Header list of 1pwj.pdb file
Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN 02-JUL-03 1PWJ
TITLE STRUCTURE OF THE MONOMERIC 8-KDA DYNEIN LIGHT CHAIN AND MECHANISM OF
TITLE 2 DOMAIN SWAPPED DIMER ASSEMBLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MONOMERIC 8KDA DYNEIN LIGHT CHAIN;
COMPND 5 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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS DYNEIN, DYNEIN LIGHT CHAIN, DIMER-MONOMER EQUILIBRIUM, DOMAIN
KEYWDS 2 SWAPPING, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.WANG,K.W.-H.LO,H.-M.KAN,J.-S.FAN,M.ZHANG
REVDAT 3 02-MAR-22 1PWJ 1 REMARK
REVDAT 2 24-FEB-09 1PWJ 1 VERSN
REVDAT 1 21-OCT-03 1PWJ 0
JRNL AUTH W.WANG,K.W.-H.LO,H.-M.KAN,J.-S.FAN,M.ZHANG
JRNL TITL STRUCTURE OF THE MONOMERIC 8-KDA DYNEIN LIGHT CHAIN AND
JRNL TITL 2 MECHANISM OF THE DOMAIN-SWAPPED DIMER ASSEMBLY
JRNL REF J.BIOL.CHEM. V. 278 41491 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12904292
JRNL DOI 10.1074/JBC.M307118200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PWJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019638.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.3
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1MM DLC8B U-15N; 1MM DLC8B U
REMARK 210 -15N, 13C; 1MM DLC8B
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
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, CNS 1.0
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 : NULL
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
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 3 100.31 -177.66
REMARK 500 1 ALA A 6 115.56 -177.78
REMARK 500 1 ASN A 10 114.62 -168.45
REMARK 500 1 SER A 14 38.01 -73.38
REMARK 500 1 GLU A 15 -43.91 68.65
REMARK 500 1 ASN A 33 27.49 -158.04
REMARK 500 1 GLU A 35 -54.46 76.56
REMARK 500 1 LYS A 49 -42.87 -138.00
REMARK 500 1 ASN A 51 142.72 62.50
REMARK 500 1 PRO A 52 173.91 -50.00
REMARK 500 1 TRP A 54 -167.29 -102.32
REMARK 500 1 HIS A 55 90.91 -176.14
REMARK 500 1 ARG A 60 -75.86 -140.97
REMARK 500 1 ASN A 61 23.10 -161.07
REMARK 500 1 TYR A 65 31.60 -165.77
REMARK 500 1 VAL A 66 -72.77 -84.60
REMARK 500 1 GLU A 69 -63.60 -103.88
REMARK 500 1 THR A 70 -116.71 -150.94
REMARK 500 1 LYS A 71 30.61 -154.29
REMARK 500 1 HIS A 72 68.05 -105.94
REMARK 500 1 ILE A 74 110.47 -160.40
REMARK 500 2 ASP A 3 48.16 -93.36
REMARK 500 2 ARG A 4 108.79 78.36
REMARK 500 2 ALA A 6 103.55 169.22
REMARK 500 2 ASN A 10 112.08 -171.90
REMARK 500 2 SER A 14 -95.25 -50.54
REMARK 500 2 GLU A 15 -36.93 -162.99
REMARK 500 2 ASN A 51 161.17 58.98
REMARK 500 2 HIS A 55 85.23 -179.98
REMARK 500 2 VAL A 58 62.39 -119.48
REMARK 500 2 ARG A 60 -65.25 -144.94
REMARK 500 2 ASN A 61 19.30 -156.87
REMARK 500 2 PHE A 62 5.16 -67.49
REMARK 500 2 SER A 64 55.47 -69.08
REMARK 500 2 TYR A 65 35.11 -99.22
REMARK 500 2 GLU A 69 45.49 156.66
REMARK 500 2 THR A 70 -84.05 -94.04
REMARK 500 2 LYS A 71 -12.41 74.84
REMARK 500 2 ILE A 74 113.16 -160.93
REMARK 500 2 PHE A 76 137.49 -170.27
REMARK 500 2 LYS A 87 76.95 -108.25
REMARK 500 3 ASP A 3 90.26 62.29
REMARK 500 3 LYS A 5 50.01 -113.90
REMARK 500 3 ALA A 6 108.86 67.27
REMARK 500 3 LYS A 9 36.40 -98.77
REMARK 500 3 ASN A 10 113.94 95.22
REMARK 500 3 SER A 14 99.71 53.72
REMARK 500 3 ASN A 33 30.07 -141.53
REMARK 500 3 GLU A 35 -52.68 76.83
REMARK 500 3 LYS A 49 -44.15 -130.25
REMARK 500
REMARK 500 THIS ENTRY HAS 380 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F3C RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DLC8 DIMER
REMARK 900 RELATED ID: 1F95 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DLC8/BIM PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1F96 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DLC8/NNOS PEPTIDE COMPLEX
REMARK 900 RELATED ID: 1PWK RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH INSERTION CODE
DBREF 1PWJ A 1 89 UNP Q9D0M5 DYL2_MOUSE 1 89
SEQRES 1 A 89 MET SER ASP ARG LYS ALA VAL ILE LYS ASN ALA ASP MET
SEQRES 2 A 89 SER GLU ASP MET GLN GLN ASP ALA VAL ASP CYS ALA THR
SEQRES 3 A 89 GLN ALA MET GLU LYS TYR ASN ILE GLU LYS ASP ILE ALA
SEQRES 4 A 89 ALA TYR 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
HELIX 1 1 GLU A 15 TYR A 32 1 18
HELIX 2 2 GLU A 35 ASN A 51 1 17
SHEET 1 A 4 VAL A 7 ALA A 11 0
SHEET 2 A 4 HIS A 72 LEU A 78 -1 O TYR A 77 N VAL A 7
SHEET 3 A 4 VAL A 81 LYS A 87 -1 O VAL A 81 N LEU A 78
SHEET 4 A 4 ILE A 57 GLY A 59 -1 N GLY A 59 O ALA A 82
CISPEP 1 PRO A 52 THR A 53 1 -0.04
CISPEP 2 PRO A 52 THR A 53 2 -0.12
CISPEP 3 PRO A 52 THR A 53 3 -0.18
CISPEP 4 PRO A 52 THR A 53 4 -0.08
CISPEP 5 PRO A 52 THR A 53 5 0.00
CISPEP 6 PRO A 52 THR A 53 6 0.10
CISPEP 7 PRO A 52 THR A 53 7 0.07
CISPEP 8 PRO A 52 THR A 53 8 -0.08
CISPEP 9 PRO A 52 THR A 53 9 -0.01
CISPEP 10 PRO A 52 THR A 53 10 0.02
CISPEP 11 PRO A 52 THR A 53 11 -0.03
CISPEP 12 PRO A 52 THR A 53 12 -0.04
CISPEP 13 PRO A 52 THR A 53 13 -0.01
CISPEP 14 PRO A 52 THR A 53 14 -0.06
CISPEP 15 PRO A 52 THR A 53 15 0.02
CISPEP 16 PRO A 52 THR A 53 16 -0.05
CISPEP 17 PRO A 52 THR A 53 17 -0.03
CISPEP 18 PRO A 52 THR A 53 18 -0.11
CISPEP 19 PRO A 52 THR A 53 19 0.07
CISPEP 20 PRO A 52 THR A 53 20 -0.18
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