Header list of 1exk.pdb file
Complete list - b 16 2 Bytes
HEADER CHAPERONE 03-MAY-00 1EXK
TITLE SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI
TITLE 2 CHAPERONE PROTEIN DNAJ.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNAJ PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 131-209;
COMPND 5 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;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET24A;
SOURCE 7 OTHER_DETAILS: SYNTHETIC GENE BASED ON E. COLI DNAJ CRD SEQUENCE
KEYWDS EXTENDED BETA-HAIRPIN, CXXCXGXG, ZINC-BINDING MOTIF, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.MARTINEZ-YAMOUT,G.B.LEGGE,O.ZHANG,P.E.WRIGHT,H.J.DYSON
REVDAT 3 16-FEB-22 1EXK 1 REMARK LINK
REVDAT 2 24-FEB-09 1EXK 1 VERSN
REVDAT 1 26-JUL-00 1EXK 0
JRNL AUTH M.MARTINEZ-YAMOUT,G.B.LEGGE,O.ZHANG,P.E.WRIGHT,H.J.DYSON
JRNL TITL SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE
JRNL TITL 2 ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.
JRNL REF J.MOL.BIOL. V. 300 805 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10891270
JRNL DOI 10.1006/JMBI.2000.3923
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, AMBER 6.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1361 UNIQUE
REMARK 3 NOE-BASED DISTANCE RESTRAINTS AND 99 TORSION ANGLE RESTAINTS AND
REMARK 3 24 STEREO ASSIGNMENTS.
REMARK 4
REMARK 4 1EXK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000010997.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293
REMARK 210 PH : 6.8; 6.8
REMARK 210 IONIC STRENGTH : 50 MM; 50 MM
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 600 UM DNAJ CRD U-15N,13C; 20 MM
REMARK 210 TRIS-D11 PH 6.8; 300 UM ZNCL2;
REMARK 210 50 MM NACL; 2 MM DTT; 0.02% NAN3;
REMARK 210 600 UM DNAJ CRD U-15N; 20 MM
REMARK 210 TRIS-D11 PH 6.8; 300 UM ZNCL2;
REMARK 210 50 MM NACL;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 13C/15N CN-
REMARK 210 NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.1.2, SANE 1.0, DYANA
REMARK 210 1.5, SPIRIT 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 112
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
REMARK 210
REMARK 210 REMARK: THE SEQUENCE-SPECIFIC ASSIGNMENTS WERE COMPLETED USING
REMARK 210 STANDARD DOUBLE AND TRIPLE RESONANCE NMR EXPERIMENTS.
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: 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 ARG A 7 55.36 -69.83
REMARK 500 1 SER A 20 -75.22 -80.05
REMARK 500 1 THR A 26 70.42 -68.56
REMARK 500 1 ARG A 43 55.94 -69.44
REMARK 500 2 THR A 3 -166.64 -166.83
REMARK 500 2 LYS A 4 -159.16 -167.92
REMARK 500 2 PRO A 9 91.08 -64.11
REMARK 500 2 ASP A 65 77.05 -109.64
REMARK 500 2 CYS A 67 94.89 -69.99
REMARK 500 3 ARG A 7 36.56 -98.36
REMARK 500 3 PRO A 9 74.76 -66.38
REMARK 500 3 PRO A 24 132.08 -39.13
REMARK 500 3 ARG A 43 41.34 -144.28
REMARK 500 3 GLN A 44 -163.69 -166.63
REMARK 500 3 PHE A 46 -60.74 -158.07
REMARK 500 3 ILE A 63 73.74 -108.62
REMARK 500 3 CYS A 67 91.65 -68.55
REMARK 500 3 ARG A 78 49.32 -75.56
REMARK 500 4 PRO A 9 103.18 -45.85
REMARK 500 4 SER A 20 -74.51 -78.00
REMARK 500 4 ARG A 43 60.69 -69.87
REMARK 500 4 GLN A 44 48.29 -77.36
REMARK 500 4 PHE A 46 -72.66 -102.35
REMARK 500 5 PRO A 24 126.73 -22.27
REMARK 500 5 HIS A 35 47.96 39.78
REMARK 500 5 ARG A 43 65.17 -62.40
REMARK 500 5 ASP A 65 68.30 -111.62
REMARK 500 6 THR A 10 54.62 -142.41
REMARK 500 6 ARG A 43 62.48 -66.21
REMARK 500 6 PHE A 46 -72.51 -98.23
REMARK 500 6 ASP A 65 79.91 -107.98
REMARK 500 6 CYS A 67 87.13 -69.32
REMARK 500 6 ARG A 78 70.84 -69.42
REMARK 500 7 VAL A 2 71.00 -54.52
REMARK 500 7 THR A 3 -78.57 -145.55
REMARK 500 7 LYS A 4 -56.36 -141.22
REMARK 500 7 ILE A 6 63.16 -69.12
REMARK 500 7 THR A 10 59.82 -59.73
REMARK 500 7 PRO A 24 121.82 -28.53
REMARK 500 7 PRO A 28 -175.97 -68.31
REMARK 500 7 ARG A 43 64.41 -68.68
REMARK 500 7 PHE A 46 -65.94 -109.68
REMARK 500 7 ASP A 65 76.79 -109.62
REMARK 500 8 PRO A 9 73.26 -68.32
REMARK 500 8 PRO A 24 122.98 -39.99
REMARK 500 8 PHE A 46 -35.84 -146.72
REMARK 500 8 CYS A 67 94.63 -69.65
REMARK 500 8 ARG A 78 76.13 -68.98
REMARK 500 9 ILE A 6 66.11 -67.49
REMARK 500 9 LYS A 23 154.01 -49.34
REMARK 500
REMARK 500 THIS ENTRY HAS 111 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 3 ARG A 7 0.07 SIDE CHAIN
REMARK 500 3 ARG A 59 0.18 SIDE CHAIN
REMARK 500 5 ARG A 59 0.16 SIDE CHAIN
REMARK 500 7 ARG A 59 0.08 SIDE CHAIN
REMARK 500 8 PHE A 47 0.08 SIDE CHAIN
REMARK 500 8 ARG A 59 0.13 SIDE CHAIN
REMARK 500 8 ARG A 75 0.12 SIDE CHAIN
REMARK 500 8 ARG A 78 0.15 SIDE CHAIN
REMARK 500 10 ARG A 59 0.08 SIDE CHAIN
REMARK 500 12 ARG A 59 0.10 SIDE CHAIN
REMARK 500 12 ARG A 75 0.14 SIDE CHAIN
REMARK 500 17 ARG A 59 0.13 SIDE CHAIN
REMARK 500 17 ARG A 75 0.09 SIDE CHAIN
REMARK 500 20 ARG A 75 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 80 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 SG 108.8
REMARK 620 3 CYS A 67 SG 109.8 112.9
REMARK 620 4 CYS A 70 SG 109.2 107.4 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 81 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 31 SG
REMARK 620 2 CYS A 34 SG 109.9
REMARK 620 3 CYS A 53 SG 109.8 110.4
REMARK 620 4 CYS A 56 SG 109.2 108.6 108.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 80
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 81
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4677 RELATED DB: BMRB
REMARK 900 DNAJ CRD SEQUENCE-SPECIFIC ASSIGNMENTS
DBREF 1EXK A 1 79 UNP P08622 DNAJ_ECOLI 131 209
SEQRES 1 A 79 GLY VAL THR LYS GLU ILE ARG ILE PRO THR LEU GLU GLU
SEQRES 2 A 79 CYS ASP VAL CYS HIS GLY SER GLY ALA LYS PRO GLY THR
SEQRES 3 A 79 GLN PRO GLN THR CYS PRO THR CYS HIS GLY SER GLY GLN
SEQRES 4 A 79 VAL GLN MET ARG GLN GLY PHE PHE ALA VAL GLN GLN THR
SEQRES 5 A 79 CYS PRO HIS CYS GLN GLY ARG GLY THR LEU ILE LYS ASP
SEQRES 6 A 79 PRO CYS ASN LYS CYS HIS GLY HIS GLY ARG VAL GLU ARG
SEQRES 7 A 79 SER
HET ZN A 80 1
HET ZN A 81 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 ASP A 15 HIS A 18 5 4
HELIX 2 2 CYS A 67 HIS A 71 5 5
SHEET 1 A 2 LEU A 11 GLU A 13 0
SHEET 2 A 2 ARG A 75 GLU A 77 -1 O VAL A 76 N GLU A 12
SHEET 1 B 2 GLN A 29 THR A 30 0
SHEET 2 B 2 THR A 61 LEU A 62 -1 N LEU A 62 O GLN A 29
SHEET 1 C 2 GLN A 39 GLN A 44 0
SHEET 2 C 2 PHE A 47 THR A 52 -1 N PHE A 47 O GLN A 44
LINK SG CYS A 14 ZN ZN A 80 1555 1555 2.29
LINK SG CYS A 17 ZN ZN A 80 1555 1555 2.30
LINK SG CYS A 31 ZN ZN A 81 1555 1555 2.29
LINK SG CYS A 34 ZN ZN A 81 1555 1555 2.30
LINK SG CYS A 53 ZN ZN A 81 1555 1555 2.29
LINK SG CYS A 56 ZN ZN A 81 1555 1555 2.29
LINK SG CYS A 67 ZN ZN A 80 1555 1555 2.30
LINK SG CYS A 70 ZN ZN A 80 1555 1555 2.29
SITE 1 AC1 4 CYS A 14 CYS A 17 CYS A 67 CYS A 70
SITE 1 AC2 4 CYS A 31 CYS A 34 CYS A 53 CYS A 56
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