Header list of 1hx7.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 11-JAN-01 1HX7
TITLE SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF GAMMA DELTA RESOLVASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSPOSON GAMMA-DELTA RESOLVASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL CATALYTIC DOMAIN;
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 BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDJ1.3
KEYWDS RECOMBINASE, CATALYTIC DOMAIN, MIXED ALPHA BETA, MONOMER, DNA BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR B.PAN,G.P.MULLEN
REVDAT 3 23-FEB-22 1HX7 1 REMARK
REVDAT 2 24-FEB-09 1HX7 1 VERSN
REVDAT 1 16-JAN-02 1HX7 0
JRNL AUTH B.PAN,M.W.MACIEJEWSKI,A.MARINTCHEV,G.P.MULLEN
JRNL TITL SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF GAMMADELTA
JRNL TITL 2 RESOLVASE. IMPLICATIONS FOR THE MECHANISM OF CATALYSIS.
JRNL REF J.MOL.BIOL. V. 310 1089 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11501998
JRNL DOI 10.1006/JMBI.2001.4821
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.PAN,G.P.MULLEN
REMARK 1 TITL 1H, 15N AND 13C RESONANCE ASSIGNMENTS FOR THE CATALYTIC CORE
REMARK 1 TITL 2 OF GAMMA DELTA RESOLVASE
REMARK 1 REF J.BIOMOL.NMR V. 13 307 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008316603457
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, XPLOR 4.0
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (XPLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE NMR RESTRAINTS INCLUDED 2109 USEFUL
REMARK 3 NOE DETERMINED UPPER DISTANCE RESTRAINTS, 35 HYDROGEN BONDS, AND
REMARK 3 297 TORSION ANGLE RESTRAINTS. STRUCTURES WERE CALCULATED IN THE
REMARK 3 DYANA USING TORSION ANGLE DYNAMICS. THE CALCULATION STARTED WITH
REMARK 3 200 RANDOMIZED STRUCTURES. THE 19 STRUCTURES WITH THE LOWEST
REMARK 3 TARGET FUNCTION WERE REFINED WITHIN XPLOR USING SIMULATED
REMARK 3 ANNEALING. THE 19 REFINED STRUCTURAL CONFORMERS DISPLAYED NO NOE
REMARK 3 VIOLATIONS >0.3 ANGSTROMS AND NO DIHEDRAL ANGLE VIOLATIONS >3
REMARK 3 DEGREES.
REMARK 4
REMARK 4 1HX7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012651.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 1M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.002 M GAMMA DELTA RESOLVASE (1
REMARK 210 -105) U-15N; 0.020 M PHOSPHATE
REMARK 210 BUFFER, PH 6.5; 90% H2O, 10% D2O;
REMARK 210 0.002 M GAMMA DELTA RESOLVASE
REMARK 210 (1-105) U-15N,13C; 0.020 M
REMARK 210 PHOSPHATE BUFFER, PH 6.5; 90%
REMARK 210 H2O, 10% D2O; 0.002 M GAMMA
REMARK 210 DELTA RESOLVASE (1-105) U-15N,
REMARK 210 13C; 0.020 M PHOSPHATE BUFFER,
REMARK 210 PH 6.5; 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, XEASY 1.3.13, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND AGREEMENT WITH
REMARK 210 EXPERIMENTAL NOESY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE 3D NMR
REMARK 210 SPECTROSCOPY FOR RESONANCE ASSIGNMENTS AND DOUBLE-RESONANCE 3D
REMARK 210 NMR SPECTROSCOPY FOR OBTAINING NOESY DATA.
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 GLN A 13 -161.09 -62.46
REMARK 500 1 ARG A 32 58.91 -111.01
REMARK 500 1 ARG A 45 56.57 -105.68
REMARK 500 1 LYS A 64 59.27 -100.52
REMARK 500 1 ASP A 67 -60.33 -176.02
REMARK 500 1 ARG A 68 131.27 179.95
REMARK 500 1 ASP A 72 -73.46 -174.60
REMARK 500 1 ALA A 74 37.88 -177.80
REMARK 500 1 ASP A 95 28.47 -162.17
REMARK 500 1 SER A 98 -69.98 -127.75
REMARK 500 1 ASP A 100 88.27 -61.31
REMARK 500 1 MET A 103 -63.33 -94.13
REMARK 500 2 SER A 10 -44.77 -136.16
REMARK 500 2 GLN A 13 -55.36 -176.99
REMARK 500 2 GLN A 14 33.43 -167.73
REMARK 500 2 ARG A 32 58.62 -110.46
REMARK 500 2 LYS A 37 81.61 -66.02
REMARK 500 2 ASP A 44 62.16 -106.66
REMARK 500 2 ASP A 67 -50.91 -155.42
REMARK 500 2 ARG A 68 133.56 179.24
REMARK 500 2 ASP A 72 39.10 -167.70
REMARK 500 2 THR A 73 -157.96 -166.32
REMARK 500 2 ALA A 74 47.79 -90.21
REMARK 500 2 GLN A 78 -70.65 -58.06
REMARK 500 2 ASP A 95 -52.30 -153.81
REMARK 500 2 SER A 98 -71.32 -66.05
REMARK 500 2 THR A 99 68.38 -177.40
REMARK 500 2 ASP A 100 94.44 -58.82
REMARK 500 3 VAL A 9 -174.63 -58.59
REMARK 500 3 SER A 10 -42.19 -164.72
REMARK 500 3 GLN A 13 -158.53 -62.45
REMARK 500 3 ARG A 32 58.66 -109.72
REMARK 500 3 LYS A 37 50.57 -94.78
REMARK 500 3 ASP A 44 43.86 -156.26
REMARK 500 3 ARG A 45 84.98 -60.71
REMARK 500 3 GLU A 57 101.96 -52.08
REMARK 500 3 ARG A 68 130.78 -175.37
REMARK 500 3 ALA A 74 77.25 -67.45
REMARK 500 3 GLN A 78 -70.55 -72.91
REMARK 500 3 ASP A 95 -68.90 -120.31
REMARK 500 3 GLU A 102 -173.26 -65.50
REMARK 500 4 LEU A 3 79.64 -105.87
REMARK 500 4 VAL A 9 -176.01 -55.63
REMARK 500 4 SER A 10 -43.04 -160.83
REMARK 500 4 THR A 11 -159.29 -83.93
REMARK 500 4 GLN A 13 -76.29 -48.39
REMARK 500 4 GLN A 14 59.34 -152.79
REMARK 500 4 ARG A 32 58.53 -110.95
REMARK 500 4 LYS A 37 57.45 -98.01
REMARK 500 4 SER A 41 -73.30 -114.76
REMARK 500
REMARK 500 THIS ENTRY HAS 282 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4269 RELATED DB: BMRB
REMARK 900 4269 IS THE 1H, 15N AND 13C CHEMICAL SHIFT ASSIGNMENTS FOR THE
REMARK 900 CATALYTIC CORE OF GAMMA DELTA RESOLVASE
DBREF 1HX7 A 1 105 UNP P03012 TNR1_ECOLI 1 105
SEQRES 1 A 105 MET ARG LEU PHE GLY TYR ALA ARG VAL SER THR SER GLN
SEQRES 2 A 105 GLN SER LEU ASP ILE GLN VAL ARG ALA LEU LYS ASP ALA
SEQRES 3 A 105 GLY VAL LYS ALA ASN ARG ILE PHE THR ASP LYS ALA SER
SEQRES 4 A 105 GLY SER SER SER ASP ARG LYS GLY LEU ASP LEU LEU ARG
SEQRES 5 A 105 MET LYS VAL GLU GLU GLY ASP VAL ILE LEU VAL LYS LYS
SEQRES 6 A 105 LEU ASP ARG LEU GLY ARG ASP THR ALA ASP MET ILE GLN
SEQRES 7 A 105 LEU ILE LYS GLU PHE ASP ALA GLN GLY VAL SER ILE ARG
SEQRES 8 A 105 PHE ILE ASP ASP GLY ILE SER THR ASP GLY GLU MET GLY
SEQRES 9 A 105 LYS
HELIX 1 1 GLN A 14 GLY A 27 1 14
HELIX 2 2 LYS A 29 ASN A 31 5 3
HELIX 3 3 LYS A 46 ARG A 52 1 7
HELIX 4 4 ILE A 77 GLN A 86 1 10
SHEET 1 A 3 ILE A 33 PHE A 34 0
SHEET 2 A 3 LEU A 3 TYR A 6 1 O GLY A 5 N PHE A 34
SHEET 3 A 3 VAL A 60 VAL A 63 1 O VAL A 60 N PHE A 4
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 23 2 Bytes