Header list of 1f3c.pdb file
Complete list - b 16 2 Bytes
HEADER CONTRACTILE PROTEIN 02-JUN-00 1F3C TITLE REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8) COMPND MOL_ID: 1; COMPND 2 MOLECULE: DYNEIN; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: 8KDA LIGHT CHAIN; COMPND 5 SYNONYM: PROTEIN INHIBITOR OF NEURONAL NITRIC OXIDE SYNTHASE; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DYNEIN, LIGHT CHAIN, DLC8, MICROTUBULES, CONTRACTILE PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.-S.FAN,Q.ZHANG,H.TOCHIO,M.ZHANG REVDAT 4 16-FEB-22 1F3C 1 REMARK REVDAT 3 24-FEB-09 1F3C 1 VERSN REVDAT 2 01-APR-03 1F3C 1 JRNL REVDAT 1 28-FEB-01 1F3C 0 SPRSDE 28-FEB-01 1F3C 1BKQ JRNL AUTH J.FAN,Q.ZHANG,H.TOCHIO,M.LI,M.ZHANG JRNL TITL STRUCTURAL BASIS OF DIVERSE SEQUENCE-DEPENDENT TARGET JRNL TITL 2 RECOGNITION BY THE 8 KDA DYNEIN LIGHT CHAIN. JRNL REF J.MOL.BIOL. V. 306 97 2001 JRNL REFN ISSN 0022-2836 JRNL PMID 11178896 JRNL DOI 10.1006/JMBI.2000.4374 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.8 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1F3C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-00. REMARK 100 THE DEPOSITION ID IS D_1000011192. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : 1.5MM DLC8; 100MM PHOSPHATE REMARK 210 BUFFER NA; 99.99% D2O; 1.5MM REMARK 210 DLC8 U-15N;100MM PHOSPHATE REMARK 210 BUFFER NA; 90% H2O, 10% D2O; REMARK 210 1.5MM DLC8 U-15N,13C;100MM REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.7, X-PLOR 3.8 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 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 HA ALA A 6 HA LEU A 78 1.18 REMARK 500 HE2 PHE A 62 HB3 SER A 64 1.23 REMARK 500 HB ILE B 34 HB2 ASP B 37 1.24 REMARK 500 HA ALA B 6 HA LEU B 78 1.25 REMARK 500 HE2 PHE B 62 HB3 SER B 64 1.26 REMARK 500 HA THR A 26 HD12 LEU A 29 1.27 REMARK 500 HG22 ILE A 74 HE1 PHE A 76 1.28 REMARK 500 HG13 VAL B 81 H ALA B 82 1.28 REMARK 500 HE2 PHE A 86 HD2 HIS B 55 1.30 REMARK 500 HD1 PHE A 73 HB3 PHE A 86 1.32 REMARK 500 HG22 ILE A 57 HG23 ILE B 57 1.34 REMARK 500 HB2 SER A 14 HG3 MET A 17 1.35 REMARK 500 HG22 ILE A 42 HD11 LEU A 85 1.35 REMARK 500 HG13 ILE A 57 HG13 ILE B 57 1.35 REMARK 500 HB2 SER A 64 HD21 LEU A 84 1.35 REMARK 500 HB2 ALA A 28 HB3 HIS A 41 1.35 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 ASP A 3 -135.28 -85.99 REMARK 500 1 ARG A 4 11.40 51.71 REMARK 500 1 LYS A 5 43.09 -74.76 REMARK 500 1 ASN A 10 112.25 -176.32 REMARK 500 1 GLU A 15 -77.69 -41.81 REMARK 500 1 GLU A 16 -19.46 -45.95 REMARK 500 1 GLU A 35 -82.72 -28.47 REMARK 500 1 ILE A 42 -71.50 -61.10 REMARK 500 1 TYR A 50 -66.75 -144.61 REMARK 500 1 ASN A 51 109.18 162.57 REMARK 500 1 ASN A 61 25.46 168.61 REMARK 500 1 PHE A 62 -166.95 -109.34 REMARK 500 1 HIS A 68 -179.24 -55.68 REMARK 500 1 GLU A 69 -166.74 176.38 REMARK 500 1 THR A 70 -100.23 58.86 REMARK 500 1 LYS A 71 28.63 179.15 REMARK 500 1 LEU A 78 173.74 -58.86 REMARK 500 1 GLN A 80 25.58 -144.80 REMARK 500 1 ASP B 3 -113.27 53.93 REMARK 500 1 ARG B 4 72.07 53.03 REMARK 500 1 LYS B 5 47.21 -93.51 REMARK 500 1 ILE B 8 157.33 -34.10 REMARK 500 1 LYS B 9 -15.08 -146.40 REMARK 500 1 ASN B 10 102.62 179.81 REMARK 500 1 ASP B 12 30.60 -89.21 REMARK 500 1 GLU B 35 -68.85 -29.83 REMARK 500 1 ILE B 42 -70.11 -43.59 REMARK 500 1 TYR B 50 -65.35 -120.02 REMARK 500 1 ASN B 51 110.19 160.27 REMARK 500 1 ARG B 60 10.71 -162.63 REMARK 500 1 ASN B 61 30.70 175.98 REMARK 500 1 PHE B 62 -166.64 -102.13 REMARK 500 1 THR B 70 -136.57 -170.16 REMARK 500 1 LYS B 71 12.47 -146.43 REMARK 500 1 GLN B 80 37.18 -149.56 REMARK 500 2 CYS A 2 -50.32 -133.49 REMARK 500 2 ASP A 3 136.27 175.36 REMARK 500 2 ILE A 8 162.15 -43.92 REMARK 500 2 LYS A 9 -22.42 -149.82 REMARK 500 2 ALA A 11 127.97 166.54 REMARK 500 2 GLU A 35 -72.71 -22.50 REMARK 500 2 LYS A 43 -70.90 -59.47 REMARK 500 2 TYR A 50 -67.30 -149.10 REMARK 500 2 ASN A 51 108.52 160.93 REMARK 500 2 PRO A 52 155.76 -43.85 REMARK 500 2 ARG A 60 5.64 -160.02 REMARK 500 2 ASN A 61 33.30 166.70 REMARK 500 2 TYR A 65 56.81 -164.22 REMARK 500 2 HIS A 68 -97.36 -175.68 REMARK 500 2 GLU A 69 75.28 43.75 REMARK 500 REMARK 500 THIS ENTRY HAS 818 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1F3C A 1 89 UNP P63170 DYL1_RAT 1 89 DBREF 1F3C B 1 89 UNP P63170 DYL1_RAT 1 89 SEQRES 1 A 89 MET CYS ASP ARG LYS ALA VAL ILE LYS ASN ALA ASP MET SEQRES 2 A 89 SER GLU GLU MET GLN GLN ASP SER VAL GLU CYS ALA THR SEQRES 3 A 89 GLN ALA LEU GLU LYS TYR ASN ILE GLU LYS ASP ILE ALA SEQRES 4 A 89 ALA HIS ILE LYS LYS GLU PHE ASP LYS LYS TYR ASN PRO SEQRES 5 A 89 THR TRP HIS CYS ILE VAL GLY ARG ASN PHE GLY SER TYR SEQRES 6 A 89 VAL THR HIS GLU THR LYS HIS PHE ILE TYR PHE TYR LEU SEQRES 7 A 89 GLY GLN VAL ALA ILE LEU LEU PHE LYS SER GLY SEQRES 1 B 89 MET CYS ASP ARG LYS ALA VAL ILE LYS ASN ALA ASP MET SEQRES 2 B 89 SER GLU GLU MET GLN GLN ASP SER VAL GLU CYS ALA THR SEQRES 3 B 89 GLN ALA LEU GLU LYS TYR ASN ILE GLU LYS ASP ILE ALA SEQRES 4 B 89 ALA HIS ILE LYS LYS GLU PHE ASP LYS LYS TYR ASN PRO SEQRES 5 B 89 THR TRP HIS CYS ILE VAL GLY ARG ASN PHE GLY SER TYR SEQRES 6 B 89 VAL THR HIS GLU THR LYS HIS PHE ILE TYR PHE TYR LEU SEQRES 7 B 89 GLY GLN VAL ALA ILE LEU LEU PHE LYS SER GLY HELIX 1 1 SER A 14 TYR A 32 1 19 HELIX 2 2 ILE A 34 TYR A 50 1 17 HELIX 3 3 SER B 14 TYR B 32 1 19 HELIX 4 4 ILE B 34 TYR B 50 1 17 SHEET 1 A 5 ASN A 10 ALA A 11 0 SHEET 2 A 5 PHE A 73 PHE A 76 -1 O TYR A 75 N ASN A 10 SHEET 3 A 5 ALA A 82 LYS A 87 -1 N ILE A 83 O PHE A 76 SHEET 4 A 5 TRP A 54 GLY A 59 -1 N HIS A 55 O PHE A 86 SHEET 5 A 5 PHE B 62 TYR B 65 -1 O GLY B 63 N VAL A 58 SHEET 1 B 5 GLY A 63 TYR A 65 0 SHEET 2 B 5 TRP B 54 GLY B 59 -1 O CYS B 56 N TYR A 65 SHEET 3 B 5 VAL B 81 LYS B 87 -1 N ALA B 82 O GLY B 59 SHEET 4 B 5 ILE B 74 LEU B 78 -1 N ILE B 74 O LEU B 85 SHEET 5 B 5 ASN B 10 ALA B 11 -1 N ASN B 10 O TYR B 75 CISPEP 1 PRO A 52 THR A 53 1 -0.21 CISPEP 2 PRO B 52 THR B 53 1 -0.10 CISPEP 3 PRO A 52 THR A 53 2 -0.05 CISPEP 4 PRO B 52 THR B 53 2 0.19 CISPEP 5 PRO A 52 THR A 53 3 -0.02 CISPEP 6 PRO B 52 THR B 53 3 0.24 CISPEP 7 PRO A 52 THR A 53 4 0.03 CISPEP 8 PRO B 52 THR B 53 4 0.17 CISPEP 9 PRO A 52 THR A 53 5 -0.05 CISPEP 10 PRO B 52 THR B 53 5 -0.02 CISPEP 11 PRO A 52 THR A 53 6 0.05 CISPEP 12 PRO B 52 THR B 53 6 0.08 CISPEP 13 PRO A 52 THR A 53 7 -0.31 CISPEP 14 PRO B 52 THR B 53 7 0.02 CISPEP 15 PRO A 52 THR A 53 8 -0.05 CISPEP 16 PRO B 52 THR B 53 8 0.07 CISPEP 17 PRO A 52 THR A 53 9 -0.04 CISPEP 18 PRO B 52 THR B 53 9 -0.01 CISPEP 19 PRO A 52 THR A 53 10 0.02 CISPEP 20 PRO B 52 THR B 53 10 0.11 CISPEP 21 PRO A 52 THR A 53 11 -0.10 CISPEP 22 PRO B 52 THR B 53 11 0.11 CISPEP 23 PRO A 52 THR A 53 12 0.06 CISPEP 24 PRO B 52 THR B 53 12 0.12 CISPEP 25 PRO A 52 THR A 53 13 -0.03 CISPEP 26 PRO B 52 THR B 53 13 0.04 CISPEP 27 PRO A 52 THR A 53 14 -0.10 CISPEP 28 PRO B 52 THR B 53 14 0.07 CISPEP 29 PRO A 52 THR A 53 15 -0.08 CISPEP 30 PRO B 52 THR B 53 15 0.14 CISPEP 31 PRO A 52 THR A 53 16 -0.10 CISPEP 32 PRO B 52 THR B 53 16 0.04 CISPEP 33 PRO A 52 THR A 53 17 0.05 CISPEP 34 PRO B 52 THR B 53 17 0.04 CISPEP 35 PRO A 52 THR A 53 18 0.17 CISPEP 36 PRO B 52 THR B 53 18 0.09 CISPEP 37 PRO A 52 THR A 53 19 -0.02 CISPEP 38 PRO B 52 THR B 53 19 -0.14 CISPEP 39 PRO A 52 THR A 53 20 -0.15 CISPEP 40 PRO B 52 THR B 53 20 0.03 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 - b 16 2 Bytes