Header list of 1re6.pdb file
Complete list - r 2 2 Bytes
HEADER CONTRACTILE PROTEIN 06-NOV-03 1RE6
TITLE LOCALISATION OF DYNEIN LIGHT CHAINS 1 AND 2 AND THEIR PRO-APOPTOTIC
TITLE 2 LIGANDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN 2;
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: DLC2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-3
KEYWDS DYNEIN LIGHT CHAIN, APOPTOSIS, DIMER, CONTRACTILE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.L.DAY,H.PUTHALAKATH,G.SKEA,A.STRASSER,I.BARSUKOV,L.Y.LIAN,
AUTHOR 2 D.C.HUANG,M.G.HINDS
REVDAT 3 02-MAR-22 1RE6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RE6 1 VERSN
REVDAT 1 23-MAR-04 1RE6 0
JRNL AUTH C.L.DAY,H.PUTHALAKATH,G.SKEA,A.STRASSER,I.BARSUKOV,L.Y.LIAN,
JRNL AUTH 2 D.C.HUANG,M.G.HINDS
JRNL TITL LOCALIZATION OF DYNEIN LIGHT CHAINS 1 AND 2 AND THEIR
JRNL TITL 2 PRO-APOPTOTIC LIGANDS.
JRNL REF BIOCHEM.J. V. 377 597 2004
JRNL REFN ISSN 0264-6021
JRNL PMID 14561217
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER AG (XWINNMR), BRUNGER, ADAMS, CLORE,
REMARK 3 DELANO, GROS, GROSSE-KUNSTLEVE, JIANG, KUSEWSKI,
REMARK 3 NILGES, PANNU, READ, RICE, SIMONSON, WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1602 RESTRAINTS, 1417 ARE NOE DERIVED DISTANCE CONSTRAINTS,99
REMARK 3 ARE INTERPROTOMER DISTANCE CONSTRAINTS, 127 ARE DIHEDRAL ANGLE
REMARK 3 RESTRAINTS AND 29 HYDROGEN BONDS.
REMARK 4
REMARK 4 1RE6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020678.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 6.7; 6.7; 6.7
REMARK 210 IONIC STRENGTH : 120MM; 120MM; 120MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DLC2, 50MM SODIUM PHOSPHATE
REMARK 210 BUFFER PH 6.7, 70MM NACL, 2MM
REMARK 210 TCEP, 0.04% SODIUM AZIDE, 95%
REMARK 210 H2O, 5% D2O; 1MM U-15N DLC2,
REMARK 210 50MM SODIUM PHOSPHATE BUFFER PH
REMARK 210 6.7, 70MM NACL, 2MM TCEP, 0.04%
REMARK 210 SODIUM AZIDE, 95% H2O, 5% D2O;
REMARK 210 1MM U-13C,15N DLC2, 50MM SODIUM
REMARK 210 PHOSPHATE BUFFER PH 6.7, 70MM
REMARK 210 NACL, 2MM TCEP, 0.04% SODIUM
REMARK 210 AZIDE, 95% H2O, 5% 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 : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, XEASY 1.3, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 256
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD 2D AND 3D
REMARK 210 HETERONUCLEAR TECHNIQUES
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 HD21 ASN B 10 HD1 TYR B 75 1.31
REMARK 500 HD21 ASN A 10 HD1 TYR A 75 1.32
REMARK 500 O GLY B 59 H ALA B 82 1.46
REMARK 500 O GLY A 59 H ALA A 82 1.46
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 0 -44.97 -130.54
REMARK 500 1 ASP A 3 40.60 -151.11
REMARK 500 1 LYS A 9 -38.16 -148.37
REMARK 500 1 ASN A 10 36.18 -92.28
REMARK 500 1 ASN A 33 39.29 -147.16
REMARK 500 1 ASN A 51 150.00 80.87
REMARK 500 1 ARG A 60 -105.65 -82.40
REMARK 500 1 PHE A 73 117.66 -160.38
REMARK 500 1 GLN A 80 28.10 -154.81
REMARK 500 1 SER A 88 -47.55 -134.48
REMARK 500 1 MET B 1 -45.49 -148.68
REMARK 500 1 LYS B 9 -38.13 -148.43
REMARK 500 1 ASN B 10 36.19 -92.24
REMARK 500 1 ASN B 33 39.26 -147.26
REMARK 500 1 ASN B 51 149.94 80.87
REMARK 500 1 ARG B 60 -105.62 -82.37
REMARK 500 1 PHE B 73 117.68 -160.39
REMARK 500 1 GLN B 80 28.08 -154.79
REMARK 500 1 SER B 88 -47.53 -134.55
REMARK 500 2 SER A 0 46.83 -87.53
REMARK 500 2 LYS A 5 136.90 -178.68
REMARK 500 2 LYS A 9 -37.41 -133.10
REMARK 500 2 TYR A 50 -73.30 -87.74
REMARK 500 2 ASN A 51 142.26 169.77
REMARK 500 2 HIS A 55 72.70 -104.62
REMARK 500 2 ARG A 60 -99.59 -92.38
REMARK 500 2 GLU A 69 -150.90 -96.18
REMARK 500 2 THR A 70 -82.05 -86.59
REMARK 500 2 HIS A 72 86.33 -59.69
REMARK 500 2 PHE A 73 126.58 -179.17
REMARK 500 2 GLN A 80 28.56 -152.24
REMARK 500 2 SER B 0 48.44 -86.23
REMARK 500 2 MET B 1 45.88 -141.43
REMARK 500 2 LYS B 9 -37.44 -133.14
REMARK 500 2 TYR B 50 -73.23 -87.84
REMARK 500 2 ASN B 51 142.19 169.73
REMARK 500 2 HIS B 55 72.59 -104.58
REMARK 500 2 ARG B 60 -99.65 -92.22
REMARK 500 2 GLU B 69 -150.83 -96.19
REMARK 500 2 THR B 70 -81.90 -86.71
REMARK 500 2 HIS B 72 86.31 -59.77
REMARK 500 2 PHE B 73 126.60 -179.16
REMARK 500 2 GLN B 80 28.41 -152.19
REMARK 500 3 PRO A -3 42.87 -76.35
REMARK 500 3 LEU A -2 44.82 -85.67
REMARK 500 3 LYS A 5 136.18 -177.82
REMARK 500 3 LYS A 9 -45.80 -135.33
REMARK 500 3 ASN A 51 141.10 77.10
REMARK 500 3 PRO A 52 156.76 -47.90
REMARK 500 3 ARG A 60 -96.07 -91.99
REMARK 500
REMARK 500 THIS ENTRY HAS 419 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RE6 A 1 89 GB 18087731 NP_080832 1 89
DBREF 1RE6 B 1 89 GB 18087731 NP_080832 1 89
SEQADV 1RE6 GLY A -4 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 PRO A -3 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 LEU A -2 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 GLY A -1 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 SER A 0 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 GLY B -4 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 PRO B -3 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 LEU B -2 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 GLY B -1 GB 18087731 CLONING ARTIFACT
SEQADV 1RE6 SER B 0 GB 18087731 CLONING ARTIFACT
SEQRES 1 A 94 GLY PRO LEU GLY SER MET SER ASP ARG LYS ALA VAL ILE
SEQRES 2 A 94 LYS ASN ALA ASP MET SER GLU ASP MET GLN GLN ASP ALA
SEQRES 3 A 94 VAL ASP CYS ALA THR GLN ALA MET GLU LYS TYR ASN ILE
SEQRES 4 A 94 GLU LYS ASP ILE ALA ALA TYR ILE LYS LYS GLU PHE ASP
SEQRES 5 A 94 LYS LYS TYR ASN PRO THR TRP HIS CYS ILE VAL GLY ARG
SEQRES 6 A 94 ASN PHE GLY SER TYR VAL THR HIS GLU THR LYS HIS PHE
SEQRES 7 A 94 ILE TYR PHE TYR LEU GLY GLN VAL ALA ILE LEU LEU PHE
SEQRES 8 A 94 LYS SER GLY
SEQRES 1 B 94 GLY PRO LEU GLY SER MET SER ASP ARG LYS ALA VAL ILE
SEQRES 2 B 94 LYS ASN ALA ASP MET SER GLU ASP MET GLN GLN ASP ALA
SEQRES 3 B 94 VAL ASP CYS ALA THR GLN ALA MET GLU LYS TYR ASN ILE
SEQRES 4 B 94 GLU LYS ASP ILE ALA ALA TYR ILE LYS LYS GLU PHE ASP
SEQRES 5 B 94 LYS LYS TYR ASN PRO THR TRP HIS CYS ILE VAL GLY ARG
SEQRES 6 B 94 ASN PHE GLY SER TYR VAL THR HIS GLU THR LYS HIS PHE
SEQRES 7 B 94 ILE TYR PHE TYR LEU GLY GLN VAL ALA ILE LEU LEU PHE
SEQRES 8 B 94 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 4 ASN A 10 ALA A 11 0
SHEET 2 A 4 ILE A 74 TYR A 75 -1 O TYR A 75 N ASN A 10
SHEET 3 A 4 ALA A 82 LYS A 87 -1 O LEU A 85 N ILE A 74
SHEET 4 A 4 TRP A 54 HIS A 55 -1 N HIS A 55 O PHE A 86
SHEET 1 B 4 ASN A 10 ALA A 11 0
SHEET 2 B 4 ILE A 74 TYR A 75 -1 O TYR A 75 N ASN A 10
SHEET 3 B 4 ALA A 82 LYS A 87 -1 O LEU A 85 N ILE A 74
SHEET 4 B 4 VAL A 58 GLY A 59 -1 N GLY A 59 O ALA A 82
SHEET 1 C 4 ASN B 10 ALA B 11 0
SHEET 2 C 4 ILE B 74 TYR B 75 -1 O TYR B 75 N ASN B 10
SHEET 3 C 4 ALA B 82 LYS B 87 -1 O LEU B 85 N ILE B 74
SHEET 4 C 4 TRP B 54 HIS B 55 -1 N HIS B 55 O PHE B 86
SHEET 1 D 4 ASN B 10 ALA B 11 0
SHEET 2 D 4 ILE B 74 TYR B 75 -1 O TYR B 75 N ASN B 10
SHEET 3 D 4 ALA B 82 LYS B 87 -1 O LEU B 85 N ILE B 74
SHEET 4 D 4 VAL B 58 GLY B 59 -1 N GLY B 59 O ALA B 82
CISPEP 1 PRO A 52 THR A 53 1 0.16
CISPEP 2 PRO B 52 THR B 53 1 0.19
CISPEP 3 PRO A 52 THR A 53 2 0.62
CISPEP 4 PRO B 52 THR B 53 2 0.69
CISPEP 5 PRO A 52 THR A 53 3 0.40
CISPEP 6 PRO B 52 THR B 53 3 0.49
CISPEP 7 PRO A 52 THR A 53 4 0.44
CISPEP 8 PRO B 52 THR B 53 4 0.45
CISPEP 9 PRO A 52 THR A 53 5 0.37
CISPEP 10 PRO B 52 THR B 53 5 0.18
CISPEP 11 PRO A 52 THR A 53 6 0.37
CISPEP 12 PRO B 52 THR B 53 6 0.37
CISPEP 13 PRO A 52 THR A 53 7 0.50
CISPEP 14 PRO B 52 THR B 53 7 0.41
CISPEP 15 PRO A 52 THR A 53 8 -0.01
CISPEP 16 PRO B 52 THR B 53 8 -0.04
CISPEP 17 PRO A 52 THR A 53 9 0.50
CISPEP 18 PRO B 52 THR B 53 9 0.56
CISPEP 19 PRO A 52 THR A 53 10 0.18
CISPEP 20 PRO B 52 THR B 53 10 0.22
CISPEP 21 PRO A 52 THR A 53 11 0.55
CISPEP 22 PRO B 52 THR B 53 11 0.29
CISPEP 23 PRO A 52 THR A 53 12 -0.22
CISPEP 24 PRO B 52 THR B 53 12 -0.17
CISPEP 25 PRO A 52 THR A 53 13 0.73
CISPEP 26 PRO B 52 THR B 53 13 0.67
CISPEP 27 PRO A 52 THR A 53 14 0.58
CISPEP 28 PRO B 52 THR B 53 14 0.59
CISPEP 29 PRO A 52 THR A 53 15 0.19
CISPEP 30 PRO B 52 THR B 53 15 0.36
CISPEP 31 PRO A 52 THR A 53 16 0.32
CISPEP 32 PRO B 52 THR B 53 16 0.46
CISPEP 33 PRO A 52 THR A 53 17 0.28
CISPEP 34 PRO B 52 THR B 53 17 0.27
CISPEP 35 PRO A 52 THR A 53 18 0.15
CISPEP 36 PRO B 52 THR B 53 18 0.21
CISPEP 37 PRO A 52 THR A 53 19 0.65
CISPEP 38 PRO B 52 THR B 53 19 0.66
CISPEP 39 PRO A 52 THR A 53 20 0.34
CISPEP 40 PRO B 52 THR B 53 20 0.42
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