Header list of 1xsf.pdb file
Complete list - r 2 2 Bytes
HEADER CELL CYCLE, HYDROLASE 19-OCT-04 1XSF
TITLE SOLUTION STRUCTURE OF A RESUSCITATION PROMOTING FACTOR DOMAIN FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE RESUSCITATION-PROMOTING FACTOR RPFB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RPFBC DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: RV1009;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS LYSOZYME-LIKE STRUCTURE, CELL CYCLE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.COHEN-GONSAUD,P.BARTHE,B.HENDERSON,J.WARD,C.ROUMESTAND,N.H.KEEP
REVDAT 5 02-MAR-22 1XSF 1 REMARK
REVDAT 4 24-FEB-09 1XSF 1 VERSN
REVDAT 3 22-MAR-05 1XSF 1 JRNL
REVDAT 2 01-MAR-05 1XSF 1 JRNL
REVDAT 1 15-FEB-05 1XSF 0
JRNL AUTH M.COHEN-GONSAUD,P.BARTHE,C.BAGNERIS,B.HENDERSON,J.WARD,
JRNL AUTH 2 C.ROUMESTAND,N.H.KEEP
JRNL TITL THE STRUCTURE OF A RESUSCITATION-PROMOTING FACTOR DOMAIN
JRNL TITL 2 FROM MYCOBACTERIUM TUBERCULOSIS SHOWS HOMOLOGY TO LYSOZYMES
JRNL REF NAT.STRUCT.MOL.BIOL. V. 12 270 2005
JRNL REFN ISSN 1545-9993
JRNL PMID 15723078
JRNL DOI 10.1038/NSMB905
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.COHEN-GONSAUD,P.BARTHE,F.POMMIER,R.HARRIS,P.C.DRISCOLL,
REMARK 1 AUTH 2 N.H.KEEP,C.ROUMESTAND
REMARK 1 TITL LETTER TO THE EDITOR: (1)H, (15)N, AND (13)C CHEMICAL SHIFT
REMARK 1 TITL 2 ASSIGNMENTS OF THE RESUSCITATION PROMOTING FACTOR DOMAIN OF
REMARK 1 TITL 3 RV1009 FROM MYCOBACTERIUM TUBERCULOSIS
REMARK 1 REF J.BIOMOL.NMR V. 30 373 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 15614636
REMARK 1 DOI 10.1007/S10858-004-3466-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GIFA 4.4, CNS 1.1
REMARK 3 AUTHORS : PONS (GIFA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1757 RESTRAINTS, 1613 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 124
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 20 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1XSF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030714.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.6
REMARK 210 IONIC STRENGTH : 25MM NA-ACETATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM RPFBC DOMAIN U-15N; 25MM
REMARK 210 NA-ACETATE; 2MM BETA-
REMARK 210 MERCAPTOETHANOL; 90% H2O, 10%
REMARK 210 D2O; 0.5MM RPFBC DOMAIN U-15N,
REMARK 210 13C; 25MM NA-ACETATE; 2MM BETA-
REMARK 210 MERCAPTOETHANOL; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED TOCSY; HNCA; HN(CO)CA;
REMARK 210 CBCA(CO)NH; HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, TALOS 3, ARIA 1.2
REMARK 210 METHOD USED : MOLECULAR DYNAMICS IN EXPLICIT
REMARK 210 SOLVENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 HB2 ASP A 32 HH21 ARG A 79 1.32
REMARK 500 HG21 ILE A 45 HA2 GLY A 53 1.33
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 VAL A 11 -71.72 -66.92
REMARK 500 1 VAL A 12 77.79 25.73
REMARK 500 1 THR A 16 -46.48 -147.87
REMARK 500 1 ALA A 71 125.22 165.33
REMARK 500 1 PRO A 72 -5.97 -53.71
REMARK 500 1 PRO A 99 -139.39 -64.73
REMARK 500 2 ALA A 7 -165.15 -124.46
REMARK 500 2 HIS A 8 -9.81 75.92
REMARK 500 2 VAL A 12 84.58 27.97
REMARK 500 2 ALA A 71 125.48 163.26
REMARK 500 2 PRO A 72 -4.00 -55.16
REMARK 500 2 PRO A 99 -94.20 -70.99
REMARK 500 3 VAL A 12 84.33 21.52
REMARK 500 3 THR A 16 -21.99 63.98
REMARK 500 3 LYS A 17 74.94 -114.05
REMARK 500 3 GLU A 21 87.94 47.01
REMARK 500 3 ALA A 71 128.92 162.67
REMARK 500 3 PRO A 72 -4.93 -57.35
REMARK 500 3 PRO A 99 -88.38 -73.95
REMARK 500 4 VAL A 11 -73.26 -99.90
REMARK 500 4 VAL A 12 75.32 21.34
REMARK 500 4 ASN A 46 103.72 -171.24
REMARK 500 4 ALA A 71 126.96 169.10
REMARK 500 4 PRO A 72 -5.90 -56.85
REMARK 500 4 PRO A 99 -138.89 -62.97
REMARK 500 5 PRO A 6 111.42 -39.18
REMARK 500 5 ALA A 10 54.19 -109.66
REMARK 500 5 VAL A 11 -67.04 -124.09
REMARK 500 5 VAL A 12 81.19 26.18
REMARK 500 5 LYS A 17 77.10 32.77
REMARK 500 5 PRO A 18 118.14 -34.10
REMARK 500 5 ALA A 71 128.73 161.57
REMARK 500 5 PRO A 72 -6.68 -54.90
REMARK 500 5 PRO A 99 -131.30 -63.08
REMARK 500 6 HIS A 8 -0.23 69.58
REMARK 500 6 VAL A 12 80.55 25.91
REMARK 500 6 LYS A 17 72.61 37.69
REMARK 500 6 ALA A 71 130.27 161.81
REMARK 500 6 PRO A 72 -2.13 -58.33
REMARK 500 6 TRP A 95 24.39 -141.17
REMARK 500 6 PRO A 99 -110.10 -67.34
REMARK 500 7 ALA A 7 24.80 -77.36
REMARK 500 7 VAL A 12 105.11 54.69
REMARK 500 7 GLU A 21 84.64 46.65
REMARK 500 7 ALA A 71 127.14 166.32
REMARK 500 7 PRO A 72 -7.18 -55.91
REMARK 500 7 PRO A 99 -88.54 -74.77
REMARK 500 8 VAL A 3 108.01 -59.29
REMARK 500 8 VAL A 12 74.76 23.02
REMARK 500 8 CYS A 37 -62.85 -97.22
REMARK 500
REMARK 500 THIS ENTRY HAS 198 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6221 RELATED DB: BMRB
REMARK 900 THE SAME PROTEIN
DBREF 1XSF A 1 108 UNP O05594 O05594_MYCTU 255 362
SEQRES 1 A 108 ASN VAL VAL VAL THR PRO ALA HIS GLU ALA VAL VAL ARG
SEQRES 2 A 108 VAL GLY THR LYS PRO GLY THR GLU VAL PRO PRO VAL ILE
SEQRES 3 A 108 ASP GLY SER ILE TRP ASP ALA ILE ALA GLY CYS GLU ALA
SEQRES 4 A 108 GLY GLY ASN TRP ALA ILE ASN THR GLY ASN GLY TYR TYR
SEQRES 5 A 108 GLY GLY VAL GLN PHE ASP GLN GLY THR TRP GLU ALA ASN
SEQRES 6 A 108 GLY GLY LEU ARG TYR ALA PRO ARG ALA ASP LEU ALA THR
SEQRES 7 A 108 ARG GLU GLU GLN ILE ALA VAL ALA GLU VAL THR ARG LEU
SEQRES 8 A 108 ARG GLN GLY TRP GLY ALA TRP PRO VAL CYS ALA ALA ARG
SEQRES 9 A 108 ALA GLY ALA ARG
HELIX 1 1 ASP A 27 ALA A 39 1 13
HELIX 2 2 ASP A 58 ASN A 65 1 8
HELIX 3 3 GLY A 66 TYR A 70 5 5
HELIX 4 4 THR A 78 GLY A 94 1 17
HELIX 5 5 PRO A 99 GLY A 106 1 8
SSBOND 1 CYS A 37 CYS A 101 1555 1555 2.03
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