,R.C.TYLER,M.S.LEE,E.M.TYLER,J.L.MARKLEY,CENTER FOR EUKARYOTIC AUTHOR 2 STRUCTURAL GENOMICS (CESG) REVDAT 5 02-MAR-22 1Y4O 1 REMARK SEQADV REVDAT 4 24-FEB-09 1Y4O 1 VERSN REVDAT 3 29-APR-08 1Y4O 1 SOURCE REVDAT 2 21-FEB-06 1Y4O 1 JRNL REVDAT 1 18-JAN-05 1Y4O 0 JRNL AUTH J.SONG,R.C.TYLER,M.S.LEE,E.M.TYLER,J.L.MARKLEY JRNL TITL SOLUTION STRUCTURE OF ISOFORM 1 OF ROADBLOCK/LC7, A LIGHT JRNL TITL 2 CHAIN IN THE DYNEIN COMPLEX. JRNL REF J.MOL.BIOL. V. 354 1043 2005 JRNL REFN ISSN 0022-2836 JRNL PMID 16289575 JRNL DOI 10.1016/J.JMB.2005.10.017 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1, XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : VARIAN, INC. (VNMR), SCHWIETERS, C.D. ET AL (XPLOR REMARK 3 -NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Y4O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-04. REMARK 100 THE DEPOSITION ID IS D_1000031111. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.2 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 10MM SODIUM ACETATE, 100MM NACL, REMARK 210 0.02% NAN3,90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCACB; 3D CBCA(CO)NH; 3D REMARK 210 HCCH-TOCSY; 3D HNCO; 3D_13C- REMARK 210 SEPARATED_NOESY; 3D_15N- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 97.027.12.56, SPARKY REMARK 210 3.72, CYANA 1.0.6 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7 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: 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-20 REMARK 470 RES CSSEQI ATOMS REMARK 470 GLU A 104 O REMARK 470 GLU B 304 O 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 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 LEU A 8 -64.60 -134.81 REMARK 500 1 ASP A 69 142.91 166.21 REMARK 500 1 PRO A 70 86.58 -60.19 REMARK 500 1 THR B 233 -6.48 -57.95 REMARK 500 1 ASP B 269 147.61 172.79 REMARK 500 1 PRO B 270 50.11 -63.33 REMARK 500 1 PRO B 302 36.83 -62.84 REMARK 500 2 ASP A 69 147.31 168.88 REMARK 500 2 PRO A 70 19.85 -58.27 REMARK 500 2 PRO A 102 101.48 -53.70 REMARK 500 2 HIS B 202 -61.09 70.20 REMARK 500 2 HIS B 203 95.99 -60.61 REMARK 500 2 HIS B 206 108.80 -161.27 REMARK 500 2 LEU B 208 -85.57 56.80 REMARK 500 2 ASP B 269 147.05 169.13 REMARK 500 2 PRO B 270 17.02 -60.77 REMARK 500 2 ASN B 284 -165.14 -105.54 REMARK 500 2 PRO B 302 101.41 -58.70 REMARK 500 3 LEU A 8 -75.72 -94.75 REMARK 500 3 ASP A 69 147.76 168.91 REMARK 500 3 PRO A 70 5.84 -55.48 REMARK 500 3 SER A 81 -167.58 -123.02 REMARK 500 3 LEU B 208 -92.04 39.29 REMARK 500 3 ASP B 269 150.68 169.05 REMARK 500 3 PRO B 270 25.37 -60.63 REMARK 500 4 HIS A 7 -56.45 -175.91 REMARK 500 4 ASP A 69 148.73 172.86 REMARK 500 4 PRO A 70 28.36 -64.46 REMARK 500 4 ASP B 269 143.03 166.84 REMARK 500 4 PRO B 270 29.61 -64.28 REMARK 500 5 GLU A 9 -41.54 -176.72 REMARK 500 5 ASP A 69 147.13 159.26 REMARK 500 5 PRO A 70 25.55 -60.43 REMARK 500 5 PRO A 102 90.33 -67.22 REMARK 500 5 ASP B 269 147.16 165.40 REMARK 500 5 PRO B 270 15.04 -61.17 REMARK 500 5 SER B 281 -165.84 -100.59 REMARK 500 6 SER A 40 99.13 -161.10 REMARK 500 6 ASP A 69 132.29 88.19 REMARK 500 6 PRO A 70 73.34 -66.50 REMARK 500 6 PRO A 102 92.32 -36.95 REMARK 500 6 SER B 240 98.89 -160.67 REMARK 500 6 ASP B 269 135.59 164.16 REMARK 500 6 PRO B 270 96.99 -58.09 REMARK 500 6 GLN B 271 -54.75 -143.87 REMARK 500 6 PRO B 302 83.96 -64.67 REMARK 500 7 LYS A 39 136.03 -171.14 REMARK 500 7 ASP A 69 136.94 170.16 REMARK 500 7 PRO A 70 25.41 -63.15 REMARK 500 7 ASP A 93 -34.82 -137.20 REMARK 500 REMARK 500 THIS ENTRY HAS 178 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 62 0.09 SIDE CHAIN REMARK 500 1 ARG B 262 0.10 SIDE CHAIN REMARK 500 14 ARG A 62 0.08 SIDE CHAIN REMARK 500 14 ARG B 262 0.08 SIDE CHAIN REMARK 500 18 ARG A 62 0.08 SIDE CHAIN REMARK 500 18 ARG B 262 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6396 RELATED DB: BMRB REMARK 900 RELATED ID: GO.34382 RELATED DB: TARGETDB DBREF 1Y4O A 10 104 UNP P62627 DLC2A_MOUSE 2 96 DBREF 1Y4O B 210 304 UNP P62627 DLC2A_MOUSE 2 96 SEQADV 1Y4O GLY A 1 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS A 2 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS A 3 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS A 4 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS A 5 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS A 6 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS A 7 UNP P62627 EXPRESSION TAG SEQADV 1Y4O LEU A 8 UNP P62627 EXPRESSION TAG SEQADV 1Y4O GLU A 9 UNP P62627 EXPRESSION TAG SEQADV 1Y4O GLY B 201 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS B 202 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS B 203 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS B 204 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS B 205 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS B 206 UNP P62627 EXPRESSION TAG SEQADV 1Y4O HIS B 207 UNP P62627 EXPRESSION TAG SEQADV 1Y4O LEU B 208 UNP P62627 EXPRESSION TAG SEQADV 1Y4O GLU B 209 UNP P62627 EXPRESSION TAG SEQRES 1 A 104 GLY HIS HIS HIS HIS HIS HIS LEU GLU ALA GLU VAL GLU SEQRES 2 A 104 GLU THR LEU LYS ARG LEU GLN SER GLN LYS GLY VAL GLN SEQRES 3 A 104 GLY ILE ILE VAL VAL ASN THR GLU GLY ILE PRO ILE LYS SEQRES 4 A 104 SER THR MET ASP ASN PRO THR THR THR GLN TYR ALA ASN SEQRES 5 A 104 LEU MET HIS ASN PHE ILE LEU LYS ALA ARG SER THR VAL SEQRES 6 A 104 ARG GLU ILE ASP PRO GLN ASN ASP LEU THR PHE LEU ARG SEQRES 7 A 104 ILE ARG SER LYS LYS ASN GLU ILE MET VAL ALA PRO ASP SEQRES 8 A 104 LYS ASP TYR PHE LEU ILE VAL ILE GLN ASN PRO THR GLU SEQRES 1 B 104 GLY HIS HIS HIS HIS HIS HIS LEU GLU ALA GLU VAL GLU SEQRES 2 B 104 GLU THR LEU LYS ARG LEU GLN SER GLN LYS GLY VAL GLN SEQRES 3 B 104 GLY ILE ILE VAL VAL ASN THR GLU GLY ILE PRO ILE LYS SEQRES 4 B 104 SER THR MET ASP ASN PRO THR THR THR GLN TYR ALA ASN SEQRES 5 B 104 LEU MET HIS ASN PHE ILE LEU LYS ALA ARG SER THR VAL SEQRES 6 B 104 ARG GLU ILE ASP PRO GLN ASN ASP LEU THR PHE LEU ARG SEQRES 7 B 104 ILE ARG SER LYS LYS ASN GLU ILE MET VAL ALA PRO ASP SEQRES 8 B 104 LYS ASP TYR PHE LEU ILE VAL ILE GLN ASN PRO THR GLU HELIX 1 1 LEU A 8 GLN A 22 1 15 HELIX 2 2 ASP A 43 ASP A 69 1 27 HELIX 3 3 HIS B 207 GLN B 222 1 16 HELIX 4 4 ASP B 243 ILE B 268 1 26 SHEET 1 A10 ILE A 36 SER A 40 0 SHEET 2 A10 VAL A 25 ASN A 32 -1 N VAL A 30 O ILE A 38 SHEET 3 A10 TYR A 94 GLN A 100 -1 O ILE A 99 N GLN A 26 SHEET 4 A10 GLU A 85 PRO A 90 -1 N GLU A 85 O GLN A 100 SHEET 5 A10 LEU A 74 SER A 81 -1 N ILE A 79 O ILE A 86 SHEET 6 A10 LEU B 274 SER B 281 -1 O PHE B 276 N ARG A 80 SHEET 7 A10 GLU B 285 PRO B 290 -1 O ILE B 286 N ILE B 279 SHEET 8 A10 TYR B 294 GLN B 300 -1 O GLN B 300 N GLU B 285 SHEET 9 A10 VAL B 225 ASN B 232 -1 N ILE B 229 O ILE B 297 SHEET 10 A10 PRO B 237 SER B 240 -1 O ILE B 238 N VAL B 230 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