Header list of 1tm9.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 10-JUN-04 1TM9
TITLE NMR STRUCTURE OF GENE TARGET NUMBER GI3844938 FROM MYCOPLASMA
TITLE 2 GENITALIUM: BERKELEY STRUCTURAL GENOMICS CENTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN MG354;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GI3844938;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOPLASMA GENITALIUM;
SOURCE 3 ORGANISM_TAXID: 2097;
SOURCE 4 GENE: MG354;
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: PSJS1244
KEYWDS ALL ALPHA HELICAL PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, BERKELEY STRUCTURAL GENOMICS CENTER, BSGC,
KEYWDS 3 UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR J.G.PELTON,J.SHI,H.YOKOTA,R.KIM,D.E.WEMMER,BERKELEY STRUCTURAL
AUTHOR 2 GENOMICS CENTER (BSGC)
REVDAT 4 02-MAR-22 1TM9 1 REMARK
REVDAT 3 24-FEB-09 1TM9 1 VERSN
REVDAT 2 24-OCT-06 1TM9 1 KEYWDS AUTHOR REMARK DBREF
REVDAT 2 2 1 MASTER
REVDAT 1 10-AUG-04 1TM9 0
JRNL AUTH J.G.PELTON,J.SHI,H.YOKOTA,R.KIM,D.E.WEMMER
JRNL TITL NMR STRUCTURE OF GENE TARGET GI3844938 FROM MYCOPLASMA
JRNL TITL 2 GENITALIUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON 850 NOE
REMARK 3 RESTRAINTS (278 INTRA-RESIDUE, 238 SEQUENTIAL, 213 MEDIUM-RANGE,
REMARK 3 AND 121 LONG-RANGE), 86 HYDROGEN BOND RESTRAINTS (43 HYDROGEN
REMARK 3 BONDS), AND 69 PHI TORSION ANGLE RESTRAINTS, USING THE PROGRAM
REMARK 3 DYANA. THE STRUCTURES WERE NOT ENERGY MINIMIZED.
REMARK 4
REMARK 4 1TM9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022767.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.14
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 MM SODIUM PHOSPHATE, 100 MM
REMARK 210 SODIUM CHLORIDE, 1 MM EDTA, 1 MM
REMARK 210 TCEP
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY; HNHA; 3D_15N-
REMARK 210 SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.0.4,
REMARK 210 XWINNMR 3.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY, STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS,
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NOES TO PHE SIDECHAINS WERE IDENTIFIED IN 2D 13C HALF
REMARK 210 -FILTERED AND 2D 13C DOUBLE HALF-FILTERED NOESY SPECTRA ON A
REMARK 210 SAMPLE WITH UNLABELED PHE AND ALL OTHER RESIDUES BOTH 15N AND
REMARK 210 13C LABELED
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 O ILE A 126 H ILE A 130 1.48
REMARK 500 O PHE A 27 H THR A 31 1.49
REMARK 500 O ILE A 11 H ASN A 15 1.50
REMARK 500 O VAL A 68 H LYS A 72 1.55
REMARK 500 OE1 GLU A 52 HZ2 LYS A 55 1.55
REMARK 500 O LYS A 65 H ASN A 69 1.59
REMARK 500 H THR A 20 OE1 GLU A 23 1.59
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 GLN A 3 158.49 -48.03
REMARK 500 1 ASN A 4 169.14 174.61
REMARK 500 1 ASN A 5 -151.03 177.36
REMARK 500 1 SER A 12 -74.33 -37.24
REMARK 500 1 GLN A 16 31.42 -90.44
REMARK 500 1 ALA A 17 -72.56 -135.54
REMARK 500 1 CYS A 18 -164.19 -58.48
REMARK 500 1 SER A 19 -89.67 -131.95
REMARK 500 1 THR A 20 -168.10 -79.73
REMARK 500 1 CYS A 29 -71.11 -90.96
REMARK 500 1 ARG A 32 46.99 -85.11
REMARK 500 1 GLU A 33 38.17 -171.26
REMARK 500 1 SER A 34 -107.73 -116.43
REMARK 500 1 ASP A 35 -51.26 -171.10
REMARK 500 1 VAL A 40 165.13 -43.54
REMARK 500 1 ASP A 41 64.98 -69.54
REMARK 500 1 GLU A 52 42.46 -88.05
REMARK 500 1 LYS A 55 30.89 -92.92
REMARK 500 1 GLU A 57 -83.38 -52.13
REMARK 500 1 ASN A 58 -37.14 -37.08
REMARK 500 1 ILE A 61 -71.68 -63.89
REMARK 500 1 SER A 75 41.03 -88.06
REMARK 500 1 SER A 76 -60.79 -169.56
REMARK 500 1 VAL A 77 80.59 39.56
REMARK 500 1 THR A 80 47.00 -94.04
REMARK 500 1 GLN A 82 -62.88 -143.11
REMARK 500 1 PHE A 87 48.70 -90.09
REMARK 500 1 PHE A 88 -43.91 -163.50
REMARK 500 1 TYR A 102 -70.12 -43.64
REMARK 500 1 ASP A 112 104.30 -168.69
REMARK 500 1 ASN A 114 112.42 162.27
REMARK 500 1 LYS A 116 -178.46 74.79
REMARK 500 1 ILE A 118 -156.69 -132.41
REMARK 500 1 ASP A 128 -62.30 -90.17
REMARK 500 1 LEU A 134 -84.93 -56.38
REMARK 500 1 ASN A 135 41.52 174.63
REMARK 500 2 GLU A 2 141.17 174.20
REMARK 500 2 GLN A 3 127.63 175.65
REMARK 500 2 ASN A 4 137.84 62.54
REMARK 500 2 ILE A 6 -81.58 -56.91
REMARK 500 2 LYS A 7 -34.06 -39.89
REMARK 500 2 PHE A 13 -83.96 -48.71
REMARK 500 2 ALA A 17 -73.67 -98.95
REMARK 500 2 CYS A 18 -158.89 -59.83
REMARK 500 2 SER A 19 -84.46 -128.04
REMARK 500 2 GLN A 22 -31.19 -39.30
REMARK 500 2 GLU A 33 31.83 -170.89
REMARK 500 2 SER A 34 -107.27 -128.81
REMARK 500 2 ASP A 35 -59.77 -171.03
REMARK 500 2 THR A 36 -143.42 -122.78
REMARK 500
REMARK 500 THIS ENTRY HAS 859 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BSGCAIR30548 RELATED DB: TARGETDB
DBREF 1TM9 A 1 137 UNP P47596 Y354_MYCGE 1 137
SEQRES 1 A 137 MET GLU GLN ASN ASN ILE LYS GLU GLN LEU ILE SER PHE
SEQRES 2 A 137 PHE ASN GLN ALA CYS SER THR HIS GLN GLU ARG LEU ASP
SEQRES 3 A 137 PHE ILE CYS SER THR ARG GLU SER ASP THR PHE SER SER
SEQRES 4 A 137 VAL ASP VAL PRO LEU GLU PRO ILE LYS ASN ILE ILE GLU
SEQRES 5 A 137 ILE THR LYS ASP GLU ASN GLN GLN ILE GLU ILE THR LYS
SEQRES 6 A 137 ILE ALA VAL ASN ASN ILE LYS THR LEU SER SER VAL GLY
SEQRES 7 A 137 ALA THR GLY GLN TYR MET ALA SER PHE PHE SER THR ASN
SEQRES 8 A 137 SER GLU PRO ALA ILE ILE PHE CYS VAL ILE TYR PHE LEU
SEQRES 9 A 137 TYR HIS PHE GLY PHE LEU LYS ASP ASN ASN LYS LYS GLN
SEQRES 10 A 137 ILE ILE LYS LYS ALA TYR GLU THR ILE ALA ASP ASN ILE
SEQRES 11 A 137 ALA ASP TYR LEU ASN GLU ASN
HELIX 1 1 ASN A 5 GLN A 16 1 12
HELIX 2 2 GLN A 22 ARG A 32 1 11
HELIX 3 3 PRO A 43 GLU A 52 1 10
HELIX 4 4 ASP A 56 SER A 75 1 20
HELIX 5 5 ALA A 85 THR A 90 1 6
HELIX 6 6 ASN A 91 PHE A 107 1 17
HELIX 7 7 ILE A 118 ILE A 130 1 13
HELIX 8 8 ILE A 130 ASN A 135 1 6
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