Header list of 1xbl.pdb file
Complete list - r 2 2 Bytes
HEADER CHAPERONE 07-OCT-96 1XBL
TITLE NMR STRUCTURE OF THE J-DOMAIN (RESIDUES 2-76) IN THE ESCHERICHIA COLI
TITLE 2 N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR CHAPERONE DNAJ,
TITLE 3 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNAJ;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL FRAGMENT (RESIDUES 2-108) OF THE MOLECULAR
COMPND 5 CHAPERONE DNAJ;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE, DNA REPLICATION, HEAT SHOCK
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.PELLECCHIA,T.SZYPERSKI,D.WALL,C.GEORGOPOULOS,K.WUTHRICH
REVDAT 3 02-MAR-22 1XBL 1 REMARK
REVDAT 2 24-FEB-09 1XBL 1 VERSN
REVDAT 1 11-JAN-97 1XBL 0
JRNL AUTH M.PELLECCHIA,T.SZYPERSKI,D.WALL,C.GEORGOPOULOS,K.WUTHRICH
JRNL TITL NMR STRUCTURE OF THE J-DOMAIN AND THE GLY/PHE-RICH REGION OF
JRNL TITL 2 THE ESCHERICHIA COLI DNAJ CHAPERONE.
JRNL REF J.MOL.BIOL. V. 260 236 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8764403
JRNL DOI 10.1006/JMBI.1996.0395
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.SZYPERSKI,M.PELLECCHIA,D.WALL,C.GEORGOPOULOS,K.WUTHRICH
REMARK 1 TITL NMR STRUCTURE DETERMINATION OF THE ESCHERICHIA COLI DNAJ
REMARK 1 TITL 2 MOLECULAR CHAPERONE: SECONDARY STRUCTURE AND BACKBONE FOLD
REMARK 1 TITL 3 OF THE N-TERMINAL REGION (RESIDUES 2-108) CONTAINING THE
REMARK 1 TITL 4 HIGHLY CONSERVED J DOMAIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 11343 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBHUL,GUNTERT,BILLETER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XBL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177245.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE PAPER *JRNL*
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : REDAC
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION (SEE PAPER
REMARK 210 *JRNL*)
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 77
REMARK 465 GLY A 78
REMARK 465 MET A 79
REMARK 465 GLY A 80
REMARK 465 GLY A 81
REMARK 465 GLY A 82
REMARK 465 GLY A 83
REMARK 465 PHE A 84
REMARK 465 GLY A 85
REMARK 465 GLY A 86
REMARK 465 GLY A 87
REMARK 465 ALA A 88
REMARK 465 ASP A 89
REMARK 465 PHE A 90
REMARK 465 SER A 91
REMARK 465 ASP A 92
REMARK 465 ILE A 93
REMARK 465 PHE A 94
REMARK 465 GLY A 95
REMARK 465 ASP A 96
REMARK 465 VAL A 97
REMARK 465 PHE A 98
REMARK 465 GLY A 99
REMARK 465 ASP A 100
REMARK 465 ILE A 101
REMARK 465 PHE A 102
REMARK 465 GLY A 103
REMARK 465 GLY A 104
REMARK 465 GLY A 105
REMARK 465 ARG A 106
REMARK 465 GLY A 107
REMARK 465 ARG A 108
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 LYS A 3 163.62 65.52
REMARK 500 1 SER A 13 70.75 -64.16
REMARK 500 1 LYS A 14 -106.47 63.17
REMARK 500 1 ALA A 16 154.51 -49.17
REMARK 500 1 ASP A 35 79.99 35.70
REMARK 500 1 ARG A 36 -0.37 57.71
REMARK 500 1 LYS A 41 -40.56 83.03
REMARK 500 1 LEU A 57 7.37 -69.97
REMARK 500 1 SER A 60 -75.49 -98.98
REMARK 500 1 GLN A 68 -72.42 -68.85
REMARK 500 1 TYR A 69 75.27 -161.04
REMARK 500 1 HIS A 71 58.90 -142.94
REMARK 500 1 ALA A 73 -62.45 -151.93
REMARK 500 2 ASP A 5 45.68 39.13
REMARK 500 2 SER A 13 171.80 -57.62
REMARK 500 2 THR A 15 56.87 -150.80
REMARK 500 2 HIS A 33 106.50 4.08
REMARK 500 2 PRO A 34 78.55 -69.48
REMARK 500 2 ARG A 36 -60.30 -126.77
REMARK 500 2 ASN A 37 81.48 68.08
REMARK 500 2 GLN A 38 109.57 -43.02
REMARK 500 2 LYS A 41 -49.20 -177.46
REMARK 500 2 ARG A 63 -71.62 -156.46
REMARK 500 2 TYR A 69 35.03 -162.92
REMARK 500 3 LYS A 3 133.05 64.97
REMARK 500 3 ASP A 5 66.35 16.95
REMARK 500 3 TYR A 7 -62.62 -101.14
REMARK 500 3 LYS A 14 -105.71 48.13
REMARK 500 3 ASP A 35 -105.39 -173.45
REMARK 500 3 ARG A 36 34.55 -80.71
REMARK 500 3 SER A 60 -74.40 -42.30
REMARK 500 3 GLN A 61 -86.46 -99.02
REMARK 500 3 LYS A 62 64.51 33.26
REMARK 500 3 ARG A 63 -75.34 174.49
REMARK 500 4 GLN A 4 99.36 -49.68
REMARK 500 4 ASP A 35 -133.41 -77.06
REMARK 500 4 GLN A 38 -173.67 -64.21
REMARK 500 4 ASP A 40 -71.32 -73.74
REMARK 500 4 LYS A 41 -26.82 96.97
REMARK 500 4 THR A 58 43.32 -87.70
REMARK 500 4 ASP A 59 117.78 56.71
REMARK 500 4 SER A 60 -106.30 -150.36
REMARK 500 4 GLN A 61 -54.82 -134.92
REMARK 500 4 ARG A 63 31.60 -65.84
REMARK 500 4 ALA A 64 -49.39 -168.66
REMARK 500 4 ALA A 72 43.88 -157.62
REMARK 500 4 ALA A 73 -53.58 -149.57
REMARK 500 4 GLU A 75 17.33 -146.90
REMARK 500 5 LYS A 3 148.20 63.78
REMARK 500 5 TYR A 6 -53.28 76.78
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 TYR A 7 0.12 SIDE CHAIN
REMARK 500 1 TYR A 32 0.13 SIDE CHAIN
REMARK 500 1 ARG A 36 0.18 SIDE CHAIN
REMARK 500 1 TYR A 54 0.10 SIDE CHAIN
REMARK 500 1 TYR A 66 0.06 SIDE CHAIN
REMARK 500 2 TYR A 6 0.11 SIDE CHAIN
REMARK 500 2 TYR A 25 0.10 SIDE CHAIN
REMARK 500 2 TYR A 32 0.17 SIDE CHAIN
REMARK 500 2 TYR A 54 0.14 SIDE CHAIN
REMARK 500 3 TYR A 69 0.09 SIDE CHAIN
REMARK 500 3 PHE A 74 0.09 SIDE CHAIN
REMARK 500 4 ARG A 19 0.15 SIDE CHAIN
REMARK 500 4 TYR A 32 0.09 SIDE CHAIN
REMARK 500 5 TYR A 7 0.10 SIDE CHAIN
REMARK 500 5 TYR A 25 0.09 SIDE CHAIN
REMARK 500 5 TYR A 32 0.07 SIDE CHAIN
REMARK 500 5 ARG A 36 0.11 SIDE CHAIN
REMARK 500 5 TYR A 54 0.10 SIDE CHAIN
REMARK 500 5 TYR A 66 0.24 SIDE CHAIN
REMARK 500 5 TYR A 69 0.10 SIDE CHAIN
REMARK 500 6 TYR A 6 0.09 SIDE CHAIN
REMARK 500 6 ARG A 19 0.13 SIDE CHAIN
REMARK 500 6 ARG A 22 0.08 SIDE CHAIN
REMARK 500 6 TYR A 25 0.11 SIDE CHAIN
REMARK 500 6 TYR A 32 0.10 SIDE CHAIN
REMARK 500 6 TYR A 66 0.10 SIDE CHAIN
REMARK 500 7 TYR A 6 0.12 SIDE CHAIN
REMARK 500 7 TYR A 7 0.25 SIDE CHAIN
REMARK 500 7 ARG A 22 0.10 SIDE CHAIN
REMARK 500 7 TYR A 25 0.08 SIDE CHAIN
REMARK 500 7 ARG A 27 0.14 SIDE CHAIN
REMARK 500 7 TYR A 32 0.08 SIDE CHAIN
REMARK 500 7 TYR A 54 0.15 SIDE CHAIN
REMARK 500 7 TYR A 66 0.13 SIDE CHAIN
REMARK 500 8 ARG A 19 0.08 SIDE CHAIN
REMARK 500 8 ARG A 22 0.09 SIDE CHAIN
REMARK 500 8 TYR A 32 0.10 SIDE CHAIN
REMARK 500 8 TYR A 54 0.11 SIDE CHAIN
REMARK 500 9 TYR A 6 0.14 SIDE CHAIN
REMARK 500 9 TYR A 7 0.08 SIDE CHAIN
REMARK 500 9 ARG A 22 0.08 SIDE CHAIN
REMARK 500 9 TYR A 32 0.11 SIDE CHAIN
REMARK 500 9 ARG A 63 0.10 SIDE CHAIN
REMARK 500 10 TYR A 6 0.07 SIDE CHAIN
REMARK 500 10 TYR A 7 0.08 SIDE CHAIN
REMARK 500 10 ARG A 22 0.08 SIDE CHAIN
REMARK 500 10 TYR A 25 0.13 SIDE CHAIN
REMARK 500 10 TYR A 32 0.12 SIDE CHAIN
REMARK 500 10 TYR A 66 0.08 SIDE CHAIN
REMARK 500 10 TYR A 69 0.12 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 102 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XBL A 2 108 UNP P08622 DNAJ_ECOLI 1 107
SEQRES 1 A 107 ALA LYS GLN ASP TYR TYR GLU ILE LEU GLY VAL SER LYS
SEQRES 2 A 107 THR ALA GLU GLU ARG GLU ILE ARG LYS ALA TYR LYS ARG
SEQRES 3 A 107 LEU ALA MET LYS TYR HIS PRO ASP ARG ASN GLN GLY ASP
SEQRES 4 A 107 LYS GLU ALA GLU ALA LYS PHE LYS GLU ILE LYS GLU ALA
SEQRES 5 A 107 TYR GLU VAL LEU THR ASP SER GLN LYS ARG ALA ALA TYR
SEQRES 6 A 107 ASP GLN TYR GLY HIS ALA ALA PHE GLU GLN GLY GLY MET
SEQRES 7 A 107 GLY GLY GLY GLY PHE GLY GLY GLY ALA ASP PHE SER ASP
SEQRES 8 A 107 ILE PHE GLY ASP VAL PHE GLY ASP ILE PHE GLY GLY GLY
SEQRES 9 A 107 ARG GLY ARG
HELIX 1 1H TYR A 6 LEU A 10 1 5
HELIX 2 2H GLU A 18 TYR A 32 1 15
HELIX 3 3H LYS A 41 LEU A 57 1 17
HELIX 4 4H GLN A 61 GLN A 68 1 8
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